GenomeNet

Database: UniProt
Entry: R8BUL2_TOGMI
LinkDB: R8BUL2_TOGMI
Original site: R8BUL2_TOGMI 
ID   R8BUL2_TOGMI            Unreviewed;       496 AA.
AC   R8BUL2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   07-JUN-2017, entry version 18.
DE   SubName: Full=Putative aspartyl aminopeptidase protein {ECO:0000313|EMBL:EOO03052.1};
GN   ORFNames=UCRPA7_1447 {ECO:0000313|EMBL:EOO03052.1};
OS   Togninia minima (strain UCR-PA7) (Esca disease fungus)
OS   (Phaeoacremonium aleophilum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Togniniales; Togniniaceae;
OC   Phaeoacremonium.
OX   NCBI_TaxID=1286976 {ECO:0000313|EMBL:EOO03052.1, ECO:0000313|Proteomes:UP000014074};
RN   [1] {ECO:0000313|Proteomes:UP000014074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-PA7 {ECO:0000313|Proteomes:UP000014074};
RX   PubMed=23814032; DOI=10.1128/genomeA.00390-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of the ascomycete Phaeoacremonium aleophilum
RT   strain UCR-PA7, a causal agent of the esca disease complex in
RT   grapevines.";
RL   Genome Announc. 1:E0039013-E0039013(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; KB932877; EOO03052.1; -; Genomic_DNA.
DR   RefSeq; XP_007912218.1; XM_007914027.1.
DR   EnsemblFungi; EOO03052; EOO03052; UCRPA7_1447.
DR   GeneID; 19321595; -.
DR   KEGG; tmn:UCRPA7_1447; -.
DR   KO; K01267; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000014074; 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:EOO03052.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000014074};
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:UP000014074};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   496 AA;  53940 MW;  676CC3DF09090E52 CRC64;
     MAPPKSAHEF VDFVNASPTP YHAVASAVER LEAAGFKNIK ERDSWSSALR PGGKYYLTRN
     GSSIVAFAIG AKWKPGNPIA MVGAHTDSPC LRLKPVSKKT NAGFLQVGVE TYGGGIWHSW
     FDRDLSIAGR VLVKDSKGDF TQKLIKVDKP ILRIPTLAIH LDRSPEFNPN KETELFPIAG
     LVAAELNRTG KEEAAKDEDA DSEDFKPLKA MAERHHPYLL DIIAEHVGVE TEHVVDFELV
     LYDTQKSCLG GLNDEFIFSA RLDNLGMTYC SIMGLIESVK STNLDDETSI RLITCFDHEE
     IGSTSAHGAN SNLLPAVIRR LCVLPAGGFP GPEDASSDKS YDHADADAEV ATAYEQTCSS
     SFLVSADMAH SVNPNYSGKY ESNHQPEMNK GTVLKINANQ RYATNSPGIV LLQETAKLAG
     VPLQLFVVRN DSPCGSTIGP MLSAKMGVRT LDLGNPQLSM HSIRETGGSY DVEHGIKLFS
     SFLSHYSALE SKILVD
//
DBGET integrated database retrieval system