ID A0A0R0GPL8_SOYBN Unreviewed; 2025 AA.
AC A0A0R0GPL8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Methyl-CpG-binding domain-containing protein 9 {ECO:0008006|Google:ProtNLM};
GN Name=100820223 {ECO:0000313|EnsemblPlants:KRH20318};
GN ORFNames=GLYMA_13G170000 {ECO:0000313|EMBL:KRH20318.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH20318.1};
RN [1] {ECO:0000313|EMBL:KRH20318.1, ECO:0000313|EnsemblPlants:KRH20318}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH20318};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH20318.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH20318}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH20318};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH20318.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH20318.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR EMBL; CM000846; KRH20318.1; -; Genomic_DNA.
DR EnsemblPlants; KRH20318; KRH20318; GLYMA_13G170000.
DR Gramene; KRH20318; KRH20318; GLYMA_13G170000.
DR OMA; EVGICKV; -.
DR Proteomes; UP000008827; Chromosome 13.
DR ExpressionAtlas; A0A0R0GPL8; baseline and differential.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd04369; Bromodomain; 1.
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); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR028942; WHIM1_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:SF10; METHYL-CPG-BINDING DOMAIN-CONTAINING PROTEIN 9; 1.
DR PANTHER; PTHR47162; OS02G0192300 PROTEIN; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15612; WHIM1; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
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:UP000008827};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 68..135
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 987..1035
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1094..1144
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 131..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1985..2025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2004..2025
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2025 AA; 224373 MW; 8F0E679FDD43470A CRC64;
MLRRRATPKA TEATMKCRFR VTNSNFNNGN ANGFEKASEV VTHAVRVGFE DILNHTQSIT
RSFEEALRDF VSERRGVLEE GWRVEFRQSV SNSELYAVYC APDGKIFDSV YEVACYLGLT
SGYNSIESEL RSERSLPSLG GPPSRKRKST RTTVANGSME NRGTSTNSNC KDPPCDGLNV
ECASARGNIP KPSEIGRKED CHSCSQQSAD GLPLQFKDFF VLSLGKVDGR PSYYDVNLIY
PVGYKSCWHD KITGSLFTCE VLEGGDSGPI FRIRRCSCSE FPVPVGSTIL SMSKLCQVVS
QTNEGERKTN ANMDLDYDEG LQMMLLDSCL PTENDILSCF PSCSIESRDM SDVLHPITSS
VQDNASNSLA DNLGFNGLGE ILVEERSSFS AWRVISQKLV NACKDILKLK GTLKFYCNHV
DKWDLRNGKS DTYCTSLDKF CGSLGSVGIP DVIYSDNDLE GIYVALGKWL EQDRFGLDVE
FVQEVLEQLP SVQDSLQYEL LNNRNNSSSL PTVENGFLVV EWRDGSKYQE EAVQALYGRS
KKVTEKSIKE SCHPPLGKPL CSRAPGELIG DIFQAWELLK RFHEILDLKE PLTLDELEKE
LINPWFDGSN FLEKSERDMD ESQVFISLGA DGNGRPLLSP RCEVDPSVSI ESSHAFIHVE
TEAMKETAQV KLASFTYARC FGVALTKAHK SLLRVLIGEL LSKVAALVDP NSEPGESRTR
RGRRKDMDSA VPAKRTKLNM LPINELTWPE LARRYMLAFL SMDGNLESAE ITARESAKVF
RCLRGDGGLL CGSLTGVAGM EADAQLLAEA TKTIFGSLSR ENDILTMEEE ESNAKGAPEI
FLANDGNVPE WAQMLEPVRK LPTNVGTRIR KCVYEALEKN PPEWAREILE HSISKEVYKG
NASGPTKKAV LSVLVKVGGE GLQSNPNKSQ KKKIVISISD IIMKQCRIVL RRAAAADDSK
VFCNLLGRKL INSSDNDDEG LLGSPAMVAR PLDFRTIDLR LATGAYGGSH EAFLEDVREL
WNNVRVAFGD QPDLVELAEK LTQNFESLYN EEVVTYVQRF VEYAKLECLS AEMRKEVGDF
IESTNEIPKA PWDEGVCKVC GIDRDDDSVL LCDTCDAEYH TYCLNPPLAR IPEGNWYCPS
CVVGKHATQN VTERTQVIGK RQSKKFQGEV NSLYLESLAH LSAAIEEKEY WEYSVGERTF
LLKFLCDELL NSSLIHQHLE QCAELSAELH QKLRAHSAEW KSLKTREDIL STKAAKIDTF
SLNTAGEVGL KEGFASLLSN TGKCLVQPHT AVDNPSNFGV FVDSLPSEEV TKDKYRFDSV
DKSISVTNSD SDSQNMNSID VEGQFRNVSG AVESQCTDKS PKSFPLPNHM PQETNGAGGA
SLVQGKNQKC EGKDIPTPVS YQQGMPVDVP QISVNESEPY HLELIAIKRD ISLLQDSITS
VASQLLKLSV RRECLGIDSI GRLYWASALP GGRSRIVVDA SAALLHGRGM TFSRDYVEKF
SVLQHCALSD KDSSLMSQPS NPLGNSSPWI AYETDVEIEE LLGWLDDSDP KERELKDSIM
LGPKSRFQQF INAQTEDRAK DQGNVSMPRN REKTVSNSLV TKATSLLEKK FGPFVEWDNS
EVLKKQNRKT RTTNDEKLYR CECLEPILPS RKHCTHCHKT VASDIEFDGH NDGKCNAGLL
AIEKNKDKNG SSKGRGNLKC DTLHEKFRAD AETALTSVSG SSKLSSRLIK FSNEESTCPF
NFEDICSKFV TNDSNKELVS EIGLIGSDGI PSFVPSVSPF VSEYTLSAQK DESIVGGVSI
VSESRVSQGN TDGAGTCLDH KSGISTGKLA ANESNKSNKS SLREQRDGKF SFCSPASVMG
ADGCCVVPSP SLRPLVGKAS HILRQLKINL LDMDAALLAI ALRPSKAVPD RRQAWRTFVK
SAKTIYEMIQ ATFTLEDMIK TEYLRNDWWY WSSFSAAAKS STLPSLALRI YSLDLAIIYE
KMPNSSFTDS SEPSVIAEPK PLMNVDTEKS KASRKSTRKR KESDS
//
