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Database: UniProt
Entry: A0A151WXX1_9HYME
LinkDB: A0A151WXX1_9HYME
Original site: A0A151WXX1_9HYME 
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
//
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