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Database: UniProt
Entry: R7T282_DICSQ
LinkDB: R7T282_DICSQ
Original site: R7T282_DICSQ 
ID   R7T282_DICSQ            Unreviewed;       468 AA.
AC   R7T282;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   07-JUN-2017, entry version 25.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EJF61312.1};
GN   ORFNames=DICSQDRAFT_60953 {ECO:0000313|EMBL:EJF61312.1};
OS   Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Polyporaceae; Dichomitus.
OX   NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF61312.1, ECO:0000313|Proteomes:UP000053319};
RN   [1] {ECO:0000313|EMBL:EJF61312.1, ECO:0000313|Proteomes:UP000053319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF61312.1,
RC   ECO:0000313|Proteomes:UP000053319};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A.,
RA   Henrissat B., Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S.,
RA   Aerts A., Benoit I., Boyd A., Carlson A., Copeland A., Coutinho P.M.,
RA   de Vries R.P., Ferreira P., Findley K., Foster B., Gaskell J.,
RA   Glotzer D., Gorecki P., Heitman J., Hesse C., Hori C., Igarashi K.,
RA   Jurgens J.A., Kallen N., Kersten P., Kohler A., Kuees U.,
RA   Kumar T.K.A., Kuo A., LaButti K., Larrondo L.F., Lindquist E.,
RA   Ling A., Lombard V., Lucas S., Lundell T., Martin R., McLaughlin D.J.,
RA   Morgenstern I., Morin E., Murat C., Nagy L.G., Nolan M., Ohm R.A.,
RA   Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J., Sabat G., Salamov A.,
RA   Samejima M., Schmutz J., Slot J.C., St John F., Stenlid J., Sun H.,
RA   Sun S., Syed K., Tsang A., Wiebenga A., Young D., Pisabarro A.,
RA   Eastwood D.C., Martin F., Cullen D., Grigoriev I.V., Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed
RT   from 31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; JH719411; EJF61312.1; -; Genomic_DNA.
DR   RefSeq; XP_007366141.1; XM_007366079.1.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EJF61312; EJF61312; DICSQDRAFT_60953.
DR   GeneID; 18843008; -.
DR   KEGG; dsq:DICSQDRAFT_60953; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   Proteomes; UP000053319; 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:EJF61312.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053319};
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:UP000053319};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   468 AA;  50948 MW;  B575B4A515DC077E CRC64;
     MTIMQQAGPE AAHKLLDFVN ASPTPYHAVR AASARLEKAG FQKIREQDDW DKSLKAGGKY
     YFARNQAALV AFTIPQGWTP GAGVSIVATH IDSPNLRVRP VSKKSKVGYL QVGVETYGGG
     IWHSWFDRDL ALAGRVVIAD KDGNFSSKLV RIDKPILRIP TLAIHLERGA ADNFQFNTET
     QFVPILGLIE SELNSSAGET KGSKKATSIQ ENHHPALLSL LASELSVAPE YIHDFELCLY
     DTQPSVLGGL NSEFIFSPRM DNQFSSFAAV EALATFASSS HFSVLEGNVN AIALFNHEEI
     GSVSTTGAES SIIPFLLQRL SPTPAAYAQS VSRSFLVSAD MGHAVHPNYK DKHEDNHAPK
     INGGVVIKTN AKQRYASDAI GTFVVKKLVE RKGGQVQEYE VRNDMACGST VGPMLSKIGV
     RTVDVGWAML SMHSIRETAG SHDVQHAIDL FTSFFEGFNE VDKSLTVE
//
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