ID A0A1R3JLK3_COCAP Unreviewed; 1516 AA.
AC A0A1R3JLK3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Methyl-CpG DNA binding protein {ECO:0000313|EMBL:OMO95714.1};
GN ORFNames=CCACVL1_05292 {ECO:0000313|EMBL:OMO95714.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO95714.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO95714.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO95714.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO95714.1}.
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DR EMBL; AWWV01007600; OMO95714.1; -; Genomic_DNA.
DR EnsemblPlants; OMO95714; OMO95714; CCACVL1_05292.
DR Gramene; OMO95714; OMO95714; CCACVL1_05292.
DR OrthoDB; 473248at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd02999; PDI_a_ERp44_like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR037472; MBD8.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR37701:SF20; -; 1.
DR PANTHER; PTHR37701; METHYL-CPG-BINDING DOMAIN-CONTAINING PROTEIN 8; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SMART; SM00384; AT_hook; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT TRANSMEM 1415..1439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 304..376
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 416..444
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 463..490
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1246..1367
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 87..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1516 AA; 168149 MW; 5A5CF6CCD42677EF CRC64;
MASATVDHRL QHRDSSLHLE SIPLVDLRLL SQPELLSLSF CSTSPSPSNA ETEIFTPKID
RSVFNESAGS RKQTFSRLRL AAPRNYLHHH HSSPSSTSFA SVPRRLNPEP LDEESSGILP
LLKSLFNIDD SLTANTNGNE PEDDKDLVPV QIEYPTGNSV LQNIPVGIVS CSGSKRKRGR
PRKDEKVNWL IESESLVVEE QKDKAVFDRV NKTSNAGEIS SCSEKKRTRG RPRRDESQSK
VIESEEKKVE SEIEKVASGS VEAILGIEEE LRRRTEGMEK EADLLEYLGG LEGEWASKSL
KKRIVVADGF GEVLPKGWKL MLFVKRRAGH AWLACSRYIS PDGQQFVSCK EVSSYLLSFG
GLKDSSQSTS SQTGCGIGSG VKPTSGNLPI TCVSSQHKKK APLLGRPIEV QRAETIKCHK
CPMTFNQQDD FIGHLLSSHQ GTAKSSGQTT QTNEEVIIKN GKYECQFCNE LFEERSCYSN
HLEIHMKNNM KKDDGSVGAS TTQNSIRPFN PPNNNEMRPD FPRSQANENA VVGRDTHADS
HECNLLSRDK EDIKFNGNEK TLVDENIEKQ NKCGLTNSEG EVTETAAVEF NVCLSSEKLL
FTASAKDEKA DVALKSIEEK KTEMVSSTSL HAANAEKNSD EKIEDRHFAS FMKKMEADFK
DKFTGDDPKA SCTNAHTRPN DVMIDIEQKN CSKGCSVIFS SNEGGNLVDH VKGTSAIIDS
AQDRGYRCSL TAYKDEQARV ITNKLTVASS GTLYDPESFV LSESGNNVST IGFQSDHCIK
KPPQQDSKSA LPTLHGRDQN CFTNNSAFKV SSQRVERPEH AEVEKSSGLM QDVHSHSRGF
DPNILDNVRQ ARTNAYSLVS SPYKKTFTNT LEERKQLKGS ESSVYEQYAN QQNSYNATSM
NNFSFSTLGE RKHKVQSPFN DNAHARVGTF DLTSTGLQSY SPLFSGNGER FSGKTYVPGI
SGDTVYEPKQ NIAGKTHVPG IGGGTVYEPK QNIAGKTHVP GISGGTVYEP KQSIAAQGEP
RLGDFENARN NEVMIGFGNH AQRPEDSMTG LTWKSDELLQ PSGYYPTFDV MSHKGESEMY
NISGKCGSVS GFEELRPDSI GHMEYDFLTA QPSSRSGGSK VSSNDSEMAV RSDSSIWFGK
EALPLLPKVA GRHQIAAENR WKADESGSWV IGLPSGRISE CSNSREQKKA LKTYVVLYEA
WQTGILLFAF WGRLTFSISV PVRVPLCPKS SVVDAIFDFR DSYCPAANSE FTESIDFVGV
TEGDEVSLLK ALNMVHKNSH EYVAVLFYAS WCPFSRSFRP SFSFLASSYP SIPHLAVEES
TVRPSILSKY GVHGFPTLFL LNSTMRVRYH GNRSFESLGA FYSEVTGIKD KSLDKTSLDT
IGCLSNHEKH NNTEQESCPF SWARSPENLL RQETYLALAT AFVMFRLLYL LYPTLLVIFQ
FTWRRLIRNV KLGSMFEHPL AYLRRAIQLF KSLKEPCKRR NLQGAMNARA WASKSLATVS
IGDANTSRAV PMSGCR
//
