ID F9WPD3_TRYVY Unreviewed; 450 AA.
AC F9WPD3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=TvY486_0021110 {ECO:0000313|EMBL:CCD19410.1};
OS Trypanosoma vivax (strain Y486).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; 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,
RC ECO:0000313|Proteomes:UP000009027};
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., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001335};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR EMBL; CAEX01003377; CCD19410.1; -; Genomic_DNA.
DR AlphaFoldDB; F9WPD3; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 1156at2759; -.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000009027};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, 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
//
