JHD1_CAEBR
ID JHD1_CAEBR Reviewed; 1063 AA.
AC Q60V67; A8XW64; E3CU71;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=JmjC domain-containing histone demethylation protein 1;
DE EC=1.14.11.27 {ECO:0000250|UniProtKB:P40034};
DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1;
GN Name=jhdm-1; ORFNames=CBG19679;
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-36'
CC of histone H3, thereby playing a central role in histone code.
CC {ECO:0000250|UniProtKB:P40034}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.27;
CC Evidence={ECO:0000250|UniProtKB:P40034};
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:0000250}.
CC -!- DOMAIN: The JmjC domain mediates the demethylation activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC {ECO:0000305}.
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DR EMBL; HE600934; CBX32964.1; -; Genomic_DNA.
DR AlphaFoldDB; Q60V67; -.
DR SMR; Q60V67; -.
DR STRING; 6238.CBG19679; -.
DR PRIDE; Q60V67; -.
DR WormBase; CBG19679; CBP44235; WBGene00038854; Cbr-jhdm-1.
DR eggNOG; KOG1633; Eukaryota.
DR HOGENOM; CLU_286864_0_0_1; -.
DR InParanoid; Q60V67; -.
DR OMA; DPRMEMM; -.
DR OrthoDB; 353641at2759; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; 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..1063
FT /note="JmjC domain-containing histone demethylation protein
FT 1"
FT /id="PRO_0000226788"
FT DOMAIN 86..266
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 379..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..630
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 165
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 1063 AA; 121968 MW; 1A904471269FDA24 CRC64;
MEPEELTIEW YEENGLEKPI HFRCDPTRIG MKLPSPSTFT VDSVLELVGG NRMIEVVQVE
DQGSVKMTLE EFVEFYKTPR DQRKNLYNVL SLEYSLTPLE DLVNSPALVR QIDWVGNIWP
DALRQRWISF NGREKKSYFP HHTFPKVQNY CLMSVANCYT DFHIDFSGTS VWYHVLKGRK
VFWLIPPTAT NFFIYQEFIK TVSDNAFFGR SVEACHVAVL EPGDTMLIPS GWIHAVYTPD
DSLVFGGNFL HSLSCQTQLR VYQVENKLNI TRKFRLPYNE ELLFYVMADY VKKWTGREYV
RPLLVEDAKL DYVGEKWKAA GGHLKKIRFE DYNVEVTSEM VKNEEESEKD EVKVIAMHAG
SSNYDNAMIS KMSYTEATGL EEEAEDEDVK PETKKEAEER RDAEIDLLAA TNSLIFYRNS
KHDFIRNKSV PDHKLPIGHE PPVYFNDEEV SRISPRLLEE LEALGAYIRR KNRVEVAEGI
CHPASLINLF NTVLKKRRAE LTGKPFQFNQ IMPRRYTRAA IETGDYDFEP VRTIEDSRRA
SQFKVEDFPD ELLESDEPDE TSRIHLPHQP SSGPLEYIPT PRGEIRENSL GFEPEYDEDM
EEYDPAEQVV KEELEEEEEE EEGEEEEEEE YVAPVTRRSS TRGSASTKEE PQEEKEEKEA
APKKEKKEKK VKKEKSSKPE KDTTEAKLKK EKKKKEMERR LRDSELEAEL RAAHGGKNAK
SKKKPEKPAY VGGLPTAPIQ NDPVVSNPYN YDPRMEMMKL GTGQLKSAYR KTKANVELHI
EKNLYKLEPK RDESESREPS MEHEDSPTTP HAPYDRYSHY HTENSHFQED QDSHRTPAKR
SKYDNISVDT SESPHIPKKR SLEGRPSPYS VISPPHNRPK LSSPAMFSPS SEPRRSNDRR
TSDPAVNAMK KGVYMPPMSR QDKMIAEAAS ASSSRHSSFS ERRPSFIPDL NSSRHSSTDT
PMYTPTAPAR SSWLPNTSNV TRHSLDDDSP IDVVSESPID VLNSPPFPRS ITPPPVSLSE
LKSQSNGRKS NYSEDGKRAK IPAREAVAEL KTLIGKLKTL NEA
