ID   SDC25_YEAS6             Reviewed;        1265 AA.
AC   B5VMS9;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Guanine nucleotide exchange factor SDC25;
GN   Name=SDC25; Synonyms=SCD25; ORFNames=AWRI1631_120390;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
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; ABSV01001554; EDZ70763.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VMS9; -.
DR   SMR; B5VMS9; -.
DR   PRIDE; B5VMS9; -.
DR   Proteomes; UP000008988; Unassembled WGS sequence.
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   Gene3D; 1.10.840.10; -; 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; PTHR23113; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48366; SSF48366; 1.
DR   SUPFAM; SSF50044; SSF50044; 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..1265
FT                   /note="Guanine nucleotide exchange factor SDC25"
FT                   /id="PRO_0000393438"
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   1265 AA;  146786 MW;  CDD978493BB58024 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 ITCVYMLFRN LRLVEDSFKK TLKKLIYTLS RFSINANIWF
     HSTPFEEREA IASQKDPERR SPLLQSILGT FQKFHFLLRL LHFLSNPNEL TILPQLTPRF
     FKDSFNTISW NNPFLRKHLN QHMSHDLPRQ MIKAVAGASG IVAENNDEIP ASKQGTSCSS
     ETSHHSPSAP FQRRRRGTIF SNVPGSSDES DTIWSKRKKP YPLNEETLSL VRARKEQLDA
     KLKQMIKSAN EYLSNTANFS KMLNFEMNFK 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 ALYSSSIYRL EKTWQAVIPQ TRDLLQSLDK
     LMDPKKNFIN YRSELKSLHS APCVPFFGVY LSDLTFTDSG NPDYLVLEHG LKGVHDEKKY
     INFNKRSRLV DILQEIIYFK KTHYDFTKDR TVIECISNSL ENIPHIEKQY QLSLIIEPKP
     RKKVVPNSNS NNKSQEKSRD DQTDEGKTST KKDRFSKFQL HKTKKKAPKV SKQRRRMFDF
     LLSVD