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Database: UniProt
Entry: A0A0D2BQ69_9EURO
LinkDB: A0A0D2BQ69_9EURO
Original site: A0A0D2BQ69_9EURO 
ID   A0A0D2BQ69_9EURO        Unreviewed;       341 AA.
AC   A0A0D2BQ69;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
GN   ORFNames=PV08_08461 {ECO:0000313|EMBL:KIW13274.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW13274.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW13274.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW13274.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847497; KIW13274.1; -; Genomic_DNA.
DR   RefSeq; XP_016233490.1; XM_016382787.1.
DR   AlphaFoldDB; A0A0D2BQ69; -.
DR   STRING; 91928.A0A0D2BQ69; -.
DR   GeneID; 27335544; -.
DR   VEuPathDB; FungiDB:PV08_08461; -.
DR   HOGENOM; CLU_017718_7_1_1; -.
DR   OrthoDB; 2732954at2759; -.
DR   Proteomes; UP000053328; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR   GO; GO:0032156; C:septin cytoskeleton; IEA:UniProt.
DR   GO; GO:0005525; F:GTP binding; 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   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:UP000053328}.
FT   DOMAIN          33..305
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          314..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   341 AA;  38846 MW;  57ADDFB1DD44ECE0 CRC64;
     MAMAMPQGNA IFPRSHVGFD SITQQIEKKL LKRGFQFNVI CVGQSGLGKS TLINTIFASH
     LLESKGRLRP DEPIRSTTEI QTVSHVIEEN GVRLRLNIVD TPGYGDLVNN DRCWDPIVKY
     IKDQHSAYLR KELTAQRERY IQDTRVHCCL FFIQPSGHAL KPIDIVVLKK LSDVVNVVPV
     IAKADSLTLE ERRAFKERIK EEFAFHNLKM YPYDNEELDD EERATNATIK DIIPFAIVGS
     EKSIIVNGKQ VRGRQNKWGI INVEDENHCE FVYLRNFLTR THLQDLIETT SQIHYETFRA
     KQLLALKESS AASGMAGSRP ISPAADRELS RSSQRMTMNG Y
//
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