ID A0A151WXX1_9HYME Unreviewed; 980 AA.
AC A0A151WXX1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=JmjC domain-containing histone demethylation protein 1 {ECO:0000256|ARBA:ARBA00015153};
DE EC=1.14.11.27 {ECO:0000256|ARBA:ARBA00013246};
DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1 {ECO:0000256|ARBA:ARBA00031083};
GN ORFNames=ALC60_08128 {ECO:0000313|EMBL:KYQ52713.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ52713.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ52713.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ52713.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ52713.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-36'
CC of histone H3, thereby playing a central role in histone code.
CC {ECO:0000256|ARBA:ARBA00003909}.
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:0000256|ARBA:ARBA00001574};
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 JHDM1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00008037}.
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DR EMBL; KQ982656; KYQ52713.1; -; Genomic_DNA.
DR RefSeq; XP_018307187.1; XM_018451685.1.
DR AlphaFoldDB; A0A151WXX1; -.
DR STRING; 64791.A0A151WXX1; -.
DR GeneID; 108724960; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd21783; CTD_Jhd1-like; 1.
DR CDD; cd15555; PHD_KDM2A_2B; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR002857; Znf_CXXC.
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; PTHR23123:SF21; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 1; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF16866; PHD_4; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00367; LRR_CC; 6.
DR SMART; SM00368; LRR_RI; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
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:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 154..322
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 474..520
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 527..597
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 600..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 112144 MW; 875A3888F1E50B19 CRC64;
MSAMADDSVP LPKRRQLRER TRKLYTDDWT IGDEEIEGRR TFQLDEKIEA KRYDLSNFSG
LFREMTGPEL NLTYLQKHGL QIPLLFRDKS GLGLRVPSSN FSVNDVRTCV GSKRVLDVMD
VNTQKNEDMT MKEWQKYYED PNKERLLNVI SLEFSHTKLE NYVQSPALVR QVDWVDVVWP
RHLKESQVES TNLLEDMMYP KVQKYCLMSV KGCYTDFHVD FGGTSVWYHI LHGGKIFWLI
PPTEKNLTLY QEWVLSGKQS DVFFGDMVDK CGRISLTAGM TLFIPTGWIH AVYTPQDSLV
FGGNFLHSFG IEMQLKVAQV EEHTKVPQKF RYPFFTEMLW YVLERYVHVL LGRSHLDISE
SQRQHLVPQH HQHVHVTEFE LHGLKSIVMY LHSLPSTKKN VPELMRDPVA LIHDVRCLVE
QHRHDNPEAA VTGNPVLPPP PPLTIVDRER LRVARKGFVK SQRHNSDKSE RAFPRRRRTR
CKKCEACTRQ DCRECVFCQD MVKFGGSGRA KQTCLMRQCL RPMLPVTSSC KVCRLDGWKQ
PPAPLTGKSF PTTPSTLMEC SICFDIVHPE CIGLNSKEIT VNDDLPNSWE CPECYERGRN
SDCRPRHARG RTRKLSISSA ASSAPTTDSE RAMTPSKQSR LDPNDAWNDS PGEPAEGEQR
MTQQRTQLAM QLIASSSRSL VRPQVVVRPA PPSLIQETDG ENEQNLVYNK TVVLAVFRFL
SIKDLLNCAL VCRTWARYST DFSLWKKLDM SHYNLRSVHL TVIVRRQPEC LSLDWTNINK
MQLAWLLERL PQLRTLSLQG CTWAGVRALK RCTCPPLEKL NLSYVTSLND TVLQEILDSP
TDSRPGIIDK TSRLKHLKNL SLAGCDLTDR GVKYIVQQLS DLETLDLSSI GRLTDSGVAH
LTSLSNLASL NLANCKLLTE TTLDHLAKCE ALKRLDLRHT TQVSTQAVIK FAAKSEHNLH
VTDVKLVEEK KKVKTDFMDT
//