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Database: UniProt
Entry: Q7PPV0_ANOGA
LinkDB: Q7PPV0_ANOGA
Original site: Q7PPV0_ANOGA 
ID   Q7PPV0_ANOGA            Unreviewed;      1494 AA.
AC   Q7PPV0;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 4.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE            EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN   Name=1275113 {ECO:0000313|EnsemblMetazoa:AGAP004854-PA};
GN   ORFNames=AgaP_AGAP004854 {ECO:0000313|EMBL:EAA09709.5};
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA09709.5};
RN   [1] {ECO:0000313|EMBL:EAA09709.5, ECO:0000313|Proteomes:UP000007062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA09709.5,
RC   ECO:0000313|Proteomes:UP000007062};
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
RN   [2] {ECO:0000313|EMBL:EAA09709.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA09709.5};
RG   The Anopheles Genome Sequencing Consortium;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAA09709.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA09709.5};
RX   PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA   Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT   "The Anopheles gambiae genome: an update.";
RL   Trends Parasitol. 20:49-52(2004).
RN   [4] {ECO:0000313|EMBL:EAA09709.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA09709.5};
RX   PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA   Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA   Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT   "Update of the Anopheles gambiae PEST genome assembly.";
RL   Genome Biol. 8:R5.1-R5.13(2007).
RN   [5] {ECO:0000313|EMBL:EAA09709.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA09709.5};
RG   VectorBase;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EnsemblMetazoa:AGAP004854-PA}
RP   IDENTIFICATION.
RC   STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP004854-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; AAAB01008905; EAA09709.5; -; Genomic_DNA.
DR   RefSeq; XP_314337.4; XM_314337.4.
DR   STRING; 7165.Q7PPV0; -.
DR   PaxDb; 7165-AGAP004854-PA; -.
DR   EnsemblMetazoa; AGAP004854-RA; AGAP004854-PA; AGAP004854.
DR   GeneID; 1275113; -.
DR   KEGG; aga:AgaP_AGAP004854; -.
DR   VEuPathDB; VectorBase:AGAP004854; -.
DR   eggNOG; KOG1246; Eukaryota.
DR   HOGENOM; CLU_000991_9_0_1; -.
DR   InParanoid; Q7PPV0; -.
DR   OMA; SAVNCKC; -.
DR   OrthoDB; 48111at2759; -.
DR   Proteomes; UP000007062; Chromosome 2L.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
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   Reference proteome {ECO:0000313|Proteomes:UP000007062};
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          76..117
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          141..231
FT                   /note="ARID"
FT                   /evidence="ECO:0000259|PROSITE:PS51011"
FT   DOMAIN          354..404
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          496..662
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1144..1168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1261..1295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1313..1391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1417..1494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1261..1275
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1341..1367
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1439..1477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1494 AA;  169444 MW;  42F4DEE810D6B130 CRC64;
     MNGGSSRHPQ SSSSLSAENI PCRTISATDI RVASVDADCL DQQQPQQPMN HHNNPHRPHI
     SLDKCDDFQF NVPPEAPVFE PSEEDFKNPL VYINKIRPTA EKFGICKIRP PSSWQPPFTV
     DVEKLTFTPR IQRLNELEAE TRIKLNFLDQ IAKFCELQGT TLKIPMVERK PLDLYTLHKI
     VNQEGGLEVV TKERKWSKVA CRMGYQQGKS VGSNLRTHYD RLLYPFDVYR SGKVVDLANI
     DPEPSEDCEY EPHCIESRQQ VQPPMTAARR SQRFAQQQNN SKPSSTTGSS AGGSVRGSSD
     EMSPSKKELR HRSMLEFASK LAAAARDQAA TNGGASKEEK VGVGGTHGYD PMAKYICHMC
     NRGDVEESML LCDGCDASYH TFCLMPPLQD IPKGDWRCPK CIVEEHSKPV EAFGFEQAQR
     EYTLQQFGEM ADQFKSNYFN MPVHLVPTEL VEREFWRIVS SIDEDVTVEY GADLHTMDHG
     SGFPTKSSSL SSTDQEYAES SWNLNNLPVL DESILGHINA DISGMKVPWM YVGMCFATFC
     WHNEDHWSYS INYLHWGEPK TWYGVPGSRA EDFELAMKSA APELFHSQPD LLHQLVTIMN
     PNILMNANVP VYRTDQHAGE FVVTFPRAYH AGFNQGYNFA EAVNFAPADW MKMGRECVNH
     YSKLRRYCVF SHDELVCKMA LEPDRLNLGI ATACYIDMAE MVDTEKKLRK NLLEWGVSNA
     EREAFELLTD DARQCEICKT TCFLSAVNCK CTKNLACLRH FAELCECPPE NHTLKYRYTL
     DELPLMVQKL KVKAESFEKW LFRVRDVLDP SVASSITLEE LQSIAHEAES QKFPNSVILE
     RLNLSILEAQ KCITVIQQLD INKIRTRTRN SLECAKYKLS MDELELFINE INNLRCVIRE
     GDSVRELQRI GQEWLRQADK ALKLRFKDTN VQQLNQLIEE GNALCIELPQ IVELRDRLTQ
     YKWYREVRTL RENTVDRLSL EEIKKLINEG MRILPHTVLE KELSQLHGIM LQIVDWEQSA
     NQCFKTETQH KISEIDSLLE RAQNIEEFLP LAGQLKDALH KSKEWLHAIE TLESSKNYNF
     FHTLQNLANR AKLLPVEVES KLLCETIFGT TTAGGGCYNR NGGQMLLFNS MGFIGASGDE
     WRNKSSLPAS SQKRKRNGSI SNLDDPVIPG SGMETIMKKI KEDSSIAEQD KRLLRAKLLL
     DWNESDGGMG TSSDKNMLGR YDNMKQQQEN RLNCSSGCDV VYHCAKCYEM VAKANVLRKY
     RHKQHHHHCR HHERHSKVKQ EQNHQQHSNS NSLSSMEQLL QMKTLSEDDF LPEKEGASER
     TTAEGGSSFD DFSFKFGEHD EAEDELDDEE AADEVKAEDE DEDEEEAACL GPPGRNGCHG
     CKPPDEKERQ PSALLPACTS ARIKEEPLDD VEHLDEKERE MRHSSKVPGG EGAVTGATKT
     ICPESTSQPL AVVSANGKSH ANGANGVSTS TNASYPPHDR QRQEHNPQSN LTSL
//
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