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Database: UniProt
Entry: B8MT98_TALSN
LinkDB: B8MT98_TALSN
Original site: B8MT98_TALSN 
ID   B8MT98_TALSN            Unreviewed;       526 AA.
AC   B8MT98;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   22-NOV-2017, entry version 46.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EED12281.1};
DE            EC=3.4.11.21 {ECO:0000313|EMBL:EED12281.1};
GN   ORFNames=TSTA_003400 {ECO:0000313|EMBL:EED12281.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 /
OS   NRRL 1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED12281.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
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; EQ962660; EED12281.1; -; Genomic_DNA.
DR   RefSeq; XP_002487935.1; XM_002487890.1.
DR   ProteinModelPortal; B8MT98; -.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EED12281; EED12281; TSTA_003400.
DR   GeneID; 8098036; -.
DR   EuPathDB; FungiDB:TSTA_003400; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   InParanoid; B8MT98; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000001745; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EED12281.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001745};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EED12281.1};
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:UP000001745};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   526 AA;  57427 MW;  74F7AA46EBD4B4C4 CRC64;
     MKSRLYSSRL LQGYSVNSAF SISSATRRIG HFGYTTMVKV NHKQAALDFL SFVNASPTPF
     HAVKSSKDLL AAAGFEQIRE KDSWTSSLQP GGKYYLTRNG STLIGFAIGK KWKPGNSVAM
     VGAHTDSPVL RIKPVSKKQG EGFVQVGVET YGGGIWHTWF DRDLGVAGRV MVRAKDGSIQ
     QKLVKVDRPI LRIPTLAIHL ERKESFDFNK ETQLFPIAGL VEAELNRTRD HTPDSSQQET
     PTTSLKPTTE RHHSYLVELV ASEIDAKPAD ILDFELILFD TQKSCLGGLL EEFIFSPRLD
     NLNMSFCAVQ GLIESVRSSK ALDNESAIRL IALFDHEEIG SKSAQGADSD ALPAVLRRLS
     VLPAKEAGNK SVDLSTAYEQ SLTTSFLLSA DMAHSVNPNY SAKYESDHKP HLNKGPVIKI
     NANQRYATNA PGIVLLQEVA QKAAEDGGDI VPLQLFVVRN DSSCGSTIGP MLSANLGART
     LDLGNPQLSM HSIRETGGTE DVGHAVRLFA SFFEHYSALA PTILVD
//
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