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Database: UniProt
Entry: W9C3R0_9HELO
LinkDB: W9C3R0_9HELO
Original site: W9C3R0_9HELO 
ID   W9C3R0_9HELO            Unreviewed;       515 AA.
AC   W9C3R0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   22-NOV-2017, entry version 13.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:ESZ90521.1};
GN   ORFNames=SBOR_9090 {ECO:0000313|EMBL:ESZ90521.1};
OS   Sclerotinia borealis F-4128.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ90521.1, ECO:0000313|Proteomes:UP000019487};
RN   [1] {ECO:0000313|EMBL:ESZ90521.1, ECO:0000313|Proteomes:UP000019487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX   PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA   Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT   "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT   pathogenic fungus.";
RL   Genome Announc. 2:E0117513-E0117513(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:ESZ90521.1}.
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DR   EMBL; AYSA01000617; ESZ90521.1; -; Genomic_DNA.
DR   EnsemblFungi; ESZ90521; ESZ90521; SBOR_9090.
DR   Proteomes; UP000019487; 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; 2.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ESZ90521.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019487};
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:UP000019487};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   515 AA;  56147 MW;  FF82A031AC229055 CRC64;
     MTNQNLSTTE AKAHDFLDFL NASPGPYHAV HSAIQRLSKA GFTEIKERDN WSTSLQPGGK
     YYLTRNASSI VAFAIGKKWK AGNPIAMIGA HTDSPTLRIK PVSKKQASGF IQVGVETYGG
     GIWTSWFDRD LSIAGRAMVK DGQGNFVQKL VKIDRPILRI PTLAIHLNRA TSFEPNKETE
     LFPIAGLVAA ELNRTGASEN GPTPTEEKKD SEEFQPLQAM TTRHHPYIVE LIAKNAGVSI
     DDVVDFEMIL YDTQKACLGG LNNELIYSGR LDNLGMTYCS VEGLIESVKD SAALDDETSI
     RLITCFDHEE IGSTSAQGAA SNLLPAVLRR LSVIPASTTA PGSSSSYDMV HRESDIEIAT
     AYEQTLASSF LISADMAHSI HPNYAQKYEQ DHRPEMNKGT VIKINANQRY ATNSPGIVLL
     QEVARKAKPS ADDKDGKNGV PLQLFVVRND SSCGSTIGPM LSAALGTRTL DLGNPMLSMH
     SIRECGGAWD VEFGVRLFES FFENYSGLEG RILVD
//
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