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SMBT_DROPS
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   03-AUG-2022, entry version 87.
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; 7237.FBpp0287617; -.
DR   eggNOG; KOG3766; Eukaryota.
DR   InParanoid; Q29L50; -.
DR   Proteomes; UP000001819; Genome assembly.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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 assembly; ISS:UniProtKB.
DR   GO; GO:0007446; P:imaginal disc growth; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd09580; SAM_Scm-like-4MBT; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   Gene3D; 3.30.60.160; -; 1.
DR   InterPro; IPR004092; Mbt.
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   Pfam; PF02820; MBT; 4.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00561; MBT; 4.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
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
 
 
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