ID B8MZP8_ASPFN Unreviewed; 434 AA.
AC B8MZP8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Vacuolar sorting ATPase Vps4, putative {ECO:0000313|EMBL:EED57840.1};
GN ORFNames=AFLA_085380 {ECO:0000313|EMBL:EED57840.1}, G4B84_000911
GN {ECO:0000313|EMBL:QMW25666.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED57840.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED57840.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED57840.1};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2] {ECO:0000313|EMBL:QMW25666.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW25666.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
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; EQ963472; EED57840.1; -; Genomic_DNA.
DR EMBL; CP059866; QMW25666.1; -; Genomic_DNA.
DR RefSeq; XP_002373452.1; XM_002373411.1.
DR AlphaFoldDB; B8MZP8; -.
DR STRING; 332952.B8MZP8; -.
DR EnsemblFungi; EED57840; EED57840; AFLA_085380.
DR VEuPathDB; FungiDB:AFLA_004123; -.
DR eggNOG; KOG0739; Eukaryota.
DR HOGENOM; CLU_000688_21_2_1; -.
DR OMA; IEWTNEF; -.
DR OrthoDB; 276256at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 1.
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}.
FT DOMAIN 3..81
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"
SQ SEQUENCE 434 AA; 47954 MW; D38219657A43BB39 CRC64;
MSNTDFLGRA IDAVKKAIEL DNSGEYEKAY QGYYSALELF MLALKWEKNP KSKEMIRAKT
GEYLDRAEKL KTHLEATESR KKPSAVGANG KVAQGSGKGD KNEDDNEDAD SKKLRSALAG
AILSDKPNVK WEDVAGLESA KEALKEAVIL PIKFPHLFTG KRQPWKGILL YGPPGTGKSY
LAKAVATEAN STFFSVSSSD LVSKWMGESE RLVKQLFNMA RENKPAIIFI DEVDALCGPR
GEGESEASRR IKTELLVQMD GVGKDSRGVL ILGATNIPWQ LDAAIRRRFQ RRVHISLPDI
NARVKMFMLA VGQTPCEMTQ ADYRTLAEMS EGYSGSDISI AVQDALMQPI RKIQTATHYK
KVLVEGQEKV TPCSPGDAGA MEMTWTSVEA DQLLEPPLVL KDFIKAVRNS RPTVSQEDLQ
RNSEWTKEFG SEGA
//
