ID W9RE34_9ROSA Unreviewed; 1187 AA.
AC W9RE34;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Lysine-specific demethylase 3A {ECO:0000313|EMBL:EXB85447.1};
GN ORFNames=L484_023680 {ECO:0000313|EMBL:EXB85447.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB85447.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KE344903; EXB85447.1; -; Genomic_DNA.
DR RefSeq; XP_010100868.1; XM_010102566.1.
DR AlphaFoldDB; W9RE34; -.
DR STRING; 981085.W9RE34; -.
DR eggNOG; KOG1356; Eukaryota.
DR Proteomes; UP000030645; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_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; PF10497; zf-4CXXC_R1; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Methyltransferase {ECO:0000313|EMBL:EXB85447.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:EXB85447.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 436..483
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 885..1120
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1187 AA; 134808 MW; 0FAB70BBF1FFBCAC CRC64;
MAANSEPPPN DGEDKKAPVS VGKVPESIEN IPENRFSLED TEGEANQKRR RGRKKVEKKD
KEARDSAMEI VGGEGVVGKK KRGRKPKNSK PLAQKGPGSK KAKLVVEGDK ENGEEVKESE
EFRVSEMEGV VEENVVGDGV EKKKRGRKKK VAKGSEVLVE DVSEKAKEVV ENGRDKESSE
HSAKNEGENV NVVVEDVLEN GENVKNAQEL GDFEMANAVE DGGNGVQKKK RGRKGRKKEV
LGESSEISVE KEKAKVLKES SEISVEEDGE KAKLVLEGDQ ENELVKREEG ERGLSGLVEE
SRDFLLKNRL RSRNTKVVYR EDVLFGFDDG NENDKRVSGR KRGRKCRTKT KDTEDKKIAI
EEDQEKDVGC VLTTKRGRKG RGKAKSKGNL DNDQKGVELS DDYKGYSLRR VNLLVQEKPK
LNQSDPKFAG GVSLMCHQCQ RNDKGRVVRC KSCKRKRFCV PCIEKWYPNT PKKDIAETCP
VCRGNCNCKA CLRLDAPITK IENLELNISK DEEIEHSRYL LQGLLPFLKK LNEEQEIESE
MEAKRQGVSL SELKIQKSHC FKDERIYCNN CKTGIVDFHR SCPLCSYDLC LSCCREIRDG
HLQGGGEDVI MPFINQGFQY LHGGESKEKA PSKNKRRKKV DQEEARSTSS CNVSVIPISE
WKANEDGSIP CPPKDLQGCS GVLLELRSLF PENFVSELVK KAEELADVYK LIDTSETSIR
QCSCLNATDA SELSSNALRK AANREDSDDN YLYCPKASKI QHEDLKHFQW HWMRGEPVIV
DNVLETTSGL SWEPFVMWRA CRQLRHVKHD RHLEVKAIDC LDLCEVDINI HQFFTGYLEG
RFDLKLWPQI LKLKDWPPSN LFGERLPRHN AEFISCLPFK EYTNPLNGIL NLFVKLPKES
LKPDMGPKTY IAYGVNVLTH TAEVKFTPEQ LATIEDLKKK HSEQDQREIF GGRVASDCEW
KDKEFSQLNS RKSQEEKLGK DEGCGNIDQS LNSGNTLEGL EEAEGGALWD IFRREDVPKL
QEYLKKHFRE FRHIYCCQVQ QVIHPVHDQT MYLTMDHKRK LKEEYGIEPW SFIQKLGDAV
FIPAGCPHQV RNLKSCIKVA LDFVSPENVD ECVRLTEEFR TLPSSHRAKE DKLEVKKMAL
YAMKEVVETL DPKERSKRKR NQGKGNEGMG KKGKGKKGKG KFKKTEP
//