ID   SDC25_YEAS8             Reviewed;        1252 AA.
AC   C8ZCV7;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Guanine nucleotide exchange factor SDC25;
GN   Name=SDC25; Synonyms=SCD25; ORFNames=EC1118_1L10_0518g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Suppresses the CDC25-5 mutation in yeast (restores cAMP
CC       level) and has similar functions as CDC25.
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DR   EMBL; FN393078; CAY81223.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8ZCV7; -.
DR   SMR; C8ZCV7; -.
DR   HOGENOM; CLU_002171_0_0_1; -.
DR   Proteomes; UP000000286; Chromosome XII, Scaffold EC1118_1L10.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   CDD; cd11883; SH3_Sdc25; 1.
DR   Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
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   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   PANTHER; PTHR23113:SF99; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 1; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48366; Ras GEF; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Guanine-nucleotide releasing factor; SH3 domain.
FT   CHAIN           1..1252
FT                   /note="Guanine nucleotide exchange factor SDC25"
FT                   /id="PRO_0000393440"
FT   DOMAIN          26..97
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          782..914
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT   DOMAIN          952..1199
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT   REGION          409..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1201..1252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1214..1236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1237..1252
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1252 AA;  145132 MW;  C58AD11F9870C560 CRC64;
     MSRTASYAGM TTPVKDKEGH GIPCLQPIDV VECTYQYFTK SQNKLSLRVG DLIYVLTKGS
     NGWWDGVLIR HSANNNNNSL ILDRGWFPPS FTRSILNELH GVPEIGNELE IFQAGLNLKL
     ELSSNPVILS LEDFLDCCRD IEFKEQLAWS PIPVHERKGC CELLYYNQDL DVYCRTLPYL
     PQNQVETVND YSSFPAISKI AGKKMPITSS PDLFYLNDCD VVYWYDLTRL VCHYVNLTER
     DLLANEREKF LTSLDLLTAQ ITYVYMLFRN LRLVEDSFKK TLKKLIYTLS RFSINANIWF
     HSTPFEEREA IASQKDPERR SPLLQSILGT FQKFHFLLRL LHFLSNPNEL TILPQLTPRF
     FKDSFNTISW NNPFLRKHLN QHMSHDLPRQ MIKAVAGASG IVAENNDEIP ASKQGTSCSS
     ETSHHSPSAP FQRRRRGTIF SNVPGSSDES DTIWSKRKKP YPLNEETLSL VRARKEQLDA
     KLKQMIKSAN EYLSNTANFS KMLNSEMNFK TYEEVSGTIP IIDILENLDL TIYLNLRELG
     DENRVFDEDV AIDDEDKEFL KHSLSSLSYI LSDYFNMKQY FHDVVVKFII VAQHLTLEDP
     FVFSPMQNDL PTGYYEPMKP SSLNLDNAKD KKNGSQNTDI QEEEDEYEPD PDSLILFHNL
     INQDSDFNDL KFFNLAHVFK KSCDDYFDVL KLSIEFVNRL ILERENLLNY AARMMKNNIT
     ELLLRGEEGY GSYDGGETAE KSDTNAVYAD SDTKDNDEWR DSQVKLPRYL QREYDSELIW
     GSNNRIKGGS KHALISYLTD NEKKDLFFNI TFLITFRSIF TTTEFLSYLI SQYNLDPPED
     LCFEEYNEWV TKKLIPVKCR VVEIMTTFFK QYWFPGYDEP DLATLNLDYF AQVAIKENIT
     GSVELLKEVN QKFKHGNMQE ATAPMKTLDQ QICQEHYWGT LYSTTESILA VDPVLFATQL
     TILEHEIYCE ITIFDCLQKI WKNKYTKSYG ASPGLNEFIS FANKLTNFIS YSIVKEADKS
     KRAKLLSHFI FIAEYCRKFN NFSSMTAIIS ALYSSPIYRL EKTWQAVIPQ TRDLLQSLDK
     LMDPKKNFID YRSELKSLHS APCVPFFGVY LSDLTFTDSG NPDYLVLEHG LKGVHDEKKY
     INFNKRSRLV DILQEIIYFK KTHYDFTKDR TVIECISNSL ENIPHIEKQY QLSLIIEPKP
     RKKVVPNSNS NNKSQEKSRD DQTDEGKTST KKDRFSKFQL HKTKKKAPKV SK
//