ID SMBT_DROPS Reviewed; 1274 AA.
AC Q29L50;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 24-JAN-2024, entry version 93.
DE RecName: Full=Polycomb protein Sfmbt;
DE AltName: Full=Scm-like with four MBT domain-containing protein 1;
GN Name=Sfmbt {ECO:0000250|UniProtKB:Q9VK33}; ORFNames=GA14249;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Polycomb group (PcG) protein that binds to the Polycomb
CC response elements (PREs) found in the regulatory regions of many genes.
CC PcG proteins act by forming multiprotein complexes, which are required
CC to maintain the transcriptionally repressive state of homeotic genes
CC throughout development. PcG proteins are not required to initiate
CC repression, but to maintain it during later stages of development. They
CC probably act via the methylation of histones, rendering chromatin
CC heritably changed in its expressibility. Necessary but not sufficient
CC to recruit a functional PcG repressive complex that represses target
CC genes, suggesting that the recruitment of the distinct PRC1 complex is
CC also required to allow a subsequent repression (By similarity).
CC {ECO:0000250|UniProtKB:Q9VK33}.
CC -!- SUBUNIT: Interacts with pho as a component of the pho-repressive
CC complex (PhoRC). {ECO:0000250|UniProtKB:Q9VK33}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9VK33}.
CC -!- DOMAIN: MBT repeats have unique discriminatory binding activity for
CC methylated Lys residues in H3 and H4; the MBT repeats bind mono- and
CC dimethylated H3K9Me1, H3K9Me2, H4K20Me1 and H4K20Me2 but fail to
CC interact with these residues if they are unmodified or trimethylated.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL32974.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH379061; EAL32974.2; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q29L50; -.
DR SMR; Q29L50; -.
DR STRING; 46245.Q29L50; -.
DR eggNOG; KOG3766; Eukaryota.
DR InParanoid; Q29L50; -.
DR Proteomes; UP000001819; Genome assembly.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031507; P:heterochromatin formation; ISS:UniProtKB.
DR GO; GO:0007446; P:imaginal disc growth; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd20119; MBT_dSfmbt_rpt1; 1.
DR CDD; cd20122; MBT_dSfmbt_rpt2; 1.
DR CDD; cd20125; MBT_dSfmbt_rpt3; 1.
DR CDD; cd09580; SAM_Scm-like-4MBT; 1.
DR Gene3D; 2.30.30.140; -; 4.
DR Gene3D; 3.30.60.160; -; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR047358; MBT_dSfmbt_rpt1.
DR InterPro; IPR047359; MBT_dSfmbt_rpt2.
DR InterPro; IPR047360; MBT_dSfmbt_rpt3.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037605; Sfmbt_SAM.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1.
DR PANTHER; PTHR12247:SF104; POLYCOMB PROTEIN SFMBT; 1.
DR Pfam; PF02820; MBT; 4.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF21319; zf-FCS_1; 1.
DR SMART; SM00561; MBT; 4.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 4.
DR PROSITE; PS51079; MBT; 4.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1274
FT /note="Polycomb protein Sfmbt"
FT /id="PRO_0000306372"
FT REPEAT 564..675
FT /note="MBT 1"
FT REPEAT 683..781
FT /note="MBT 2"
FT REPEAT 789..899
FT /note="MBT 3"
FT REPEAT 907..1003
FT /note="MBT 4"
FT DOMAIN 1194..1258
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 331..366
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 266..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1112
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
SQ SEQUENCE 1274 AA; 138546 MW; 52C1D68FCCD7EBD6 CRC64;
MNPTELHMMW MSSQYNAANN MTLEDATALL NHPTVGLLEE MSGHHHQPTL EMNPMMGLVG
GDFNGHAATL SGTLPPGTLI ATNSNNLYSF AHLGGLQHQL LQQSAAVAAF QNYTEVMDAD
GMTVGLATDP HGELMDETCD DEDQVYGHQI DDGYDDGGAG LEPKQEIINI DDFVMMNEDN
NSYDGTDFMT SSDKDISQSS SSGLTHMQGG GVSLGVAGAE HDLLVPLGDG LMHHKLLGAT
LAPAMPLNVG NSNVFGNIMV TGADPPSSKQ MKGYRNSNSS GTSSATVTTV ASTAVMRAQR
KTRKIEPVNR PGLVLKTPIA YKGNIDPSVI PIQKDGMAVC ERCGAIGVKH TFYTKSRRFC
SMACARGELY SLVLNNKMET TGATTSNNQS TSSSPLPAAS GTSLDVTEDA LLASDQPQSD
IELDLHAAHI KNANYRFRIT DQSKITQLNS FGEPMSLGGD AAAHNVQMAA DETIAALNGA
AVGDAAAPGG EANGSGNDTS TPNTASSGYL SAAPTPKALR LFKDVYPQDD LPQIPKYERL
PAPCPQMEKV LSIRRRMYDP THSYDWLPRL NKENFNAAPV TCFPHAPGCE VWDNLGVGMK
VEVENTDCDN IEIIQPGQTP TSFWVATILE IKGYKALMSY EGFDTDSHDF WVNLCNAEVH
SVGWCATRGK PLIPPRTIEH KYKDWKDFLV GRLSGARTLP SNFYNKINDS LQSRFRLGLN
LECVDKDRIS QVRLATVTKI VGKRLFLRYF DTDDGFWCHE DSPIIHPVGW ATTVGHNLAA
PQDYLERMLA GREAMIEVHE DDATIELFKM NFTFDEYFLD GKTNGFIEGM KLEAVDPLNL
SSICPATVMA VLKFGYMMIR IDSYQPDESG SDWFCYHEKS PCIFPAGFCS ANNISVTPPN
GYDSRTFTWE VYLRNTGAVA ANQHLFHRVV PEHGFETGMS LECADLMDPR LVCVATVARV
VGRLLKVHFD GWTDEYDQWL DCESADIYPV GWCILVGHKL EGPPRVSYQQ VAKPAPKPKV
PRKKKTKKGA STTGGGAAKQ QNDNTQTTQT VKPRTIALKT TPHLPKLSIK LELKPEHHNA
AFYENNQPED GDGDEEDPDP DADADLDADA DGDGDGSTSH ISEQSTTHSS SDQILGSGSG
GGSTSAPVVT AATGSIGGNS NKMNSSATSS KYIPRLADID ASEAAHLELQ PDSWNVYDVS
QFLRVNDCTA YCDTFSRSKI DGKRLLQLTK DDIMPLLGMK VGPALIISDL ITQLKCKVNP
GRARSHKTNK SSYL
//
