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Database: UniProt
Entry: F9WPD3_TRYVY
LinkDB: F9WPD3_TRYVY
Original site: F9WPD3_TRYVY 
ID   F9WPD3_TRYVY            Unreviewed;       450 AA.
AC   F9WPD3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   12-APR-2017, entry version 19.
DE   SubName: Full=Aspartyl aminopeptidase, putative {ECO:0000313|EMBL:CCD19410.1};
GN   ORFNames=TvY486_0021110 {ECO:0000313|EMBL:CCD19410.1};
OS   Trypanosoma vivax (strain Y486).
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma;
OC   Duttonella.
OX   NCBI_TaxID=1055687 {ECO:0000313|EMBL:CCD19410.1, ECO:0000313|Proteomes:UP000009027};
RN   [1] {ECO:0000313|EMBL:CCD19410.1, ECO:0000313|Proteomes:UP000009027}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Y486 {ECO:0000313|EMBL:CCD19410.1};
RX   PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA   Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA   Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H.,
RA   Gamble J., Gilderthorp R., Marcello L., McQuillan J., Otto T.D.,
RA   Quail M.A., Sanders M.J., van Tonder A., Ginger M.L., Field M.C.,
RA   Barry J.D., Hertz-Fowler C., Berriman M.;
RT   "Antigenic diversity is generated by distinct evolutionary mechanisms
RT   in African trypanosome species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CAEX01003377; CCD19410.1; -; Genomic_DNA.
DR   MEROPS; M18.002; -.
DR   Proteomes; UP000009027; Unassembled WGS sequence.
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:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:CCD19410.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009027};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009027};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   450 AA;  49334 MW;  B20F36591EA00EBC CRC64;
     MLSPKDSQVQ ELANDFVGFI NKSSTPFHVV EVVSSWLLEA GFARLVEGEK WPETVNGGKY
     FVTRNDSSVV AFAVGGKFVP ENGLKIVGAH TDSPNLALKP RTRSDKGGYQ GVSVQCYGGG
     LWHTWFDRDL TVAGRVFISG NGTEKRLIKL DKSVMRIPSL AIHLSSAQER ESFAPNKEKQ
     LVPITSTTII DAVNDVSLHH NAQLMKSIAE AARCRPNDII DFDLSVIDSQ NATIGGICDE
     FIFAPRLDNL ISCYCGIKAL IKACPNLHDD DMIRMVCLFD NEEVGSETAQ GAGGTLIPDI
     VEYINKTKTL RATIVANSFL LSVDGSHAVH PNYQEKHEDQ HRPFLHHGPV IKYNANMRYA
     TNGATAAVIK LIAKKASIPL QEFCVRNDSP CGSTIGPVLS TLSGIKTVDL GNPMLSMHSI
     REMCGTVDLL HLLNLIEAFF VNYRRDLIVN
//
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