ID A0A165EF24_EXIGL Unreviewed; 774 AA.
AC A0A165EF24;
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_840473 {ECO:0000313|EMBL:KZV86783.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV86783.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV86783.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV86783.1,
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; KZV86783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EF24; -.
DR STRING; 1314781.A0A165EF24; -.
DR InParanoid; A0A165EF24; -.
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 80..382
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 682..774
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 85552 MW; 10A4C67A5A22513D CRC64;
MSTAGSQSAE SSPGSPPSHT SGFSFEDSRS ATPDPDNGGH RSRNTRMTAA TSFGASAYAR
DRRALLKLLA ELHGTGIQNL LNLPQIAVVG SQSVGKSSLI ESISGIKLPR DSGTCTRCPM
ECRLEYTTSE AWTCRVSLRI ASSSEAAQEV QFGEILTSPD GVERRIRQAQ RALLNPGIDP
QTFLGGADPN PSGAGALSFT DNCVCIHIRG PDVTDLHFYD LPGIIVNVAE GQDPGDIDLV
RSMVGRYISR PGCIILLVVS CETDFENQVA GRLVRDVDPT GQRTVGVLTK PDKADADSAP
KWQRINNDYH LETGWFVLKL PNSSELRENI SPAVACERAN AFFQSSELWH DYAQQNAARV
GTANLTEYLA QRLSEQLRES LPRIREAVQK ALMETTARLA ALPPHLESDP TAEVFARITS
FAQEVSRHIR GTSPLQVDRQ GLVQRVYAAY RLFKTDIQGT APKFDARKDR ERVSFTELDC
DDNRERFSEV DGAVHILDVM RVATEARTRE LPGNYPFSVK AYYIFCFLEK WESPTFQCLD
GAFSAFSEEV AHLVDVNFGL YIHGGLLAQV QAAVTAQLQA CAAYARGTLR MEMLKETDSI
YTQNEHYLEA YKAKFLAHYK LVRQKAAEEL SEVPHAVYPV PHAVRPEDPI AIALRSLRTA
GYSHVTAADL HKLVPSDGLE PAFDIMAEVR AYFQVAYKRY IDAVPLCIEQ ALVRKFEGQL
SAGLVNDLGL FKTGARAKCE MWVREPPIIA AQRRELLAKK ETLEQAQHLL MQFG
//