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Database: UniProt
Entry: W6MTF3_9ASCO
LinkDB: W6MTF3_9ASCO
Original site: W6MTF3_9ASCO 
ID   W6MTF3_9ASCO            Unreviewed;       413 AA.
AC   W6MTF3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
GN   ORFNames=KUCA_T00005711001 {ECO:0000313|EMBL:CDK29718.1};
OS   Kuraishia capsulata CBS 1993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX   NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK29718.1};
RN   [1] {ECO:0000313|EMBL:CDK29718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29718.1};
RA   Genoscope - CEA;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDK29718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29718.1};
RA   Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA   Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA   Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA   Gabaldon T., Wincker P., Dujon B.;
RT   "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT   features among budding yeasts (/Saccharomycotina/).";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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; HG793131; CDK29718.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6MTF3; -.
DR   STRING; 1382522.W6MTF3; -.
DR   HOGENOM; CLU_017718_8_0_1; -.
DR   OrthoDB; 1967924at2759; -.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR   GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR   GO; GO:0032156; C:septin cytoskeleton; IEA:UniProt.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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   PANTHER; PTHR18884; SEPTIN; 1.
DR   PANTHER; PTHR18884:SF24; SPORULATION-REGULATED PROTEIN 3; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51719; G_SEPTIN; 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}.
FT   DOMAIN          28..293
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
SQ   SEQUENCE   413 AA;  47277 MW;  E880382968430BBC CRC64;
     MRINFSSHIH CCVSYHTNHI SERKASKKGA QFTVVLAGQS GLGKTSFINT LFDEDLLQLK
     DYYEENGAPR STTKINSHKI ELVEDGHVLN FTCIDTPGFG DYENNKFCWF PIVRYIEEQF
     RSYACQETQP DRSNLIDTRV HACLYFLVPT AKGVSALDVE AMKELCKRVN LIPVVAKADA
     YTRSEMQEFK KAFKETIDAY DIRLCDWLIK EDVNSDFIED MPYSVINSAG RFTRADGVTV
     RGREYVWGIA EVEDSDHCDY LKLRELLLGT NILDLIVSTE AHYEMYRSDY LTLWLKKGWE
     KKSESDLSGS DQVAAEEPMV IPENPVELMK LLRNTSRSEL EQELVFRNPA YVAAEAKLRK
     SFSDNVLNQE AVFKNWKFGL QEKQAGFNDD IQILHSTAIA LQEDIKALES IMS
//
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