ID A0A166AC58_EXIGL Unreviewed; 728 AA.
AC A0A166AC58;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EXIGLDRAFT_720227 {ECO:0000313|EMBL:KZV90539.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV90539.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV90539.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV90539.1,
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; KV426046; KZV90539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166AC58; -.
DR STRING; 1314781.A0A166AC58; -.
DR InParanoid; A0A166AC58; -.
DR OrthoDB; 1052588at2759; -.
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; 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; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF237; INTERFERON-INDUCED GTP-BINDING PROTEIN MX; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 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 43..314
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 618..711
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 554..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 728 AA; 82135 MW; 7D762E29BD51AD81 CRC64;
MSAPDSKTTN DDSSSGRSDG LMHLTRKLIE IRSILLSVDQ KDGLKLPSIV VIGSQSSGKS
SVLEAIVGQE FLPKGDNMVT RRPIELTLVH LPTENGKAVE YGEFPALGLG KITDFSQIQR
TLTDLNLAVP TSEAVSNDPI DLRIYSSRVP DLTLIDLPGY VQIASMDQPE TLKEKIAALC
DRYIREPNII LAVCAADVDL ANSPALRASR RVDPLGLRTI GVLTKMDLVE PEQGAAILRG
NRYPLHLGYV GVVCKGAARK SGDNMGDVAR RSEHNFFSRH QEYYGQSSSL MVGTDTLRKR
LMEVLESSMA SSLHGITNAV QLELEEATYQ FKVQYNDRKI SAESYVAETM DALKARFKDS
QAQFAKPAVR ARLKSMLDDR VMDVLEQLYW PDARTPELSA LVADGKLRVE DIEPYWRYKL
DAASSLLTKS GVGRDATQLV ADGLRALIDS IARNEPFNHH PRAAERLVQL SHGILRDRMG
VTSDQVENCI KPYKYEVEID DREWDEGRTR AVELFEREIG MCETKLREIR KRVGGSRKLN
RIVDYVKTLE ENEKERKRRR IEAGEGETST SAPEAVEEYR YSPASIVDAR HARLYADRLA
VLKFRIQTLK GKRCKAGPNN DVLCPEVFLN VVANKLAYTS AMFINIELLD QFFYQFPREI
DSRLIYDLDR SEISRFAREN PAIRRHLDLQ ERKEKLEHVM QQLQSLANLR KDAQPTPRRS
QGLFGSFF
//
