ID A0A182MSI7_9DIPT Unreviewed; 1508 AA.
AC A0A182MSI7;
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 culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA025224-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
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 culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA025224-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA025224-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; AXCM01002067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 139723.A0A182MSI7; -.
DR EnsemblMetazoa; ACUA025224-RA; ACUA025224-PA; ACUA025224.
DR VEuPathDB; VectorBase:ACUA025224; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000075883; 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 79..120
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 144..234
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 357..407
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 500..666
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1283
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1381
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1508 AA; 169980 MW; EFA53CDDF86ED8C1 CRC64;
MSGGNSPSGS VGNADAGASG LGGDCADEHL DPTAMNYHNH NAHHNNRSHL YQQQKQGSNR
PHISLDKCDD FLFNVPPEAP VFEPSEEDFK NPLVYINKIR PTAEKYGICK IRPPSSWQPP
FTVDVEKLTF TPRIQRLNEL EAETRIKLNF LDQIAKFCEL QGTTLKIPMV ERKPLDLYTL
HKIVNQEGGL EVVTKERKWS KVACRMGYQQ GKSVGSNLRI HYDRLLYPFD VYRSGKVVDL
GNIDPEPSED CEYEPHCIES RQQVQPPMTA ARRSQRFAQQ QSNSKPSSTA GSSAGGSVRG
SSDEMSPSKK ELRHRSMLEF ASKLAAAARE QAASNGSASK EEKSAVGGTH GYDPMAKYIC
HMCNRGDVEE SMLLCDGCDA SYHTFCLMPP LQDIPKGDWR CPKCIVEENS KPVEAFGFEQ
AQREYTLQQF GEMADQFKSN YFNMPVHLVP TDLVEKEFWR IVSSIDEDVT VEYGADLHTM
DHGSGFPTKA SPYLTANDQE YAESSWNLNN LPVLDESILG HINADISGMK VPWMYVGMCF
ATFCWHNEDH WSYSINYLHW GEPKTWYGVP GSRAEDFELA MKSAAPELFH SQPDLLHQLV
TIMNPNILMN ANVPVYRTDQ HAGEFVVTFP RAYHAGFNQG YNFAEAVNFA PADWMKMGRE
CVNHYSKLRR YCVFSHDELV CKMALEPDRL NLGIATACYI DMAEMVDTEK KLRKNLLEWG
VSNAEREAFE LLTDDARQCE ICKTTCFLSA VNCKCTKNLA CLRHFAELCE CPPENHTLKY
RYTLDELPLM VQKLKVKAES FEKWLFRVRD VLDPSVASSI TLEELQSIAH EAESQKFPNS
VILERLNLSI LEAQKCITVI QQLDINKIRT RTRNSLECAK YKLSMDELEL FINEINNLRC
VIREGDSVRE LQRIGQEWLR QADKALKLRF KDTNVQQLNQ LIEDGNALCI ELPQITELKD
RLTQYKWYRE VRTLRENTVD RLSLEEIKKL INEGMRILPH TVLEKELSQL HGIMLQIVDW
EQSANQCFKT ETQHKISALD SLLERTQNIE AFLPYAGQLK DMLNKSKEWL HAIETLESSK
NYNFFHTLQN LANRAKLLPV EMESKLLCET IFGTTTAGGC CYNRNGGQML LFNSHGFIGA
SGDEWRSKAA TSPSTSLKRK RNGSISNLDD PVIPARGLET VMKKIKEDSN IGEHDKRLLR
AKLLQDWNET DGGLGSSSDR HTVGRYDTAH RQQQQQHRLN GSGCDVVYHC AKCYEMVAKA
NVLRKYRHKQ HHHHCRHHER HSSSRVVAMK QEQNQQQPPA NASNVSAMEQ LLQIKTLCEE
DFGVENGTSE RTAAAEGDSS FDDFSFKFAE HDDGDDEPDD EEVADEVKAE DEDDDDEEEE
AAGVGQLGRN GCHGCKPPDE HERTTDVLKP LLASPGGRIK QEPLDSVKEE AHGRYGSKGT
GAGGGGSVLA ATTLNLESTS QALVALAANG SRSSNGSGAN GVSGTKNTSP QSDRQRQEQH
QQSNVESL
//
