ID A0A1L9V3X6_ASPGL Unreviewed; 434 AA.
AC A0A1L9V3X6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Vesicle-fusing ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPGLDRAFT_160455 {ECO:0000313|EMBL:OJJ78616.1};
OS Aspergillus glaucus CBS 516.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ78616.1, ECO:0000313|Proteomes:UP000184300};
RN [1] {ECO:0000313|Proteomes:UP000184300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004481}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; KV878931; OJJ78616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9V3X6; -.
DR STRING; 1160497.A0A1L9V3X6; -.
DR VEuPathDB; FungiDB:ASPGLDRAFT_160455; -.
DR OrthoDB; 276256at2759; -.
DR Proteomes; UP000184300; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd02678; MIT_VPS4; 1.
DR CDD; cd19521; RecA-like_VPS4; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Spast_Vps4_C.
DR InterPro; IPR045253; VPS4_MIT.
DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23074:SF83; VESICLE-FUSING ATPASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; MIT domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003651};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000184300}.
FT DOMAIN 3..80
FT /note="MIT"
FT /evidence="ECO:0000259|SMART:SM00745"
FT DOMAIN 164..299
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 74..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 47854 MW; 86349E255F4E1A62 CRC64;
MSNTDFLGRA IDTVKKAIEN DNEGEYEKAY QTYYSALELF MLALKWEKNP KSKEMIRAKT
GEYMDRAEKL KNHLAQSDGQ QKPSAVGANG KVAQGSGKGG EKDDDNEDAD SKKLRSALAG
AILTDKPNVQ WEDVAGLESA KEALKEAVIL PIKFPHLFTG KRQPWKGILL YGPPGTGKSY
LAKAVATEAN STFFSVSSSD LVSKWMGESE RLVKQLFNMA RENKPAIIFI DEVDALCGPR
GEGESEASRR IKTELLVQMD GVGKDSKGVL ILGATNIPWQ LDAAIRRRFQ RRVHISLPDL
NARMKMFALA VGSTPCEMTQ ADYKTLAEMS EGYSGSDISI AVQDALMQPI RKIQTATHYK
KVILDGAEKV TPCSPGDQGA TEMSWVNVEA DQLLEPTLIL KDFVKSVRSS RPTISYEDLK
RNAEWTEEFG SEGA
//
