ID   DPH4_YARLI              Reviewed;         163 AA.
AC   Q6C6T1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Diphthamide biosynthesis protein 4;
GN   Name=DPH4; OrderedLocusNames=YALI0E06545g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The DPH-type metal-binding (MB) domain can bind either zinc or
CC       iron ions. {ECO:0000255|PROSITE-ProRule:PRU00456}.
CC   -!- SIMILARITY: Belongs to the DPH4 family. {ECO:0000305}.
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DR   EMBL; CR382131; CAG79213.1; -; Genomic_DNA.
DR   RefSeq; XP_503631.1; XM_503631.1.
DR   AlphaFoldDB; Q6C6T1; -.
DR   STRING; 4952.CAG79213; -.
DR   PRIDE; Q6C6T1; -.
DR   EnsemblFungi; CAG79213; CAG79213; YALI0_E06545g.
DR   GeneID; 2912398; -.
DR   KEGG; yli:YALI0E06545g; -.
DR   VEuPathDB; FungiDB:YALI0_E06545g; -.
DR   HOGENOM; CLU_017633_7_0_1; -.
DR   InParanoid; Q6C6T1; -.
DR   OMA; CWYRGCR; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   Gene3D; 3.10.660.10; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR044248; DPH3/4-like.
DR   InterPro; IPR007872; DPH_MB_dom.
DR   InterPro; IPR036671; DPH_MB_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR21454; PTHR21454; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF05207; zf-CSL; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF144217; SSF144217; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51074; DPH_MB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Metal-binding; Nucleus; Reference proteome; Zinc.
FT   CHAIN           1..163
FT                   /note="Diphthamide biosynthesis protein 4"
FT                   /id="PRO_0000071153"
FT   DOMAIN          2..74
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   DOMAIN          89..159
FT                   /note="DPH-type MB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
SQ   SEQUENCE   163 AA;  18232 MW;  CB3B1D8FC4FBB810 CRC64;
     MNHYTILGLS EPPHVPELTS ADLKTAYKQA LLKNHPDKLQ EREAYTGSVQ ITAITTAYAC
     LSNSKLKKEY DLSLKNGANG VKSGPGSDVF DLTELEERED ADGMFSWYKP CRCGEAGGYV
     LTEEHLENNE KYYEGVDVQF HEIVVQCGTC SLWITVQYGV EEE