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
//