ID A7A089_YEAS7 Unreviewed; 1043 AA.
AC A7A089;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Peroxisomal ATPase PEX1 {ECO:0000256|ARBA:ARBA00034532};
DE AltName: Full=Peroxin-1 {ECO:0000256|ARBA:ARBA00032509};
GN Name=PEX1 {ECO:0000313|EMBL:EDN59828.1};
GN ORFNames=SCY_3499 {ECO:0000313|EMBL:EDN59828.1};
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796 {ECO:0000313|EMBL:EDN59828.1, ECO:0000313|Proteomes:UP000007060};
RN [1] {ECO:0000313|EMBL:EDN59828.1, ECO:0000313|Proteomes:UP000007060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN59828.1,
RC ECO:0000313|Proteomes:UP000007060};
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00034440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00034440};
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDN59828.1}.
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DR EMBL; AAFW02000153; EDN59828.1; -; Genomic_DNA.
DR AlphaFoldDB; A7A089; -.
DR HOGENOM; CLU_000688_1_1_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0007031; P:peroxisome organization; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd19526; RecA-like_PEX1_r2; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.10.330.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015342; PEX1-N_C-lobe.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF12; PEROXISOME BIOGENESIS FACTOR 1; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09262; PEX-1N; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 453..626
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 730..866
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 1043 AA; 117263 MW; C08475145F24B3B4 CRC64;
MTTTKRLKFE NLRIQFSNAI VGNFLRLPHS IINVLESTNY AIQEFGIAVH SHNSDIPIVH
LGWDGHDSGS SENVVLINPV LATVYDLNQK SPLVDLYIQR YDHTHLATEV YVTPETSDDW
EIIDANAMRF QNGEILHQTR IVTPGETLIC YLEGIVTKFK IDRVEPSMKS ARITDGSLVV
VAPKVNKTRL VKAEYGHSNK TILKNGAIQL LKKVILRSTV CKMDFPKDNL FVVYISDGAQ
LPSQKGYASI VKCSLRQSKK SDSDNKSVGI PSKKIGVFIK CDSQIPENHI ALSSHLWDAF
FTHPMNGAKI KLEFLQMNQA NIISGRNATV NIKYFGKDVP TKSGDQYSKL LGGSLLTNNL
ILPTEQIIIE IKKGESEQQL CNLNEISNES VQWKVTQMGK EEVKDIIERH LPKHYHVEET
GEVSRTSKDE DDFITVNSIK KEMVNYLTSP IIATPAIILD GKQGIGKTRL LKELINEVEK
DHHIFVKYAD CETLHETSNL DKTQKLIMEW CSFCYWYGPS LIVLDNVEAL FGKPQANDGD
PSNNGQWDNA SKLLNFFINQ VTKIFNKDNK RIRVLFSGKQ KTQINPLLFD KHFVSETWSL
RAPDKHARAK LLEYFFSKNQ IMKLNRDLQF SDLSLETEGF SPLDLEIFTE KIFYDLQVER
DCDNVVTREL FSKSLSAFTP SALRGVKLTK ETNIKWGDIG ALANAKDVLL ETLEWPTKYE
PIFVNCPLRL RSGILLYGYP GCGKTLLASA VAQQCGLNFI SVKGPEILNK FIGASEQNIR
ELFERAQSVK PCILFFDEFD SIAPKRGHDS TGVTDRVVNQ LLTQMDGAEG LDGVYILAAT
SRPDLIDSAL LRPGRLDKSV ICNIPTESER LDILQAIVNS KDKDTGQKKF ALEKNADLKL
IAEKTAGFSG ADLQGLCYNA YLKSVHRWLS AADQSEVVPG NDNIEYFSIN EHGRREENRL
RLKTLLQQDV VHETKTSTSA ASELTAVVTI NDLLEACQET KPSISTSELV KLRGIYDRFQ
KDRNGEMPNG ENSIDIGSRL SLM
//
