# STOCKHOLM 1.0 #=GF ID 3.30.465.10/FF/000017 #=GF DE Xanthine dehydrogenase, FAD binding subunit #=GF AC 3.30.465.10/FF/000017 #=GF TP FunFam #=GF DR CATH: v4.3 #=GF DR DOPS: 96.938 #=GS 1ffvF03/60-173 AC P19914 #=GS 1ffvF03/60-173 OS Hydrogenophaga pseudoflava #=GS 1ffvF03/60-173 DE Carbon monoxide dehydrogenase medium chain #=GS 1ffvF03/60-173 DR CATH; 1ffv; F:60-173; #=GS 1ffvF03/60-173 DR ORG; Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Hydrogenophaga; Hydrogenophaga pseudoflava; #=GS 1ffvF03/60-173 DR GO; GO:0018492; #=GS 1ffvF03/60-173 DR EC; 1.2.5.3; #=GS Q46800/56-173 AC Q46800 #=GS Q46800/56-173 OS Escherichia coli K-12 #=GS Q46800/56-173 DE Putative xanthine dehydrogenase FAD-binding subunit XdhB #=GS Q46800/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS Q46800/56-173 DR GO; GO:0004854; GO:0006150; GO:0071949; #=GS Q46800/56-173 DR EC; 1.17.1.4; #=GS Q4J6M6/57-173 AC Q4J6M6 #=GS Q4J6M6/57-173 OS Sulfolobus acidocaldarius DSM 639 #=GS Q4J6M6/57-173 DE Glyceraldehyde dehydrogenase medium chain #=GS Q4J6M6/57-173 DR ORG; Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; Sulfolobus; Sulfolobus acidocaldarius; #=GS Q4J6M6/57-173 DR GO; GO:0005737; GO:0016903; GO:0050660; #=GS Q4J6M6/57-173 DR EC; 1.2.99.8; #=GS Q0QLF4/57-177 AC Q0QLF4 #=GS Q0QLF4/57-177 OS Eubacterium barkeri #=GS Q0QLF4/57-177 DE Nicotinate dehydrogenase FAD-subunit #=GS Q0QLF4/57-177 DR ORG; Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; Eubacterium; Eubacterium barkeri; #=GS Q0QLF4/57-177 DR GO; GO:0050138; GO:0051187; #=GS Q0QLF4/57-177 DR EC; 1.17.1.5; #=GS D7REY4/58-176 AC D7REY4 #=GS D7REY4/58-176 OS Pseudomonas sp. CBB1 #=GS D7REY4/58-176 DE Caffeine dehydrogenase subunit beta #=GS D7REY4/58-176 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas; Pseudomonas sp. CBB1; #=GS D7REY4/58-176 DR GO; GO:0016491; GO:0055114; #=GS D7REY4/58-176 DR EC; 1.17.5.2; #=GS Q5LT94/59-165 AC Q5LT94 #=GS Q5LT94/59-165 OS Ruegeria pomeroyi DSS-3 #=GS Q5LT94/59-165 DE Carbon monoxide dehydrogenase, medium subunit, putative #=GS Q5LT94/59-165 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Ruegeria; Ruegeria pomeroyi; #=GS Q5LT94/59-165 DR GO; GO:0006730; GO:0018492; #=GS Q5LVP6/229-342 AC Q5LVP6 #=GS Q5LVP6/229-342 OS Ruegeria pomeroyi DSS-3 #=GS Q5LVP6/229-342 DE Xanthine dehydrogenase, A subunit #=GS Q5LVP6/229-342 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Ruegeria; Ruegeria pomeroyi; #=GS Q5LVP6/229-342 DR GO; GO:0004854; #=GS 1ffvC03/60-173 AC P19914 #=GS 1ffvC03/60-173 OS Hydrogenophaga pseudoflava #=GS 1ffvC03/60-173 DE Carbon monoxide dehydrogenase medium chain #=GS 1ffvC03/60-173 DR CATH; 1ffv; C:60-173; #=GS 1ffvC03/60-173 DR ORG; Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Hydrogenophaga; Hydrogenophaga pseudoflava; #=GS 1ffvC03/60-173 DR GO; GO:0018492; #=GS 1ffvC03/60-173 DR EC; 1.2.5.3; #=GS 1ffuF03/60-173 AC P19914 #=GS 1ffuF03/60-173 OS Hydrogenophaga pseudoflava #=GS 1ffuF03/60-173 DE Carbon monoxide dehydrogenase medium chain #=GS 1ffuF03/60-173 DR CATH; 1ffu; F:60-173; #=GS 1ffuF03/60-173 DR ORG; Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Hydrogenophaga; Hydrogenophaga pseudoflava; #=GS 1ffuF03/60-173 DR GO; GO:0018492; #=GS 1ffuF03/60-173 DR EC; 1.2.5.3; #=GS 1ffuC03/60-173 AC P19914 #=GS 1ffuC03/60-173 OS Hydrogenophaga pseudoflava #=GS 1ffuC03/60-173 DE Carbon monoxide dehydrogenase medium chain #=GS 1ffuC03/60-173 DR CATH; 1ffu; C:60-173; #=GS 1ffuC03/60-173 DR ORG; Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Hydrogenophaga; Hydrogenophaga pseudoflava; #=GS 1ffuC03/60-173 DR GO; GO:0018492; #=GS 1ffuC03/60-173 DR EC; 1.2.5.3; #=GS 1zxiF02/60-174 AC P19920 #=GS 1zxiF02/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1zxiF02/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1zxiF02/60-174 DR CATH; 1zxi; F:60-174; #=GS 1zxiF02/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS 1zxiC02/60-174 AC P19920 #=GS 1zxiC02/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1zxiC02/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1zxiC02/60-174 DR CATH; 1zxi; C:60-174; #=GS 1zxiC02/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS 1n63F03/60-174 AC P19920 #=GS 