ID I2GVL5_TETBL Unreviewed; 488 AA.
AC I2GVL5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN Name=TBLA0A03690 {ECO:0000313|EMBL:CCH58167.1};
GN ORFNames=TBLA_0A03690 {ECO:0000313|EMBL:CCH58167.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH58167.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH58167.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE806316; CCH58167.1; -; Genomic_DNA.
DR RefSeq; XP_004177686.1; XM_004177638.1.
DR AlphaFoldDB; I2GVL5; -.
DR STRING; 1071380.I2GVL5; -.
DR GeneID; 14493193; -.
DR KEGG; tbl:TBLA_0A03690; -.
DR eggNOG; KOG2596; Eukaryota.
DR HOGENOM; CLU_019532_2_0_1; -.
DR InParanoid; I2GVL5; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000002866; Chromosome 1.
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:UP000002866};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 488 AA; 54285 MW; BB6B06E1930B3A27 CRC64;
MLKMTSTQYA KEFVNFLNAS PSPYHTVYNI KNHLISNGFK ELSERDQWNG KVEKLGKYFV
TRNNSSIIAF IVGNNWKPGN PIAITGAHTD SPVLRIKPIS KRTTENFLQI GVECYGGGIW
HSWFDSDLSV AGRVFVNDKS TGKHISKLVN LNKPLLKIPT LAIHLDRGVN EKFQFNKESQ
LLPVGGLLKE DEKTQGKEKS HDCTGIDTSS KDATFIKSII ERHHKDLLQL IVEDLSLESI
DYIEDFELIL YDNKSSCLGG LHDEFIFSGR LDNLTSCFTS MHGLTEATSN LENESGIRLM
ASFDHEEIGS SSAQGADSNF LPNILERITS LKFDKTDITE PLAKSLILES SAKSFFLSSD
VSHGVHPNYA SKHESNHKPL LGKGPVIKVN ANQRYMTNSP GIVLINQITK EAKVPLQFFV
AANDSPCGST IGPILASKTG IRTLDLGNPI LSMHSIRETG ASNDIEYQIK LFKTFFERYS
QVEESIVV
//
