ID W3WJH7_PESFW Unreviewed; 382 AA.
AC W3WJH7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Septin {ECO:0000313|EMBL:ETS73924.1};
GN ORFNames=PFICI_13790 {ECO:0000313|EMBL:ETS73924.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS73924.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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; KI912120; ETS73924.1; -; Genomic_DNA.
DR RefSeq; XP_007840562.1; XM_007842371.1.
DR AlphaFoldDB; W3WJH7; -.
DR STRING; 1229662.W3WJH7; -.
DR GeneID; 19278803; -.
DR KEGG; pfy:PFICI_13790; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_7_4_1; -.
DR InParanoid; W3WJH7; -.
DR OMA; TNMYLRS; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000030651; 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:SF123; CELL DIVISION CONTROL PROTEIN 11; 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 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:UP000030651}.
FT DOMAIN 15..292
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 359..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 314..359
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 382 AA; 43415 MW; 46D9D7AD0BB82503 CRC64;
MPLQKMIRRK KNVKKGIQFC LMVCGASGTG RTTFVNTLCG KSVLAHKDSD DASAAHVEDG
VKIKPITVEL ELDEEGTRIS LTIVDTPGFG DQIDNEASFS EIVGYLERQY DDILAEESRI
KRNPRFRDNR VHAMLYFITP TGHGLRELDI ELMKRLAPRV NVIPVIGRAD SLTPHELAES
KKLVMEDIEH YRIPVYNFPY DIEEDDEDTV EENAELRGLM PFAIVGSEDI IEIGGRTVRA
RQYPWGVVEV DNPRHSDFLA IRSALLHSHL ADLKEITHDF LYENYRTEKL SKSVEGGAGV
DSSMNPEDLA SQSVRLKEEQ LRREEEKLRE IEIKVQREIN EKRQELLARE SQLREIEARM
QREASALSQA SPIPEANGDH EA
//
