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Database: UniProt
Entry: N4VA20_COLOR
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Original site: N4VA20_COLOR 
ID   N4VA20_COLOR            Unreviewed;       489 AA.
AC   N4VA20;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   22-NOV-2017, entry version 21.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:ENH77871.1};
GN   ORFNames=Cob_12800 {ECO:0000313|EMBL:ENH77871.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 /
OS   LARS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:ENH77871.1, ECO:0000313|Proteomes:UP000014480};
RN   [1] {ECO:0000313|Proteomes:UP000014480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=23252678; DOI=10.1111/nph.12085;
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Comparative genomic and transcriptomic analyses reveal the
RT   hemibiotrophic stage shift of Colletotrichum fungi.";
RL   New Phytol. 197:1236-1249(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KB726076; ENH77871.1; -; Genomic_DNA.
DR   EnsemblFungi; ENH77871; ENH77871; Cob_12800.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000014480; 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:ENH77871.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000014480};
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:UP000014480};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   489 AA;  53266 MW;  D14125400E0D5DBE CRC64;
     MAPNKAALDF VDFVNASPTP YHACATAAAR LEKAGFTKIK ERDSWNSSLR PGGKYHLTRN
     GSSIVAFAIG KKWKPGNPVA MIGAHTDSPT LRIKPVSKKN NVGFLQVGVE TYGGGIWHSW
     FDRDLSIAGR VLVKDAEGNF VQKLIKVDKP LLRIPTLAIH LDRSSSFDPN KENELFPIAG
     LAAAELNKGA KSEGDESEED FKPLKAMTER HHPHILHVIA SHAEVKPEAV IDFELVLYDV
     QKSCLGGLND EFIFSARLDN LNMTYCSIEG LIASVREDSV LDNDTTIRLV TCFDHEEIGS
     TSAHGANSNL LPAVLRRLAS LPGSRDTASD GSYVAVSHDG DYESTAYEQT LSRSFLVSAD
     MAHSVHPNYA GKYEASHQPA MNGGTVIKVN ANQRYATNSP GIVLLQECAR LAGVPLQLFV
     VRNDSPCGST IGPMLSAKLG VRTLDLGNPQ LSMHSIRETG GSEDVEHAIK LFESFYERFG
     ELEEKILVD
//
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