ID   KDM5_CAEBR              Reviewed;        1482 AA.
AC   Q61T02; A8X185;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Lysine-specific demethylase rbr-2;
DE            EC=1.14.11.67 {ECO:0000250|UniProtKB:Q23541};
DE   AltName: Full=Histone demethylase rbr-2;
DE   AltName: Full=Jumonji/ARID domain-containing protein rbr-2;
DE   AltName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase rbr-2 {ECO:0000305};
GN   Name=rbr-2; ORFNames=CBG05959;
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: Histone demethylase that specifically demethylates 'Lys-4' of
CC       histone H3, thereby playing a central role in histone code. Does not
CC       demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79'
CC       or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not
CC       monomethylated H3 'Lys-4'. Involved in larval development and vulva
CC       formation. {ECO:0000250|UniProtKB:Q23541}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC         [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC         H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC         Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC         Evidence={ECO:0000250|UniProtKB:Q23541};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC       ECO:0000255|PROSITE-ProRule:PRU00537}.
CC   -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC       {ECO:0000305}.
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DR   EMBL; HE600909; CAP26395.3; -; Genomic_DNA.
DR   AlphaFoldDB; Q61T02; -.
DR   SMR; Q61T02; -.
DR   STRING; 6238.CBG05959; -.
DR   PRIDE; Q61T02; -.
DR   EnsemblMetazoa; CBG05959.1; CBG05959.1; WBGene00028313.
DR   WormBase; CBG05959; CBP37609; WBGene00028313; Cbr-rbr-2.
DR   eggNOG; KOG1246; Eukaryota.
DR   HOGENOM; CLU_000991_2_2_1; -.
DR   InParanoid; Q61T02; -.
DR   OMA; DGISYME; -.
DR   OrthoDB; 664180at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR   GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR   GO; GO:0034720; P:histone H3-K4 demethylation; IEA:EnsemblMetazoa.
DR   GO; GO:0040028; P:regulation of vulval development; IEA:EnsemblMetazoa.
DR   Gene3D; 1.10.150.60; -; 1.
DR   Gene3D; 3.30.40.10; -; 2.
DR   InterPro; IPR001606; ARID_dom.
DR   InterPro; IPR036431; ARID_dom_sf.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR003349; JmjN.
DR   InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR   InterPro; IPR004198; Znf_C5HC2.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF01388; ARID; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF02375; JmjN; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF08429; PLU-1; 1.
DR   Pfam; PF02928; zf-C5HC2; 1.
DR   SMART; SM00501; BRIGHT; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00545; JmjN; 1.
DR   SMART; SM00249; PHD; 3.
DR   SUPFAM; SSF46774; SSF46774; 1.
DR   SUPFAM; SSF57903; SSF57903; 2.
DR   PROSITE; PS51011; ARID; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51183; JMJN; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Coiled coil; Dioxygenase; Iron; Metal-binding;
KW   Nucleus; Oxidoreductase; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1482
FT                   /note="Lysine-specific demethylase rbr-2"
FT                   /id="PRO_0000292419"
FT   DOMAIN          61..102
FT                   /note="JmjN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT   DOMAIN          126..223
FT                   /note="ARID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT   DOMAIN          471..637
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   ZN_FING         322..374
FT                   /note="PHD-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         1206..1260
FT                   /note="PHD-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         1416..1471
FT                   /note="PHD-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1361..1403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1377..1398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         517
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         520
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         605
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ   SEQUENCE   1482 AA;  170811 MW;  4047E2EC941EBE88 CRC64;
     MRGRRQEDIA TTSSAPSTST SHKKKTVSSN GSFRPRTQSN PGGKMEMYDH FYKNFQRPPM
     APVYYPTSEE FADPIEYVAK IRPDAERYGV VKIVPPSDFK PPFAIDKEKF TFRPRTQKLN
     EVEAIVKEKH TFIERLVNFN RYSGLQFEFP VDRDGNVVDL YRLHRIVQNF GGCEEVNDEE
     RWRDVAREYL PKEQMTRGVP SYFINLIRAH YNLHIEPFNR NLKEKAMKNE DESDDELEEL
     KHKYQHHHGT MRSEPENTDG KNTEDVEEEC PMSMQSGRRR SKNKKPVPAK KSSNGTPKKG
     SRGKKNSKTE EDEEENEDVI EQVYCVSCNE GKDEDLLLLC DIEGCNSGRH TYCCDPVLDE
     VPEGEWRCPK CIESEDAKIG LDWGFYDAET EYNLNTFTEF ANKWKCDYFG VDNVSKVSCD
     ALEKEFWKNV VSHDNPVAVK YGADLITSRV GSGFPRKEDK HTGPDSKLKQ QYANHAWNLN
     NMPVLSESVL SYFNTGISGM MVPWVYVGMC FSTFCWHTED HWTYSVNYNH FGERKIWYGV
     GGDDAEKFEE ALKRLAPGLT GRQRDLFHHM TTAANPSLLR SLGVPIYSVH QNAGEFVITF
     PRAYHAGYNE GLNFAEAVNF APIDWLAKGR ECVQSYSNVR RYLVFSHDEL LFKMIEAMDR
     LGLSTTLAAY DELKRVIEKQ KRLRQFIAQL GVPARNVEQV AFEKIPDEQR SCRFCKTTLF
     MCALICNKHK RMTCVEHHDH LCKTCTPKDY KYQYRYEIDN LTHLFDELGK RTVDTAGWQE
     DDDDMYTQEE MPKLEPMVDL YNVEEQSSSR QKNQVHNIIA IQHTAKSAIE KANQLLFKKV
     RTRTKTRCQR ADTRTDADGV KSLIEQMQGM DCNLSGLIDK LQKFLDQIDA WRSKAQIMMS
     QEHKYSKDDF EHFIEEGDEY DIKLSEIEEL RKVVGMKEWS ERAIEITSWA PTSNMEKDID
     FEYKMRYTNK DVIALIREGS RSSSNHTSQL IAKLQHMLAE ANKREAEATE YFDNPSLDKL
     QSIWKNLRTS DWFYEPYINL VRFEIGQIAK IKSMIDSTIP ALSGLDLKPQ LLRLGDSSIT
     FAKAVELSKA CELSKTLHKS QEHSSLLELI NRMNLFTERI AKLFKPMNSY HNLFEIVSER
     DDLTPLAEGQ VLQLYYQGET INSGNEWHQI KDFDSLEQML HHQSSLREMQ SRIFEKVKQT
     NSARGLEGCC CLGGNKSDSS ESVLSCIMCE SQFHVRCCEW STFFQHLPKG CFMCVRCLRG
     QRPVIDDVAN ALNGTPSGCM ETHLVRNLIQ KSRIITQNLM DCSNKRQSGE VASDEMCKKA
     LFDWLACEIM NPNGLPKAVE LIHEFFGDYL EKQASAALEL QQRPVKSKPS ASLFDPKLNS
     KRKRPNPSQK DSSKSKSRKR QGQISPIDYC EEETEFKSCQ ARSCLKPFGD SVNWVMCDAG
     CKNWFHVICV GFTLREINDM HEYRCSSCLD HADSPASSVS TE