ID A0A6D2JFH2_9BRAS Unreviewed; 2189 AA.
AC A0A6D2JFH2;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Methyl-CpG-binding domain-containing protein 9 {ECO:0008006|Google:ProtNLM};
GN ORFNames=MERR_LOCUS25918 {ECO:0000313|EMBL:CAA7038683.1};
OS Microthlaspi erraticum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Coluteocarpeae; Microthlaspi.
OX NCBI_TaxID=1685480 {ECO:0000313|EMBL:CAA7038683.1, ECO:0000313|Proteomes:UP000467841};
RN [1] {ECO:0000313|EMBL:CAA7038683.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mishra B.;
RL Submitted (JAN-2020) 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:CAA7038683.1}.
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DR EMBL; CACVBM020001196; CAA7038683.1; -; Genomic_DNA.
DR OrthoDB; 1903104at2759; -.
DR Proteomes; UP000467841; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:UniProtKB-ARBA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProtKB-ARBA.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-ARBA.
DR GO; GO:0048731; P:system development; IEA:UniProtKB-ARBA.
DR CDD; cd15519; PHD1_Lid2p_like; 1.
DR Gene3D; 3.30.160.360; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47162:SF8; METHYL-CPG-BINDING DOMAIN-CONTAINING PROTEIN 9; 1.
DR PANTHER; PTHR47162; OS02G0192300 PROTEIN; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000467841};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 83..133
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 258..327
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 1276..1326
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 329..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1913..1935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2105..2134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1563..1597
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1451..1467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1922..1935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2118..2134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2189 AA; 241937 MW; F5CBAEA5DB403602 CRC64;
MELTDSTNEQ LGETRSAGLK EDNRSFLGID LNEIPTGATL GVGCTGGQDD DADYEPVEVV
RSIHDNPDPA PGAPAEVPGP DRDAACGACG RPESMELVVV CDACERGFHI CCVNDGAEAA
PSADWMCSDC VTGGERSKLW PLGVKSKLIL DMNASPPSDA EGYGGEETSD SRKHMLASSS
CMGNSFDYAM THSSFLNPGR GHASLEASGI MLRNSITGVD ALDSHTLGFG FPLSLNNSSL
PSRFPSLDPS ELLLQNLRHF ISERQGVLED GWRVEFKQPL NGYHLCAVYC APNGKSFSSI
QDVACYLGLA INGNYSCMDT EIRNESSPLH ERLQMPKRRK TSRWPNNGFP EQKGSSVRRF
PFNGQTMPPF AIKSLFQAGE SLSSANNGCG CEEANEGLPM QFEDFFVLSL GRIDIRQSYH
NVNMIYPIGY KSCWHDKITG SLFTCEVSDG SSGPVFKVTR SPCSKSFIPI GSTVFSCPKI
DEMVKQNIVK RDDHTQEHDD HSVEILLADP CPPLGDDILS CLREKNFSKS VNCLRSEVGS
SQVGFDKNIS YNQEHEFEIG NIVVEEDSLS VAWRKVSEKL VDACSNVLKQ KGTINFLCKH
VDRETRETNW NMINEKDSVI LSLSRFCSSF APHSVRCGER DKSESATLVD ALSSWLDQSR
FGLDADFVQE MIEHMPDAES CSNYRSLKSR TSSSVSVTVA AGALVVKPKG GGNVKDEMFG
EMSRKTKKPK LHGGQGVSNP HPPPGRPVCL RLPPGLVGDF LQVSEVFWRF HEVLGLEEAF
SPEKLEQELI NPVFDGLFLE KSGKDVNRSE MNFSDKDCTA TSICSLFDES RQPFSSENTS
ASVLKEIKAG DSTEFNISYS SRGPCLGTLL TRTHISLLQV LICELQSKVA AFVDPNFDSG
EPRSRRGRRK DDITLSAKRN KLHMLPVNEF TWPELARRYI LSVLSMDGNL ESADIAARES
GKVFRCLQGD GGLLCGSLTG VAGMEADSML LAEAIKKIFG SLTREKDVLF VEDDDSDGVI
ATETTACNGD IPEWAQVLEP VKKLPTNVGT RIRKCVYEAL ERNPPEWAKK ILEHSISKEV
YKGNASGPTK KAVLSLLADV RGGDLVQRSV GTKKKTSIGV SDIIMKKCRA VLRDVAAADE
DKVFCTLLGR KLLNSSDNDD DGLLGSPAMV SRPLDFRTID LRLAAGAYDG STEAFLEDVL
ELWSGIRAMY ADQPDCVELV DILSEKFKSL FEAEVLPLVQ KLMDYKKFEC LSAEMKKEIK
DVITSINKLP KAPWDEGVCK VCGVDKDDDS VLLCDTCDAE YHTYCLNPPL IRIPDGNWYC
PSCVIAKRMA QDALESYKLV RRRKGKKYQG ELTRASMETI AHLAGVMEVK DYWEFSAEER
ILLLKLLCDE LLSSSLVHQH LEQCTEAIIE MQQKLRSLSS EWKNTKMREE FLTAKLAKVE
PSILKEMGDP QKSSSFPDHV GCNQQPQEGG GDRFTHDVDT SSAAFLNKNQ GKASLETDAQ
AGESLVISDE SKISSLEKAT SPERHELLIA DASPHVTDGL SCENHELELQ TAQDATSLAS
QELQACQQDL NTTSTEIENL QQSIRSIESQ LLRQSIRRDF LGSDASGRLY WGCCFPEEHP
RILVDGSISL QKSAQVDLTG SKVPSPFLHA VDHGRLMVSP WTYYETEAEI TELVQWLHDD
DLKERDLRES ILCWKRLRSG DLQKEMKPAQ NFPSPISAGG LVTKAAMSME KRHGPCIKLE
TETLKKRGKK TKVVEREKLC RCECLESILP SKIHCLVCHK TFASDDEFEE HTESKCTLYS
LAPEEGKEVP DSSKAKESLK PDYLNVKSGA GKDVADISNV SELDSGLIRY QEEESISPYQ
FEEICSKFLT KDSNRDLVKE IGLIGSNGTP TFLPSSSTHL NDSMLISTNS NKLDGGGDSG
DQVMSTGSGA NDESLISESN TSLDRFVTND LGGPLDKPSG LGFGFSEQKN KKASGSGLKR
SCCVVPQASL KRITGKALPV FRFLKTSLLD MDVALPEEAL RTSKSHPDRR RALRAYVKSA
QSIYELVQAA IVVEDMIKTE YLKNEWWYWS SLSAAAKIST LSALSVRIFS LDAAIVYDKP
VTQSDPMDET KPISLPDNKS EPVSDPQERS SRANRRSDIG CKFWMLRSGL VVHQDKFGLG
VSWNGMERRF KVVQQLDEPR EYVYTYVED
//
