SDC25_YEAS1
ID SDC25_YEAS1 Reviewed; 1252 AA.
AC B3LTF3;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Guanine nucleotide exchange factor SDC25;
GN Name=SDC25; Synonyms=SCD25; ORFNames=SCRG_04972;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408054; EDV09296.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LTF3; -.
DR SMR; B3LTF3; -.
DR EnsemblFungi; EDV09296; EDV09296; SCRG_04972.
DR HOGENOM; CLU_002171_0_0_1; -.
DR Proteomes; UP000008335; 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..1252
FT /note="Guanine nucleotide exchange factor SDC25"
FT /id="PRO_0000393437"
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; 145121 MW; 31BB86C99DE2F721 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 SK
