ID A1C7W1_ASPCL Unreviewed; 1231 AA.
AC A1C7W1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Cell division control protein Cdc25, putative {ECO:0000313|EMBL:EAW14482.1};
GN ORFNames=ACLA_075200 {ECO:0000313|EMBL:EAW14482.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14482.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW14482.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027045; EAW14482.1; -; Genomic_DNA.
DR RefSeq; XP_001275908.1; XM_001275907.1.
DR AlphaFoldDB; A1C7W1; -.
DR STRING; 344612.A1C7W1; -.
DR EnsemblFungi; EAW14482; EAW14482; ACLA_075200.
DR GeneID; 4707556; -.
DR KEGG; act:ACLA_075200; -.
DR VEuPathDB; FungiDB:ACLA_075200; -.
DR eggNOG; KOG2398; Eukaryota.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_002632_0_0_1; -.
DR OMA; DWPGPDS; -.
DR OrthoDB; 68574at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; 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 Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
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 4: Predicted;
KW Cell cycle {ECO:0000313|EMBL:EAW14482.1};
KW Cell division {ECO:0000313|EMBL:EAW14482.1};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 83..143
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 816..949
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 985..1221
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 32..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1231 AA; 137642 MW; 59BD515A38F13925 CRC64;
MYETRVAESL LVDTRSALAT KTHTFATTFE FTEEQGSTPP TTVARSRSRG NSISVQQRGA
AVGQASPMKT NGDGRYTPSP EPAPALFVRA MYDYDADDHT SLSFRRGDII QVLNQLETGW
WDGVINNSIR GWFPSNYCAI ITDPSELEEQ VAHVRDEGET SADSGPGEDD YEEEHENDHE
HEHDEDEVDS AGNPRDSAPI LPIEGVVPPK EQEEAAFWIP QATPDGRLFY FNTLTGYSTM
ELPFENPSVN ESGPFDRNNF FVPDQTRPPP ELMARGFERD EDDYDGSASE AEGESLMLAS
HDSMSHRRRS LIDGVSPATS MDSLHPPSTT KSIPEGKISH QSSRDLQRIT TAGSNTSASI
HFHRPSISSQ APSRFVDDGL TAPVTWPMLV DNMRHAVESY RQTLLKGDRS EYVRKAEDIS
DHLRMLLAAG SDTTDNHSGN PSIISTNKPL YPHFRDMMSK FSKLVLSSHI AAADWPGPDS
VNKCLQEADG VMQGVYGYVE VARQQRGESI RRIVPGFVVG SSAGGGWQNN GVTLDESGPT
SFLDQDGAES RVEPSVPLDA ALLDHIDILR RSFVGNIRRL EERLTLNQKK IVTYAGLHEI
SDPVAAAALK VVEQFRPWIS AVESINLAPL GTSFQNPQLV DFSLQKQRTY DAIADFVISC
QAVSAPLGDE WAELRGDSLE DRLNAVRAIA RQLENSVSQI GFSLSLLLEQ IPDPASTFRS
ESRLGADESF KGMHSRGDSQ ARIATETIGI PSSYSIEPSS GKVRRNMEKA QRFFGQAPPA
AITREPIREP VREPEEAPWF LKMDHEGEVF YDTKADTPAL KCGTLAGLVE HLTRHDKLDA
SFNNTFLLTY RSFTTASELF EMLAERFNIQ PPFGLNQDEM QMWIDRKQKP IRFRVVNILK
SWFEHFWMEP NDEAHMNLLA RVHAFTNDSI ATTKTPGSPQ LMAVIDQRLR GQDTTVKRLV
PTQATAAPTP IVPKNMKKLK FLDIDPTEFA RQLTIIESRL YSKIRPIECL NKTWQKKVGP
DEPEPATNVK ALILHSNQLT NWVAEMILTQ TDVKKRVVVI KHFVNVADKC RTLNNYSTLT
SIISALGTAP IHRLGRTWGQ VSARTSTILE QMRRLMASTK NFGEYRETLH LANPPCIPFF
GVYLTDLTFI EDGIPSLTPS ELINFNKRAK TAEVIRDIQQ YQNVPYLLQP VPELQDYILS
NLQAAGDVHD MYDRSLEVEP REREDEKIAS Q
//