1n63F03/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1n63F03/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1n63F03/60-174 DR CATH; 1n63; F:60-174; #=GS 1n63F03/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS 1n63C03/60-174 AC P19920 #=GS 1n63C03/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1n63C03/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1n63C03/60-174 DR CATH; 1n63; C:60-174; #=GS 1n63C03/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS 1n62F03/60-174 AC P19920 #=GS 1n62F03/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1n62F03/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1n62F03/60-174 DR CATH; 1n62; F:60-174; #=GS 1n62F03/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS 1n62C03/60-174 AC P19920 #=GS 1n62C03/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1n62C03/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1n62C03/60-174 DR CATH; 1n62; C:60-174; #=GS 1n62C03/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS 1n61F03/60-174 AC P19920 #=GS 1n61F03/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1n61F03/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1n61F03/60-174 DR CATH; 1n61; F:60-174; #=GS 1n61F03/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS 1n61C03/60-174 AC P19920 #=GS 1n61C03/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1n61C03/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1n61C03/60-174 DR CATH; 1n61; C:60-174; #=GS 1n61C03/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS 1n60F03/60-174 AC P19920 #=GS 1n60F03/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1n60F03/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1n60F03/60-174 DR CATH; 1n60; F:60-174; #=GS 1n60F03/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS 1n60C03/60-174 AC P19920 #=GS 1n60C03/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1n60C03/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1n60C03/60-174 DR CATH; 1n60; C:60-174; #=GS 1n60C03/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS 1n5wF03/60-174 AC P19920 #=GS 1n5wF03/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1n5wF03/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1n5wF03/60-174 DR CATH; 1n5w; F:60-174; #=GS 1n5wF03/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS 1n5wC03/60-174 AC P19920 #=GS 1n5wC03/60-174 OS Oligotropha carboxidovorans OM5 #=GS 1n5wC03/60-174 DE Carbon monoxide dehydrogenase medium chain #=GS 1n5wC03/60-174 DR CATH; 1n5w; C:60-174; #=GS 1n5wC03/60-174 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha; Oligotropha carboxidovorans; #=GS A0A3V4X2Y8/56-173 AC A0A3V4X2Y8 #=GS A0A3V4X2Y8/56-173 OS Salmonella enterica subsp. enterica #=GS A0A3V4X2Y8/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS A0A3V4X2Y8/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Salmonella; Salmonella enterica; Salmonella enterica subsp. enterica; #=GS A0A3V4X2Y8/56-173 DR EC; 1.17.1.4; #=GS A0A355ZGT8/56-173 AC A0A355ZGT8 #=GS A0A355ZGT8/56-173 OS Shigella sp. #=GS A0A355ZGT8/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS A0A355ZGT8/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Shigella; Shigella sp.; #=GS A0A355ZGT8/56-173 DR EC; 1.17.1.4; #=GS A0A1H0E1T9/56-173 AC A0A1H0E1T9 #=GS A0A1H0E1T9/56-173 OS Shigella sonnei #=GS A0A1H0E1T9/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS A0A1H0E1T9/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Shigella; Shigella sonnei; #=GS A0A1H0E1T9/56-173 DR EC; 1.17.1.4; #=GS Q0T112/56-173 AC Q0T112 #=GS Q0T112/56-173 OS Shigella flexneri 5 str. 8401 #=GS Q0T112/56-173 DE Putative dehydrogenase #=GS Q0T112/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Shigella; Shigella flexneri; #=GS Q0T112/56-173 DR EC; 1.17.1.4; #=GS A0A1H4DVT1/57-177 AC A0A1H4DVT1 #=GS A0A1H4DVT1/57-177 OS Eubacterium aggregans #=GS A0A1H4DVT1/57-177 DE Purine hydroxylase gamma subunit apoprotein #=GS A0A1H4DVT1/57-177 DR ORG; Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; Eubacterium; Eubacterium aggregans; #=GS P19914/57-174 AC P19914 #=GS P19914/57-174 OS Hydrogenophaga pseudoflava #=GS P19914/57-174 DE Carbon monoxide dehydrogenase medium chain #=GS P19914/57-174 DR ORG; Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Hydrogenophaga; Hydrogenophaga pseudoflava; #=GS