ID K3V4G9_FUSPC Unreviewed; 188 AA.
AC K3V4G9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Diphthamide biosynthesis protein 4 {ECO:0000256|ARBA:ARBA00021797};
GN ORFNames=FPSE_11818 {ECO:0000313|EMBL:EKJ68007.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ68007.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ68007.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ68007.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
CC -!- FUNCTION: Required for the first step of diphthamide biosynthesis, the
CC transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a
CC histidine residue. Diphthamide is a post-translational modification of
CC histidine which occurs in elongation factor 2.
CC {ECO:0000256|ARBA:ARBA00003474}.
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DPH4 family.
CC {ECO:0000256|ARBA:ARBA00006169}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKJ68007.1}.
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DR EMBL; AFNW01000612; EKJ68007.1; -; Genomic_DNA.
DR RefSeq; XP_009263210.1; XM_009264935.1.
DR AlphaFoldDB; K3V4G9; -.
DR EnsemblFungi; EKJ68007; EKJ68007; FPSE_11818.
DR GeneID; 20370435; -.
DR KEGG; fpu:FPSE_11818; -.
DR eggNOG; KOG0714; Eukaryota.
DR HOGENOM; CLU_017633_7_0_1; -.
DR OrthoDB; 1054714at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000007978; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.10.660.10; DPH Zinc finger; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR007872; DPH_MB_dom.
DR InterPro; IPR036671; DPH_MB_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR21454:SF46; DIPHTHAMIDE BIOSYNTHESIS PROTEIN 4; 1.
DR PANTHER; PTHR21454; DPH3 HOMOLOG-RELATED; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF05207; zf-CSL; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF144217; CSL zinc finger; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51074; DPH_MB; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007978}.
FT DOMAIN 15..88
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 106..168
FT /note="DPH-type MB"
FT /evidence="ECO:0000259|PROSITE:PS51074"
SQ SEQUENCE 188 AA; 20645 MW; 19E6F558D7D791F2 CRC64;
MTSSQSISSS AGTATHYQVL NITSALLDTQ HDSTPLIKRA YHRALLRNHP DKVANSDPSS
VFFTVDQITT ALNVLSSPSA RAAYDAALRV SRPTGAAGRD GSYQTGVENV DLDDLAFDEN
QECWYRPCRC GNEHSYEFRE ADLEEVSEEG ELVVGCLDCS LWLRVHFAVL DENEDDAQPS
STASKDKI
//
