ID A0A091H1L7_BUCRH Unreviewed; 1636 AA.
AC A0A091H1L7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
DE Flags: Fragment;
GN ORFNames=N320_00641 {ECO:0000313|EMBL:KFO88525.1};
OS Buceros rhinoceros silvestris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO88525.1, ECO:0000313|Proteomes:UP000054064};
RN [1] {ECO:0000313|EMBL:KFO88525.1, ECO:0000313|Proteomes:UP000054064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO88525.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00006801}.
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DR EMBL; KL517532; KFO88525.1; -; Genomic_DNA.
DR Proteomes; UP000054064; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd16873; ARID_KDM5A; 1.
DR CDD; cd15602; PHD1_KDM5A; 1.
DR CDD; cd15606; PHD2_KDM5A; 1.
DR CDD; cd15686; PHD3_KDM5A; 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); 3.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR047974; KDM5A_ARID.
DR InterPro; IPR047973; KDM5A_PHD1.
DR InterPro; IPR047970; KDM5A_PHD2.
DR InterPro; IPR047972; KDM5A_PHD3.
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:SF17; LYSINE-SPECIFIC DEMETHYLASE 5A; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 2.
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; SM00249; PHD; 3.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KFO88525.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054064};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KFO88525.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 29..119
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 237..287
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 381..547
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1105..1162
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1551..1605
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1271..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1436..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1485..1520
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO88525.1"
FT NON_TER 1636
FT /evidence="ECO:0000313|EMBL:KFO88525.1"
SQ SEQUENCE 1636 AA; 186430 MW; F05845C811202F17 CRC64;
DWQPPFACEV QSFRFTPRIQ RLNELEAMTR VKLDFLDQLA KFWELQGSNL KIPVVERKIL
DLYGLSKIVA SKGGFEVVTK EKKWSKVASR LGYLPGKGTG SLLKSHYERI LYPYELFQSG
VSLMGIQKSN LDLKEKVEAE DHSLDAQTSP KQASRMNVVL KRTRRVKSQA EAGEMSRNTE
LKKLQIFGAG PKMMGLALGT KDKEDEVTRR RKGTRSEAFG MQMRQRKGTL SVNFVDLYVC
LFCGRGNNED KLLLCDGCDD SYHTFCLIPP LPDVPKGDWR CPKCVAEECN KPREAFGFEQ
AVREYTLQSF GEMADNFKSD YFNMPVHMVP TELVEKEFWR LVSSIEEDVI VEYGADISSK
DFGSGFPVKD GRRKLMPEEE DYALSGWNLN NMPILEQSVL AHINADISGM KVPWLYVGMC
FSSFCWHIED HWSYSINYLH WGEPKTWYGV PSHAAEQLED VMKELAPELF ESQPDLLHQL
VTIMNPNVLM EHGVPVYRTN QCAGEFVVTF PRAYHSGFNQ GYNFAEAVNF CTADWLPIGR
QCVSHYRRLG RHCVFSHEEL IFKMAADPEC LDVGLAAMVC KEMTLMIEEE TRLRDSVVQM
GVLMSEEEVF ELVPDDERQC TACRTTCFLS ALTCSCNPER LVCLYHPSDL CPCPMQKKCL
RYRYPLEDLP SLLYGVKVRA QSYDTWVSRV TEALSANLNH KKDVIELRVM LEDAEDRKYP
ENDLFRRLRD AVKEAETCAS VAQLLLSKKQ KHRQSQESGR TRTKLTMEEL KAFVQQLFSL
PCVISQARQV KNLLDDVEEF HERAQEAMMD EIPDSSKLQE LIDMGSGLYV ELPELPRLKQ
ELQQARWLDE VRSTLLDPQR VTLDVMKKLI DSGVGLAPHH AVEKAMAELQ ELLTVSERWE
EKAKVCLQAR PRQSMMALEG IVNEAKNIPA YLPNVLALKE ALQRARDWTA KVEAIQNGSN
YAYLEQLENL TAKGRPIPVR LDALPQLESQ VAAARAWRER TGRTFLKKNS SYSLLQVLSP
RTDIGVYGSS KNRRKRVKEL MEKEKEKELD LESLSELEDG LEEARDTAAV VAIFKEREQK
EIEAMHALRA ANLAKMTMVD RIEEVKFCIC RKTAIGFMLQ CELCKDWFHS GCVPLPKTSS
QKKGSSWQAK EVKFLCPLCM RSRRPRLETI LSLLVSLQKL PVRLPEGEAL QCLTERAMSW
QDRARQALAT DELSSALAKL SVLSQRMVEQ AAREKTEKII SAELQKAAAN PDLQGHLTNF
QQSAFNRVIG SVSSSPRQTL DYDDEETDSD EDIRETYGYD IKDNASVKSS SSLEPNLFCD
EEIPIKSEEV VTHMWTAPSF CAEHAYSSAS KSCSQGSSTP RKQPRKSPLV PRSLEPPVLE
LSAGAKAQLE DLMMVGDLLE VSLDETQHIW RILQATHPPS EDRFLHVMED DSMDEKPLKM
RGRDSSERKR KRKLERAEQF FGDMKQKSKE LKKLEKPKKK KLKLSIDKTK ELNKLAKKLA
KEEERKKKRE KAVVAKVELA KESTEKKREK KVLDIPSKYD WSGAEDSDDE NAVCAAQNCQ
RPCKDKVDWV QCDGGCDEWF HQVCVGVSPE MAENEDYICI NCAKKPVQGP SSPAHAPPPP
FILSYKLPME DLKETS
//