JMJD6_CAEBR
ID JMJD6_CAEBR Reviewed; 397 AA.
AC Q623U2; A8WR01;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Bifunctional arginine demethylase and lysyl-hydroxylase psr-1;
DE EC=1.14.11.-;
DE AltName: Full=Phosphatidylserine receptor 1;
GN Name=psr-1; ORFNames=CBG01722;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Dioxygenase that can both act as a histone arginine
CC demethylase and a lysyl-hydroxylase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with ced-5 and ced-12. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JMJD6 family. {ECO:0000305}.
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DR EMBL; HE601298; CAP22909.1; -; Genomic_DNA.
DR RefSeq; XP_002634158.1; XM_002634112.1.
DR AlphaFoldDB; Q623U2; -.
DR SMR; Q623U2; -.
DR STRING; 6238.CBG01722; -.
DR GeneID; 8576153; -.
DR KEGG; cbr:CBG_01722; -.
DR CTD; 8576153; -.
DR WormBase; CBG01722; CBP44155; WBGene00024914; Cbr-psr-1.
DR eggNOG; KOG2130; Eukaryota.
DR HOGENOM; CLU_016785_8_0_1; -.
DR InParanoid; Q623U2; -.
DR OMA; DLFKYCG; -.
DR OrthoDB; 609279at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0033749; F:histone H3-methyl-arginine-3 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106140; F:P-TEFb complex binding; IBA:GO_Central.
DR GO; GO:0070815; F:peptidyl-lysine 5-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0018395; P:peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine; ISS:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR003347; JmjC_dom.
DR Pfam; PF13621; Cupin_8; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..397
FT /note="Bifunctional arginine demethylase and lysyl-
FT hydroxylase psr-1"
FT /id="PRO_0000129377"
FT DOMAIN 146..310
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 334..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 202
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 290
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 45954 MW; DAA3E0270659CE71 CRC64;
MSLGKDRYSL PRSYKRVSHA KEKARPELRK FGWDTLGYAE SFNPPPLKDT IPRVDGKKIS
VDEFRRDFER PRIPVILTGL TDDWNAHEKW TLERLSKKYR NQNFKCGEDD HGNSVRMKMK
YYHDYMLNNR DDSPLYIFDS SFAERRKTKK LSEDYKVPKF FEDDLFHYAD HKKRPPHRWF
VMGPARSGTA IHIDPLGTSA WNSLLLGYKR WVLIPPNAPR DLVKPMAHEK GKHPDEGITW
FQTVYKRVRS PAWPKEYAPI ECRQGPGETM FVPSGWWHVV INEGLTVAVT HNYCSVENLH
LVWPKTVRGR PKLSKHWHRK LAESRPEVLK IINSCTDTPP QSLNDSSSDS SSSSSSSDDS
SDSETEEDSG RCGLGNRKRR NDVCTSECPE KISNSMV
