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Database: UniProt
Entry: G2XHN2_VERDV
LinkDB: G2XHN2_VERDV
Original site: G2XHN2_VERDV 
ID   G2XHN2_VERDV            Unreviewed;       499 AA.
AC   G2XHN2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   07-JUN-2017, entry version 30.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EGY19326.1};
GN   ORFNames=VDAG_09786 {ECO:0000313|EMBL:EGY19326.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales;
OC   Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|Proteomes:UP000001611};
RN   [1] {ECO:0000313|Proteomes:UP000001611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC   {ECO:0000313|Proteomes:UP000001611};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R.,
RA   Santhanam P., Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z.,
RA   Inderbitzin P., Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R.,
RA   Galagan J., Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; DS572721; EGY19326.1; -; Genomic_DNA.
DR   RefSeq; XP_009652940.1; XM_009654645.1.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EGY19326; EGY19326; VDAG_09786.
DR   GeneID; 20711249; -.
DR   KEGG; vda:VDAG_09786; -.
DR   InParanoid; G2XHN2; -.
DR   KO; K01267; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000001611; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EGY19326.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001611};
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:UP000001611};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   499 AA;  54444 MW;  C44C305C15A543F6 CRC64;
     MAPDKTALDF IDFVNASPTP YHACANAAAR LEKAGFSKIK ERDSWASTLR PGGKYYLTRN
     GSSIVAFAIG KKWRPGNPVG MIGAHTDSPC LRIKPVSKKG NNGFLQVGVE TYGGGIWHSW
     FDRDLSIAGR VLVKDSTGTF TQKLIKVDKP LLRIPTLAIH LDRSSSFDPN KEVELFPIAG
     LASAELNKSA SETQVEGNEE TEEDFKPLRD LTERHHPHII DVIASHAEVD VSNVVDFELV
     LYDTQPACLG GLNDEFVFSP RLDNLGMTYC SIMGLITSLR DSAALDEDHT IRLVTCFDHE
     EIGSTSAQGA NSNLLPAILR RLSVLPAGRS DTASDASYDS VNDALPHLEE SIQSTAYEQT
     LSRSFLVSAD MAHSVHPNYA GKYEASHQPA MNGGTVIKIN ANQRYATNSP GIVLLQESAR
     HAGVPLQLFV VRNDSPCGST IGPMLSAKLG VRTLDLGNPQ LSMHSIRETG GSKDVEFAVR
     LFESFYERYG ELEEKILVD
//
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