ID   PEX1_SCHPO              Reviewed;         937 AA.
AC   O74941;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Peroxisomal ATPase pex1;
DE   AltName: Full=Peroxin-1;
DE   AltName: Full=Peroxisome biogenesis protein pex1;
GN   Name=pex1; ORFNames=SPCC553.03;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Component of the peroxisomal protein import machinery.
CC       Together with pex6, mediates the ATP-dependent relocation and recycling
CC       of the peroxisomal targeting signal-1 (PTS1) import receptor pex5 from
CC       the peroxisomal membrane to the cytosol, where it is then available for
CC       another round of protein import into the organelle (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC       Peroxisome membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA19256.1; -; Genomic_DNA.
DR   PIR; T41400; T41400.
DR   RefSeq; NP_587770.1; NM_001022763.2.
DR   AlphaFoldDB; O74941; -.
DR   SMR; O74941; -.
DR   BioGRID; 275970; 20.
DR   STRING; 4896.SPCC553.03.1; -.
DR   MaxQB; O74941; -.
DR   PaxDb; O74941; -.
DR   EnsemblFungi; SPCC553.03.1; SPCC553.03.1:pep; SPCC553.03.
DR   GeneID; 2539405; -.
DR   KEGG; spo:SPCC553.03; -.
DR   PomBase; SPCC553.03; pex1.
DR   VEuPathDB; FungiDB:SPCC553.03; -.
DR   eggNOG; KOG0735; Eukaryota.
DR   HOGENOM; CLU_013900_0_0_1; -.
DR   InParanoid; O74941; -.
DR   OMA; IESPVKY; -.
DR   PhylomeDB; O74941; -.
DR   PRO; PR:O74941; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
DR   GO; GO:0016558; P:protein import into peroxisome matrix; IBA:GO_Central.
DR   GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; ISO:PomBase.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR029067; CDC48_domain_2-like_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015342; PEX-N_psi_beta-barrel.
DR   InterPro; IPR025653; Pex1.
DR   PANTHER; PTHR23077:SF12; PTHR23077:SF12; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF09262; PEX-1N; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54585; SSF54585; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Membrane; Nucleotide-binding; Peroxisome;
KW   Peroxisome biogenesis; Reference proteome; Repeat.
FT   CHAIN           1..937
FT                   /note="Peroxisomal ATPase pex1"
FT                   /id="PRO_0000374017"
FT   BINDING         379..386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         647..654
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   937 AA;  105905 MW;  CF4550406886543F CRC64;
     MRCIVSYKSL RSCLVNVPEL LLESISEPVQ NYAVQAVVCK NDIKKTFYFG ISGIPSQFSF
     EIDSTYAHTL KLAENQEINL SIIDCTHEIE QLEIEPVTSN DWEIAERNAA WLEENLLVQY
     RVATTERFII YLPSGTFIQF QPLKLIPSSL CGRLLRTTEV LITPKPNTSA IEVKENRKVN
     LRCVVENRLL PDSVTADSPA LCVFLPLNFP DRPDVVYMDG GNLKSTIVCQ CVSCPFQIPG
     HFFISKSLAL SYSIKTGFKF QIWKAHNPPS SSKFILEQKG LPPESNLSSE LVAAKLKNSY
     LMDGMTLKLV DIAVSYSVSG LSGVVKNPIQ DIKITSDTNV PVNAGIRNNS PRLSMQPFPH
     EFAQVRNAVF LHQNIYINGP KGCGKSNLVH SLFDYYSLNS IYFQMIVSCS EIDRSSFAKF
     QSFWNNVFIQ AERYEPSIIY LDDVHCLISS SNENGELGFV EEREIAFLQH QIINLKRKRK
     IIFIGFGEEF LTFSENLVLP LLFQIKIALP SLAVTRRKEI LTTIFQENFS DITMDSIEFI
     SVKTEGYLMT DLVLFVKRLL SEAFVEKIQN GPKHLMNKGL IEKTLKDFVP LQLRKAKFVK
     SSIRWIDIAG MQEAKEAVRD IIESPVKYSL IYKQCRLRLP TGILLFGYPG CGKTYLASAI
     SSTFPVQFIS IKGPELLDKY IGKSEQGVRD LFSRAQMAKP CVLFFDEFDS VAPRRGQDST
     GVTDRVVNQI LTQMDGAESL DGVYIVAATT RPDMIDPALL RPGRLDKLIF CDLPNEEERL
     EVLQKLANRF HIENAAMLKK LSTLTDGYTY ADLSSLLYDA HLIAVHKLLK RVSINAVDPS
     QTTSSFTNLT TESKRNASML ALPPESRYNQ NMQSMSDSKS VVIEDYMLME ALKKNSPSLN
     SEEFEHLSNL YRDFRSKLFE PELNARNTDV GSKTRQI