ID C5M5P8_CANTT Unreviewed; 1381 AA.
AC C5M5P8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=RHO1 GDP-GTP exchange protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CTRG_01178 {ECO:0000313|EMBL:EER34318.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER34318.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER34318.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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DR EMBL; GG692396; EER34318.1; -; Genomic_DNA.
DR RefSeq; XP_002546873.1; XM_002546827.1.
DR STRING; 294747.C5M5P8; -.
DR EnsemblFungi; CTRG_01178-t43_1; CTRG_01178-t43_1-p1; CTRG_01178.
DR GeneID; 8295903; -.
DR KEGG; ctp:CTRG_01178; -.
DR VEuPathDB; FungiDB:CTRG_01178; -.
DR eggNOG; KOG4305; Eukaryota.
DR HOGENOM; CLU_001251_6_1_1; -.
DR OrthoDB; 5100844at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd04435; DEP_fRom2; 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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041675; PH_5.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46572; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46572:SF2; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF15405; PH_5; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002037}.
FT DOMAIN 684..874
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1070..1362
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1381 AA; 156531 MW; 85006CB1E8918389 CRC64;
MSSSANIPPY NARNNNTNGN NFNHMNHQQH SAVPQQNHQA MNVPEHLLPQ AFMNQQQQQQ
QQQPSPQQHY SQPHLNQHPQ QYSFPSQSRP HPPQQQHYPN AQQRSQSFTS YSANPLGSQK
TMDPGSPSLA NPIQFQGISG SSSTEQQYPS SPKRAFSQPA VMTSPQSGLQ QPYVAQRQND
LAGLNQGQYP SKNRSASSLT YDRSYSHHQQ GPPQQSSQQH PQPPYPINNG LNGPPQSHSL
DPQQPQAPYP QQRRQLRKAP SSNLPPIQND QVYNSPDARR IVSTPNHQQN FPTPVPLEAR
TQSLTSMSFK NQQQQQQQQQ DQLTQPPNFD SPVREPSSRS ASSSSLHHTF SLGSKSRSFT
SISKLSSLST KKFGSTSSVN TNKLDRHQTS STIKTYGSNH PHGHHHHHHP PKPSVYPAIL
SEVAKLFKEA IILTINTKDG LEYHDTFTGK MAVDILCRII RTNDRNLALL LGRSLDAQKF
FHDVTYNHRL RDSVHEVYAF NHVYNDVDFF HDDGNGTQTN GNNSALNSKH GSFVDSSSLQ
NALNDHILQE QLPSHISKPA LEHNNSQSNG SLSRIASGVG ISGNGSSAVV AGKELTASQQ
TGVNGVFTIL TECYSPTCSR NRLCYSIACP RRLEQQARLN LKPQGGLQRA VSRLSLHDQE
ESETLWHKTV PQSVLDKLDK HEKTRQELIY EFVYTERDYV KDLEFMTDFY IMPLRNPANN
IIPEYQRETF IQTVFGGVPD LLRLAKRLSE ALTRRQQQQK PVVETIGDVF LDYVGDFDPF
ITYSGNKVFA TFEHERQQQV NMKYARFLDA IEKKPESRRQ DLSSFLIKGV QRPARYQLLL
SGILKHTKPE SPDYKYLTKA KEEIEKLLVK INIQTGECTD RHKVMVLHRL LGKQTLENRF
NFKLSYNNRI IYQVTLNRKR DNEKIDLYLF EHALLLVKHK IQNKREQHKV FEKPMYLPLL
FVNSGMEVPT SRTIMPYRNN MSLVSDTSIK PQKPESTNYI GNTLNSSSNS KFQLNFFGLG
SNQVHASLFA EDLAIQNQVL SQISAQQKKL IETNDIFSLS KFETRRFTGN NKINCAVPCY
GGKKLLYGTD SGVWVSTVRS ISATSNEKIC SDPTMVISKT YVSQIEVIVE YSKLLVLTDK
YLYEYDLSCT DSLDHVKNTK SGKLLMTHIS FFKVGVCDGK LLVIGAKTGS QHSICILEPT
NPFDKSNKNK NKKTEIQEVY FSSDPISISF LKTKLCVGCA KGFEILSAQT GTKESILDEA
DPSLDFATQR ETVTPLAIHR LGRDFLLCYS EFVFLINRNG WRTNHDWGIF WEGNPQNVAI
FFPYLLSFDE SFIEIRDLHT TNLLRALAGE NIRFLHSNEH AAMFACEEKG YDIIISIDFL
K
//