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Database: UniProt
Entry: S8C8G7_DACHA
LinkDB: S8C8G7_DACHA
Original site: S8C8G7_DACHA 
ID   S8C8G7_DACHA            Unreviewed;       779 AA.
AC   S8C8G7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
GN   ORFNames=H072_2052 {ECO:0000313|EMBL:EPS43932.1};
OS   Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS   (Monacrosporium haptotylum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Dactylellina.
OX   NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS43932.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS43932.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS43932.1,
RC   ECO:0000313|Proteomes:UP000015100};
RX   PubMed=24244185;
RA   Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   PLoS Genet. 9:E1003909-E1003909(2013).
RN   [2] {ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA   Ahren D.G.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   Submitted (APR-2013) 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}.
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:EPS43932.1}.
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DR   EMBL; AQGS01000063; EPS43932.1; -; Genomic_DNA.
DR   RefSeq; XP_011108040.1; XM_011109738.1.
DR   AlphaFoldDB; S8C8G7; -.
DR   STRING; 1284197.S8C8G7; -.
DR   eggNOG; KOG2655; Eukaryota.
DR   HOGENOM; CLU_018628_0_0_1; -.
DR   OMA; ANEDIVH; -.
DR   OrthoDB; 2723505at2759; -.
DR   Proteomes; UP000015100; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR046707; DUF6780.
DR   InterPro; IPR030379; G_SEPTIN_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18884; SEPTIN; 1.
DR   PANTHER; PTHR18884:SF110; SEPTIN-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF20571; DUF6780; 1.
DR   Pfam; PF00735; 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|RuleBase:RU004560};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        742..767
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          272..573
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   779 AA;  84279 MW;  BF2422F0E5D43D7B CRC64;
     MRPASGDVLT GRSRKSSGAD LSPPGSVDSA TSSTSTAAAS PSMVTYFLAN ESAMSNVSGS
     TSSSQAAPAS QPRRTSIASP NDAEDLLLRR RRLSGKLERE DTLTPDTPKP IPILAPPFAI
     SSMPEAVRDD DAASDCEKPP YEGLESEPLT DDEDVERSSN LSFPLSITDT LPPGSPAKPL
     SRNFSPGPSL PTNSLASTRN TSSKSLADSF ADGENPLSEL QPRKSGKGKG RITDPRDPTV
     IENLDDSTLS TQFIMPTIRM PSRRPFTARG KELGRLKILV AGDSGIGKTS LIKSMIQANE
     DIVHVDPWVY TTPDSSVTSS FYGGKDNLGT TNALTEIYGS TKPYPTWWSD FEDSRVLRRR
     KSSGETVLER NVCFVDTPGY GAGTSYSECI EPVFKYVERQ LERTTSIMNG DEGDQLSFLT
     GNGSPQVDVV LYVILHRLKP VDIDFMRRLS SLTNVFPVIA KSDTLTATQT TELKLSILND
     LRNAGIRAFL FGKSADDVAR GLPSCPPFAT SSAQAPDETM DASLLMSPEY VPPLVASELD
     ELINHLFDPD NASWLRHSST KKFLSWKASH PALNPTIIPN PSPPSSSTQL IRSRSPSYGK
     HSSLIPLSGT GVGHGITGTS SSFVLARVAD HTRREEHMAQ LHLAKWAADL QKSIKAERER
     FERIAKGDRA IWLTEKLGEC VIDGSLVPLD KMGKMLVKTS SGETMAVEPI VRFGKGKMGA
     AGLDRRDPMG WLKLNQQVRK GAYLLVQITG TAGVVGVITI FVVKYVFGAT PAWMQRLGI
//
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