ID C5MF04_CANTT Unreviewed; 610 AA.
AC C5MF04;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
GN ORFNames=CTRG_04647 {ECO:0000313|EMBL:EER31864.1};
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:EER31864.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER31864.1, 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).
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000256|ARBA:ARBA00004266}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
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DR EMBL; GG692400; EER31864.1; -; Genomic_DNA.
DR RefSeq; XP_002550349.1; XM_002550303.1.
DR AlphaFoldDB; C5MF04; -.
DR STRING; 294747.C5MF04; -.
DR EnsemblFungi; CTRG_04647-t43_1; CTRG_04647-t43_1-p1; CTRG_04647.
DR GeneID; 8296594; -.
DR KEGG; ctp:CTRG_04647; -.
DR VEuPathDB; FungiDB:CTRG_04647; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_7_4_1; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:1990317; C:Gin4 complex; IEA:EnsemblFungi.
DR GO; GO:0031105; C:septin complex; IEA:EnsemblFungi.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:EnsemblFungi.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IEA:EnsemblFungi.
DR GO; GO:0000917; P:division septum assembly; IEA:EnsemblFungi.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; IEA:EnsemblFungi.
DR GO; GO:0010458; P:exit from mitosis; IEA:EnsemblFungi.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR GO; GO:0097271; P:protein localization to bud neck; IEA:EnsemblFungi.
DR GO; GO:0000921; P:septin ring assembly; IEA:EnsemblFungi.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR PANTHER; PTHR18884:SF84; SEVENTH HOMOLOG OF SEPTIN 1; 1.
DR Pfam; PF00735; Septin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037}.
FT DOMAIN 29..346
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 69697 MW; 6B4219D17AF9C2FC CRC64;
MSQYSYRGST DNSESHHSPL INYRKDAKKG IKFTFMVVGE SGTGKTTFIN SLLNKKVLNH
RYEKVGHTAG ETKTLSFTSA KSVALPNTSI LTKNEFNPRT INEEPGIALT ETHIEIVDDD
NQKLLLNIID TPGFGENLNN ELCFVEIENY LKQQFDLVLA EETRIKRNPR FVDTRVHVML
YFITPTGHGL REIDIQCMKR LSKYVNIIPV IGKADSFTPN ELQYFKQQIR IDIQKFNVPT
FQFDNSLDDY DEDEDYDLIQ ECKFLTNLQP FAVITSEDVF EVSNNGEQPK IIRARKYPWG
LVDINDTRFS DFPILRSVLL GSHLQDLKDL THDFLYERYR TERLTKVTGN GQAFEDEEGD
DGEFHDTVEH QVNETRERGG LQDNSTIPSL SNLAQLTNGN DNSYNNHSNV NGDNNSITSA
SSSIKKSSSM LIDDDHHTPK LKNLSSFTSS TSTVSLENGE KEKDRAPNNN AFKRLSIGPQ
RNQLRQISET VPYVLRHERI LERQQKLEEM EQASARELAN RAALLEKKAA ELKAKEKILR
QLEMARAEQS ANSSLHRNES NVDGEQEEEI TTRYDNSEYQ HDDSTPNYET SRLQKDETLT
DLHSIVSNGH
//
