ID A0A182QGU4_9DIPT Unreviewed; 1497 AA.
AC A0A182QGU4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
OS Anopheles farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF009884-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF009884-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF009884-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR EMBL; AXCN02001921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 69004.A0A182QGU4; -.
DR EnsemblMetazoa; AFAF009884-RA; AFAF009884-PA; AFAF009884.
DR VEuPathDB; VectorBase:AFAF009884; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000075886; 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 CDD; cd16864; ARID_JARID; 1.
DR CDD; cd15605; PHD1_Lid_like; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
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 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; 1.
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; 1.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
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; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 43..84
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 108..198
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 331..381
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 474..640
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 224..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1358
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1497 AA; 169139 MW; 2D880DD149A1AB73 CRC64;
LNNHHSHQNN RNHLYQQQKL GSNRPHISLD KCDDFQFNVP PEAPVFKPSE EDFKNPLVYI
NKIRPMAEKY GICKILPPSS WQPPFTVDVE KLTFTPRIQR LNELEAETRI KLNFLDQIAK
FCELQGTTLK IPMVERKPLD LYTLHKIVNQ EGGLEVVTKE RKWSKIACRM GYQQGKSVGS
NLRAHYDRLL YPFDLYRSGK VVDWANIDPE PSEDCEYEPH CIESRQQVQP PMAVTARRSQ
RFAQQQNNNS KPSSAAGSSA GGSVRGSSDE MSPGKKELRH RNMLEFASKI ATAARDQAAA
AAASTNGAGS KDEKSAGAGA GGTHGYDPMA KYICHMCNRG DVEESMLLCD GCDASYHTFC
LMPPLQDIPK GDWRCPKCIV EENSKPVDAF GFEQAQREYT LQQFGEMADQ FKSNYFNMPV
HLVPTKLVEK EFWRIVSSID EDVTVEYGAD LHTMDHGSGF PTKASPYLTT SDQEYAESCW
NLNNLPVLDE SILGHINADI SGMKVPWMYV GMCFATFCWH NEDHWSYSIN YLHWGEPKTW
YGVPGSRAED FELAMKSAAP ELFHSQPDLL HQLVTIMNPN ILMNANVPVF RTDQHAGEFV
VTFPRAYHAG FNQGYNFAEA VNFAPADWMK MGRECVNHYS KLRRYCVFSH DELVCKMALE
PDRLNLGIAT ACYIDMAEMV DTEKKLRKNL LEWGVSNAER EAFELLTDDA RQCEICKTTC
FLSAVNCKCT KNLACLRHFA ELCECPPENH TLKYRYTLDE LPLMVQKLKV KAESFEKWLF
RVRDVLDPSV ASSITLEELQ SIAHEAESQK FPNSVILERL NLSILEAQKC ITVIQQLDIN
KIRTRTRNSL ECAKYKLTMD ELELFINEIN NLRCVIREGD SVRELQRIGQ DWLRQADKAL
NLRFKDTNVQ QLNQLIEEGN ALCIELPQIA ELKERLTQYK WYREVRTLRE YTVDRMSLED
IKKLINEGMR ILPHTVLEKE LSQLHGIMLQ IVDWEQSANQ CFKTETQHKI SEIDNLLERA
QNIEAFLPLA GQLKDALHKS KEWLHAIETL ESSKNYNFFH TLQNLANRAK LLPVEMESKL
LCETIFGTTT TNTTTTTTGG GCYNRTGGQT LLFNSVGFIG ASGDDWRGKA ASSPSTSLKR
KRNGSITSLD DPVLPASGIE TIMKKIKEDS GIGEQDKRLL RAKLLLDWNE SEQGSDKHML
GRYDSIQEQQ QQQQQQPQQE QRNRSNNSCD VVYHCAKCYE MVAKANVLRK YRHKQHHHHC
RHHEKHSRVV AKEEPTHAQP VTGNSGSLSS LEQLLQIKTL TEEDFRVESS AIEGGSSFDD
FSLKFGDHYD AEDEPEDEEA ADEPMKAEED EEDEEAEATT GSVGQLGRKG CHGCKPPEPV
HERAKLSAGM PNCAGGRIKL EPMDNDDDDG DGRLTMEGEK AEARSRSSAK SVVGGVGATV
TSVCTTESTS QLSEVPSGNV GSRHSNGGGT GTSTNATATL HEHQHQQTTN QKHTESL
//
