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Database: UniProt
Entry: A0A165FSD7_9BASI
LinkDB: A0A165FSD7_9BASI
Original site: A0A165FSD7_9BASI 
ID   A0A165FSD7_9BASI        Unreviewed;       498 AA.
AC   A0A165FSD7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-NOV-2017, entry version 7.
DE   SubName: Full=Vacuolar aminopeptidase 1 {ECO:0000313|EMBL:KZT57144.1};
GN   ORFNames=CALCODRAFT_289984 {ECO:0000313|EMBL:KZT57144.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Dacrymycetes; Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT57144.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT57144.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT57144.1,
RC   ECO:0000313|Proteomes:UP000076842};
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; KV423967; KZT57144.1; -; Genomic_DNA.
DR   EnsemblFungi; KZT57144; KZT57144; CALCODRAFT_289984.
DR   Proteomes; UP000076842; 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:KZT57144.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076842};
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:UP000076842};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   498 AA;  53194 MW;  92CD93E799FA0D46 CRC64;
     MPAISFPAYS EAKPDRPRDD DVHSLDEDSP PPYADEFIHF IDSAPTVYHA CAYFASALKA
     AGYIELPERA SWQHIAPGGK YYTTRNSSAI VAFAVGGQYK PPNGIAVVSA HIDALCWKVK
     PVSKDSKGGY DRLSAAPYSG GGPTTTWDAS HHTWWDRDLG LGGRVLVKGK DGKIVQKLVN
     LGRPIARIPT LARHFGAPAL GPFNFETNMV PIIGMTPTPP SDEQLDDIPG VMGKQHSARL
     LRAVAKELGV SVLDIVDFDL ELFDVTPSVY LGLDKEFISA PRLDDKLCSF AAVSALLAAS
     SDPSFLANSG TISMAACFDT EEVGSGLRQG AKSNFLQVVV ERAVEVLAGS SAKGIVGQVV
     GRSFMASADV THALNPNFSD AYLLTTAPLL NVGIACKVDP NAHFTSNSTS IALVRAIAEK
     CDSAVQLFHI RNDGRSGSTV GPMLSERLGM PTVDIGIPQF SMHSIRGLTG ASDPGLGVRW
     MEGLFREFEG LGDYVPFE
//
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