ID A0A3A2ZME3_9EURO Unreviewed; 1210 AA.
AC A0A3A2ZME3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Cell division control protein {ECO:0000313|EMBL:RJE24312.1};
GN ORFNames=PHISCL_03367 {ECO:0000313|EMBL:RJE24312.1};
OS Aspergillus sclerotialis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Polypaecilum.
OX NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE24312.1, ECO:0000313|Proteomes:UP000266188};
RN [1] {ECO:0000313|Proteomes:UP000266188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA Tafer H., Lopandic K.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RJE24312.1}.
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DR EMBL; MVGC01000086; RJE24312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A2ZME3; -.
DR STRING; 2070753.A0A3A2ZME3; -.
DR Proteomes; UP000266188; 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:RJE24312.1};
KW Cell division {ECO:0000313|EMBL:RJE24312.1};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168};
KW Reference proteome {ECO:0000313|Proteomes:UP000266188};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 85..145
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 776..909
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 945..1181
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 30..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1210 AA; 135178 MW; 20ED326143B51077 CRC64;
MYVPHMAESL PGHNGPTLVS KSGTFATAVE YPDERAPTPT TVPRNRSRGN SLSHHLDPSQ
SSPKRQPSPV KMANARTFTP SPEPPPALFV RAMYDYDADD HTSLSFRRGD IIQVLNQLET
GWWDGVINNS VRGWFPSNYC AVVTDPRDLG EEESYAHDDT DVSAESGVDD DYDGARDGEE
LDSEGNPRDS QPILPIEGAG PKDQEEAAFW IPQATPDGRL FYFNTLTGYS TMELPFENPT
SANETGPRDR TNFLVPDQTR PPPEMMARGF ERDEDDYDGS ASEAEGESLM LASHDSMSRR
RQSLIDGVSP ATSMDSLYPQ SSKAPLSKSH KLYATTSSTN VSSGNFHRPS ISSEAPQHFA
DDGLSAPLTW HVLVENMRYA IEAYRQTLLN GDRSEYVRRA EDISDHLRML LAAGSETTDN
HSGNPSIIST NKALYGHFRD MMSKFSKLVL SSHIAAADWP GLILQQRGDS IRRIVPGFVV
GSTSGGYWQN NGVSLNDSGP TSFLVQDGSD SRAEPSVPLD AALLDHIDIL RRSIVGSIRR
LEERSSLNQK KIVTAAEQGE VADAVAAAAI NVVEHFRPWI SCVESINLAP LGTSFQNPQL
VDFSLQKQRV YDAVADFVLS CQAVSSPLGD EWAELRGDSL DDRLSAVRSI TRQLENYVSQ
IGFSLSLLLE QIPAPSAPKA DSRLGENEPY KGAHSRSESQ ANDTMETIGI PSTYSIGKSP
DKMRRNMNKA QRFFGQAPPT EITREPIREP VREPEETPWF LKIDHEGEVF YDTKGDVPLL
KCGTLAGLVE HLTRHDKLDA SFNSTFLLTY RSFTTATELF ELLVQRFNIQ PPFGLTPDEM
QMWVDRKQKP IRFRVVNILK SWFEHFWMEP GDESNMKLLE RVHAFTKDSI ATTKTPGSPQ
LLGVIEQRLR GQDTTAKRLV PTQATAAPTP IIPKNMKKLK FLDIDPTEFA RQLTIIESRL
YSKIRPTECL NKTWQKKVKP DDPEPASNVK ALILHSNQLT NWVAEMILNQ TDVKKRVAVV
KHFVNVADKC RIFNNYSTLT SIISALGTAP IHRLGRTWAQ VSGRTLSILE QMRRLMASTK
NFGEYRETLH LANPPCIPFF GVYLTDLTFI EDGIPSLTPS ELINFNKRAK TAEVIRDIQQ
YQNVPYLLQP VPELQDYILS NLQSAGDVHD MYEKSLALEP REREDEKIAR YATTGREINT
VIMASMAALR
//