ID Q0CVG2_ASPTN Unreviewed; 1228 AA.
AC Q0CVG2;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Cell division control protein 25 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ATEG_02322 {ECO:0000313|EMBL:EAU37284.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU37284.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CH476596; EAU37284.1; -; Genomic_DNA.
DR RefSeq; XP_001211500.1; XM_001211500.1.
DR AlphaFoldDB; Q0CVG2; -.
DR STRING; 341663.Q0CVG2; -.
DR EnsemblFungi; EAU37284; EAU37284; ATEG_02322.
DR GeneID; 4316550; -.
DR VEuPathDB; FungiDB:ATEG_02322; -.
DR eggNOG; KOG2398; Eukaryota.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_002632_0_0_1; -.
DR OMA; WMEDQSD; -.
DR OrthoDB; 68574at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; 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 Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 86..146
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 808..941
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 977..1213
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 30..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1228 AA; 137816 MW; DBB4B61FDD605ADF CRC64;
MYQTSVAEPL ASADARSMLA TKSNTIATAV EYPEERVSTP TTGHRSRSRG SSLSFHQTVT
DQSPQRHRSP MKLTPDGRFT PSPEPEPALF VRAMYDYDAD DHTSLSFRRG DVIQVLNQLE
TGWWDGVINN SVRGWFPSNY CTIITDLSEL EEEQVSHGRE DADASADSGA GEEDYDEERD
DDEVDSAGNP RDSQPILPIE GTGPPNEQEE AAFWIPQATP DGRLFYFNTL TGFSTMELPF
ENPSKTETGP YDRNHFYVPD QTRPPPEMMA RGFERDEDDY DGSASEAEGE SLMLASHDSM
SRRRRSYIDG VSPATSMDSL HPPKPIDGTN RHTQQTYGSM AASSSTTSLS DNFHRPSISS
EAPSHFVDDG ASIPLTWPLL VDNMRQAIEV YRQTLLRGDR SDYVRKAEDI SDHLRMLLAA
GSDTTDNHSG NPSIISTNKA LYPHFRDMMS KFSKLVLSSH IAAADWPSPD SANKCLQEAD
GVMQGVYGYV EVARQQRGDS IRRIVPGFVV GSYSGGGWQN NAVTLHDSGP TSFLDQDASD
VRAEPSVVLD AALLDHIDIL RRSFVGSIRR LEERLTLNQK KIVTESEHRQ IGDSVSAAAI
KVVEQFRPWI SSVESINLAP LGTSFQNPQL VDFSLQKQRA YDAIADFVLS CQAVTAPLGD
EWAELRGDSL EDRLNAVRGV TRQLENYVSQ IGFSLSLLLE QVPDPTTVFR SESRLDAEID
GFNKGMHSRG DSRAGVADES IGIPSSYAVE KPTKVRRNMD KAQRFFGQAP PAAITREPIR
EPVREPEETP WFLKIDHEGE VFYDTKNDVP TLKCGTLAGL VEHLTRHDKL DASFNNTFLL
TYRSFTTASE LFEMLTQRFN IQPPFGLNQD EMQMWIDRKQ KPIRFRVVNI LKSWFENFWM
EPNDDAHIQL LERVHAFTKD SIATTKTPGS PQLLTVIEQR LRGQDTTVKR LVPTQATAAP
TPIIPKNMKK LKFLDIDPTE FARQLTIIES RLYSKIRPTE CLNKTWQKKV GPDEPEPATN
VKALILHSNQ LTNWVAEMIL NQSDVKKRVV VIKHFVNVAD KCRALNNYST LTSIISALGT
APIHRLGRTW GQVSGRTSAI LEQMRRLMAS TKNFGEYRET LHLANPPCIP FFGVYLTDLT
FIEDGIPSLT PSELINFNKR AKTAEVIRDI QQYQNVPYLL QPVPELQDYI LSNLQAAGDV
HDMYDRSLEV EPREREDEKI ASIIMSAK
//
