ID F0XUD2_GROCL Unreviewed; 797 AA.
AC F0XUD2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Heat shock protein {ECO:0000313|EMBL:EFW98894.1};
GN ORFNames=CMQ_4746 {ECO:0000313|EMBL:EFW98894.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFW98894.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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; GL630006; EFW98894.1; -; Genomic_DNA.
DR RefSeq; XP_014168377.1; XM_014312902.1.
DR AlphaFoldDB; F0XUD2; -.
DR STRING; 655863.F0XUD2; -.
DR GeneID; 25977991; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_018628_0_0_1; -.
DR InParanoid; F0XUD2; -.
DR OrthoDB; 2723505at2759; -.
DR Proteomes; UP000007796; 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; 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 Nucleotide-binding {ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW Stress response {ECO:0000313|EMBL:EFW98894.1}.
FT DOMAIN 274..585
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 90..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 86558 MW; ED1CC1A2ECA69346 CRC64;
MRPPEAFARR RSVAAAVDAD LSVHMAGDSG SGSTAPAMTY FLAAEDEIDA AVESSCGAGF
HLRELIASSQ PQPSQHRRVE ATTVEVEAAA VVASSSTPLS RDDGHVRRED HEDDSRPAPV
DVPSISHRPR TPAATRHDLN LDHDRDLVRS ICSPSLSRPS TPSLFGTPGP ASLSALSSPS
SRHNSLASSF LDDSEPDPVV LPEGGEHGRF GSFDGSHHHI HQIAASSPPS LAASALSIAT
ADDSRMMDSG SAPQLIMPSI QMPSRRPFTA TGRQLGRLKV LIAGDTGLGK TSLIKAIVQS
CQHIVHVDHI APASTVGRRR SAPASRPALG HAHTHRRPSR FSPPDQSTGK ITEIYASTKP
YPAWWSELDD SRAPTKRKSL GDNVLDRNIC FVDTPGYSGQ TSVMDAITPV VQYVESFLHR
LRSNALSDAD LVSLLTGDGG LSIDVVFYLV SGDLKPADIE YLRLLAPLTN IIPLLARADT
IASETEVAWA KERMAKQLLE ANIQPFAFAA PATALVLPYA ISSTPGVDLD TMDASLLMSP
DYVQPLVPTE LAQLVDRVFC PDGASRLRHA AARKSVQWRK CGLDADAGSS LLLSSPSSPP
VPSRPQHLYR PLNLNLSLAR MADHTQREER LAQIRLATWA AELQRHLDSE RARFENLARN
ERAVWLTERL SECVQDGSLV AVAADHRSRS QSQGHGLKRH DTRTHHGYRA DLFGQNKKKS
RRPWSTRSVS ASLCHEDPLG LLEVTAGLRA RGWLVLEVLG SLSMLGGMAL WVARYNYHLQ
LYGWVVDEWA KFWGGGR
//