ID A1CK47_ASPCL Unreviewed; 434 AA.
AC A1CK47;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Vacuolar sorting ATPase Vps4, putative {ECO:0000313|EMBL:EAW09521.1};
GN ORFNames=ACLA_037280 {ECO:0000313|EMBL:EAW09521.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW09521.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW09521.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027056; EAW09521.1; -; Genomic_DNA.
DR RefSeq; XP_001270947.1; XM_001270946.1.
DR AlphaFoldDB; A1CK47; -.
DR STRING; 344612.A1CK47; -.
DR EnsemblFungi; EAW09521; EAW09521; ACLA_037280.
DR GeneID; 4703128; -.
DR KEGG; act:ACLA_037280; -.
DR VEuPathDB; FungiDB:ACLA_037280; -.
DR eggNOG; KOG0739; Eukaryota.
DR HOGENOM; CLU_000688_21_2_1; -.
DR OMA; IEWTNEF; -.
DR OrthoDB; 276256at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:1990621; C:ESCRT IV complex; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblFungi.
DR GO; GO:0097352; P:autophagosome maturation; IEA:EnsemblFungi.
DR GO; GO:0070676; P:intralumenal vesicle formation; IEA:EnsemblFungi.
DR GO; GO:0061764; P:late endosome to lysosome transport via multivesicular body sorting pathway; IEA:EnsemblFungi.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IEA:EnsemblFungi.
DR GO; GO:0090148; P:membrane fission; IEA:EnsemblFungi.
DR GO; GO:0036258; P:multivesicular body assembly; IEA:EnsemblFungi.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IEA:EnsemblFungi.
DR GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
DR GO; GO:0016125; P:sterol metabolic process; IEA:EnsemblFungi.
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:UP000006701}.
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 75..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..434
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"
FT COMPBIAS 414..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 48147 MW; 8FED0A342CFECE44 CRC64;
MSNTDFLGRA IDTVKKAIEH DNEGEYEKAY QTYYSALELF MLALKWEKNP RSKEMIRAKA
GEYMDRAEKL KNHLAQAENR KKPSAVGANG KVAQGSGKSG KEEDDNEDAE AKKLRSALAG
AILSDKPNVK WEDVAGLESA KEALKEAVIL PIKFPHLFTG KRQPWKGILL YGPPGTGKSY
LAKAVATEAN STFFSVSSSD LVSKWMGESE RLVKQLFNMA RENKPAIIFI DEVDALCGPR
GEGESEASRR IKTELLVQMD GVGKDSRGVL ILGATNIPWQ LDAAIRRRFQ RRVHISLPDI
NARMKMFMLA VGQTPCEMTQ ADYRTLAEMS EGYSGSDISI AVQDALMQPI RKIQTATHYK
KVMVDGAEKL TPCSPGDSGA MEMSWVNVEA DQLLEPPLVL KDFIKAVHNS RPTVSQEDLK
RNEEWTKEFG SEGA
//
