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Database: UniProt
Entry: I2GVL5_TETBL
LinkDB: I2GVL5_TETBL
Original site: I2GVL5_TETBL 
ID   I2GVL5_TETBL            Unreviewed;       488 AA.
AC   I2GVL5;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   28-FEB-2018, entry version 29.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCH58167.1};
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 /
OS   NBRC 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
OC   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.,
RA   Byrne K.P., Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type
RT   switching accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; HE806316; CCH58167.1; -; Genomic_DNA.
DR   RefSeq; XP_004177686.1; XM_004177638.1.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; CCH58167; CCH58167; TBLA_0A03690.
DR   GeneID; 14493193; -.
DR   KEGG; tbl:TBLA_0A03690; -.
DR   InParanoid; I2GVL5; -.
DR   KO; K01267; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000002866; Chromosome 1.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:EnsemblFungi.
DR   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002866};
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:UP000002866};
KW   Zinc {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
//
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