ID A0A2U9C0R1_SCOMX Unreviewed; 474 AA.
AC A0A2U9C0R1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative methyl-CpG-binding domain protein 4-like {ECO:0000313|EMBL:AWP09938.1, ECO:0000313|EMBL:AWP09940.1};
GN ORFNames=SMAX5B_014450 {ECO:0000313|EMBL:AWP09938.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP09938.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP09938.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP026253; AWP09938.1; -; Genomic_DNA.
DR EMBL; CP026253; AWP09940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9C0R1; -.
DR STRING; 52904.ENSSMAP00000022861; -.
DR Proteomes; UP000246464; Chromosome 11.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008263; F:pyrimidine-specific mismatch base pair DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd01396; MeCP2_MBD; 1.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR017352; MBD4.
DR InterPro; IPR045138; MeCP2/MBD4.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR PANTHER; PTHR15074:SF7; METHYL-CPG-BINDING DOMAIN PROTEIN 4; 1.
DR PANTHER; PTHR15074; METHYL-CPG-BINDING PROTEIN; 1.
DR Pfam; PF01429; MBD; 1.
DR PIRSF; PIRSF038005; Methyl_CpG_bd_MBD4; 2.
DR SMART; SM00391; MBD; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR PROSITE; PS50982; MBD; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 23..95
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT REGION 108..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 53636 MW; 464CC96683F6BC73 CRC64;
MYPAGCGIQL EASRDVHNPS HNDGDDSCHI SKMPPGWIRE VRQRRAGKTA GKLDVYITSP
QGQKFRSRAS LDAFLQKNGD GNLDMNLFEF TASKDNVITI PQILPTQRKL GRRKKQKETT
QDATDILDPP PNKSKRSNEE ENVKSSNDTN YTNTNILPEV CRDKTDETVE VCVQAVPSAV
VDVLQRSPQR AIGLREKLLR LASPSKQKNT SCAQEDERAD SEPSVPTLNV EPPTESEEEE
EGEDGRGGGG GEIQIHSEGV DKPNSELETD ADGHQDVEEE VLSPDITVSC TPVRDSQNNS
KSSTDKRKTS PYFSGKLLKD GLSPPRRKAF KKWTPPRSPF NLVQETLFHH PWKLLVATIF
LNKTTGKMAI PVLWQFFERY PSAEVTREAD WKSMSELMKP LGLYELRAKT LVRFSDEYLT
KQWRYPIELH GIGKYGNDSF RIFCVGEWKQ VTPEDHMLNK YHAWLWENHE ALGM
//
