ID   DPH4_CANGA              Reviewed;         175 AA.
AC   Q6FWM1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Diphthamide biosynthesis protein 4;
GN   Name=DPH4; OrderedLocusNames=CAGL0C04565g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380949; CAG58279.1; -; Genomic_DNA.
DR   RefSeq; XP_445373.1; XM_445373.1.
DR   AlphaFoldDB; Q6FWM1; -.
DR   STRING; 5478.XP_445373.1; -.
DR   EnsemblFungi; CAG58279; CAG58279; CAGL0C04565g.
DR   GeneID; 2886952; -.
DR   KEGG; cgr:CAGL0C04565g; -.
DR   CGD; CAL0127468; CAGL0C04565g.
DR   VEuPathDB; FungiDB:CAGL0C04565g; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   HOGENOM; CLU_017633_7_0_1; -.
DR   InParanoid; Q6FWM1; -.
DR   OMA; CWYRGCR; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000002428; Chromosome C.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:EnsemblFungi.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IEA:UniProtKB-UniPathway.
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   PRINTS; PR00625; JDOMAIN.
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..175
FT                   /note="Diphthamide biosynthesis protein 4"
FT                   /id="PRO_0000071146"
FT   DOMAIN          10..82
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   DOMAIN          97..169
FT                   /note="DPH-type MB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
SQ   SEQUENCE   175 AA;  19869 MW;  5738D2D257A9CADC CRC64;
     MTVKSKSRIS HYEVLGVPVD ASTDEIKLTY RKMLLTLHPD KSKTVPIDST IKIRSGVSIN
     QIQEAYRVLS NDQLRAAYNR ALNDSNKLAG FNNFGDGLDE FNLDEFEFNE EKLEYVMTCP
     RCQSGGGFVL SEDMLEECIE DGLTESEEQG YQVLTQCTAC SLWLKVNFFI NDEEE