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Database: UniProt
Entry: A0A421J6E9_9ASCO
LinkDB: A0A421J6E9_9ASCO
Original site: A0A421J6E9_9ASCO 
ID   A0A421J6E9_9ASCO        Unreviewed;       327 AA.
AC   A0A421J6E9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Cell division control protein 10 {ECO:0000313|EMBL:RLV84027.1};
GN   ORFNames=JA9_003453 {ECO:0000313|EMBL:RLV84027.1};
OS   Meyerozyma sp. JA9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV84027.1, ECO:0000313|Proteomes:UP000286412};
RN   [1] {ECO:0000313|EMBL:RLV84027.1, ECO:0000313|Proteomes:UP000286412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA9 {ECO:0000313|EMBL:RLV84027.1,
RC   ECO:0000313|Proteomes:UP000286412};
RA   Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT   "Physiological and comparative genomic analysis of newly identified yeasts
RT   Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT   production.";
RL   Submitted (AUG-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLV84027.1}.
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DR   EMBL; NSDU01000021; RLV84027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421J6E9; -.
DR   STRING; 2028340.A0A421J6E9; -.
DR   Proteomes; UP000286412; Unassembled WGS sequence.
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   GO; GO:0051301; P:cell division; 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:SF57; CELL DIVISION CONTROL PROTEIN 10; 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   Cell cycle {ECO:0000313|EMBL:RLV84027.1};
KW   Cell division {ECO:0000313|EMBL:RLV84027.1};
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:UP000286412}.
FT   DOMAIN          28..300
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          307..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   327 AA;  37553 MW;  218A28840FFC0AA0 CRC64;
     MDEKVTQPQK YVGFDTITTQ IENRLLKRGF SLNVMVVGRS GLGKSTLINT LFSSKLVDSS
     GRRRADLPVE KTTEIVVSSH VLTENNVRLN INVVDTPGFG DQINNDKCWE PLVKYIKEQY
     SQYLRKELTA ERERHIPDTR VHCVLYFLAP NGQPLSQTDV VALRKLSEIA NVIPVIAKSD
     SLTLEERSEY KKLLQNEFIR HNFNIYPYDS DDLYDDERQL NEDIKSLIPF AVVGSDKEIV
     INGEMVRGRK TRWGAINVED VSQCEFVFLR DFLTRTHLQD LIETTAMVHY EGFRSKQLIA
     LKENAGNRQS TAEMRSQQST ESIYQRA
//
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