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Database: UniProt
Entry: Q5YKJ0_PICAN
LinkDB: Q5YKJ0_PICAN
Original site: Q5YKJ0_PICAN 
ID   Q5YKJ0_PICAN            Unreviewed;       439 AA.
AC   Q5YKJ0;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Vps4p {ECO:0000313|EMBL:AAR28448.1};
GN   Name=VPS4 {ECO:0000313|EMBL:AAR28448.1};
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730 {ECO:0000313|EMBL:AAR28448.1};
RN   [1] {ECO:0000313|EMBL:AAR28448.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 4732 {ECO:0000313|EMBL:AAR28448.1};
RA   Leao-Helder A.N., Krikken A.M., Lunenborg M.G.J., Kiel J.A.K.W.,
RA   van der Klei I.J., Veenhuis M.;
RT   "Hansenula polymorpha Tup1p is important for selective peroxisome
RT   degradation.";
RL   Submitted (SEP-2003) 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; AY383553; AAR28448.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5YKJ0; -.
DR   PhylomeDB; Q5YKJ0; -.
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}.
FT   DOMAIN          4..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          76..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  48915 MW;  C0BAD8AA6DB7A735 CRC64;
     MSSASEFLDK GVDLVKKAIE ADSTSKYDEA YRLYYNGLDY LMLALKYEKN PKSKETIRSK
     FTEYLSRAEQ LKEYLDKKQQ QDQTGEASAT SGSVKAKKTS GGEDDDNDSD TKKLRGALAS
     SILSERPNVQ WSDIAGLELA KEALKEAVIL PVKFPHLFRG KRKPVSGILL YGPPGTGKSY
     LAKAVATEAN STFFSVSSSD LVSKWMGESE RLVKQLFTMA REQKPAIIFI DEVDALCGPR
     GEGESEASRR IKTELLVQMN GVGNDSDGVL VLGATNIPWQ LDAAIRRRFE RRIYIPLPDQ
     EARVEMFKLN IGDTPCSLTT QDYHTLAQMT DGYSGHDVSV VVKDALMQPI RKIQMATHFK
     KVVSTDEEGR ELVQYTPCSP GDSEAIEMSW LDLDGEQLKE PELGIKDFIK AIKTNKPTVN
     QKDLEKFIEF TNDFGSEGN
//
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