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Database: UniProt
Entry: A0A166EU35_9HOMO
LinkDB: A0A166EU35_9HOMO
Original site: A0A166EU35_9HOMO 
ID   A0A166EU35_9HOMO        Unreviewed;       468 AA.
AC   A0A166EU35;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   07-JUN-2017, entry version 7.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KZV69191.1};
GN   ORFNames=PENSPDRAFT_652527 {ECO:0000313|EMBL:KZV69191.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV69191.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV69191.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV69191.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KV424544; KZV69191.1; -; Genomic_DNA.
DR   EnsemblFungi; KZV69191; KZV69191; PENSPDRAFT_652527.
DR   Proteomes; UP000077086; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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   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:KZV69191.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077086};
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:UP000077086};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   468 AA;  50905 MW;  CE5F0C8FA30F22C6 CRC64;
     MMLYPTAPEA ATRFLHFVNA SPTPFHAVHN AALRLEKAGF RKVKELDDWE KGLTAGGKYY
     FTRNQSALLA FTLPASWQPG AGVSIVATHI DSPNLRVRPV SKRSKAGYLQ VGVETYGGGL
     WHTWFDRDLS LAGRVVVGKD GEYKSRLVKI ERPVLRIPNL AVHLNRNSAD NFQFNTETEF
     VPVLGLIASE LNATAAEKQD APKVEGSSIQ ANHHSSLLEL LANELDITPD QIQDFEMHLY
     DTQPSALGGL NNEFIFSPRM DNQFSSFCAV EALADHASSP GFASLEGNVN CIALFNHEEI
     GSVSTTGADG NLIPSLLERL AGSPGLLGRA TARSFLVSSD MGHAVHPNYL SKHEDNHRPL
     VNGGVVIKTN AKQRYASDAP GSFIVRKLIE KAGGRVQEYE VRNDMACGST VGPMLSKNGL
     RTVDVGGAML SMHSIRETAG SHDVKHMTDF FGAFFSDFSK LDATVNVD
//
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