ID K3XUR0_SETIT Unreviewed; 1856 AA.
AC K3XUR0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=[Histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0008006|Google:ProtNLM};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQL12365, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EnsemblPlants:KQL12365, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL12365,
RC ECO:0000313|Proteomes:UP000004995};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EnsemblPlants:KQL12365}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL12365};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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 EMBL; AGNK02002713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 4555.K3XUR0; -.
DR EnsemblPlants; KQL12365; KQL12365; SETIT_005667mg.
DR Gramene; KQL12365; KQL12365; SETIT_005667mg.
DR eggNOG; KOG1246; Eukaryota.
DR HOGENOM; CLU_000946_1_0_1; -.
DR InParanoid; K3XUR0; -.
DR OMA; MMIAKLE; -.
DR Proteomes; UP000004995; Chromosome IV.
DR ExpressionAtlas; K3XUR0; baseline.
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:0032452; F:histone 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:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd16100; ARID; 1.
DR CDD; cd15543; PHD_RSF1; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; PF00628; PHD; 2.
DR Pfam; PF08429; PLU-1; 3.
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; 3.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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:PRU00175}.
FT DOMAIN 11..52
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 78..181
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 261..311
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 402..568
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1462..1508
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1717..1764
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 183..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1833..1856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1856 AA; 209725 MW; F4EE0677C1984BBB CRC64;
MGKGSTSVPE APVFHPTEEE FADPLAYVAR IRPLAEPYGI CRIVPPSSWS PPHALDFASL
SFPTKRQPIH RLLARPAPAD PDTFLLDYRR FLRASSAHRR GRRKGLPKSP ALSDGRPVDL
CRLFHAVKRF GGYDGACEGK RWGDVVRLVD DKAPMHVSEC AKHVLAQLYY EHLYDYEKFT
NRSLSQDGNK GKQPGVESDE QPSVSGSQDE VSDTGEMAEE VSGVRSWKRR NAFSKKSDRN
SAASAGARKR KRRKPDAAAV DQVCEQCSSG LHGDVMLLCD RCDKGWHLYC LSPPLERVPP
GNWYCSDCLN SDRDCFGFVH RRKSCLLETF RRFEERVRKR WFGQRSPTRV QVEKQFWEIV
EGKAGELEVM YGSDLDTSIY GSGFPRLSDP VPSSVDQETW RKYCSSPWNL NNFPNLPGSV
LRTVRDKIAG VMVPWLYIGM LFSSFCWHVE DHCFYSINYL HWGEPKCWYG VPGAEANTFE
QVMRQALPDL FDAQPDLLFH LVTMLNPSIL RANGVPVYSV MQEPGNFVIT FPRSFHGGFN
LGLNCAEAVN FAPADWLPHG GIGADLYRLY RKAPVLSHEE LLYVVAKNGV DAESLPHLKG
EIERLFINER RRREELWING IIKSSPMLPR SNPNFIGSEE DPTCIICRQY LYLSAVSCNC
RLSSYVCLEH WKHLCECSPE KHCLLYRHTL AELGDLVCDV SLASLPGDDV KQNPHLLNDV
CVPSKKVKDR YISYAQLAED WVSKSEHILQ MPFLDKSYAT ALEEAEQFLW GDHDMDSVRN
MTLRLTEAKN WALGVRKCLS KIEDFLKDSC SEKVNYVEID ELVAMRCIPC CEPSLTTLQA
YAEKGKMLID EVNSALSSRL TVDKLETLYS RVSEFPVKLT QSLTLFREIS SAKSWLKKAN
DCLEQNKLGT IDIDVLNKLK LEIIQLRVLL PEIDIISKLW KDAESWQMRC QLYLQDFPGL
EELEGFLLSA DGASFSIPEL NRLKQHYLDG CSWVNHAKNI LGKLHTRSDY HNVAEELTGI
LKDAEFLGVK VDELPIVEKE LKRSLCRKQA SEALATVMSM DVVEDVLKEA SILTIEEEQP
FVDLSRMLKE ATAWEEKARL ILEQSASLSE YEDHMRRSDD IRIILPSEPR MKAEIDIAKL
WIDKCQAYLR PKCNKLALGG FLQVEDIKDL INQAGNLKVI LDTSALNSVL NIVEKWEGNS
LSLLSNLRTL LHLNHIGSTV DPLKRNLEEL QDKLNTEIES GSSLGFEFRV LDELKDSLLV
LRWILDSLSL CCMIPLLQLI LIFQDVDRLI EAVVHLPASL SDCSLVTLLM RGLSCLRKAL
ILLPDRETSV KSQLKDVENI LAEFKEIDVP YLIITSKLED AVNKHTSWTE QCNTYFMLPD
GQSWAGLLNL RDNGQSVAFD CPEMDKVIVE VKKVEEWLNQ CHRTLFLDGN NSSLLSALVK
IRQSLDGVCS LLAEDCVKKG LCAICLCDMG DSLASRCVTC QEWYHDSCVE NLSVSTQMTS
ECICPFCSLL QSEDLLENQI HVKMSKGNCP ALTALNELLS SATGFCTGIE EINLLEEIVQ
KARNLNAYLM QILDDSGSYH GEDLTVICKS LLVALKATSA SGLYDHHVSC KIESVLSRYL
WKKQIHKLLC SGKKALIEEV LHLDKEGSHL EIFGQDFFKL EISKIKETSL QWLAKAEKVA
CDSGELALDL VYGLIVEGEN LSVHFEKELK LLRDRSVLYC ICRKPYDNRA MIACDECDEW
YHFDCINLIG PPPETFFCPA CRPNNGEESI SLPRSDHDED RSSTGGGAPP HTPPASCDAP
GRAVDANKCE KRGKSQIRVD LIKILRCHGE TDGSWREGKR VPHRTARRRS SFVGLL
//
