DPH4_SCHPO
ID DPH4_SCHPO Reviewed; 139 AA.
AC Q9UUG3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Diphthamide biosynthesis protein 4;
GN Name=dph4; ORFNames=SPAC926.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=28775286; DOI=10.1038/s41598-017-07647-1;
RA Villahermosa D., Fleck O.;
RT "Elp3 and Dph3 of Schizosaccharomyces pombe mediate cellular stress
RT responses through tRNALysUUU modifications.";
RL Sci. Rep. 7:7225-7225(2017).
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|UniProtKB:P47138}.
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47138}. Nucleus
CC {ECO:0000250|UniProtKB:P47138}.
CC -!- DOMAIN: The DPH-type metal-binding (MB) domain can bind either zinc or
CC iron ions. {ECO:0000255|PROSITE-ProRule:PRU00456}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to methyl methanesulfonate (MMS, causes
CC DNA breaks) and hydroxyurea (HU, ribonucleotide reductase inhibitor).
CC {ECO:0000269|PubMed:28775286}.
CC -!- SIMILARITY: Belongs to the DPH4 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB54153.1; -; Genomic_DNA.
DR PIR; T39203; T39203.
DR RefSeq; NP_594366.1; NM_001019787.2.
DR AlphaFoldDB; Q9UUG3; -.
DR SMR; Q9UUG3; -.
DR BioGRID; 279951; 1.
DR STRING; 4896.SPAC926.05c.1; -.
DR iPTMnet; Q9UUG3; -.
DR MaxQB; Q9UUG3; -.
DR PaxDb; Q9UUG3; -.
DR EnsemblFungi; SPAC926.05c.1; SPAC926.05c.1:pep; SPAC926.05c.
DR GeneID; 2543534; -.
DR KEGG; spo:SPAC926.05c; -.
DR PomBase; SPAC926.05c; dph4.
DR VEuPathDB; FungiDB:SPAC926.05c; -.
DR eggNOG; KOG0714; Eukaryota.
DR eggNOG; KOG2923; Eukaryota.
DR HOGENOM; CLU_017633_7_1_1; -.
DR InParanoid; Q9UUG3; -.
DR OMA; YPCRCGE; -.
DR PhylomeDB; Q9UUG3; -.
DR UniPathway; UPA00559; -.
DR PRO; PR:Q9UUG3; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0030544; F:Hsp70 protein binding; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISO:PomBase.
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 PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 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..139
FT /note="Diphthamide biosynthesis protein 4"
FT /id="PRO_0000071152"
FT DOMAIN 2..69
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 76..133
FT /note="DPH-type MB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
SQ SEQUENCE 139 AA; 16097 MW; D8230DBBCEB09FAC CRC64;
MNHYSVLNLK DGKTYTDDEI KEAYRKALLL FHPDKCKEKP SVVYTIDQVK EAYQVLSSEK
DRQQYQIKQE EESSHYYSIV DLSEFEELDN GSYYYPCRCG DLGGYVVTED DLENNRSVVP
CMGCSLTIQV DYEIAESDS
