ID F0X9B2_GROCL Unreviewed; 871 AA.
AC F0X9B2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Dynamin-like GTPase {ECO:0000313|EMBL:EFX05429.1};
GN ORFNames=CMQ_3498 {ECO:0000313|EMBL:EFX05429.1};
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:EFX05429.1, 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 dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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DR EMBL; GL629735; EFX05429.1; -; Genomic_DNA.
DR RefSeq; XP_014174911.1; XM_014319436.1.
DR AlphaFoldDB; F0X9B2; -.
DR STRING; 655863.F0X9B2; -.
DR GeneID; 25976604; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; F0X9B2; -.
DR OrthoDB; 1052588at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF21; DYNAMIN-1-LIKE PROTEIN; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|RuleBase:RU003932};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003932};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796}.
FT DOMAIN 27..319
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 784..871
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 543..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 94459 MW; DE1F0F97395B848C CRC64;
MAVLGDDLLT TVNKLQDLVF NTIGNDSLDL PQIVVVGSQS AGKSSVLENI VGRDFLPRGS
GIVTRRPLIL QLINVPEEEG ANGAAAINDN RIQFLDPNAA RRSEWAEFHH LPNRRFIDFT
EVRREIENET ARVAGTNKGI TRQPINLKIY SPHVLNLTLV DLPGLTKVPI GDQPTDIEKQ
TRNLISEYIA KPNSIVLAVS PANVDIVNSE ALKLARHVDP LGRRTIGVLT KIDLMDHGTN
ALDILSGRVY PLKLGWIGVV NRSQQDIMGS KPMDEALKSE VEFFRHHPAY RNISARCGTP
YLAKTLNSTL MTHIRDRLPD IKARLNTLMG QTQQELASYG DMHFSGKEHR GSLILQLMTR
FATSFISSID GTSTEISTKE LCGGARIYYI FNSVFGSALE SIDPTSNLSA LDIRTAIRNS
TGPRPSLFVP EMAFDLLVKP QIKLLEIPSQ RCVELVYEEL IKICHTCGST ELSRFPRLQA
KLIEVVSDLL RERLGPASNY VESLISIQRA YINTNHPNFL GAAAAMSHVV NEKQERERRR
LIQEERERRD RRRAKELGGA SVAGSNTHGY HGTETPDDDE DSVSNAGGGG GGGSVMAAAS
ASLRKGGPAA AAMAAASRNG RSASLARDHN GGIAAALNGG SVRGQSPSRY ANPQALGSTK
DSFLNYFFGK EGGATHMLPP SSSGINGNSG ANSSSLAPPA SALGANIGRH VSQASEPSFS
QSMRRPDDQR PLRSPLAPPS AMDDYGTAGS VAGSVVTAGG GGGSSSNDFF GGEPALTDRE
AMETELIRAL ISSYFNIVRE SIGDQVPKAI MHLLVNHCKD VVQNRLVSEL YKETLFQELL
YEDDGVKKER EKCEQLLETY KEAAKIIGEV V
//
