ID A0A165FKI6_9APHY Unreviewed; 639 AA.
AC A0A165FKI6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
GN ORFNames=LAESUDRAFT_756755 {ECO:0000313|EMBL:KZT09111.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT09111.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT09111.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT09111.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV427612; KZT09111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165FKI6; -.
DR STRING; 1314785.A0A165FKI6; -.
DR InParanoid; A0A165FKI6; -.
DR OrthoDB; 1699019at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
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 PANTHER; PTHR18884:SF123; CELL DIVISION CONTROL PROTEIN 11; 1.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR Pfam; PF00735; Septin; 3.
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 Nucleotide-binding {ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT DOMAIN 129..618
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..434
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 70330 MW; 69C85A27946E0747 CRC64;
MFGFRWRSRT KAEPDRSGPP YIRTSPSLPE LASEGIPWPE NLVDPASVSQ ADAASPSDPP
KGAAKTLFRA DGSGPIAFHK PWSLPDKPAG GTISALYTSP PPPPPPSAFE TRKQPARIRT
RVNQRKVRAP TSFNVMVVGA QGTGKTSLLR LLLDTADVSP TATPEQKASM DRFLNGRPKR
TESIQTTCVE ICESRYDRIL LSVIDTPGLD FHEGHELRLE RQVTGVVKYL DAQFADTLSE
ESKVVRQSKG DQHVHLCIYM IDPKSIMSTS LRRALSSLPE KTRSQATISH PPDLSSFSDD
STSDDSDDES SSELTMSPAD LRVIKRLSTR ANVLPVIAHA DSLTDDTLAE MKRAVRRDLH
RSGLDFGVFG PVPEEDPSSK RSTKVEAHQD ANGSAQHEDS EPEEEPVEER RSRPVIKLRP
TRHAQGRRSS RSRSRSRMSL SELAAHEQAL PDTTDAESIA SVRFSAHVVF KNDLGAQLPF
ALISPERIRR GRPLKPPAPP PGLDRRSVHT DTGTVVTTAL SEDGHAVSTA ESTQASPVTP
TSPISHRNLP LPYLAGPPAD LKGMFTRKFR WGTIDVLNPA HCDFAAMRIA VLSTHLKMLK
IRTREVLYEQ FRTEKLLAKR ATSQFTEAET RKLLADLGI
//
