ID R9XCU9_ASHAC Unreviewed; 761 AA.
AC R9XCU9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 03-MAY-2023, entry version 47.
DE SubName: Full=AaceriADR388Cp {ECO:0000313|EMBL:AGO12049.1};
GN ORFNames=AACERI_AaceriADR388C {ECO:0000313|EMBL:AGO12049.1};
OS Ashbya aceri (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=566037 {ECO:0000313|EMBL:AGO12049.1, ECO:0000313|Proteomes:UP000016920};
RN [1] {ECO:0000313|Proteomes:UP000016920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006023; AGO12049.1; -; Genomic_DNA.
DR AlphaFoldDB; R9XCU9; -.
DR HOGENOM; CLU_007879_0_0_1; -.
DR OrthoDB; 23973at2759; -.
DR Proteomes; UP000016920; Chromosome IV.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd05992; PB1; 1.
DR CDD; cd13246; PH_Scd1; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR010481; Cdc24/Scd1_N.
DR InterPro; IPR033511; Cdc24/Scd1_PH_dom.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR47339; CELL DIVISION CONTROL PROTEIN 24; 1.
DR PANTHER; PTHR47339:SF1; CELL DIVISION CONTROL PROTEIN 24; 1.
DR Pfam; PF06395; CDC24; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF15411; PH_10; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
FT DOMAIN 130..241
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 263..439
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 463..605
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 680..761
FT /note="PB1"
FT /evidence="ECO:0000259|PROSITE:PS51745"
SQ SEQUENCE 761 AA; 85889 MW; 4A2577E09AEC70FD CRC64;
MSNQASQSTI SLRSVVSTAT QQLMNKKVSE EDSLYHICVG VKRKLECLPQ LKPYLALAHA
SAALASEQQA VLLAQKDAAE VAEAPLSPLN PPHNSMISAS AGAATSPVSE IRPTSISSST
LDESEDSNAV NMEDTVLTFA MGILPSSVAC DPVTELSKLF QQGSPLCIIF NAVKPHCKLP
VVSSDDTKIC KKSIYDFIMG LKLHFAFNDE ELFTISDVFS NSTDHFTKVL DVVIALLNSV
PQIFFKQPSP TVEEPQVNGY LSDHNKIVKE FVETERKYVH DLEVLSKYRQ QLLENQIISS
EELYMLFPNL NEIIDFQRRF LVALEINGQV PAQAQRIGAL FMHSKHFFKL YEPWSIGQNA
AINFISSSFD KMQSQEFVIG NKMELQSFLL KPVQRLCRYP LLLKDLLKLS VKTKSDVDTK
ELQTALEISK SIARSINENQ RRTENHEVVK KLYGRVVNWK GYRIAKFGEL LYFDKVNIST
SNSNEPEKEF EVYLFEKIII LFSEVQQKKS NSRSLKIKTN SISSSSLHLS GANSPSSSAV
SLTGDSKLDL RGRIMIVNLI QILPIENHSL NITWESAKEQ GNFILKFKNE ETRDNWSSCL
QNLLRQIRSE SYKSTATGST DRSSFSSPYG HPHYSAASIN SSAVRQISEV MPKQLNHHQT
FEHEYRSISE NYKNSIPESM LMVRVSFNND FYTLLVSMEA EIDDVLVMLK KKLAHAGSIC
KIKYQDEDGD FVMLESEDDW SVVKDMLKES KERILNVWAF V
//