ID R7TNE9_CAPTE Unreviewed; 1166 AA.
AC R7TNE9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Son of sevenless {ECO:0008006|Google:ProtNLM};
GN ORFNames=CAPTEDRAFT_226962 {ECO:0000313|EMBL:ELT95072.1};
OS Capitella teleta (Polychaete worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Scolecida; Capitellidae; Capitella.
OX NCBI_TaxID=283909 {ECO:0000313|EMBL:ELT95072.1};
RN [1] {ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELT95072.1, ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELT95072.1,
RC ECO:0000313|Proteomes:UP000014760};
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:CapteP226962}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
CC {ECO:0000256|ARBA:ARBA00002001}.
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DR EMBL; AMQN01011974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB309218; ELT95072.1; -; Genomic_DNA.
DR AlphaFoldDB; R7TNE9; -.
DR STRING; 283909.R7TNE9; -.
DR EnsemblMetazoa; CapteT226962; CapteP226962; CapteG226962.
DR HOGENOM; CLU_002744_0_0_1; -.
DR OMA; KNTHRED; -.
DR Proteomes; UP000014760; Unassembled WGS sequence.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 6.10.250.3060; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 2.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR23113:SF373; PROTEIN SON OF SEVENLESS; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00233; PH; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 4: Predicted;
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168};
KW Reference proteome {ECO:0000313|Proteomes:UP000014760};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1166
FT /note="Son of sevenless"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008787182"
FT DOMAIN 169..342
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 408..512
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 560..677
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 714..956
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 957..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 132332 MW; C3ECE46576D55DB5 CRC64;
MAREDALAYI ETLILQLLGM LCAAQPHTVQ DVEERVVKTF PHPIDKWAIG DALNALDKGK
GKKSPLVLPV DKIHPLLSKE VLNYKLDHQV TIYIVAVLEY IAADILKLTG NYVKNIKHHE
ITLQDIKVAM CADKVLMDMF FQDSDEDTTT PAAAAIMDDH TSVRRDSLTY EDIVKDLILE
ETQYMRDLSL IIKVFRDPFA RLFPKSKDLE VIFGDILDVH ELSANLLSSL EDTVEATEEQ
QVPWIGTCFE ELIEGAEFDV YERYTENLLR PNSTDRLNTL LQRNDVIRTC QSQGRGFKES
IKYVLPKLLL GPIYHFLHYF DVIRALIDTS GDEEDLECLK QAQGILSLPK VNIERNLSSV
GLKKKPRGTT LRFQGRAERE IALNKMNELQ KCIDGWEGGK GIGQNCHEFI MEGMLMKHAN
RRLTERYVFL FDCLIIFTKL NTKRSSVTGP VGDYKLKEKF NIRKIDVADR EDTEDVKFSF
ELQPRQHPAI TLVARSQEEK NNWMAALFSL LNKSMLERLL DSSLKEKQQP LSLPSASIYR
FSELDSAENL VLEEAEPDAE SPMIKGGTLL KLVERLTYHT YADPKFIPEP SLMHDDDSSD
MLHLVREDVK RFRKEYSKPV QFRVLNVLRH WVDQHWYDFE WNQEQLLAKL NTFLESVKGK
AMRKWVESIN KVITRKQNAL GAEKHKQLTF QSQPPNVEWH ITRKPHDFDI MTLHPIEIAR
QVTLLEFDLY RAVKPSEMVG SVWVKKQKTV TSPNLLRMMQ HSTCFTFWLE KCILTAEQFE
ERVAVLSRIL EIMMVFQELN NFNGVLEVIS ALHSAPVFRL EHSFEEVDQK NHKLMKAFDE
AKDLNSDHFK RYIEKLRSID PPCVPFLGMY LTNIILTEEG NPDFLPNRPE GIINFSKRRK
VAEITAEIQQ YQNQPYCLQL QHDIRQFFEE LDPLEGMTEK DFNDLLYKKS LELEPRNCKQ
PTKAERKREY SLKSPGIKPM SSRHSASTLK SERQHPASLS SSSLQRTPDD PAPSEVDFAL
PSCGATPPTP GTPITTPPPR DSSDNSVFAP VMLPGSASFA GSTPGSILAA PLCSSSSSLP
SGGLSGGPIQ VSMPPPPPKD LPPRLPPRRK QRDSSVGGCG ELSPVRVMPV LPPRDSQPPP
CPLAPPGLPS TAICTASPPP PPTTST
//
