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Database: UniProt
Entry: A0A0F4Z612_TALEM
LinkDB: A0A0F4Z612_TALEM
Original site: A0A0F4Z612_TALEM 
ID   A0A0F4Z612_TALEM        Unreviewed;       499 AA.
AC   A0A0F4Z612;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   07-JUN-2017, entry version 12.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KKA25541.1};
DE            EC=3.4.11.21 {ECO:0000313|EMBL:KKA25541.1};
GN   ORFNames=T310_0421 {ECO:0000313|EMBL:KKA25541.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA25541.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA25541.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA25541.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z.,
RA   Wu L., Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKA25541.1}.
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DR   EMBL; LASV01000018; KKA25541.1; -; Genomic_DNA.
DR   RefSeq; XP_013332153.1; XM_013476699.1.
DR   EnsemblFungi; KKA25541; KKA25541; T310_0421.
DR   GeneID; 25312475; -.
DR   Proteomes; UP000053958; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KKA25541.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053958};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KKA25541.1};
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:UP000053958};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   499 AA;  54149 MW;  8714ED1E955F7C13 CRC64;
     MAKIDHKQAA LDFLSFVNAS PTLVGRERQA YPSRTQEKES WSSTCRPGGK YYLTRNGSTI
     IAFAIGKKWK PGNPIAMIGA HTDSPVLRLK PVSKKQNEGY LQVGVEVYGS GIWHTWFDRD
     LGVAGRVMVR TKDGSIVQKL VKIDRPILRI PTLAIHLERQ ETFSFNKETQ LFPIAGLVAA
     ELNRTAGGSK ESESKDAAGK EGTAAPLKAI TERHHPYLIE LIASDLGAQP ADILDFELVL
     FDTNKSCLGG LLEEFIFSPR LDNLNMSFCA VKGLINSVAE ETALDGETSI RLIALFDHEE
     IGSTSAQGAD SNILPSVIRR LSVLPPSHFE DAGSEKSYHQ VGGEADVSTA YEQTLATSFL
     LSADMAHAVN PNFSFKYEAD HKPEINKGPV IKINANVRYA TNSPGIVLVQ EVARKAAEDG
     GDVVPLQLIV VRNDSSCGST IGPMLSAALG ARTLDLGNPQ LSMHSIRETG GSHDVGHAIR
     LFTSFFNHYS TLSPTILVD
//
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