P19914/57-174 DR GO; GO:0018492; #=GS P19914/57-174 DR EC; 1.2.5.3; #=GS Q8X6C5/56-173 AC Q8X6C5 #=GS Q8X6C5/56-173 OS Escherichia coli O157:H7 #=GS Q8X6C5/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS Q8X6C5/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS Q8X6C5/56-173 DR EC; 1.17.1.4; #=GS D3QQJ2/56-173 AC D3QQJ2 #=GS D3QQJ2/56-173 OS Escherichia coli O55:H7 str. CB9615 #=GS D3QQJ2/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS D3QQJ2/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS D3QQJ2/56-173 DR EC; 1.17.1.4; #=GS A0A1Z3V042/56-173 AC A0A1Z3V042 #=GS A0A1Z3V042/56-173 OS Escherichia coli O157 #=GS A0A1Z3V042/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS A0A1Z3V042/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A1Z3V042/56-173 DR EC; 1.17.1.4; #=GS A0A0H3PWI4/56-173 AC A0A0H3PWI4 #=GS A0A0H3PWI4/56-173 OS Escherichia coli O157:H7 str. EC869 #=GS A0A0H3PWI4/56-173 DE Xanthine dehydrogenase, FAD-binding subunit #=GS A0A0H3PWI4/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A0H3PWI4/56-173 DR EC; 1.17.1.4; #=GS A0A0F6C8J4/56-173 AC A0A0F6C8J4 #=GS A0A0F6C8J4/56-173 OS Escherichia coli Xuzhou21 #=GS A0A0F6C8J4/56-173 DE Xanthine dehydrogenase subunit XdhB #=GS A0A0F6C8J4/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A0F6C8J4/56-173 DR EC; 1.17.1.4; #=GS C3SW73/56-173 AC C3SW73 #=GS C3SW73/56-173 OS Escherichia coli #=GS C3SW73/56-173 DE Putative dehydrogenase #=GS C3SW73/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS C3SW73/56-173 DR EC; 1.17.1.4; #=GS I2WVR9/56-173 AC I2WVR9 #=GS I2WVR9/56-173 OS Escherichia coli 4.0967 #=GS I2WVR9/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS I2WVR9/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS I2WVR9/56-173 DR EC; 1.17.1.4; #=GS W8SUQ2/56-173 AC W8SUQ2 #=GS W8SUQ2/56-173 OS Escherichia coli #=GS W8SUQ2/56-173 DE Nicotinate dehydrogenase FAD-subunit #=GS W8SUQ2/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS W8SUQ2/56-173 DR EC; 1.17.1.4; #=GS S1I8Y9/56-173 AC S1I8Y9 #=GS S1I8Y9/56-173 OS Escherichia coli KTE107 #=GS S1I8Y9/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS S1I8Y9/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS S1I8Y9/56-173 DR EC; 1.17.1.4; #=GS U9XWM7/56-173 AC U9XWM7 #=GS U9XWM7/56-173 OS Escherichia coli 113303 #=GS U9XWM7/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS U9XWM7/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS U9XWM7/56-173 DR EC; 1.17.1.4; #=GS A0A1X3KZM4/56-173 AC A0A1X3KZM4 #=GS A0A1X3KZM4/56-173 OS Escherichia coli H420 #=GS A0A1X3KZM4/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS A0A1X3KZM4/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A1X3KZM4/56-173 DR EC; 1.17.1.4; #=GS V6FWN2/56-173 AC V6FWN2 #=GS V6FWN2/56-173 OS Escherichia coli 99.0741 #=GS V6FWN2/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS V6FWN2/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS V6FWN2/56-173 DR EC; 1.17.1.4; #=GS C8UF73/56-173 AC C8UF73 #=GS C8UF73/56-173 OS Escherichia coli O111:H- str. 11128 #=GS C8UF73/56-173 DE Xanthine dehydrogenase, FAD-binding subunit #=GS C8UF73/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS C8UF73/56-173 DR EC; 1.17.1.4; #=GS A0A402YHR0/56-173 AC A0A402YHR0 #=GS A0A402YHR0/56-173 OS Escherichia coli O26 #=GS A0A402YHR0/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS A0A402YHR0/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A402YHR0/56-173 DR EC; 1.17.1.4; #=GS D6I0I7/56-173 AC D6I0I7 #=GS D6I0I7/56-173 OS Escherichia coli B088 #=GS D6I0I7/56-173 DE Xanthine dehydrogenase subunit XdhB #=GS D6I0I7/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS D6I0I7/56-173 DR EC; 1.17.1.4; #=GS K4Y199/56-173 AC K4Y199 #=GS K4Y199/56-173 OS Escherichia coli O111:H11 str. CVM9455 #=GS K4Y199/56-173 DE Xanthine dehydrogenase subunit XdhB #=GS K4Y199/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS K4Y199/56-173 DR EC; 1.17.1.4; #=GS A0A070UUQ8/56-173 AC A0A070UUQ8 #=GS A0A070UUQ8/56-173 OS Escherichia coli 2-177-06_S3_C2 #=GS A0A070UUQ8/56-173 DE FAD binding domain in molybdopterin dehydrogenase family protein #=GS A0A070UUQ8/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A070UUQ8/56-173 DR EC; 1.17.1.4; #=GS A0A0E0U2S2/56-173 