ID A0A1V9X663_9ACAR Unreviewed; 1544 AA.
AC A0A1V9X663;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ORFNames=BIW11_01959 {ECO:0000313|EMBL:OQR68762.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR68762.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR68762.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR68762.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR68762.1}.
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DR EMBL; MNPL01023354; OQR68762.1; -; Genomic_DNA.
DR STRING; 418985.A0A1V9X663; -.
DR InParanoid; A0A1V9X663; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
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 GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15515; PHD1_KDM5A_like; 1.
DR CDD; cd15610; PHD3_KDM5A_like; 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); 2.
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:SF133; LYSINE-SPECIFIC DEMETHYLASE LID; 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; 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; SM00545; JmjN; 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; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
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 Methyltransferase {ECO:0000313|EMBL:OQR68762.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:OQR68762.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 13..54
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 78..168
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 293..343
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 436..602
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1468..1522
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 209..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1471
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1544 AA; 174818 MW; 128C09858CF9618F CRC64;
MADDSEFVPP PQCHVFEPTA EDFKDPLAYI AKIRHVAETS GICKVIPPKD WQPPFVVDVD
NFRFTPRVQR LSELEASSRL KLNFLDKIAK FWHLRGNTLK IPMVERKSLD LFKLHRIVQS
EGGFHKVGRE RKWFQVVQRL GLPPVKSLST VLRNHYERIL LPYDIFKQTG GFLAPETKPA
VKAEEVCKES LAPKINIQEK VDRDYVPHEI VQRQNIPPPS TTGQRRSKRH CDASQNEEGT
SGVTAAVAGG GEVSDNKELK RLAFYGAGPK LPGYSPPKKK VKDEPIGDEA VAHIMCKACE
KGDDEDRLLL CDKCDAPFHT FCLRPPLHEI PKGEWRCPKC VASEVLKPKE AFGFEQARQE
YTLQEFGEKA DRFKRDYFHM PIHKINTEVV EKEFWKVLSD IHADVTVEYG ADLHSAEVGS
GFPTENTPGL MPEDREYVTC PWNLNNLANL NASVLRHIDS DISGMKVPWV YVGMCFSTFC
WHNEDHWSYS INYLHWGEPK TWYGVPGDAA EKFESAMAAK APELFEAQPD LLHQLVTIMN
PTVMQASGVP IYRVDQKPGE FIITFPRAYH AGFNQGYNFA EAVNFCPADW LPIGRACVRH
YALLNRFCVF SHDELVCKMA SDPDKIDIGL AAATFHDMLT MVEGECQLRN GVSDWGVTKS
ERLIFEIIPD DERQCHTCKT TCFLSAITCQ CREEKTRRGD KDNKDEKVQS NMVCLNHARN
LCESCKPGQH ILKYRYALDE LPTMLENLRR KVEAFDEWVR KIKELLIKNR NPKPSLEDLK
ALLNEANEHN YPSVDVGAAL KKAVRQAETY AQFAQQLLAT KVRTRRQDVN NQPVGRLTKE
ELAKFYQEMQ TMQCTIKETS IIRGLMDNVE NFCTQAEGFL KMDDSDEAIP LDKLKELTVR
GESLDVELPQ LTQLRHKMER VSWLRRVNRL LAARRDSEDN VEVSLQDIRG LLREGVNLAP
HRNVESRAGQ LQQLLVDCEK HEDWASEALK AKPKPSITDI EGRLQEALQI PVTLPSVLLL
EEALFKAKDW VEQMQELTSR QRHPYLEQLE ALMNKARHIQ LGLEPSWGKL EGIVDGARAW
RDRAAKTFMK KNTPAGLQLL DILSPRDDPL NSRGVRINKK DEISVAEAFE AAATKELDYY
RRLRRHNQLR RQRRHSNKGH FNNSNEDLSV LEEKHCICHR PFTRNMLQCV LCNDFFHLTC
VPPSCVSQAV GASGDRSPST GIGANNEGSN SSAGDSNGKS QTSTVTNTAN LTPPKFLCVW
CQRGRRPRLE TILHLLVQLE SLPVRVMEGE ALQWLTERAM LWQNKARQTL QGREVTGAVQ
KLHQIGLMIQ RGELEHLEST YGFAAKRNSS GTQEGWYYSR PLIHLPGDIL AKLEDLMMEG
DLLEVSLEET MSLWRVISAT RSNLPPLSAS GIDSAEESPR KRGRKPGSAL EDGRRRRAQA
PAGAVSLSVQ EYDDSSTGGA DDEDDDDEDK CSADQCERPE GEAVNWVQCD GGCDKWFHMR
CVGLPDDHQM DDDFVCNACN AQDESLSAGD IQASTSRSSG VAIR
//
