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ERFB_GIBZE
ID   ERFB_GIBZE              Reviewed;         679 AA.
AC   Q4I2M7; A0A098DEP0; A0A0E0S072; V6RLF6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Palmitoyltransferase ERF2;
DE            EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8VDZ4};
DE   AltName: Full=DHHC cysteine-rich domain-containing protein ERF2;
DE   AltName: Full=Ras protein acyltransferase;
GN   Name=ERF2; ORFNames=FGRRES_08531, FGSG_08531;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
CC   -!- FUNCTION: Palmitoyltransferase specific for Ras proteins.
CC       {ECO:0000250|UniProtKB:Q06551}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC         EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:Q8VDZ4};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q06551}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q06551}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q06551}.
CC   -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q9UIJ5}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       ERF2/ZDHHC9 subfamily. {ECO:0000305}.
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DR   EMBL; DS231667; ESU14802.1; -; Genomic_DNA.
DR   EMBL; HG970333; CEF76897.1; -; Genomic_DNA.
DR   RefSeq; XP_011320227.1; XM_011321925.1.
DR   AlphaFoldDB; Q4I2M7; -.
DR   STRING; 5518.FGSG_08531P0; -.
DR   PRIDE; Q4I2M7; -.
DR   EnsemblFungi; ESU14802; ESU14802; FGSG_08531.
DR   GeneID; 23555530; -.
DR   KEGG; fgr:FGSG_08531; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G10187; -.
DR   eggNOG; KOG1311; Eukaryota.
DR   HOGENOM; CLU_021757_0_0_1; -.
DR   InParanoid; Q4I2M7; -.
DR   PHI-base; PHI:1676; -.
DR   Proteomes; UP000070720; Chromosome 2.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..679
FT                   /note="Palmitoyltransferase ERF2"
FT                   /id="PRO_0000212943"
FT   TOPO_DOM        1..368
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        390..393
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        415..511
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        512..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        533..554
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        555..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        576..679
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          468..518
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          1..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        498
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
SQ   SEQUENCE   679 AA;  75486 MW;  750C5F56F728B8F1 CRC64;
     MASKPDDDGF LAPYVSRSDA QRPLSIVSSR MTDIASEDGD GPEVQNNRLS IPQSTDMGSR
     PDTARTGASS SRGPWQSQSL RNKTYLAGVQ AKRGSVESST AGSTSQPPSL SSRSHVPSLQ
     SHAFFRPMSS QKLQAQRGGS HRPSTMSQMS AAASPSSPTS PTSPTSPRSD EHGESSSSQM
     RQSIISNPIA QLQRQMSNEE NMRPPPSRGT EMTEQETLDR ITANTSPSHG HYPAGSLTDS
     VRPLQGMSSD TGHFQHSIIV DKSYKDLSNL PSPIKTPRSF RSSFLMPGRS NDGQLSQNRS
     TEGAEKLSSA ASSPQFRPVD SHNEQQHPRV PYKPSQKSDL GRVHQYFDGN TVFCLGGRWQ
     NTRGRPINIA TGIFVVVPCA LFFGFEAPWL WNNVSPAIPI VFAYLAYICF SSFIHASVTD
     PGILPRNLHQ FPPVDDDDDP LQLSPPTTDW ALIKSAESTT AAMEVPVKHC RTCNIWRPPR
     AHHCRLCDNC IETHDHHCVW LNNCVGKRNY RYFFTFVTSA TVLAAYLIAT SLTQILLYRN
     RQGISFGQAV DHFRVPFALV FLGFITFLYP AALMGYHIFL MARGETTREY MNSHKFAKKE
     RFRAFSQASV FKNFIVVLCR PRQPTYYQFK AHYHEGDQRL GIRRDKRPRS SSQGLEMHDV
     NPGSSGFQGP VSLRNDTPH
 
 
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