ID A0A484BJC8_DRONA Unreviewed; 1356 AA.
AC A0A484BJC8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=[histone H3]-dimethyl-L-lysine(36) demethylase {ECO:0000256|ARBA:ARBA00013246};
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=AWZ03_004751 {ECO:0000313|EMBL:TDG48848.1};
OS Drosophila navojoa (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG48848.1, ECO:0000313|Proteomes:UP000295192};
RN [1] {ECO:0000313|EMBL:TDG48848.1, ECO:0000313|Proteomes:UP000295192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG48848.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:TDG48848.1};
RX PubMed=30423125; DOI=.1093/jhered/esy059;
RA Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT the mojavensis Cluster.";
RL J. Hered. 110:118-123(2019).
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}.
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:TDG48848.1}.
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DR EMBL; LSRL02000029; TDG48848.1; -; Genomic_DNA.
DR RefSeq; XP_017958728.1; XM_018103239.1.
DR STRING; 7232.A0A484BJC8; -.
DR GeneID; 108653004; -.
DR KEGG; dnv:108653004; -.
DR OMA; HTHLTHY; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000295192; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0140680; F:histone H3K36me/H3K36me2 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR003347; JmjC_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002857; Znf_CXXC.
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; PF13516; LRR_6; 1.
DR Pfam; PF16866; PHD_4; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00367; LRR_CC; 5.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000295192};
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 171..339
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 667..713
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 1074..1120
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1069
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1356 AA; 148425 MW; 92CE89C063201659 CRC64;
MSTAETGSSP GKSNSNNNNG VAAGGNAKGV QRRQLRERKQ RKLYLEECLL GDDDAEGARG
FSVAEKLESS KFAQAGMVRE MRGCDLTVSF LQQHGFNIPL LFREKNGLGL RMPDAQEFTV
NDVRLCVGSR RLLDVMDVNT QKNLQMTMKE WQQYYDNPQK DRLLNVISLE FSHTRLDNFV
QSPEIVRQID WVDVVWPKQL KDAQKEGTNL LGGMMYPKVQ KYCLMSVKNC YTDFHIDFGG
TSVWYHILKG SKVFWLIPPT DRNLQLYEKW VLSGKQADVF FGDTVEKCAR VYLTAGNTFF
IPTGWIHAVY TPTQSLVFGG NFLHSFGIVK QLKTASVEDN TKVPQKFRYP FFTEMLWYVL
ARYVYTLLGH SHLEGEPSVS EIEMSARPHI HLTHYELFGL KEIVMYLYDL PPQKKNVPSL
VLDPVALIKD VRTLVERHCK DQQDLAVTGM SVLRPAAEHQ PVFQLYDRTR VKQEIKQEIA
RKNAEVIREQ QQLEAAREAE SEAGHGGHNS SNNGCNSANS SSGNNNNHSY NSQGVEYSNG
VLKKEHLENG SSTAAHGSQQ EATFVLPTDT LKYRPPKKMH LANAVAAAAS SNTSSSNNTN
TNTNNNSSSQ AHSSSPTNVG NTNNAVSVIA TSSNYADGSM STSLDNCLSP GEASAKLSPH
LTGTGQPRRR RTRCKNCAAC QRSDCGTCPF CMDMVKFGGP GRAKQTCMMR QCLSPMLPVT
AQCVYCHLDG WRQMPVSPQT KQLASLEGPS ALMECSVCYE IAHPDCALSQ LDGTDDAADA
KGIVNEDLPN SWECPSCCRS GKNYDYKPRH FRARQKSSEV RRVSVSHGNN TSDCQEGAGG
AAGVGSILPP PVGQYNDFVF TSESEMESGS MHTTHWKHGL KRHHQLEVKT ERNNSCDTPS
PGISPNASHL LGEKVKRRKS DDGTSVSSSM HESNDAPCSS SMEVTSGAGT GVASSGHGGS
GSGSRKKNSI RSQLAQQMLN SSTRVLKKPQ YVVRPACASS STAGSGLSNG AINGLNNGAG
TSAAAGLAGA VSGGVAGGAQ HSNGANGHSH HHGSGNSHGH GHGHGHGHSH SNSSAHNLAL
DPTVLKIIFR YLPPETLVTC CLVCKAWSNA AVDPDLWKRM NCSELKISAS LLTAIVRRQP
EHLILDWTQL AKRQLAWLVA RLPALKNLSL QNCPIQAVLA LHTCLCPPLQ ILDLSFVRGL
NDAAIRDILS PPKDSRPGLS DSKTRLRDLK TLKLAGTDIS DVAVRYIMQS LPHLKHLDLS
SCQRITDAGV AQIGTSPTAI ERLAELNLSA CRLVSENSLE HLSKCESLIW LDLRHVPQVS
TQSVIRFASN SKHDLCVKDI KLVERRRLSL TNSWRD
//
