ID V5K5H8_HAECO Unreviewed; 973 AA. AC V5K5H8; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 11-DEC-2019, entry version 21. DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040}; DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040}; OS Haemonchus contortus (Barber pole worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida; OC Trichostrongyloidea; Haemonchidae; Haemonchus. OX NCBI_TaxID=6289 {ECO:0000313|EMBL:AGT79010.1}; RN [1] {ECO:0000313|EMBL:AGT79010.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MHco3 {ECO:0000313|EMBL:AGT79010.1}; RX PubMed=24289031; RA Roberts B., Antonopoulos A., Haslam S.M., Dicker A.J., McNeilly T.N., RA Johnston S.L., Dell A., Knox D.P., Britton C.; RT "Novel expression of Haemonchus contortus vaccine candidate aminopeptidase RT H11 using the free-living nematode Caenorhabditis elegans."; RL Vet. Res. 44:111-111(2013). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU364040}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU364040}; CC -!- SIMILARITY: Belongs to the peptidase M1 family. CC {ECO:0000256|RuleBase:RU364040}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KF381362; AGT79010.1; -; mRNA. DR MEROPS; M01.015; -. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR CDD; cd09601; M1_APN-Q_like; 1. DR Gene3D; 2.60.40.1730; -; 1. DR InterPro; IPR042097; Aminopeptidase_N-like_N. DR InterPro; IPR024571; ERAP1-like_C_dom. DR InterPro; IPR034016; M1_APN-typ. DR InterPro; IPR001930; Peptidase_M1. DR InterPro; IPR014782; Peptidase_M1_dom. DR Pfam; PF11838; ERAP1_C; 1. DR Pfam; PF01433; Peptidase_M1; 1. DR PRINTS; PR00756; ALADIPTASE. DR SUPFAM; SSF63737; SSF63737; 1. PE 2: Evidence at transcript level; KW Aminopeptidase {ECO:0000256|RuleBase:RU364040, KW ECO:0000313|EMBL:AGT79010.1}; Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrolase {ECO:0000256|RuleBase:RU364040, ECO:0000313|EMBL:AGT79010.1}; KW Metal-binding {ECO:0000256|RuleBase:RU364040}; KW Metalloprotease {ECO:0000256|RuleBase:RU364040}; KW Protease {ECO:0000256|RuleBase:RU364040}; KW Zinc {ECO:0000256|RuleBase:RU364040}. FT DOMAIN 304..532 FT /note="Peptidase_M1" FT /evidence="ECO:0000259|Pfam:PF01433" FT DOMAIN 618..930 FT /note="ERAP1_C" FT /evidence="ECO:0000259|Pfam:PF11838" FT COILED 890..910 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 973 AA; 111469 MW; 05BC0EE812B2FA56 CRC64; MTVQWTKRTV LKFTPITLLL LLFLVAASIG LSIGLTYYFT RKAYDTTEKN KDHGADDNSP SAEELRLPKN IEPLLYDLSI KTYLPGYVSF PPEKNLTFDG QVGISLRVVE PTKSIVLNSK NITVIPDKCE LFSGDKKLEI ESIKEHERLE KLEILLKNRL EKDQEVLLKV GYTGIISNTL GGLYQATYTD TDGTVKRIAA ATQHCPSDAR RLVPCLDEPS FKASWTVTVI HPKGTKAVSN GIETNGKGEV SGDWIISKFE TTPRMSSYLL AVVVSEFDYI EGFTKSGVRF RIWSRPEAKN MTAYARDAGI RCLEFYENFF DIKFPLKKQD MVALPDFSFG AMENWGLITY RESSLLYDDR YYTPIIQATQ LVALVVAHEL AHQWFGDLVT LKWWDDLWLN EGFARFVEYI GTDEINNKTI RMDDFFLPNV LVKALDADAV SSTHPLSFRV DKAAEVVEAF DRITYEKGAS VLKMLQALIG QKNYKQAVTQ YLRKFSYSNA QASDLWDVFD EVVKDVKGPD GNLMKTTEFA SQWTTQVQMG FPLVTVKAFN ATSLQITQTR YKTNKDALEP EKYRHPKYGF KWDVPLWYQE GDNKDIKFAW LTREKPLYLH MTKPDTTIVV NADRHGFYRQ NYDANGWRKI IKQLKKNHKV CSARTRNAII GDAFAAALID ELEYETVFKL LEYAKNEEEY LPWTEAISGF YAILDFFGNE PESISAKAFM KNILKPMYKK TSMKYIADNY ENDSLFFEVN LQTSIIDAYC FLGARECIKN YADLFDKEVM KKCKDGDKAS KCVSIAAPLR AKAYCYGVKE GGEAAFDKVM KLYYAENVQL EKDVLLQGLG CHKDITALKR LLLLALDRNS SFVRLQDVAA VYYAVSSNPI GKEFMFNFLL ERWEEILEGL TTEHRAVERV IKACTAGIRL EQQIDQLRSL QKNGEHAREY GAFDGQIERA EHKINWIKKH MRKLSDFFEK STR //