ID M7TYE7_EUTLA Unreviewed; 500 AA.
AC M7TYE7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Diphthamide biosynthesis protein 4 {ECO:0000256|ARBA:ARBA00021797};
GN ORFNames=UCREL1_1246 {ECO:0000313|EMBL:EMR71700.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR71700.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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 -!- SIMILARITY: Belongs to the DPH4 family.
CC {ECO:0000256|ARBA:ARBA00006169}.
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DR EMBL; KB705597; EMR71700.1; -; Genomic_DNA.
DR RefSeq; XP_007789199.1; XM_007791008.1.
DR AlphaFoldDB; M7TYE7; -.
DR STRING; 1287681.M7TYE7; -.
DR KEGG; ela:UCREL1_1246; -.
DR eggNOG; KOG0714; Eukaryota.
DR HOGENOM; CLU_052080_0_0_1; -.
DR OrthoDB; 1054714at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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 InterPro; IPR037507; Ribosomal_mL59.
DR InterPro; IPR040922; Ribosomal_mL59_dom.
DR PANTHER; PTHR28041; 54S RIBOSOMAL PROTEIN L25, MITOCHONDRIAL; 1.
DR PANTHER; PTHR28041:SF1; 54S RIBOSOMAL PROTEIN L25, MITOCHONDRIAL; 1.
DR Pfam; PF18126; Mitoc_mL59; 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:UP000012174}.
FT DOMAIN 207..315
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 356..418
FT /note="DPH-type MB"
FT /evidence="ECO:0000259|PROSITE:PS51074"
FT REGION 242..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 54512 MW; E8EABA0A76E1D86E CRC64;
MASATSARYI ELAKALHPRL QRFFAKYPPT QILPSTTRTN TEAATAAAAT AGDGGVASTT
PPVNPFLPYK HSVTGKWQDP VFSLRRQAEL VKLAREQGVE ELLPFTTKGT EEQIRQRVEF
GLRVRGTGVG QKVKGHLHER MLAAKYVLIV AIFPCSDLTW DGEEENGYAR DAEIGQGVAE
GGEEQVVEIS AMSHYFNDIG CGGGRPTHYE ILSITPKHLE GQSDPSQAKV IKKAYHRALL
RHHPDKANAS NSRSSSTGTG PSRESHSKSK PSKPQSSSSS TTTTTTTTTY TVDQIQEAYS
VLSDSKRRTE YNRTLFQKTT HNNNNNNNST SSSHSNSNNS SSGKSTTAAT WSFRTGVETV
DLDDLGFDER TGVYYRSCRC GNARGYRFED ADLEECEGEG VLMVECLDCS LWLRVLFAPA
GDDGDVDNHD EEEKTVVNNN NNNHHHQPNN NREVASGERS GGGETSRGFK FNWSFSWGVS
VGGSASASTS ASSAARRIGN
//
