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Database: UniProt
Entry: B6QFW2_TALMQ
LinkDB: B6QFW2_TALMQ
Original site: B6QFW2_TALMQ 
ID   B6QFW2_TALMQ            Unreviewed;       508 AA.
AC   B6QFW2;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 39.
DE   SubName: Full=Vacuolar aspartyl aminopeptidase Lap4, putative {ECO:0000313|EMBL:EEA24347.1};
GN   ORFNames=PMAA_083510 {ECO:0000313|EMBL:EEA24347.1};
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX   NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA24347.1, ECO:0000313|Proteomes:UP000001294};
RN   [1] {ECO:0000313|Proteomes:UP000001294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC   {ECO:0000313|Proteomes:UP000001294};
RX   PubMed=25676766; DOI=10.1128/genomeA.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; DS995901; EEA24347.1; -; Genomic_DNA.
DR   RefSeq; XP_002147858.1; XM_002147822.1.
DR   ProteinModelPortal; B6QFW2; -.
DR   STRING; 441960.XP_002147858.1; -.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; EEA24347; EEA24347; PMAA_083510.
DR   GeneID; 7025481; -.
DR   EuPathDB; FungiDB:PMAA_083510; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
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:EEA24347.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001294};
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:UP000001294};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   508 AA;  54736 MW;  B777BD8755098F8D CRC64;
     MKQRISSLHS SVSRLQLSEH VEEPSPIASP QQQQQEPATA LSPEAYTQPF IDFMSKNPTI
     FHAVNHFSKQ LEAQGYKKLS ERDTWTSELK RGGKYYLTRN DSSLIAFAVG SEYKSGNGIG
     LVAGHIDALT ARLKPVPTLP TKVGFKQIAV APYAGALNKT WWDRDLGIGG RVLVKGTDGV
     VKSKLVKLDW PIARIPTLAP HFGAASTAAN PETNMVPIIG IDNSDLFGAS GSDETVDAIK
     PGTFAATQPP KLVQVIAGEL GITDYSSIIN WELELFDSQP AQVGGLEKDL IFAGRIDDKL
     CCFAAQEALL ASPDSTSPGL VKLVGMFDDE EVGSLLRQGA RSTYLSSVIE RITEAFAEGN
     YGPNLYNQTV ANSFLISSDV IHAVNPNFLN AYLPNHMPRL NVGVTVSADP NGHMATDAVS
     HAILQQVAEK CDSTLQIFQI RNDSRSGGTI GPMTSAQIGL RTIDAGIPQL SMHSIRATTG
     SLDPGLGVKL FKGFFDHFEE VDKSFPSL
//
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