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Database: UniProt/TrEMBL
Entry: W2TP03_NECAM
LinkDB: W2TP03_NECAM
Original site: W2TP03_NECAM 
ID   W2TP03_NECAM            Unreviewed;       650 AA.
AC   W2TP03;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-SEP-2017, entry version 18.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   ORFNames=NECAME_01815 {ECO:0000313|EMBL:ETN83508.1};
OS   Necator americanus (Human hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Strongylida; Ancylostomatoidea; Ancylostomatidae; Bunostominae;
OC   Necator.
OX   NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN83508.1, ECO:0000313|Proteomes:UP000053676};
RN   [1] {ECO:0000313|Proteomes:UP000053676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24441737; DOI=10.1038/ng.2875;
RA   Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K.,
RA   Martin J., Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V.,
RA   Minx P., Warren W.C., Wang Q., Zhan B., Hotez P.J., Sternberg P.W.,
RA   Dougall A., Gaze S.T., Mulvenna J., Sotillo J., Ranganathan S.,
RA   Rabelo E.M., Wilson R.K., Felgner P.L., Bethony J., Hawdon J.M.,
RA   Gasser R.B., Loukas A., Mitreva M.;
RT   "Genome of the human hookworm Necator americanus.";
RL   Nat. Genet. 46:261-269(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361144};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU361144};
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|RuleBase:RU361144}.
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DR   EMBL; KI658196; ETN83508.1; -; Genomic_DNA.
DR   RefSeq; XP_013305735.1; XM_013450281.1.
DR   GeneID; 25341855; -.
DR   KEGG; nai:NECAME_01815; -.
DR   CTD; 25341855; -.
DR   KO; K01283; -.
DR   Proteomes; UP000053676; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; PTHR10514; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053676};
KW   Glycoprotein {ECO:0000256|RuleBase:RU361144};
KW   Hydrolase {ECO:0000256|RuleBase:RU361144};
KW   Metal-binding {ECO:0000256|RuleBase:RU361144};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW   Protease {ECO:0000256|RuleBase:RU361144};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053676};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
SQ   SEQUENCE   650 AA;  72975 MW;  1C46A8E3BD9EC03C CRC64;
     MQAKQFDMES IKDPALKRQL AYVSFEGMSA LSPADYAAFN QAQNSVCEMC SINRDKLNRV
     ASDVTICDKD LPPPCALKKI DLESIFRNEK DAARLSHLWI SYLTELAREK PTYQKLIELS
     NKGAKANGFS DGGAMWRSAF DLSGKNTPKV IDLNAQIENI YTKIEPLYKQ LHAYMRRQIA
     GIYGNPTGLS KNGPIPAHLF GSVDGGDWSA HYEQTKPYDD ESTLPEDMLF SFHTQNYTTK
     QMFVKAYRYF KSVGFPSLPK SFWTNSHFAR VWSRDMICNP PAALDMRDGM DFRVKSCAQL
     GMPDFELAHS LMAQVYYQYM YREQPLLFRE PASSSVTDAI AKVFAHLSTN PHYLFSQKLV
     NSSHLDIKDS WIINKLFREA LEYFAKLPFD IVADKWRYEQ FEEKIPHGKI NDRWWALRTK
     YEGIRAPQPY NSSNVDALMH NAISQVHSPA TRGLISYVVQ FQILKAMCPP GTILSEGCIL
     SEDTTEKLRE TMMKGSSITW LKALELITGK AELDPTPLLE YFEPLANWLR NTNEIDQTIL
     GWDGDGALFT AEEIPKPRTG MDGGSGILSE DRVAFPGGLC ANGQECLLDS HCNGTICVCN
     EGLFTLEIGS TVNCVPGNPA DSGFGDGKLL VKTYAKNIVS IFVACNSTTK
//
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