ID   DJC24_BOVIN             Reviewed;         149 AA.
AC   Q0VBY7;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 3.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=DnaJ homolog subfamily C member 24;
DE   AltName: Full=CSL-type zinc finger-containing protein 3;
DE   AltName: Full=Diphthamide biosynthesis protein 4;
GN   Name=DNAJC24; Synonyms=DPH4, ZCSL3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Stimulates the ATPase activity of several Hsp70-type
CC       chaperones. This ability is enhanced by iron-binding. The iron-bound
CC       form is redox-active and can function as electron carrier. Plays a role
CC       in the diphthamide biosynthesis, a post-translational modification of
CC       histidine which occurs in translation elongation factor 2 (EEF2) (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC   -!- SUBUNIT: Monomer and homooligomer. Iron binding promotes
CC       oligomerization (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {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}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; BC120442; AAI20443.1; -; mRNA.
DR   RefSeq; NP_001071570.1; NM_001078102.1.
DR   AlphaFoldDB; Q0VBY7; -.
DR   SMR; Q0VBY7; -.
DR   STRING; 9913.ENSBTAP00000000600; -.
DR   PaxDb; Q0VBY7; -.
DR   GeneID; 768227; -.
DR   KEGG; bta:768227; -.
DR   CTD; 120526; -.
DR   eggNOG; KOG0715; Eukaryota.
DR   HOGENOM; CLU_017633_7_3_1; -.
DR   InParanoid; Q0VBY7; -.
DR   OrthoDB; 1580122at2759; -.
DR   TreeFam; TF326955; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR   GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
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; IPR042978; DNAJC24.
DR   InterPro; IPR007872; DPH_MB_dom.
DR   InterPro; IPR036671; DPH_MB_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR45255; PTHR45255; 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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Electron transport; Iron; Metal-binding;
KW   Reference proteome; Transport; Zinc.
FT   CHAIN           1..149
FT                   /note="DnaJ homolog subfamily C member 24"
FT                   /id="PRO_0000376799"
FT   DOMAIN          11..82
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   DOMAIN          93..148
FT                   /note="DPH-type MB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         117
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         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
SQ   SEQUENCE   149 AA;  17135 MW;  F22FE94CE5DB9545 CRC64;
     MMAFEQIPKK DWYSILGADP SASVSDLKQK YQKLILMYHP DKQSADAPAG SVEECIQKFI
     EIDQAWKILG NEETKKEYDL QRHEDDLRNM GPVDARIYLE EMSWNEDDHS FSLSCRCGGK
     YSVSKDEAEE VTLISCDTCS LIIELLHYC