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Database: UniProt
Entry: A0A0C7N7X2_9SACH
LinkDB: A0A0C7N7X2_9SACH
Original site: A0A0C7N7X2_9SACH 
ID   A0A0C7N7X2_9SACH        Unreviewed;       409 AA.
AC   A0A0C7N7X2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=LALA0S06e00386g1_1 {ECO:0000313|EMBL:CEP62643.1};
GN   ORFNames=LALA0_S06e00386g {ECO:0000313|EMBL:CEP62643.1};
OS   Lachancea lanzarotensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP62643.1, ECO:0000313|Proteomes:UP000054304};
RN   [1] {ECO:0000313|EMBL:CEP62643.1, ECO:0000313|Proteomes:UP000054304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP62643.1,
RC   ECO:0000313|Proteomes:UP000054304};
RA   Neuveglise Cecile;
RL   Submitted (DEC-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; LN736365; CEP62643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C7N7X2; -.
DR   STRING; 1245769.A0A0C7N7X2; -.
DR   HOGENOM; CLU_017718_7_4_1; -.
DR   OrthoDB; 2732954at2759; -.
DR   Proteomes; UP000054304; Unassembled WGS sequence.
DR   GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR   GO; GO:0031105; C:septin complex; IEA:UniProt.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProt.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054304}.
FT   DOMAIN          19..297
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          296..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          349..408
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        318..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  46398 MW;  1A1B53415B71B199 CRC64;
     MASIIEASAA LRKRKNLKRG INFTLMVVGE SGSGRSTFVN TLCGQQVVDV STTVMLPTDA
     STQIELQLRE ETVELEDDEG VKIQLNIIDT PGFGGSLDNS QNFNVISDYI KHQYDEILLE
     ESRVRRNPRF KDGRVHCCLY LVNPTGHGLK EMDVEFMRTL APLVNVIPII SKADSLTPAE
     LKLNKKLIME DIDYYHLPIY NFPFEETDIS DEDYENNMHL RSLMPFSVVG SNEVYDLGDG
     TLIRGRQYPW GTLDVEDSTI SDFVHLRNTL LISHLHDLKD YTHEILYERY RTEALSGEPS
     APSSRGAHLA AHENGTASPV ASGKSSFHAA DHESATSSLK QSAGGQDTYL AREEQIRLEE
     ERLKAFEERV QQELLLKRQE LLQREQELRD IEERIEREAK QRAESESLQ
//
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