ID E3M8V1_CAERE Unreviewed; 746 AA.
AC E3M8V1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Lysine-specific histone demethylase {ECO:0000256|PIRNR:PIRNR038051};
DE EC=1.14.99.66 {ECO:0000256|PIRNR:PIRNR038051};
GN Name=Cre-spr-5 {ECO:0000313|EMBL:EFO95716.1};
GN ORFNames=CRE_13937 {ECO:0000313|EMBL:EFO95716.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of
CC histone H3, a specific tag for epigenetic transcriptional activation,
CC thereby acting as a corepressor. Acts by oxidizing the substrate by FAD
CC to generate the corresponding imine that is subsequently hydrolyzed.
CC Demethylates both mono- and di-methylated 'Lys-4' of histone H3.
CC {ECO:0000256|PIRNR:PIRNR038051}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2
CC AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3]; Xref=Rhea:RHEA:60244,
CC Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:61976; EC=1.14.99.66;
CC Evidence={ECO:0000256|PIRNR:PIRNR038051};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR038051,
CC ECO:0000256|PIRSR:PIRSR038051-1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR038051}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|PIRNR:PIRNR038051}.
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DR EMBL; DS268429; EFO95716.1; -; Genomic_DNA.
DR RefSeq; XP_003107396.1; XM_003107348.1.
DR AlphaFoldDB; E3M8V1; -.
DR STRING; 31234.E3M8V1; -.
DR EnsemblMetazoa; CRE13937.1; CRE13937.1; WBGene00061218.
DR GeneID; 9806028; -.
DR KEGG; crq:GCK72_003543; -.
DR CTD; 9806028; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_5_1_1; -.
DR InParanoid; E3M8V1; -.
DR OMA; SSRGEMF; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IEA:EnsemblMetazoa.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:EnsemblMetazoa.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR017366; Hist_Lys-spec_deMease.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF351; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1-RELATED; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 1.
DR PIRSF; PIRSF038051; Histone_Lys-demethylase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR038051};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW FAD {ECO:0000256|PIRNR:PIRNR038051, ECO:0000256|PIRSR:PIRSR038051-1};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR038051};
KW Nucleus {ECO:0000256|PIRNR:PIRNR038051};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR038051};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Repressor {ECO:0000256|PIRNR:PIRNR038051};
KW Transcription {ECO:0000256|PIRNR:PIRNR038051};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR038051}.
FT DOMAIN 29..127
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT REGION 722..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 291..325
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 167
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 173
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 656
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
SQ SEQUENCE 746 AA; 83390 MW; 44701383F64458E8 CRC64;
MSSEATSSDY VDDELRGEDF GPSIDDNALA AAARQARLPF DRPTEHELAF FPELWEHKTA
VEVFLLIRNS TLATWQYNPQ KECTASDVRN NIFPPFNSDL DLIQNVVHFL TRHGLINFGR
YVRSTRITRF LVRDRRKVII IGAGTAGISA AIQLISTGFD VTILEGRGRI GGRVHSFKTK
SGQVMETGGD TLRKLEDSPM TTLLHQVSLE EHGVYDYTTI YVDGKPLNDD KIHIFLTHYE
SAKGALNWEA HQREHRDENG LFVSRQRAYE NLMNLSERST LIKYFNHCKS LEEVARAREK
HYNQMKNLRN TALMAENRLK KLEEQGLLDN DPIMRRSLKR DVATSIQKFD EVSNAFEAAD
NHWKLLNEHP QAKQFMHPGS DFNTYNFMLG FEEYLIGAQL EKVQFSCDSA VNKEHGVAAR
LTEGVAELLL RITQRRNLDI HLNHKVVDID YSGVDDVKVR VQKKDGEIEE LTAAIVISTL
PIGVLKKSIA GDARAPTFTP PLPAEKAKSI RNMGSGLINK CILEFDKAFW ATGSRANNQS
TQFVTVSPNI RTRGSLSIWS STPGSKVLTT YMVGDSCKDS PDDVIIQRAL QTLHKVFGNN
CPRTPLSAHI TRWHEDEFAF GSGSFMSLRT EKSDFDELMK PLKTSDGKNR VYFAGEHTSS
SYAATIQGAW MSGARAAADI ANDYVGFGFV DMSGTKNVKG EDEEGGDMHI DHDGPLPEGM
LADGQQANGG VVNGEIPEAK KAKIDN
//
