ID W1Q0S2_AMBTC Unreviewed; 1219 AA.
AC W1Q0S2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=JmjC domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMTR_s00021p00232350 {ECO:0000313|EMBL:ERN14091.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN14091.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01002}.
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DR EMBL; KI392560; ERN14091.1; -; Genomic_DNA.
DR AlphaFoldDB; W1Q0S2; -.
DR EnsemblPlants; ERN14091; ERN14091; AMTR_s00021p00232350.
DR Gramene; ERN14091; ERN14091; AMTR_s00021p00232350.
DR eggNOG; KOG1356; Eukaryota.
DR HOGENOM; CLU_001811_2_0_1; -.
DR OMA; PYSDYTD; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR014977; WRC_dom.
DR InterPro; IPR018866; Znf-4CXXC_R1.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12549:SF11; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLASE 2, ISOFORM A; 1.
DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF08879; WRC; 1.
DR Pfam; PF10497; zf-4CXXC_R1; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51667; WRC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 1..44
FT /note="WRC"
FT /evidence="ECO:0000259|PROSITE:PS51667"
FT DOMAIN 220..267
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 678..1162
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 37..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1025
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1219 AA; 139204 MW; 2520F52D7EBF2534 CRC64;
MEVPQCKRSD GKGWRCSAMA FGGRTYCERH WLMQKKTRDR KLNSKIGNGE NEKKSIKRKK
SSDEKENGFH KRKKVKREKK RESEDGVSDN YSDEGSVGLI DERERECRLS KGLGSVGLVD
ERERECRLLK GLSGKKQKEV RSLYGKNPKA GTGFEKKKLD SGLSTEKKKR VSGLSSEKKK
VVRVNSGEVG CKVYGALDRD DELKREDGTC KNKEKKGLMC HQCLHSYKDG VVVCSYCEKK
RYCYTCVTKW YPEQTREEIE NACPYCRGNC NCKACLRESI AVMANRKEVD ASVKLRRLQY
LLRRVLPVLE KIYAEQDLEK EIEAKIRGVQ PADLDVERSK LNPDERIYCN NCNTSIVDFH
RSCSNPKCDY DLCLSCCREL REGRQPGGNK AETAHQQSIE RTQNRVSDDS SKDVNSKPCI
PRKRYGWESQ AAAANGHIVM PPSLPLPDWK ANEDGNIPCP PKVRGGCGAY TLTLKRNFKT
NWVVKLFNNA KELIDSNDEL SKDSGFSQRC LRCPPYWHSE IIGDDNKKCD LRLAAHRGDS
DDFLYCPSAL DVGSDGIDHF QEHWIRGEPV IVRDVNERTS GLSWEPMVMW RAVRETSRKK
LQEEKTTVKA IDCLDWCEVE INIHKFFKGY LEGRMHRGGW PEMLKLKDWP SSSRFEERLP
RHGAEFIASL PYFDYTHPNL GLLNLATKLP DGCLKPDLGP KTYIAYGSYE ELGRGDSVTK
LHCDMSDAVN VLTHTKEVKF ASWQRKRIRQ MQHRHEEEDE IELYGGADKA VDNAAEEKVD
NSDIGRGQTA NKGSLSPKCG DKVDRNFPLP EKMDLEIVPE KLDQKMSIYT KISDDHESEM
TQGCSKSEGS EENLPLSVKI DNDRQWLGGS EKLDPKMDLE TKFSDANLSA MRVEFSKCVE
SNVENLVLLR KMDIGPERLD GSEELGQNDT ESEMREGCSE WKNRIEEQSP LSEEMDIYPV
RLGHQQIEMK ASSSTRNDSE VVEPQRSHSL SPAEVHSFEV TPDKDADNAE GTSGVSEEDR
AEASKSSGEA LVNGFVHQDD VSDVVYGGAV WDIFRRQDVP KLIEYLEKHW KEFRHISNLP
VNSVIHPIHD QTLYLNEKHK KQLKEEFNIE PWTFEQHFGE AVFIPAGCPH QVRNRKSCIK
VALDFVSPDN VEECVRLTEE FRLLPKSHRA KEDKLEVKKM VLYSVSAAVR EARQLITELN
WDSGTSFTDY NVGRWNTKS
//
