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Database: UniProt
Entry: A0A0C7N8C4_9SACH
LinkDB: A0A0C7N8C4_9SACH
Original site: A0A0C7N8C4_9SACH 
ID   A0A0C7N8C4_9SACH        Unreviewed;       526 AA.
AC   A0A0C7N8C4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=LALA0S10e02850g1_1 {ECO:0000313|EMBL:CEP64120.1};
GN   ORFNames=LALA0_S10e02850g {ECO:0000313|EMBL:CEP64120.1};
OS   Lachancea lanzarotensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP64120.1, ECO:0000313|Proteomes:UP000054304};
RN   [1] {ECO:0000313|EMBL:CEP64120.1, ECO:0000313|Proteomes:UP000054304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP64120.1,
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; LN736369; CEP64120.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C7N8C4; -.
DR   STRING; 1245769.A0A0C7N8C4; -.
DR   HOGENOM; CLU_017718_8_0_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; SEPTIN; 1.
DR   PANTHER; PTHR18884:SF126; 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   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          105..420
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  59146 MW;  656146E4F2D1A3A9 CRC64;
     MQAETSVEDF RSTSLAGTTS GVANGGVKLE NSPTIEETHA IPDASEGKPT AELETEVESE
     QDANQQQTGQ QLPQQTGIKV LHHRVSGYVG FANLPKQWHR KSIRRGFSLN LLCVGQKGLG
     KSTLINTLFN KPLYDLSAAA TADLAALKLG NAGDRMAGAD IDPSQQPREE LGTQQQQQQE
     AGQARDPTKV EVKIETHTTT IEENGVALTL NVIDAPGFGD GINNADAWVP IVREIDHRFD
     QYLDAENRVD RNSIEDNRVH ACLYFIEPTN HSLKALDLEF CKAVHQKCNL IPVIAKSDIL
     TDEEIEEFKA TIRGQLENEG IELFEPPQYV LDDKETAARS LQLHSQMPYA IVGSTTQVST
     ADGRQVRGRA YPWGVIEVDN AAHSDFVHLR DLLIKVYLME LRRKTENVLY ERYRSEKLGF
     LNIKQDNSVF KEYDPELKQK EEKQLHEAKL AKLEAEMKAV FQQKVNEKEK KLQKSEAELF
     NRHKEMKDKL TKQLKALEDK KHQLEMSLVN QSANSPAQTK KKGFLR
//
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