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Database: UniProt
Entry: M7V0T5_BOTF1
LinkDB: M7V0T5_BOTF1
Original site: M7V0T5_BOTF1 
ID   M7V0T5_BOTF1            Unreviewed;       515 AA.
AC   M7V0T5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   22-NOV-2017, entry version 15.
DE   SubName: Full=Putative aspartyl aminopeptidase protein {ECO:0000313|EMBL:EMR89782.1};
GN   ORFNames=BcDW1_1571 {ECO:0000313|EMBL:EMR89782.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR89782.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomeA.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble
RT   rot of grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KB707722; EMR89782.1; -; Genomic_DNA.
DR   EnsemblFungi; EMR89782; EMR89782; BcDW1_1571.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000012045; 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:EMR89782.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000012045};
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:UP000012045};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   515 AA;  55924 MW;  0028B0143AF75062 CRC64;
     MSNRNLSTAE AKAHDFLDFL NASPGPYHAV HSAIQRLSKA GFTEIKERDN WSTSLQPGGK
     YYLTRNASSI VAFAIGKKWK AGNPIAMIGA HTDSPTLRIK PVSKKQASGF IQVGVETYGG
     GIWTSWFDRD LSIAGRAMVK DGDGNFVQKL VKIDRPILRI PTLAIHLNRA TSFDPNKETE
     LFPIAGLVAA ELNRTGASEN GPTPSEESKD SDEYKPLQAM TARHHPYIVE LIAKNVGVGI
     DDIVDFEMIL YDTQKACLGG LNNELIYSGR LDNLGMTYCS VEGLIESVKD SAALDDESSI
     RLITCFDHEE IGSTSAHGAA SNLLPAVLRR LSVIPASTAG PGSSSSYDMV HRESDVEIAT
     AYEQTLASSF LISADMAHSI HPNYAQKYEQ DHRPEMNKGT VIKINANQRY ATNSPGIVLL
     QEVARKAKPS ADSKDGKSGV PLQLFVVRND SSCGSTIGPM LSAALGTRTL DLGNPMLSMH
     SIRECGGAFD VEHGIRLFES FFNHFSHLEG KILVD
//
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