ID A0A421JRZ9_9ASCO Unreviewed; 448 AA.
AC A0A421JRZ9;
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 3 {ECO:0000313|EMBL:RLV94334.1};
GN ORFNames=JA1_001829 {ECO:0000313|EMBL:RLV94334.1};
OS Spathaspora sp. JA1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV94334.1, ECO:0000313|Proteomes:UP000285775};
RN [1] {ECO:0000313|EMBL:RLV94334.1, ECO:0000313|Proteomes:UP000285775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA1 {ECO:0000313|EMBL:RLV94334.1,
RC ECO:0000313|Proteomes:UP000285775};
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:RLV94334.1}.
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DR EMBL; NSGQ01000010; RLV94334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421JRZ9; -.
DR STRING; 2028339.A0A421JRZ9; -.
DR Proteomes; UP000285775; 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; 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 Cell cycle {ECO:0000313|EMBL:RLV94334.1};
KW Cell division {ECO:0000313|EMBL:RLV94334.1};
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:UP000285775}.
FT DOMAIN 56..338
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 423..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 51124 MW; D2D4BED37A86191B CRC64;
MASIEQAQPL GTPASVSQQS PINFQPQDIK IIKKVLNGYV GFANLPKQWH RKSVRRGFSL
NIMAIGESGL GKATLINTLF NREIVNHNND EEILENGGVG ETEEAGGVPV KIKSTQAEIE
EDGVRLKVSV ITAPGFGESI NNTDYWKPIV DEINTRFDSY LEAECKINRS TIVDERIHAF
LYFIEPTGHS LTALDIALMK LVHEKVNLIP IIAKSDSLTD EEIAEFKQRI LADIKYQGIK
IFTPEDSAED DEETVLNTKS IVNTFPFAVV GSTKEVQTPD GRTVRGRQYP WGVIEVDNEA
HNDFVKLRQL LIRNFLEELK EHTANVLYEN YRSEKLKKMG IEQDNTVFRE FDPLAKQQEE
RALHEAKLAK METEMKQVFQ QKVTEKEKKL QRSEADLFAR HKEMKEKLTK QIKILEDKKV
QLEKQRSLPQ EPVAQQPAQQ KTRKGFLR
//
