ID   JMJD4_CHICK             Reviewed;         425 AA.
AC   Q5ZHV5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=2-oxoglutarate and iron-dependent oxygenase JMJD4 {ECO:0000250|UniProtKB:Q9H9V9};
DE            EC=1.14.11.-;
DE   AltName: Full=JmjC domain-containing protein 4;
DE   AltName: Full=Jumonji domain-containing protein 4;
DE   AltName: Full=Lysyl-hydroxylase JMJD4 {ECO:0000250|UniProtKB:Q9H9V9};
GN   Name=JMJD4; ORFNames=RCJMB04_32n10;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Catalyzes the 2-oxoglutarate and iron-dependent C4-lysyl
CC       hydroxylation of ETF1 at 'Lys-63' thereby promoting the translational
CC       termination efficiency of ETF1. {ECO:0000250|UniProtKB:Q9H9V9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-lysyl-[protein] + O2 = 4-hydroxy-L-lysyl-
CC         [protein] + CO2 + succinate; Xref=Rhea:RHEA:57156, Rhea:RHEA-
CC         COMP:9752, Rhea:RHEA-COMP:15084, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:141495;
CC         Evidence={ECO:0000250|UniProtKB:Q9H9V9};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q9H9V9};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H9V9}.
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DR   EMBL; AJ721029; CAG32688.1; -; mRNA.
DR   RefSeq; NP_001026130.1; NM_001030959.1.
DR   AlphaFoldDB; Q5ZHV5; -.
DR   SMR; Q5ZHV5; -.
DR   STRING; 9031.ENSGALP00000008687; -.
DR   PaxDb; Q5ZHV5; -.
DR   GeneID; 420400; -.
DR   KEGG; gga:420400; -.
DR   CTD; 65094; -.
DR   VEuPathDB; HostDB:geneid_420400; -.
DR   eggNOG; KOG2131; Eukaryota.
DR   InParanoid; Q5ZHV5; -.
DR   OrthoDB; 609279at2759; -.
DR   PhylomeDB; Q5ZHV5; -.
DR   PRO; PR:Q5ZHV5; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106156; F:peptidyl-lysine 4-dioxygenase activity; IEA:RHEA.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0010629; P:negative regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0045905; P:positive regulation of translational termination; ISS:UniProtKB.
DR   GO; GO:0018126; P:protein hydroxylation; ISS:UniProtKB.
DR   InterPro; IPR003347; JmjC_dom.
DR   Pfam; PF02373; JmjC; 1.
DR   SMART; SM00558; JmjC; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..425
FT                   /note="2-oxoglutarate and iron-dependent oxygenase JMJD4"
FT                   /id="PRO_0000291961"
FT   DOMAIN          141..300
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         188
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT   BINDING         190
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT   BINDING         268
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NYC1"
SQ   SEQUENCE   425 AA;  49121 MW;  962A7BDCB3BD567B CRC64;
     MDRATFACST AFFHDYSSSA QGTFSTGHVD FIDKIESFTY SDFFRDYLIP NQPCVFSEKF
     TDGWGSRRNW VTWGGKPDFD HLLQEFGEAI VPVANCDVKE YNSNPKEQLP FKEYISYWKE
     YIKNGYRSSR GCLYLKDWHL SRAFPEQDVY TTPVYFSSDW LNEYWDAIAV DDYRFVYMGP
     KGSWTPFHAD VFRSYSWSAN ICGRKKWLLY PPGQEDYLKD CHGNLPFDVT APGLQDRSVY
     PRYNQSQPPV EIVQEAGEIV FIPSGWHHQV YNLEDTISIN HNWVNGCNVA IMWCFLQDEL
     AAVQREINEW KDPMDDWHLQ CQLIMKSCTG IDYKEFYNFL KVIAENRISI LENGLDDEAS
     AKNTPKAAIS TLGMLHAVFD LKRTVKVLTS LSANEDFKKL DLTSLSPPQE ALLHHLKAAI
     DTALL