ID A0A0C9YWR9_9AGAM Unreviewed; 828 AA.
AC A0A0C9YWR9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Septin-type G domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PISMIDRAFT_109647 {ECO:0000313|EMBL:KIK18384.1};
OS Pisolithus microcarpus 441.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK18384.1, ECO:0000313|Proteomes:UP000054018};
RN [1] {ECO:0000313|EMBL:KIK18384.1, ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|EMBL:KIK18384.1,
RC ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
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; KN833807; KIK18384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9YWR9; -.
DR STRING; 765257.A0A0C9YWR9; -.
DR HOGENOM; CLU_017509_0_0_1; -.
DR OrthoDB; 1699019at2759; -.
DR Proteomes; UP000054018; Unassembled WGS sequence.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00067; GAL4; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 2.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR18884:SF123; CELL DIVISION CONTROL PROTEIN 11; 1.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR Pfam; PF00735; Septin; 3.
DR Pfam; PF00172; Zn_clus; 2.
DR PRINTS; PR00755; AFLATOXINBRP.
DR SMART; SM00066; GAL4; 2.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 2.
DR PROSITE; PS51719; G_SEPTIN; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 2.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 2.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|RuleBase:RU004560};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000054018}.
FT DOMAIN 7..402
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT DOMAIN 499..529
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT DOMAIN 702..732
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 259..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 90114 MW; B96846FC7DDF7A35 CRC64;
MRPGVSPSYR GYTLMVAGQR SGKTSFLRLL LDTSDISSTA TKDQLASVAK FVQGCSGHTA
HVRSVSVNVD LDPGSNANNG APQVLALTLI DTPSLDFSDD HAAERTIQDI LRQVDARFAE
GIDDEWKAQT GDHHIHLCIY FVDPDVIVPP PSCVPGPPAP LLSRARTNSF SHTDSEPVIL
EPPVTTNPLL CRSTLPPAEI NTIKRLSARV NVLPVIARAD TLTNDRLLAV KTAIRRDLAE
AGIGFGIFDM DVHPQYQHRK DVAESGHPVK SEIPNGYAPR TNRSSPGHPS PPTSPTTPSY
LRLPYALISP EFYSHSDGVT RVPPPRHELV QQYTPSPHYP PLSKLVRGKF IRSYRWGSMD
VLDPNQCDFM PLRSAIFHHM ETLQKYTREY LFEKFRAEYL AQHHPPNHHL HTQPNIVPRS
QLPLSHSIRP ALNIETSPSH GATVRHASLS ISRDGVPPGT DMRPLPISRP LSDGINSSHS
NVKVAPRSSK QRTKKITVAC NFCRSRKLKC DGGRPACSQC VKRSNSCDYM PQNSKRRNSH
RRKEDESESD ISGEDRSVDE NDPSVSPPEM APQPLSRKSS NADKRPVLDG FAQPPAAATA
SAGPSEHREV LPAIAPIVRP KPSVPGGSTV SEGRSLFKDN ELPHITTLSL PDRSPTAAAM
TALPLPLIRP ASEQQAAQRK RASTMPGRSS RQTTSAGPKV VACNFCRARK TKCDGAHPAC
SSCARRQLSC DYNHSTGHNG GNKKGARRAS MSSKIVPAGG PPSGTLTPAH SPPSSTVVGD
SRFLNGTPSE ETTGGEPMDV DLKRKIDDVD SPQTQKRIRV GNVNENIP
//