AC A0A0E0U2S2 #=GS A0A0E0U2S2/56-173 OS Escherichia coli UMNK88 #=GS A0A0E0U2S2/56-173 DE Xanthine dehydrogenase, FAD binding subunit XdhB #=GS A0A0E0U2S2/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A0E0U2S2/56-173 DR EC; 1.17.1.4; #=GS V2SZU7/56-173 AC V2SZU7 #=GS V2SZU7/56-173 OS Escherichia coli HVH 50 (4-2593475) #=GS V2SZU7/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS V2SZU7/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS V2SZU7/56-173 DR EC; 1.17.1.4; #=GS A0A070FEI9/56-173 AC A0A070FEI9 #=GS A0A070FEI9/56-173 OS Escherichia coli O128:H2 str. 2011C-3317 #=GS A0A070FEI9/56-173 DE Xanthine dehydrogenase #=GS A0A070FEI9/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A070FEI9/56-173 DR EC; 1.17.1.4; #=GS C8UAM1/56-173 AC C8UAM1 #=GS C8UAM1/56-173 OS Escherichia coli O103:H2 str. 12009 #=GS C8UAM1/56-173 DE Xanthine dehydrogenase, FAD-binding subunit #=GS C8UAM1/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS C8UAM1/56-173 DR EC; 1.17.1.4; #=GS A0A1X3IIC3/56-173 AC A0A1X3IIC3 #=GS A0A1X3IIC3/56-173 OS Escherichia coli E1114 #=GS A0A1X3IIC3/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS A0A1X3IIC3/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A1X3IIC3/56-173 DR EC; 1.17.1.4; #=GS V0YA42/56-173 AC V0YA42 #=GS V0YA42/56-173 OS Escherichia coli 908525 #=GS V0YA42/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS V0YA42/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS V0YA42/56-173 DR EC; 1.17.1.4; #=GS A0A026UVK0/56-173 AC A0A026UVK0 #=GS A0A026UVK0/56-173 OS Escherichia coli O174:H8 str. 04-3038 #=GS A0A026UVK0/56-173 DE Xanthine dehydrogenase #=GS A0A026UVK0/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A026UVK0/56-173 DR EC; 1.17.1.4; #=GS A0A028E7D5/56-173 AC A0A028E7D5 #=GS A0A028E7D5/56-173 OS Escherichia coli O118:H16 str. 2009C-4446 #=GS A0A028E7D5/56-173 DE Xanthine dehydrogenase #=GS A0A028E7D5/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A028E7D5/56-173 DR EC; 1.17.1.4; #=GS A0A3W2R9F2/56-173 AC A0A3W2R9F2 #=GS A0A3W2R9F2/56-173 OS Escherichia coli O103 #=GS A0A3W2R9F2/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS A0A3W2R9F2/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A3W2R9F2/56-173 DR EC; 1.17.1.4; #=GS M9FPK8/56-173 AC M9FPK8 #=GS M9FPK8/56-173 OS Escherichia coli MP021561.2 #=GS M9FPK8/56-173 DE FAD binding domain in molybdopterin dehydrogenase family protein #=GS M9FPK8/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS M9FPK8/56-173 DR EC; 1.17.1.4; #=GS A0A1X3JDY3/56-173 AC A0A1X3JDY3 #=GS A0A1X3JDY3/56-173 OS Escherichia coli H386 #=GS A0A1X3JDY3/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS A0A1X3JDY3/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A1X3JDY3/56-173 DR EC; 1.17.1.4; #=GS I2SMD5/56-173 AC I2SMD5 #=GS I2SMD5/56-173 OS Escherichia coli 1.2264 #=GS I2SMD5/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS I2SMD5/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS I2SMD5/56-173 DR EC; 1.17.1.4; #=GS V8F701/56-173 AC V8F701 #=GS V8F701/56-173 OS Escherichia coli ATCC BAA-2209 #=GS V8F701/56-173 DE Xanthine dehydrogenase subunit B #=GS V8F701/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS V8F701/56-173 DR EC; 1.17.1.4; #=GS I2XBX5/56-173 AC I2XBX5 #=GS I2XBX5/56-173 OS Escherichia coli 2.3916 #=GS I2XBX5/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS I2XBX5/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS I2XBX5/56-173 DR EC; 1.17.1.4; #=GS F4SPD5/56-173 AC F4SPD5 #=GS F4SPD5/56-173 OS Escherichia coli H736 #=GS F4SPD5/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS F4SPD5/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS F4SPD5/56-173 DR EC; 1.17.1.4; #=GS E9TJP0/56-173 AC E9TJP0 #=GS E9TJP0/56-173 OS Escherichia coli MS 117-3 #=GS E9TJP0/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS E9TJP0/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS E9TJP0/56-173 DR EC; 1.17.1.4; #=GS A0A070SGX9/56-173 AC A0A070SGX9 #=GS A0A070SGX9/56-173 OS Escherichia coli 2-210-07_S3_C3 #=GS A0A070SGX9/56-173 DE FAD binding domain in molybdopterin dehydrogenase family protein #=GS A0A070SGX9/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A070SGX9/56-173 DR EC; 1.17.1.4; #=GS A0A069X5V4/56-173 AC