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Database: UniProt
Entry: A0A074S7J5_9HOMO
LinkDB: A0A074S7J5_9HOMO
Original site: A0A074S7J5_9HOMO 
ID   A0A074S7J5_9HOMO        Unreviewed;       476 AA.
AC   A0A074S7J5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   22-NOV-2017, entry version 11.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KEP55371.1};
GN   ORFNames=V565_006010 {ECO:0000313|EMBL:KEP55371.1};
OS   Rhizoctonia solani 123E.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX   NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP55371.1, ECO:0000313|Proteomes:UP000027456};
RN   [1] {ECO:0000313|EMBL:KEP55371.1, ECO:0000313|Proteomes:UP000027456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=123E {ECO:0000313|EMBL:KEP55371.1,
RC   ECO:0000313|Proteomes:UP000027456};
RA   Cubeta M., Pakala S., Fedorova N., Thomas E., Dean R., Jabaji S.,
RA   Neate S., Toda T., Tavantzis S., Vilgalys R., Bharathan N., Pakala S.,
RA   Losada L.S., Zafar N., Nierman W.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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:KEP55371.1}.
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DR   EMBL; AZST01000007; KEP55371.1; -; Genomic_DNA.
DR   EnsemblFungi; KEP55371; KEP55371; V565_006010.
DR   Proteomes; UP000027456; 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:KEP55371.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000027456};
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:UP000027456};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   476 AA;  51979 MW;  6EB3485B89F78C1D CRC64;
     MVTMVHPSIP PAAASFLEFI NASPTPFHAV HNASERLEAA GFQRIHEKDN WEGQLKEGGR
     YFFTRNQSAL IAFTIPKGWK EGAGLSIVAT HTDSPCLRVR PVSKRAKAGY MQVGVETYGG
     GIWHSWFDRD LSLAGRVIVT DKTGTKFTSR LVNLKRPLLR IPTLAIHLDR TVNDNFKFNQ
     ETQFIPILGQ VASQLNGPAT LEINDKNPVI GVAGSNVQTN HHTSLVELIA EEASASPENI
     HDFELCLYDV QPSQAGGIHN EFIFSPRLDN LMSSFCAVEA MAESVSADRA LPLEGNVNVI
     ALFNHEEIGS VSTSGAESSL LPTLFHRLSP TPAVHAQSIA QSFLVSADMG HAIHPSYVDS
     HELVHRPEIN GGLVVKTNAK QRYATDAVGT FLIRKLVEKR GGRIQEFEVR NDMPCGSTVG
     PMLSKLGVRT VDVGMPMLSM HSIRETGGTK DVQSYIDAFS SLFEGFKDLD ASLSID
//
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