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Database: UniProt
Entry: A0A165E1M3_9BASI
LinkDB: A0A165E1M3_9BASI
Original site: A0A165E1M3_9BASI 
ID   A0A165E1M3_9BASI        Unreviewed;       496 AA.
AC   A0A165E1M3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-FEB-2018, entry version 8.
DE   SubName: Full=Putative vacuolar aspartyl aminopeptidase Lap4 {ECO:0000313|EMBL:KZT53919.1};
GN   ORFNames=CALCODRAFT_500455 {ECO:0000313|EMBL:KZT53919.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Dacrymycetes; Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT53919.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT53919.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT53919.1,
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; KV424025; KZT53919.1; -; Genomic_DNA.
DR   EnsemblFungi; KZT53919; KZT53919; CALCODRAFT_500455.
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   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
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:KZT53919.1};
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   496 AA;  53622 MW;  84B80D9647B37768 CRC64;
     MGGGQPTKDF REDDVVSLDE DAVPEYAEEF CTFIDECVTT YHACEFFKRE LTQAGYVEIK
     ERESWVPTLK AGGKYFVTRN TSSIIAFAIG EQYSPGNGFA LITSHIDALC MKVKPVSRAN
     KDGFDRIAVA PYAGGGASQS FDGSFSTWWD RDLGLGGRVL IKGGDGKILQ KLVCLPKPVA
     RIPSLAAHFG EPAKGPFNYE INMVPITGLT AAGTEEAVPT TMGKQHSTRL LKAVAKELGV
     SVLDIVDFDL ELFDKTPCCL LGFDSEFISA PRIDDKLCSF AAMTALINAT SDDSFLGKSG
     IVSIVGCFDM EEVGSALRAG AKSNFMQTVM ERIVEAQIGA EGDDVSPYTT ELFGITAANS
     FMISADVNHA YNPDFDGIYL EGAKPMLNKG VVIACDPNAH FTTTAPSIAF ARTVAELSEV
     ETQLFQIRND SRSGGTVGPM LSERLGVPAI DLSICQLSMH SIRAMTGAKD PGFGIKYLEG
     FFRHYQTVFG IVQQDY
//
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