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Database: UniProt
Entry: I4Y694_WALMC
LinkDB: I4Y694_WALMC
Original site: I4Y694_WALMC 
ID   I4Y694_WALMC            Unreviewed;       478 AA.
AC   I4Y694;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   25-OCT-2017, entry version 25.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EIM19486.1};
GN   ORFNames=WALSEDRAFT_61468 {ECO:0000313|EMBL:EIM19486.1};
OS   Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi
OS   (CBS 633.66)).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiales incertae sedis; Wallemia.
OX   NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM19486.1, ECO:0000313|Proteomes:UP000005242};
RN   [1] {ECO:0000313|EMBL:EIM19486.1, ECO:0000313|Proteomes:UP000005242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX   PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA   Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA   Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA   Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA   Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT   "The genome of the xerotolerant mold Wallemia sebi reveals adaptations
RT   to osmotic stress and suggests cryptic sexual reproduction.";
RL   Fungal Genet. Biol. 49:217-226(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; JH668250; EIM19486.1; -; Genomic_DNA.
DR   RefSeq; XP_006960518.1; XM_006960456.1.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EIM19486; EIM19486; WALSEDRAFT_61468.
DR   GeneID; 18474549; -.
DR   KEGG; wse:WALSEDRAFT_61468; -.
DR   InParanoid; I4Y694; -.
DR   KO; K01267; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000005242; 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   InterPro; IPR023367; Peptidase_M42_dom2.
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:EIM19486.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005242};
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:UP000005242};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   478 AA;  52688 MW;  A4F70D28C1CD0200 CRC64;
     MTAIKSAMSR QAAERFLKFV DASTDPFHAT YTAVQALEKA GFKKLHENAS WNGQLQAGSK
     YYFTRNQSSV IAFTLGAKYN GSGGISLIGA HTDSPNLRVK PVSNKTAQAY LQVKCETYGG
     GIWHSWFDRD LSISGRVIVS EKGSTSKFVS RLVKLDKPIL RIPSLAIHLD RDVNPFKFNP
     ETHLIPVLGL VNEQLNATTD KEAMKSKSLY DSHPVDKHHP ALLEAVAKEL DVEVSQIQDF
     ELSLYDTQKA AIGGINDEFI LSARQDNLMS CFASIEALIE ASDRLENDDR VRCVCLFDHE
     EVGSASTAGA DGSLLPDLIH RLTSELSKAN QSKSSFEEVA ARSFIISADM AHAVHPNYAE
     KHDDLLRPKL NGGPVIKTNV KQRYATTSIT SFLLGRIAEK VNVPLQHFSV RNDIPCGSTI
     APMLASKSGI QTVDIGLPQL SMHSIREMSG SEDPQHLIDL FRSFFEHYGQ LQSEITVD
//
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