ID W9SA50_9ROSA Unreviewed; 1623 AA.
AC W9SA50;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative lysine-specific demethylase ELF6 {ECO:0000313|EMBL:EXC32933.1};
GN ORFNames=L484_013048 {ECO:0000313|EMBL:EXC32933.1};
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:EXC32933.1, 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 ---------------------------------------------------------------------------
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; KE346316; EXC32933.1; -; Genomic_DNA.
DR RefSeq; XP_010112224.1; XM_010113922.1.
DR STRING; 981085.W9SA50; -.
DR eggNOG; KOG1246; Eukaryota.
DR eggNOG; KOG1721; Eukaryota.
DR Proteomes; UP000030645; Unassembled WGS sequence.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProt.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF45; LYSINE-SPECIFIC DEMETHYLASE ELF6-RELATED; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Methyltransferase {ECO:0000313|EMBL:EXC32933.1};
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:EXC32933.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 16..57
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 297..483
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1534..1563
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1564..1593
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1594..1623
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 79..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1623 AA; 181301 MW; 2C74A480B19000AE CRC64;
MGNVEIPNWL EGLPLAPEFR PTDTEFADPI AYISKIEKEA SAFGICKIIP PLPKPSKKYV
FSNLNKSLSK CPELGSVENL SNDCPSSSKT GSLDGSNDGE VRAVFTTRHQ ELGQSVRKTK
GGVQNPPLGV QKQVWQSGEI YTLEQFESKS KAFAKSQLGM IKEVSPLVVE AIFWKAACEK
PIYLEYANDV PGSGFGEPEG QFRYFHRRRR KRNFYRRSRD NSSCKRDEMV SDRIAVSKTN
DVKDSAPKND SDSFVDVSKP PTSLPVLPCN ETPQSSKKKS QNSCHDKEGT AGWKLSNSPW
NLQVISRSPG SLTRFMPDDI PGVTSPMVYI GMLFSWFAWH VEDHELHSMN FLHSGSSKTW
YSVPGDYAFT FEEVVRSEAY GGNIDRLVVC YYFGIIFVTQ VQFLLLPAAL ALLGEKTTLM
SPEVVVASGI PCCRLVQNPG EFVVTFPRAY HVGFSHGFNC GEAANFGTPQ WLKVAKEAAV
RRAAMNYLPM LSHQQLLYLL TMSFVSRVPR SLLPGVRSSR LRDRQKEERE LLVKQAFIED
ILHENKTLSV LLGKDSSYHA ILWNPDLLTY PSKESLSPIA GATDSTPATE NPQKHNGEQH
YLVNEMSLYM ENMNDLYFDC DDLSCDFQVD SGTLACVACG ILGFPFMSVV QPSQKASEEL
LHNEHALVQE CQGISGYLNS CSFQDLDASN KCYVAENPPT VSNSSLMVDL PLPSTIMSKN
GWNANNKSLR PRSFCLEHAV EIVELLQSKG GANVIVICHS DYQKIKAHAT TIAEEIGSPF
NYSEVPLDIA SKDDLNLIDL AIDNEEHDEC GEDWTSKLGI NLRHCVKIRK NSPSKQVQHA
LTLGGLFSDK CPSVDFLTIK WQLRRSRSKK ICLPDHFKPC DTIQLKNDVA MGERSLSVKK
EKKLIQYSRR NFKKKPGGST GTPKVCVTGA SLGDLDEHNR IVSENNIQND GNSTGFDVSP
SYENEIQMLE ATEDENSKDG VACVETQIKN HVLEDTNTGH FAALDDSEME DEPNVETQKV
SSTDELREEQ YASPFVNDTQ KSFQAHEEKQ IVGQFNRVNE VCSLVSERHS EVQVDKDVLD
NTVSKFSKMS CSHVDPCDEN FEGQRANATV DKGCKCDEVC DSLPVEAQGV HATGNKDKKE
FPCNSTAIKD QEQCCEGPRQ SCSAGDSSNH ISLEVKPPQE IRTVINEHSL VSIEEIYEVP
KETCSTEGLG NYACLEVKPE QEIKTTITEV VSASIEKISE IPSDVSAALK LCYSLTSDEE
LQQKLESAAG SSEELASSSV TQTEAHHPCV SAEEYSNVPR GISREEDSGN DVTSDNGSRR
ETLMENPDQG LVSNLAIQAR NQPIPVNVEE FEVTNHAKDH LGDNLTFNNN REREIQSMND
EEKTDLPTAI PFQKYYRVKR DSRSTEDLCI GSEVCSPQDD RELEIIDSNM GKARKRKREL
EQLTESKFSC NGFIRSPCEG LRPRTGKDAA TSSSGIDIDG EVKEKPATKV KKSTNARGPT
KDKKENSRKS HKCDIDGCRM SFDTKAELNV HKRNRCPHEG CGKRFSSHKY AMIHHRVHDD
QRPLKCPWKG CSMSFKWAWA RTEHIRVHTG ERPYQCKIEG CGLSFRFVSD FSRHRRKTGH
YVN
//
