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Database: UniProt
Entry: A0A1S3I5Z6_LINUN
LinkDB: A0A1S3I5Z6_LINUN
Original site: A0A1S3I5Z6_LINUN 
ID   A0A1S3I5Z6_LINUN        Unreviewed;      1257 AA.
AC   A0A1S3I5Z6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Son of sevenless homolog 1-like isoform X1 {ECO:0000313|RefSeq:XP_013393700.1};
GN   Name=LOC106161320 {ECO:0000313|RefSeq:XP_013393700.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013393700.1};
RN   [1] {ECO:0000313|RefSeq:XP_013393700.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013393700.1};
RG   RefSeq;
RL   Submitted (NOV-2023) 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   RefSeq; XP_013393700.1; XM_013538246.1.
DR   AlphaFoldDB; A0A1S3I5Z6; -.
DR   STRING; 7574.A0A1S3I5Z6; -.
DR   EnsemblMetazoa; XM_013538246.1; XP_013393700.1; LOC106161320.
DR   GeneID; 106161320; -.
DR   KEGG; lak:106161320; -.
DR   InParanoid; A0A1S3I5Z6; -.
DR   OrthoDB; 68574at2759; -.
DR   Proteomes; UP000085678; Unplaced.
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; cd01261; PH_SOS; 1.
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; 1.
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:UP000085678}.
FT   DOMAIN          207..394
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          445..550
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          601..744
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50212"
FT   DOMAIN          780..1019
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   REGION          1017..1069
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1124..1185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1212..1257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1051..1065
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1148
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1158..1180
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1212..1235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1257 AA;  143774 MW;  998FAE31D4A2A245 CRC64;
     MSILSPIAVS GSEQSIYNFE SEDNSAKWKS LLVAALQKVQ HQVHPSLSCR EDALEYIETL
     IFQLLGMLCS CQPHNVQEVE DRVQKTFPHP IDKWAVSDAQ NALEKGKKKS PLVLPVDKIH
     PLLIREVLGY KVDFQVSLYV VAVLEYIAAD ILKLAGNYVK NIKHQEITCQ DIKVAMCADK
     VLMDMFFQDD EVSLTVEEEP VRRDSLTYEE IVKDLVLEET QYLRELDMII KVFRAPFANL
     FPKSKDLEVI FSNVLDIRNL TSKLLSSLED TVEMTDENTP PLIGGCFEEI AEGAEFEVYG
     KYTEDMMKPH ARDRLNTLLQ RKDVSLTFQT AGQGFVEAVK YVLPKLLLGP IYHFLHYFES
     IKALKDASID EEDKQSLEEA ESMLLPLKTE VEKKSAGLLA KRKPGESTFR LHGQLGRQAT
     LHKINELQKQ IDGWEGKAIR QSCNEFVMEG VLLKQTGRNL RERQAFLFDG LIILCKQNLR
     RSSVTIGPAV EFRLKEKFYM RKVDVIDHED AEDLKNAFEL QVRDHPSVTL VAKTYEEKCN
     WMAALIALHT RSMLDRKLDS ILVEEEKNAP LRLPSKEEYR FGDEDTPENI VFEQNLKYEG
     ESPLIKGGTL LKLVERLTYH MYRYADPKFV RTFLTTFRSF CTPQELLDLL IERFNIPEPL
     PVDPVKELDD LAYREEIKRF RKEFVKPIQF RVLNVLRHWV NNHFYDFERD SDLQDKLKEF
     LDTVKGKAMR KWVESITKII QRRQEIPGGE KPEVVLSVTP PQIEWYAART PDEYNLMTLH
     PIEIARQVTL LEFDLYRAVK PSELVGSVWI KKEKNQTSPN LLKMIHHSTM FTFWLERCII
     EADNFEERIA VMSRTLEILL VFQELNNFNG MLEVVSALHS APVYRLEHTF IELPHKLLKA
     FDEAKELNSD HFKKYIEKLR SINPPCVPFL GMYLTNILYT EEGNPDFLVN RGPGLINFSK
     RRKVAEICGE IQQYQNQPYC LIPEPSIRQF FENLNPLEDM TEKEFNDYLY NKSLELEPRH
     AKGPTKHPRK NGYPLKSPGI KPSSGRDSVL KPSSIRDRHG TLPKSLHEGR AFSFARLQEE
     DIDLPGSQCG TPSTPSTPLT PPAVSQGNVS DSDSSVFAQV LIGPGEGIQG NNEPPEVPPI
     PPPLPPRRRD HSSSSEPPSS VPPVPPRPDQ PPPPLPPRRT TDPNMRTHSA YALQHFYHGD
     IISHAGSTSS LFTRRNSDRE TSSSSSSSAF VNGDSEPNSV PALPPKTYKT LQRNQSS
//
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