ID A0A165EF09_EXIGL Unreviewed; 786 AA.
AC A0A165EF09;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EXIGLDRAFT_774260 {ECO:0000313|EMBL:KZV86781.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV86781.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV86781.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV86781.1,
RC ECO:0000313|Proteomes:UP000077266};
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).
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DR EMBL; KV426144; KZV86781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EF09; -.
DR STRING; 1314781.A0A165EF09; -.
DR InParanoid; A0A165EF09; -.
DR OrthoDB; 5350357at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
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; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
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:SF131; GTPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07630)-RELATED; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 78..374
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 694..786
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 786 AA; 87895 MW; 282C385D2E32E1D6 CRC64;
MSAAGLGSSE SSPGSPHTHT SDFSFDRSRA ATPERTDVAG HHTRHSRTKS FGTSAYARDR
RALLKLLAEL HGTGIQNLLN LPQIAVVGSQ SVGKSSLIES ISGIKLPRES GTCTRCPMEC
RLEYSDSGSW TCRVSLRIQD GDSAEEVPFG DVLTNPDDVE RRIRQAQRAL LRPSLEPHTF
LDDSDLNLRG GHILSFTDNC VCVHIRGPDV TDLHFYDLPG ILGQNTSDID LVRSMVKRYI
SRPGCIILLV VSCETDFENQ VAGRLVRDVD PTGERTVGVL TKPDKTDAES APKWQRINDV
YRLQTGWFVL KLPDSKELRE GINADAARER ANAFFQANEH WHAYAQNNAS RVGTANLTEY
LAQRLSEQLR ESLPRIREAV QKALIDTISE LVSMPPELKN DPTAEVFARI TSFAQDVSRH
IRGTSQLQID RQGLVQRLYA AFRRFKTGIR ATAPKFDARN ESAAAGGVDF TELDSDDGEE
LRSSDDSAVK VADVMRVATE ARTRELPGNY PFSVKAYYIF RFLKMWEGPT FDCFEVAFKG
FVEDLAILID EHFGLYVNGG LLSQVQTVVN SQLQACAADA RIVLRMEMLK ETESIYTQNE
HYLEAYKAKF LGHYKQVRMK QPPPPPRPSS VEASRSGIYD DYEPVIYNDP YQHVRSPQVD
PTDAAVRALQ AAGYTHVKST DLPKLLPSHG LDPAFDIMAE VRAYFQVAYK RYIDAVPLCI
EQALIRKFEK QLSASLVNDL GLFKPGARTK CAIWVREPPI VAEQRRELLA RKETLEEAQS
LLVQFG
//