ID A0A165R282_9APHY Unreviewed; 694 AA.
AC A0A165R282;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE SubName: Full=VpsA protein {ECO:0000313|EMBL:KZT70202.1};
GN ORFNames=DAEQUDRAFT_709173 {ECO:0000313|EMBL:KZT70202.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT70202.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT70202.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT70202.1,
RC ECO:0000313|Proteomes:UP000076727};
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).
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; KV429053; KZT70202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165R282; -.
DR STRING; 1314783.A0A165R282; -.
DR OrthoDB; 1052588at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
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; 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; 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:SF220; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 1; 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:UP000076727}.
FT DOMAIN 30..316
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 608..694
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
SQ SEQUENCE 694 AA; 76641 MW; 6BD0B58B0FFBE62C CRC64;
MGTQTIGSEI VSVVNKLQDV FSAVGSSASQ IDLPQICVLG SQSSGKSSVL ENLVGRDFLP
RGTGIVTRRP LVLQLINRQP SGQTNGAPKM PTEDPHANPD EWGEFLHLPG EKFYDFNKIR
AEIVRDTEAK TGKNAGISPL PINLRIYSPN VLTLTLVDLP GLTKVPVGDQ PRDIEKQIRD
MLHKYISKPA CIILAVTAAN TDLANSDGLK LAREVDPEGQ RTIGVLTKVD LMDAGTDVVD
ILAGRIIPLR LGYVPVVNRG QRDIDSNKSI SAALDHEKQF FENHPAYRGK AQYCGTPFLA
RKLNVILMAH IRATLPDIKA RISQQLQKFN AELQSLGGVV GDNSANVVLS VITDFCSEFR
TIIDGNTNDL SLNELSGGAR ISFVYHELFN NGIKTIDPFD QVKDGDIRTI LYNSSGSTPA
VFVGTQAFEV IVKQQIKRLE DPSLKCCQLV YDELIRILGQ ALNKLQAFRR FPALRDRFNA
TVVNFFKTAM TPTTKLVSDL VAMQACYVNT THPDFLNGHR AMAIVQDRLN ASKPGTPTPD
PKTKLLPGQV NNNKDLDVEA KQQETSFFGS FFSAGKNAPK KKGAALMDAP PAIIRPQAAL
NEREQMETEV IKILIHSYFN IVKREMIDMV PKAITLTLVN HSKENLQREL LQELYKPEVL
DDLLKESEYV VTRRKECIQM VQALNKAEEI VAGV
//