A0A069X5V4 #=GS A0A069X5V4/56-173 OS Escherichia coli 3-373-03_S4_C2 #=GS A0A069X5V4/56-173 DE FAD binding domain in molybdopterin dehydrogenase family protein #=GS A0A069X5V4/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A069X5V4/56-173 DR EC; 1.17.1.4; #=GS I2RYW0/56-173 AC I2RYW0 #=GS I2RYW0/56-173 OS Escherichia coli 97.0246 #=GS I2RYW0/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS I2RYW0/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS I2RYW0/56-173 DR EC; 1.17.1.4; #=GS L2VHX6/56-173 AC L2VHX6 #=GS L2VHX6/56-173 OS Escherichia coli KTE10 #=GS L2VHX6/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS L2VHX6/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS L2VHX6/56-173 DR EC; 1.17.1.4; #=GS G0F5G4/56-173 AC G0F5G4 #=GS G0F5G4/56-173 OS Escherichia coli UMNF18 #=GS G0F5G4/56-173 DE FAD binding domain in molybdopterin dehydrogenase family protein #=GS G0F5G4/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS G0F5G4/56-173 DR EC; 1.17.1.4; #=GS S1HMK2/56-173 AC S1HMK2 #=GS S1HMK2/56-173 OS Escherichia coli KTE108 #=GS S1HMK2/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS S1HMK2/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS S1HMK2/56-173 DR EC; 1.17.1.4; #=GS A0A140N5N6/56-173 AC A0A140N5N6 #=GS A0A140N5N6/56-173 OS Escherichia coli BL21(DE3) #=GS A0A140N5N6/56-173 DE Molybdopterin dehydrogenase FAD-binding #=GS A0A140N5N6/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A140N5N6/56-173 DR EC; 1.17.1.4; #=GS B6I701/56-173 AC B6I701 #=GS B6I701/56-173 OS Escherichia coli SE11 #=GS B6I701/56-173 DE Putative dehydrogenase #=GS B6I701/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS B6I701/56-173 DR EC; 1.17.1.4; #=GS A0A365QGV6/56-173 AC A0A365QGV6 #=GS A0A365QGV6/56-173 OS Escherichia coli O111:NM #=GS A0A365QGV6/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS A0A365QGV6/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A365QGV6/56-173 DR EC; 1.17.1.4; #=GS A0A0A0FJ49/56-173 AC A0A0A0FJ49 #=GS A0A0A0FJ49/56-173 OS Escherichia coli G3/10 #=GS A0A0A0FJ49/56-173 DE Xanthine dehydrogenase #=GS A0A0A0FJ49/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A0A0FJ49/56-173 DR EC; 1.17.1.4; #=GS K4V2E0/56-173 AC K4V2E0 #=GS K4V2E0/56-173 OS Escherichia coli O111:H8 str. CVM9634 #=GS K4V2E0/56-173 DE Xanthine dehydrogenase subunit XdhB #=GS K4V2E0/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS K4V2E0/56-173 DR EC; 1.17.1.4; #=GS A0A0A8UIU5/56-173 AC A0A0A8UIU5 #=GS A0A0A8UIU5/56-173 OS Escherichia coli O26:H11 #=GS A0A0A8UIU5/56-173 DE Xanthine dehydrogenase, FAD-binding subunit #=GS A0A0A8UIU5/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A0A8UIU5/56-173 DR EC; 1.17.1.4; #=GS F4NJ49/56-173 AC F4NJ49 #=GS F4NJ49/56-173 OS Escherichia coli D9 #=GS F4NJ49/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS F4NJ49/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS F4NJ49/56-173 DR EC; 1.17.1.4; #=GS E1ILW2/56-173 AC E1ILW2 #=GS E1ILW2/56-173 OS Escherichia coli MS 145-7 #=GS E1ILW2/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS E1ILW2/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS E1ILW2/56-173 DR EC; 1.17.1.4; #=GS A0A3W4NSN3/56-173 AC A0A3W4NSN3 #=GS A0A3W4NSN3/56-173 OS Escherichia coli O11 #=GS A0A3W4NSN3/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS A0A3W4NSN3/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A3W4NSN3/56-173 DR EC; 1.17.1.4; #=GS V0A4W9/56-173 AC V0A4W9 #=GS V0A4W9/56-173 OS Escherichia coli 909945-2 #=GS V0A4W9/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS V0A4W9/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS V0A4W9/56-173 DR EC; 1.17.1.4; #=GS B7LF53/56-173 AC B7LF53 #=GS B7LF53/56-173 OS Escherichia coli 55989 #=GS B7LF53/56-173 DE XdhB protein #=GS B7LF53/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS B7LF53/56-173 DR EC; 1.17.1.4; #=GS A0A028ADL4/56-173 AC A0A028ADL4 #=GS A0A028ADL4/56-173 OS Escherichia coli O69:H11 str. 08-4661 #=GS A0A028ADL4/56-173 DE Xanthine dehydrogenase #=GS A0A028ADL4/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A028ADL4/56-173 DR EC; 1.17.1.4; #=GS S1EQJ8/56-173 AC S1EQJ8 #=GS S1EQJ8/56-173 OS Escherichia coli KTE73 #=GS S1EQJ8/56-173 DE Xanthine dehydrogenase FAD-binding subunit #=GS S1EQJ8/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS S1EQJ8/56-173 DR EC; 1.17.1.4; #=GS A0A0E0XV89/56-173 AC A0A0E0XV89 #=GS A0A0E0XV89/56-173 OS Escherichia coli O104:H4 str. 2011C-3493 #=GS A0A0E0XV89/56-173 DE Xanthine dehydrogenase subunit XdhB #=GS A0A0E0XV89/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A0E0XV89/56-173 DR EC; 1.17.1.4; #=GS I2WJQ4/56-173 AC I2WJQ4 #=GS I2WJQ4/56-173 OS Escherichia coli 9.0111 #=GS I2WJQ4/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS I2WJQ4/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS I2WJQ4/56-173 DR EC; 1.17.1.4; #=GS I2UE98/56-173 AC I2UE98 #=GS I2UE98/56-173 OS Escherichia coli 4.0522 #=GS I2UE98/56-173 DE FAD binding domain in molybdopterin dehydrogenase #=GS I2UE98/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS I2UE98/56-173 DR EC; 1.17.1.4; #=GS A0A222QQ01/56-173 AC A0A222QQ01 #=GS A0A222QQ01/56-173 OS Escherichia coli NCCP15648 #=GS A0A222QQ01/56-173 DE Xanthine dehydrogenase, FAD-binding subunit #=GS A0A222QQ01/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A222QQ01/56-173 DR EC; 1.17.1.4; #=GS E0IWE6/56-173 AC E0IWE6 #=GS E0IWE6/56-173 OS Escherichia coli W #=GS E0IWE6/56-173 DE Xanthine dehydrogenase, FAD-binding subunit #=GS E0IWE6/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS E0IWE6/56-173 DR EC; 1.17.1.4; #=GS A0A0E1SSE6/56-173 AC A0A0E1SSE6 #=GS A0A0E1SSE6/56-173 OS Escherichia coli 53638 #=GS A0A0E1SSE6/56-173 DE Xanthine dehydrogenase, FAD-binding subunit #=GS A0A0E1SSE6/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A0E1SSE6/56-173 DR EC; 1.17.1.4; #=GS A0A1H3FYA8/57-177 AC A0A1H3FYA8 #=GS A0A1H3FYA8/57-177 OS Eubacterium barkeri #=GS A0A1H3FYA8/57-177 DE Purine hydroxylase gamma subunit apoprotein #=GS A0A1H3FYA8/57-177 DR ORG; Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; Eubacterium; Eubacterium barkeri; #=GS A0A1H3FYA8/57-177 DR EC; 1.17.1.5; #=GS M1I8F8/57-173 AC M1I8F8 #=GS M1I8F8/57-173 OS Sulfolobus acidocaldarius N8 #=GS M1I8F8/57-173 DE Carbon monoxide dehydrogenase medium chain #=GS M1I8F8/57-173 DR ORG; Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; Sulfolobus; Sulfolobus acidocaldarius; #=GS M1I8F8/57-173 DR EC; 1.2.99.8; #=GS M1JFQ1/57-173 AC M1JFQ1 #=GS M1JFQ1/57-173 OS Sulfolobus acidocaldarius Ron12/I #=GS M1JFQ1/57-173 DE Carbon monoxide dehydrogenase medium chain #=GS M1JFQ1/57-173 DR ORG; Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; Sulfolobus; Sulfolobus acidocaldarius; #=GS M1JFQ1/57-173 DR EC; 1.2.99.8; #=GS A0A0U3GXB0/57-173 AC A0A0U3GXB0 #=GS A0A0U3GXB0/57-173 OS Sulfolobus acidocaldarius #=GS A0A0U3GXB0/57-173 DE Carbon monoxide dehydrogenase #=GS A0A0U3GXB0/57-173 DR ORG; Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; Sulfolobus; Sulfolobus acidocaldarius; #=GS A0A0U3GXB0/57-173 DR EC; 1.2.99.8; #=GS Q5LQT7/59-175 AC Q5LQT7 #=GS Q5LQT7/59-175 OS Ruegeria pomeroyi DSS-3 #=GS Q5LQT7/59-175 DE Carbon monoxide dehydrogenase, medium subunit #=GS Q5LQT7/59-175 DR ORG; Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Ruegeria; Ruegeria pomeroyi; #=GS Q5LQT7/59-175 DR GO; GO:0006730; GO:0018492; #=GS A0A0V9RJ53/56-173 AC A0A0V9RJ53 #=GS A0A0V9RJ53/56-173 OS Escherichia coli #=GS A0A0V9RJ53/56-173 DE Xanthine dehydrogenase #=GS A0A0V9RJ53/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A0H2VA97/56-173 AC A0A0H2VA97 #=GS A0A0H2VA97/56-173 OS Escherichia coli CFT073 #=GS A0A0H2VA97/56-173 DE Xanthine dehydrogenase, FAD binding subunit #=GS A0A0H2VA97/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A454A750/56-173 AC A0A454A750 #=GS A0A454A750/56-173 OS Escherichia coli 536 #=GS A0A454A750/56-173 DE Xanthine dehydrogenase, FAD binding subunit #=GS A0A454A750/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia coli; #=GS A0A0H2V3F2/56-173 AC A0A0H2V3F2 #=GS A0A0H2V3F2/56-173 OS Shigella flexneri #=GS A0A0H2V3F2/56-173 DE Putative dehydrogenase #=GS A0A0H2V3F2/56-173 DR ORG; Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Shigella; Shigella flexneri; #=GF SQ 95 1ffvF03/60-173 ---LRGIR-EEGSTVVIGAMTVENDLISSPIVQARLPLLAEAAKLIADPQVRNRGTIGGDIAHGDPGNDHPALSIAVEAHFVLEGPN-GRRTVPADGFFLGTY---MTLLEENEVMVEIRVP-- Q46800/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- Q4J6M6/57-173 -NELNYVK-TSLNGVSIGALTRYHDILSNDIVKSKVPLMHHATRTIGDMQVRNMGTIGGAISNADPASDMPVVLTALNATIILSSAS-GSRSVKALDFFKGPF---TTDTNKGELVTQIEVPV- Q0QLF4/57-177 -KELEYIR-VEENTIHIGALSTFTQIENHPFIRSHVRALYKAASQVGSPQIRNLGTIGGNLSTSSVAGDGVSAMTTLDATVVLESVR-GTRQMKLTDFFDGEGFKRRNALEADEIMTEVIIDRP D7REY4/58-176 -SELQQVR-CENDTLYVGSMVRHCRVEQEEIFRSTIPLMSEAMTSVAHIQIKTRGTLGGNLCNAHPASEMPAVITALGASMVCKSEKRGERVLTPEEFFEGAL---QNGLQSDELLCEIRIPVP Q5LT94/59-165 -----VCR-NDDGSLSIGGGTTHAEVARA--AAAHYPALAALAGGIGDPAVRNRGTIGGSLANNDPSACYPAAALGSGATIVT-----DRREIAADDYFQGLF---TTALEEGEIITSVRFPV- Q5LVP6/229-342 --DLKDIE-ITDTHVRLGAMVDMNRM--RDALAPLHPSYGEMIRRYASVQVRNAATVGGNIANGSPIGDNPPALIALGATLHLRKGD-TRRDLPLEAFFLDYG---KQDRAPGEFVEAVSFPR- 1ffvC03/60-173 ---LRGIR-EEGSTVVIGAMTVENDLISSPIVQARLPLLAEAAKLIADPQVRNRGTIGGDIAHGDPGNDHPALSIAVEAHFVLEGPN-GRRTVPADGFFLGTY---MTLLEENEVMVEIRVP-- 1ffuF03/60-173 ---LRGIR-EEGSTVVIGAMTVENDLISSPIVQARLPLLAEAAKLIADPQVRNRGTIGGDIAHGDPGNDHPALSIAVEAHFVLEGPN-GRRTVPADGFFLGTY---MTLLEENEVMVEIRVP-- 1ffuC03/60-173 ---LRGIR-EEGSTVVIGAMTVENDLISSPIVQARLPLLAEAAKLIADPQVRNRGTIGGDIAHGDPGNDHPALSIAVEAHFVLEGPN-GRRTVPADGFFLGTY---MTLLEENEVMVEIRVP-- 1zxiF02/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- 1zxiC02/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- 1n63F03/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- 1n63C03/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- 1n62F03/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- 1n62C03/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- 1n61F03/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- 1n61C03/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- 1n60F03/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- 1n60C03/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- 1n5wF03/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- 1n5wC03/60-174 ---LVGIR-EEGTDVVIGAMTTQHALIGSDFLAAKLPIIRETSLLIADPQIRYMGTIGGNAANGDPGNDMPALMQCLGAAYELTGPE-GARIVAARDYYQGAY---FTAIEPGELLTAIRIPV- A0A3V4X2Y8/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDSITQRHLPALCAAASSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A355ZGT8/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A1H0E1T9/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- Q0T112/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A1H4DVT1/57-177 -KELEYIR-VEENTIHIGALSTFTQIENHPFIRSHVRALYKAASQVGSPQIRNLGTIGGNLSTSSVAGDGVSAMTTLDATAVLESVR-GTRKMKLTDFFDGEGFKRRNALEADEIMTEVIIDRP P19914/57-174 IPELRGIR-EEGSTVVIGAMTVENDLISSPIVQARLPLLAEAAKLIADPQVRNRGTIGGDIAHGHPGNDHPALSIAVEAHFVLEGPN-GRRTVPADGFFLGTY---MTLLEENEVMVEIRVPA- Q8X6C5/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDSITQRHLPALCAAASSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- D3QQJ2/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDSITQRHLPALCAAASSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A1Z3V042/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDSITQRHLPALCAAASSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A0H3PWI4/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDSITQRHLPALCAAASSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A0F6C8J4/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDSITQRHLPALCAAASSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- C3SW73/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDSITQRHLPALCAAASSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- I2WVR9/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- W8SUQ2/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- S1I8Y9/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- U9XWM7/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A1X3KZM4/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- V6FWN2/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- C8UF73/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A402YHR0/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- D6I0I7/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- K4Y199/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A070UUQ8/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A0E0U2S2/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- V2SZU7/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A070FEI9/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- C8UAM1/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A1X3IIC3/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- V0YA42/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A026UVK0/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A028E7D5/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A3W2R9F2/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- M9FPK8/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A1X3JDY3/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- I2SMD5/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- V8F701/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- I2XBX5/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- F4SPD5/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- E9TJP0/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A070SGX9/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A069X5V4/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- I2RYW0/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- L2VHX6/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- G0F5G4/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- S1HMK2/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A140N5N6/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- B6I701/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A365QGV6/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A0A0FJ49/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- K4V2E0/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A0A8UIU5/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- F4NJ49/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- E1ILW2/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A3W4NSN3/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- V0A4W9/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- B7LF53/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A028ADL4/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- S1EQJ8/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A0E0XV89/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- I2WJQ4/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- I2UE98/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A222QQ01/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- E0IWE6/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A0E1SSE6/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A1H3FYA8/57-177 -KELEYIR-VEENTIHIGALSTFTQIENHPFIRSHVRALYKAASQVGSPQIRNLGTIGGNLSTSSVAGDGVSAMTTLDATVVLESVR-GTRQMKLTDFFDGEGFKRRNALEADEIMTEVIIDRP M1I8F8/57-173 -NELNYVK-TSLNGVSIGALTRYHDILSNDIVKSKVPLMHHATRTIGDMQVRNMGTIGGAISNADPASDMPVVLTALNATIILSSAS-GSRSVKALDFFKGPF---TTDTNKGELVTQIEVPV- M1JFQ1/57-173 -NELNYVK-TSLNGVSIGALTRYHDILSNDIVKSKVPLMHHATRTIGDMQVRNMGTIGGAISNADPASDMPVVLTALNATIILSSAS-GSRSVKALDFFKGPF---TTDTNKGELVTQIEVPV- A0A0U3GXB0/57-173 -NELNYVK-TSLNGVSIGALTRYHDILSNDIVKSKVPLMHHATRTIGDMQVRNMGTIGGAISNADPASDMPVVLTALNATIILSSAS-GSRSVKALDFFKGPF---TTDTNKGELVTQIEVPV- Q5LQT7/59-175 --GMSDIE-IGSDSIRIGAMVTQHDIIDNDALAQAAPILREAALQIADPQVRYMGTVGGNVANGDPGNDMPGLMQCLNATFTVVGSD-GEREIPAREFYEAAY---MTAREDDEVLTAVTIPMP A0A0V9RJ53/56-173 -AELQGITQAEDGALRIGSATTFTQLIEDPVIQRNLPALCAAAASIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLELHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A0H2VA97/56-173 -AELQGITQAEDGALRIGSATTFTQLIEDPVIQRNLPALCAAAASIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLELHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A454A750/56-173 -AELQGITQAEDGALRIGSATTFTQLIEDPVIQRNLPALCAAAASIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLELHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- A0A0H2V3F2/56-173 -AELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATFIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPR-GVRFVPINGFHTGPG---KVSLEHDEILVAFHFPP- #=GC scorecons 0238457514754464896576454764445454568564466448757878656959976577555584555444559445646640849375546764854000354574596656555840 #=GC scorecons_70 ___*__*___*___*_**__**___**________**_*__*___**_*****__*_***__**____*_________*______*__*_*_*____*__*_________*__*_*_____*__ #=GC scorecons_80 ___*__*___*_____**__*_______________*________**_****___*_**___*_____*_________*_________*_*_*____*__*_________*__*_______*__ #=GC scorecons_90 ___*____________**__________________*________*___*_*___*_**_________*_________*_________*_*_________*____________*_______*__ //