ID A5DBA2_PICGU Unreviewed; 302 AA.
AC A5DBA2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=GTP-binding RHO-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PGUG_00557 {ECO:0000313|EMBL:EDK36459.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK36459.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK36459.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
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).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000256|ARBA:ARBA00010142}.
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DR EMBL; CH408155; EDK36459.2; -; Genomic_DNA.
DR RefSeq; XP_001487180.1; XM_001487130.1.
DR AlphaFoldDB; A5DBA2; -.
DR STRING; 294746.A5DBA2; -.
DR GeneID; 5128947; -.
DR KEGG; pgu:PGUG_00557; -.
DR VEuPathDB; FungiDB:PGUG_00557; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_1_1; -.
DR InParanoid; A5DBA2; -.
DR OMA; KDTWFPE; -.
DR OrthoDB; 2016743at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR24072:SF181; GTP-BINDING PROTEIN RHO4; 1.
DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
DR PROSITE; PS51420; RHO; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997}.
SQ SEQUENCE 302 AA; 34463 MW; 5029E308563EB396 CRC64;
MSNPYEAAKR KSVLNQERKS GYNGLKVIVR EDPAVPQYQI LPTFSKKSDY QMKLVVVGDG
GCGKTCLLVS YTQQKFPEIY VPTVFENYVA NVRTPEQKLI ELALWDTAGQ EEYDRLRPLS
YPDVDILLIC FSLDNLTSLQ NVTDTWYPEV NHFCPGVPII LVGTKADLHS SIDDQLPIEV
ATDINAVGYV KCSAKSMFNI KTVFNFALHH FQRQINVKEQ MERTRQHRLS RAFGHTRNQS
SISTKRGHNK NSSIESALLL EQPLTDGDGD YNPYVASDNK YNDDEFAFTR EKAKKRRRCI
IL
//
