ID M7X1P1_RHOT1 Unreviewed; 146 AA.
AC M7X1P1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Diphthamide biosynthesis protein 4 {ECO:0000256|ARBA:ARBA00021797};
GN ORFNames=RHTO_06039 {ECO:0000313|EMBL:EMS24035.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS24035.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS24035.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS24035.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(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 -!- SIMILARITY: Belongs to the DPH4 family.
CC {ECO:0000256|ARBA:ARBA00006169}.
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DR EMBL; KB722645; EMS24035.1; -; Genomic_DNA.
DR RefSeq; XP_016275154.1; XM_016419700.1.
DR AlphaFoldDB; M7X1P1; -.
DR GeneID; 27370052; -.
DR eggNOG; KOG0714; Eukaryota.
DR HOGENOM; CLU_017633_7_1_1; -.
DR OrthoDB; 1054714at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR042978; DNAJC24.
DR InterPro; IPR007872; DPH_MB_dom.
DR InterPro; IPR036671; DPH_MB_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR45255; DNAJ HOMOLOG SUBFAMILY C MEMBER 24; 1.
DR PANTHER; PTHR45255:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 24; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF05207; zf-CSL; 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 1..56
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 70..142
FT /note="DPH-type MB"
FT /evidence="ECO:0000259|PROSITE:PS51074"
SQ SEQUENCE 146 AA; 16687 MW; 3CAD367D245B979C CRC64;
MSTYIRTAYR HLILRHHPDR ALHGQDEQGI GEARELNEAW EVLGDEETRD EYDQARRQYL
AASRASSNAY AISLSLDLFE PHYASLSSTS PSSSSPEDEE PIYYTHPCRC SSHFLVTREQ
LEEGVEVVGC EGCSERCRVE YEVVEE
//
