ID A0A0J7B9D5_COCIT Unreviewed; 210 AA.
AC A0A0J7B9D5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Diphthamide biosynthesis protein 4 {ECO:0000256|ARBA:ARBA00021797};
GN ORFNames=CIRG_06293 {ECO:0000313|EMBL:KMP06612.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP06612.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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}.
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DR EMBL; DS028096; KMP06612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7B9D5; -.
DR STRING; 404692.A0A0J7B9D5; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000054565; Unassembled WGS sequence.
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; 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;
FT DOMAIN 13..102
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 125..190
FT /note="DPH-type MB"
FT /evidence="ECO:0000259|PROSITE:PS51074"
FT REGION 43..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 22962 MW; 77F890BAEFF560F5 CRC64;
MTPPLGEWVL LTTHYDILGL PRPPALLRQP DLKAAYHRAL LKHHPDKSGS STPSEDTSSG
RTATPVAKSG FQAPRTFTVD QVTMAYKVLS NPRAKAEYDR SLLCLASGAG GQHAVDSESQ
PFRTGLEVFD LDDMEVGEES EGAGFWYRGC RCGDKRGFLV HEEDLENEME RGEIMVGCQG
CSLWAKVLFA VDEEDVPDAG NDENCVDGKS
//
