DPH4_DICDI
ID DPH4_DICDI Reviewed; 170 AA.
AC Q54CI5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=DPH4 homolog;
DE AltName: Full=DnaJ homolog subfamily C member 24;
GN Name=dph4; Synonyms=dnajc24; ORFNames=DDB_G0292980;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Stimulates the ATPase activity of several Hsp70-type
CC chaperones. Plays a role in the diphthamide biosynthesis, a post-
CC translational modification of histidine which occurs in translation
CC elongation factor 2 (By similarity). {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; AAFI02000197; EAL61039.1; -; Genomic_DNA.
DR RefSeq; XP_629431.1; XM_629429.1.
DR AlphaFoldDB; Q54CI5; -.
DR STRING; 44689.DDB0238861; -.
DR PaxDb; Q54CI5; -.
DR EnsemblProtists; EAL61039; EAL61039; DDB_G0292980.
DR GeneID; 8628950; -.
DR KEGG; ddi:DDB_G0292980; -.
DR dictyBase; DDB_G0292980; dph4.
DR eggNOG; KOG0714; Eukaryota.
DR HOGENOM; CLU_1753329_0_0_1; -.
DR InParanoid; Q54CI5; -.
DR OMA; SWPVDAC; -.
DR PhylomeDB; Q54CI5; -.
DR PRO; PR:Q54CI5; -.
DR Proteomes; UP000002195; Chromosome 6.
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; ISS:dictyBase.
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; IPR018253; DnaJ_domain_CS.
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; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51074; DPH_MB; 1.
PE 3: Inferred from homology;
KW Iron; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..170
FT /note="DPH4 homolog"
FT /id="PRO_0000328197"
FT DOMAIN 15..102
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 112..168
FT /note="DPH-type MB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
SQ SEQUENCE 170 AA; 19882 MW; 94F8994BCDB63F8D CRC64;
MTNSSNNSNK CENKNYYEIL KVSIDADIEE IKKSYRKLAL LYHPDKLNKE ENIEENINNF
SNCLVNNNNN NNNSNTKDFN DIQIAWETLK DDLLRKQYDS LLLEQKRQKY SVSDEIDLDD
MEFIEENSEY VYPCRCGDHY IITEDQLSEG SDVVCCSGCS LSIKVIYQME
