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Database: UniProt
Entry: A0A0B2X7F5_9HYPO
LinkDB: A0A0B2X7F5_9HYPO
Original site: A0A0B2X7F5_9HYPO 
ID   A0A0B2X7F5_9HYPO        Unreviewed;       554 AA.
AC   A0A0B2X7F5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   10-MAY-2017, entry version 8.
DE   SubName: Full=Vacuolar aspartyl aminopeptidase Lap4 {ECO:0000313|EMBL:KHO01435.1};
GN   ORFNames=MAM_00436 {ECO:0000313|EMBL:KHO01435.1};
OS   Metarhizium album ARSEF 1941.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Metarhizium.
OX   NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHO01435.1, ECO:0000313|Proteomes:UP000030816};
RN   [1] {ECO:0000313|EMBL:KHO01435.1, ECO:0000313|Proteomes:UP000030816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHO01435.1,
RC   ECO:0000313|Proteomes:UP000030816};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and
RT   host adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KHO01435.1}.
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DR   EMBL; AZHE01000001; KHO01435.1; -; Genomic_DNA.
DR   EnsemblFungi; KHO01435; KHO01435; MAM_00436.
DR   Proteomes; UP000030816; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:KHO01435.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030816};
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:UP000030816};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   554 AA;  60046 MW;  88E92FDFE78958FB CRC64;
     MTRRTPVPYH QYSVLPLRQP PAAAPPSPSP APVTTTPNSS LGSKNLVLAD MDGRTCRENR
     ACASCISRLM PSEIGQVNLA DDQTCRLCRV ARCEPEAFTK PFCDFLQENP TVFHTVHYFQ
     RKLSDSGFKE LSARDAWNGK IHPGGKYWVT RNGSTIIAFT VGEAYKPGNG AAMIGGHIDA
     LTARLKPVSH RPNKAGYVQL GVAQYAGGLN HTWWDRDLSI GGRVVFRDPE TGKTSTRLVK
     LDWPIAKIPT LAPHFGIGMF GNNNKETQAV PIIGLQGSSR QDAEPLGPDG AFVNTQPPRL
     VQLIAKELGI SSYSSILDWE LELYDSQPAQ RMGMDKEFIT AGRIDDKLCS WAALMGLLAA
     DNNPTDGHIK LVALFDDEEI GSLLRQGARS NFLPIVIERT VEALNPSSYG PGLLGQTYAR
     SFLLSADVTH AGNPNFLETY MDGHVPQLNV GIVICGDSNG HMTTDAVSTA ILRRVGEMVG
     AKTQNFQIRN DSRSGGTIGP SLSSAMGCRA ADAGLPQLSM HSVRATTGAL DPGLGVQYFK
     GFLDLWEQID GEWS
//
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