ID A0A182K3D7_9DIPT Unreviewed; 1277 AA.
AC A0A182K3D7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=JmjC domain-containing protein {ECO:0000259|PROSITE:PS51184};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR005272-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA 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 christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR005272-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR005272-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 UTX family. {ECO:0000256|ARBA:ARBA00034483}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A182K3D7; -.
DR STRING; 43041.A0A182K3D7; -.
DR EnsemblMetazoa; ACHR005272-RA; ACHR005272-PA; ACHR005272.
DR VEuPathDB; VectorBase:ACHR005272; -.
DR OrthoDB; 20251at2759; -.
DR Proteomes; UP000075881; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032452; F:histone demethylase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1370; -; 1.
DR Gene3D; 2.10.110.20; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR046941; KDM6_GATAL_sf.
DR InterPro; IPR048562; KDM6A_B-like_C-hel.
DR InterPro; IPR048560; KDM6A_B-like_GATAL.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14017:SF1; LD02225P; 1.
DR PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21322; KDM6_C-hel; 1.
DR Pfam; PF21326; KDM6_GATAL; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 908..1071
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 210..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1277 AA; 138242 MW; E3168C7D99455C11 CRC64;
RFHIAHLYEV QNKYKTAKEA YERLLANKQL TSSLKADIYR QLGWMYHTVD LLGDKVQRER
LAIHCLQRSI EAEPRSGQTL YLLGRCFAGI NKVHDAFIAY RNSVEKREGE RRHMVLHWVS
YKSAEWRRPA VLNGFIVLYQ QQNQPMDALQ AYICAVQLDK SHSAAWTNLG ILYESCNQPR
DAYACFRNAT INQDQQKDRT VSACEKSTVP ATAAATTTGS TGKANQSASG GTAGTTTTTT
SGTSVAPGSS ATGTSETSST ANSSTGGGPN SLLSTVLCDL SNSNNGGNNS NSRSQSLTQR
IKFLQQHLGN APMPSITSKR RQLPSIEEAW NLPISNEMSS RQQQTAQAQQ RQFQKGYGQG
TQYHPGQQQP VGSNNGLPNK RFKQEDGRPG SGAPGGVVGT VAGQPVPPFY LNQQQLLQLQ
FLQNQNNLTA QQQAMLQTLT NQYRLMQQHQ LRLQQQQQQR SQQLQQQQQH PSLQGQPQGG
GGNGGFGLAA GNKTPQSGIV PQTGFVNDGH FSPATGQSQQ TAGMPYKSAG TYAPSGFTVP
SSQPAGGFTQ ITSTSNHQAD IAIQSILDDK ATFAESLLKQ LSSPTGESKD ATENATSTAT
NNSSTKSPPI KAEATSTTTP AVGGAKRQLL SSKQQDNIKL EPVVKLEKLP SSTSALDGSS
GTVGGDFKIS MCSKDIQQLV RKQRNAGELK DVPAVCSVLS ADAPPPCPPD CPPTRLTREQ
LQPPTPSVFL ENKKDAFSPQ LQEFCLKHPI AVVRQLGAAL KLDLGLFSTK TLVEANPDHT
VEVRTQVHQS PDENWDGNKN SKVWACISHR SHTTIAKYAQ YQASSFSDKI KEERDKLAGI
STASTNSDSD SKDSISNSSS ACGTGATSGA GGAGGNSSAT GNGKRKKCKN GNKMLRFGTN
VDLSDERKWK TQLQELQKLP PFARVVSAAN MLSHVGHMIL GMNTVQLYMK VPGSRTPGHQ
ENNNFCSINI NIGPGDCEWF ATPDSYWGGI QALCEKNNIN YLHGSWWPAL EDLYAENIPV
YRFTQRPGDL VWVNAGCVHW VQAIGWCNNI AWNVGPLTGR QYQLAVERYE WNKLESYKSI
VPMVHLSWNL ARNIKVSDPK LFESIKTCLM QTMKHCMQVL EYVKSLHIEV RFHGRGKNEA
SHYCGQCEVE VFNVLFIREQ EKRHIVHCMG CARKQSPGLQ GFVCLEEYTL DELMQVYDSF
VLHTPPPPLP AIAAATASVP AQSPQPASSP SAAAGGGGGS LANVSSSTAT SCSSSSASVS
GGGGTSGASV PVSSVAS
//
