ID A0A421J302_9ASCO Unreviewed; 406 AA.
AC A0A421J302;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Sporulation-regulated protein 3 {ECO:0000313|EMBL:RLV82619.1};
GN ORFNames=JA9_003923 {ECO:0000313|EMBL:RLV82619.1};
OS Meyerozyma sp. JA9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV82619.1, ECO:0000313|Proteomes:UP000286412};
RN [1] {ECO:0000313|EMBL:RLV82619.1, ECO:0000313|Proteomes:UP000286412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA9 {ECO:0000313|EMBL:RLV82619.1,
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:RLV82619.1}.
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DR EMBL; NSDU01000025; RLV82619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421J302; -.
DR STRING; 2028340.A0A421J302; -.
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 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:SF24; SPORULATION-REGULATED PROTEIN 3; 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:UP000286412}.
FT DOMAIN 25..281
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 386..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..385
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 406 AA; 46781 MW; F310469C16E57744 CRC64;
MSDDDPAKVG LHCIARQQVT KCARDGCRFT MIIVGASGSG RTTLMNTLFG AEIFPYDTLE
HGSFRRYEYQ LCEDGVNLQV SLIDTGGLHP SEYSYSSVAR YIDAQHFQHI FQEEQPKRNS
LKDNRIHCCL FFISPKIREI SSHELNAMRE LSTRVNLVPI LGKCDTFSPA ELETIKIRVR
ETLQQNSIVC DLSSDGSYQD MTEQVRAQMP YAVIGSNQVH PNYEGNMVRG RKYAWGLAEV
ENVNHCDFVT LRTLLMTNHM LDFIQSTEVH YEKFREFCLM KRLDYFEKTY GGPVDKSSSL
SIYAGYHRVS MEITSNNLIF EDVSLRGKEE EIKNKITRDV QLQESKFKEW KRELVATQDF
LNNDIDQMQE KCHQLKREIA MYESSEHSLS DDTLSSPEDM SLDTIE
//
