ID M7BKT8_CHEMY Unreviewed; 1277 AA.
AC M7BKT8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Son of sevenless like protein 1 {ECO:0000313|EMBL:EMP32658.1};
GN ORFNames=UY3_10225 {ECO:0000313|EMBL:EMP32658.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP32658.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB539463; EMP32658.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BKT8; -.
DR STRING; 8469.M7BKT8; -.
DR eggNOG; KOG3417; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
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: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 CDD; cd00160; RhoGEF; 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; 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:SF168; SON OF SEVENLESS HOMOLOG 1; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR Pfam; PF00621; RhoGEF; 1.
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:UP000031443}.
FT DOMAIN 183..373
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 418..521
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 572..716
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 755..997
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 967..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1277 AA; 146074 MW; 3D8419417B9B2DDA CRC64;
MACFTRLLLD LQVQVQVHPK LSSAEDALQY VEELILQLLN MLCQAQPRSF LDVEDRVQKS
FPHPIDKWAI ADAQSAIEKR KRRNPLSLPV EKIHPLLKEV LGYKIDHQVS VYIVAVLEYI
SADILKLVGN YVRNIRHYEI TKQDIKVAMC ADKVLMDMFH QDVEDISTLT LSDEEPSTSG
EQTYYDLVKS FMAEVRQYIR ELNLIIKVFR EPFVSNSKLF SAHDVENIFS RISDIHELSV
KLLGHIEDTV EMTDEGSPHP LVGSCFEDLA EELAFDPYES YAQDILRPAF HDHFLGQLSK
PGAAFYLQSI GEGFKEAVQY VLPRLLLAPV YHCLHYFELL KQLEEKSEDE EDKECLKQAI
TALLNLQSSM ERICSKSLAK RRLSQQMKGK QLAIKKMNEI QKNIDGWEGK DIGQCCNEFI
MEGTLTRVGA KHERHIFLFD GLMICCKSNH GQPRLPGASN AEYRLKEKIF MRKVQINDKD
DTNEYKHAFE IILKDENSVI FAAKSAEEKN NWMAALISLQ YRSTLERMLD VTMLQEEKEE
QMRFPSPELY RFAEPDSEEN IVFEENMQPK SGIPILKAGT VVKLIERLTY HMYADPNFVR
TFLTTYRSFC KPQELLSLLI ERFEIPEPEP TEADRIAMEN GDQPLSAELK RFRKEYIQPV
QLRVLNVCRH WVEHHFYDFE RDVDLLHRLE EFIGTVRGKA MKKWVESITK IIYRKKQAQA
IGPSHNITFE SSPPAIEWHI SKPGQPETFD LLTLHPIEIA RQLTLLESDL YRAVQPSELV
GSVWTKEDKE INSPNLLKMI RHTTNLTLWF EKCIVETENL EERVIVVSRI IEILQVFQEL
NNFNGVLEVV SAMNSSPVYR LDHTFEQIPG RQKKILEEAH ELSEDHYKKY LAKLRSINPP
CVPFFGIYLT NILKTEEGNP EFLKRHGKEL INFSKRRKVA EITGEIQQYQ NQPYCLRIEP
DIRPKKYNYS LKSPGVRPSN PRPGTMRHPT PLQQEPRKIS YSRIPESESE STTSAPNSPR
TPLTPPPASA TSSTTDVCSV FDSDPSSPFH SSRTNKGQIK YIMLKVFVFK YPSGSASVSS
ISFTKISDET SGPPPVPPRR RPESAPAESS PSKITSAHLD SPPAIPPRQP TSKVYSPRYS
VPDRTSISDP PESPPVLPPR EPVRTPDVFS SSPLHLQPPP LGRKSELGNT FFPNSPSPFT
PPPPQTPSPH VARRHLPSPP LIPQDVDLHS VEGPPVPPRQ STSQHIPKLP PKTYKREHTH
PSMHRDGPPL LENAHSS
//