ID A0A182PC23_9DIPT Unreviewed; 1348 AA.
AC A0A182PC23;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI004479-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., 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 epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI004479-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI004479-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR STRING; 199890.A0A182PC23; -.
DR EnsemblMetazoa; AEPI004479-RA; AEPI004479-PA; AEPI004479.
DR VEuPathDB; VectorBase:AEPI004479; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000075885; 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; PF02373; JmjC; 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 SUPFAM; SSF57802; Rubredoxin-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 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 135..303
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 647..693
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 1059..1105
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 433..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1348 AA; 149036 MW; A9CEC6FD17BA6740 CRC64;
RERKQRKLYS DDWTLGDDDY EGARGFSVAE KLESPRFAQS GMVREMKGEN LTVGFLQHNG
FNIPLLFKEK TGLGLQVPTA NFSISDVRMC VGSRRMLDVM DVNTQKNIEM TMKEWEKYYE
DPMKKKLLNV ISLEFSHTKL ENYVQSPAIV RQIDWVDVVW PKQLKESQVE STNLLNDMMY
PKVQKYCLMS VKNCYTDFHV DFGGTSVWYH ILRGSKVFWL IPPTDKNLQL YEKWVLSGKQ
SDVFFGDTVE KCARVYLTAG NTFFIPTGWI HAVYTPTDSL VFGGNFLHSF GIVKQLKITQ
VEDNTKVPQK FRYPFFTEML WYVLAKYVYT LLGHSHLEGE PGREHELVGK PHVHLTHYEL
FGLKDIVMYL YDLPAQKKNV PELIKDPVAL IKDVRTLVER HCKDIPELAV TGVPVLHPDL
NVSNNSYIRE HYEYYSGDGG GNRTTDNEGP RENRERRDED EEDEDEEEAE DRRRILHEGD
ESHKNGDNRM VDGGEGGRTD QQSQHAQQQH RPVIVEQQQQ QQGQQEQQQE QNHSQSRHNH
MGTRVCETGG IGGSDASALT SSRSPIGSSN GGTTMGPPAR YNNHHHHGNG DDRNFVSPQP
TAANRLPSTG GGSGRGPYKK HGSTGNSGHG SEKRDGGGGG GGGGNGPRRR RTRCKNCEAC
QRSDCGECSF CLDMVKFGGP GRAKQTCMMR QCLQPMLPVT AQCIHCNLDG WRQAPITAPA
QAKLQAQMQE GPSALMECSV CYEISHPDCA QRAAPEAQGI VNDDLPNSWE CPTCCKSGKN
TDYRPRHFRA RLKSSEIRRM SCSSDASSAH NAEYGRIGGG GHAGAGSGGE GSINSTGEGM
LPGANVSAPR APRFQDDMLY DFAVSGSAVI VGSKGGNILF ERKPKIKDED ISSGSEYDSS
GVVGKKMHHS LSSSGGGGGA VKVEVKDEPL DHHHAQSNHG YSSNHHHTTS VIKDGREMQR
EQLAASCTGS GDGVPVKRRK SDEGGAINTN HHSGGGVGAG CADGNDSKNN HHGSTLPRKK
STQRMQLAHQ IHSSSTKPMK KPLYPIRPAS VAHAPTMSLS GNYALDTTCL LHVFRYLPPE
TLVTCTMVCK TWSTIAVDPS LWKRMNCAEY KLSPNLLSAI VRRQPEHLIM DWIGLGKRQV
TWLISRIPGL KNLSLQGTHI QAVLGLHTCM CPPLQVLDLS FIAGLNDFAI REILSPPKDS
RPGLADSKSR LRNLKMLKVA GADISDVALR YITQGLPNLT HLDLSSCQRI TDAAIAQIGT
SPAAIKTLVE LDLSCCKLIT ELSLDHLAKC DALTRLDLSH VPQVSTQSMI KFASISKNDL
QLHDIKLVDK RKTPSQQQQQ SQQSPDAQ
//
