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Database: UniProt/TrEMBL
Entry: E0VYZ7_PEDHC
LinkDB: E0VYZ7_PEDHC
Original site: E0VYZ7_PEDHC 
ID   E0VYZ7_PEDHC            Unreviewed;       664 AA.
AC   E0VYZ7;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   05-JUL-2017, entry version 39.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   Name=8231723 {ECO:0000313|VectorBase:PHUM522390-PA};
GN   ORFNames=Phum_PHUM522390 {ECO:0000313|EMBL:EEB18603.1};
OS   Pediculus humanus subsp. corporis (Body louse).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura;
OC   Pediculidae; Pediculus.
OX   NCBI_TaxID=121224 {ECO:0000313|Proteomes:UP000009046};
RN   [1] {ECO:0000313|EMBL:EEB18603.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB18603.1};
RA   Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA   Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA   Amedeo P., Strausberg R.;
RT   "Annotation of Pediculus humanus corporis strain USDA.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB18603.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB18603.1};
RG   The Human Body Louse Genome Consortium;
RA   Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT   "The genome of the human body louse.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000009046, ECO:0000313|VectorBase:PHUM522390-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA {ECO:0000313|Proteomes:UP000009046,
RC   ECO:0000313|VectorBase:PHUM522390-PA};
RX   PubMed=20566863; DOI=10.1073/pnas.1003379107;
RA   Kirkness E.F., Haas B.J., Sun W., Braig H.R., Perotti M.A.,
RA   Clark J.M., Lee S.H., Robertson H.M., Kennedy R.C., Elhaik E.,
RA   Gerlach D., Kriventseva E.V., Elsik C.G., Graur D., Hill C.A.,
RA   Veenstra J.A., Walenz B., Tubio J.M., Ribeiro J.M., Rozas J.,
RA   Johnston J.S., Reese J.T., Popadic A., Tojo M., Raoult D., Reed D.L.,
RA   Tomoyasu Y., Krause E., Mittapalli O., Margam V.M., Li H.M.,
RA   Meyer J.M., Johnson R.M., Romero-Severson J., Vanzee J.P.,
RA   Alvarez-Ponce D., Vieira F.G., Aguade M., Guirao-Rico S., Anzola J.M.,
RA   Yoon K.S., Strycharz J.P., Unger M.F., Christley S., Lobo N.F.,
RA   Seufferheld M.J., Wang N., Dasch G.A., Struchiner C.J., Madey G.,
RA   Hannick L.I., Bidwell S., Joardar V., Caler E., Shao R., Barker S.C.,
RA   Cameron S., Bruggner R.V., Regier A., Johnson J., Viswanathan L.,
RA   Utterback T.R., Sutton G.G., Lawson D., Waterhouse R.M., Venter J.C.,
RA   Strausberg R.L., Berenbaum M.R., Collins F.H., Zdobnov E.M.,
RA   Pittendrigh B.R.;
RT   "Genome sequences of the human body louse and its primary endosymbiont
RT   provide insights into the permanent parasitic lifestyle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:12168-12173(2010).
RN   [4] {ECO:0000313|VectorBase:PHUM522390-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|VectorBase:PHUM522390-PA};
RG   VectorBase;
RL   Submitted (FEB-2017) to UniProtKB.
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; DS235848; EEB18603.1; -; Genomic_DNA.
DR   RefSeq; XP_002431341.1; XM_002431296.1.
DR   ProteinModelPortal; E0VYZ7; -.
DR   STRING; 121225.PHUM522390-PA; -.
DR   EnsemblMetazoa; PHUM522390-RA; PHUM522390-PA; PHUM522390.
DR   GeneID; 8231723; -.
DR   KEGG; phu:Phum_PHUM522390; -.
DR   VectorBase; PHUM522390-RA; PHUM522390-PA; PHUM522390.
DR   CTD; 8231723; -.
DR   InParanoid; E0VYZ7; -.
DR   KO; K01283; -.
DR   OMA; ICQASAW; -.
DR   PhylomeDB; E0VYZ7; -.
DR   Proteomes; UP000009046; Partially assembled 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   CDD; cd06461; M2_ACE; 1.
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   ECO:0000313|EMBL:EEB18603.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009046};
KW   Glycoprotein {ECO:0000256|RuleBase:RU361144};
KW   Hydrolase {ECO:0000256|RuleBase:RU361144,
KW   ECO:0000313|EMBL:EEB18603.1};
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:UP000009046};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
SQ   SEQUENCE   664 AA;  77728 MW;  BB96F343075F3A57 CRC64;
     MSVLTSGRGY DSQPPVYLYG QQGTTATTTT TTTNSYQTNT RYDPSQNQYY DDNFKNVSYN
     VDPSPFGQNN QNVFIPIHEL MLLLSNLDNV GSEQCSANVY AQWEYETNVN DITQINALSA
     QQNHAAFDRE ISEILKQIQY NKFYNSKLWR ELRYLSVVGA AALPIDDYER YNRMISEMVA
     VYGRASICAY NEPFRCNLRL SPDLTVIMAR SRDWDELQHT WVEFRRRTGQ YIKDMYDQLV
     DLTNEAAKLN NFTDAEEMWN FPYDSPNFEQ EIEEVWSQIR PLYEQLHAYV RRKLRDLYGP
     EKISNRAPLP SHILGNMWAQ SWTNILDVTL PYPGKTLLDV TPNMQIQGYT PLTMLQLAEE
     FFISMNLSAM PPEFWAGSII TEIPERVINC QASAWDFCNR QDYRLKMCAK VNMKDFVSMH
     HEMGHIQYFL QYKNQPKVFR DGANPGFHEA IGEMIALSVG GPTHLQKLGL IQTSIDDVPL
     DINYLFSLAM DKLPFLPFAY VMDKWRWDVF KRVVSKEQFN CHWHSLRERY LGVKPPLLRS
     EFDFDPGSKY HIPANVPYIR YFFSTVLQFQ LHRHLCRISG QYDPNDSTKS LHKCDIYRKI
     QAGNVLKELM KYGSSLSWKE VLYRSIGENK LDGSALRDFF RPLEEWLRNE NLRRNEYPGW
     IYGK
//
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