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Database: UniProt
Entry: W6MVV0_9ASCO
LinkDB: W6MVV0_9ASCO
Original site: W6MVV0_9ASCO 
ID   W6MVV0_9ASCO            Unreviewed;       362 AA.
AC   W6MVV0;
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_T00002537001 {ECO:0000313|EMBL:CDK26565.1};
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:CDK26565.1};
RN   [1] {ECO:0000313|EMBL:CDK26565.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26565.1};
RA   Genoscope - CEA;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDK26565.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26565.1};
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; HG793127; CDK26565.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6MVV0; -.
DR   STRING; 1382522.W6MVV0; -.
DR   HOGENOM; CLU_017718_7_4_1; -.
DR   OrthoDB; 2732954at2759; -.
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:SF123; CELL DIVISION CONTROL PROTEIN 11; 1.
DR   PANTHER; PTHR18884; SEPTIN; 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   Coiled coil {ECO:0000256|SAM:Coils};
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          1..276
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   COILED          311..360
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   362 AA;  41464 MW;  55617A76F020B9B8 CRC64;
     MAVGQSGSGR STFINSLCDQ VIVEPSSTII SPDIADQPNR DLELRKSIVE LEDEEGVRIS
     LTIIDTPGFG DSIENESSFG IISDYLRHQF DEILTEESRL KRNPRFKDGR VHACLYFIVP
     TGHGLRELDV EIIKALGNLV NVIPVISKSD SLTTKELALN KKLIKEDIEF YQLPVFDFKD
     EFLESYGDED NLELNDYLQK TLPFAVMGSN DVVVDPETKE RKRVRTYPWG SVNIEDNEIS
     DFQTLKNTLL ISHLNDMKDF THEVLYENYR TKALGSEDDD LYSADYNPSV QAPKSIKSQS
     TVPHSPNVPE YMEREEQIKL EEERLKAFEE RVQRDLLAKR EELEAREREL AEIEQKLALE
     AN
//
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