ID A0A2U3X1Z7_ODORO Unreviewed; 1443 AA.
AC A0A2U3X1Z7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN Name=LOC101375635 {ECO:0000313|RefSeq:XP_004416115.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004416115.1};
RN [1] {ECO:0000313|RefSeq:XP_004416115.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000604};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00006801}.
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DR RefSeq; XP_004416115.1; XM_004416058.1.
DR STRING; 9708.A0A2U3X1Z7; -.
DR GeneID; 101375635; -.
DR KEGG; oro:101375635; -.
DR InParanoid; A0A2U3X1Z7; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16875; ARID_KDM5C_5D; 1.
DR CDD; cd15604; PHD1_KDM5C_5D; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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 PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF141; LYSINE-SPECIFIC DEMETHYLASE 5D; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 14..55
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 79..169
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 222..272
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 366..532
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1220..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1358
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1396
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1443 AA; 163695 MW; 9E5A17326525DC0D CRC64;
MEPGSDDFLP PPECPVFEPT WAEFRDPLGY IAKIRPIAEK SGICKIRPPV DWQPPFAVEV
DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERRIL DLYGLSKIVM
EEGGYEAICK DRRWARVAQR LNYPPGKNIG SLLRSHYERI IYPYEMFQSG ANLVQCNTHP
FDNEEKDKEY KPHSIPLRQS VQPSKFSSYS RRAKRLQPDI DSYVCRICSR GDEDDKLLLC
DGCDDNYHIF CLIPPLLEIP RGVWRCPKCI MEECKRPPEA FGFEQATQEY TLQSFGEMAD
SFKTDYFNMP VHMVPTELVE KEFWRLVSSI EEDVTVEYGA DIHSKEFGSG FPVSNSKGNL
SPEEEEYATS GWNLNVMPVL DQSVLCHINA DISGMKIPWL YVGMVFSAFC WHIEDHWSYS
INYLHWGEPK TWYGVPSLAA EQLEEVMKRL TPELFDSQPD LLHQLVTLMN PNTLMSHGVP
VVRTNQCAGE FVITFPRAYH SGFNQGYNFA EAVNFCTADW LPAGRQCIEH YRRLRRYCVF
SHEELICKMA AFPEKLDLNL AVAVHKEMFI MVQEERRLRK ALLEKGITEA EREAFELLPD
DERQCMKCKT TCFLSALACY DCPDGLVCLS HINDLCKCSS SRQYLRYRYT LDELPAMLHK
LKIRAESFDT WANKVRVALE VEDGRKRSFE ELRALESEAR ERRFPNSDLL QRLRNCLNEA
EACVSQVLGL VSGQEARIET PQLTLTELRV LLEQMGSLPC AMHQIGDVKD VLEQVEAYQI
EAREALASLP PSVGLLRSLL EKGQQLGVEV PEAHQLQQQV EQARWLDEVK QALAPSAQRG
SLVIMQGLLV TGAKIASSPS VDKARAELQE LLTIAERWEE KAHFCLEARQ KHPPSTLEAI
IREAENIPVH LPNIQALKDA LAKAHAWIAD VDEIQNGDHY PCLDDLEGLV AIGRDLPVGL
EELRQLELQV LTAHSWREKA SKTFLKKNSC YALLEVLCPC TDAGSDTSKR SRWIEKELGL
YRSDTELLGL SAQDLRDPGS VIVAFKEGEQ KEKEGILQLR RTNSAKPSPL ASSTAVSSAT
SICVCGQVPA GVGALQCDLC QDWFHGQCVS VPRLFSSSRP SSTSSPLLAW WEWNTKFLCP
LCMRSRRPRL ETILALLVAL QRLPVRLPEG EALQCLTERA IVWQGRARQA LASEDVTALL
GQLAELRQQL QDVSRLEEPL TYPSTPACDP HREGSGNDMP KVPGLLPNVD SMATHGKIAP
VQGSDLEVLS SLLPQLTGPV LNLPEATRAP LEELMLEGDL LEVTLDENHS IWQLLQAGQP
PDIERIRTLL ELEKPEHQGN RTRGRALEKR RRRRQQKIDL GRKSKEELQS KKARNSDIKP
DEGQEEEFEE ETDSENIFLT STEHSPILKG NQNSFQQNDS GSVASFPSLT PLLHQPYPQR
EEL
//
