ID   PEX6_SCHPO              Reviewed;         948 AA.
AC   O13764;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Peroxisomal ATPase pex6;
DE   AltName: Full=Peroxin-6;
DE   AltName: Full=Peroxisome biosynthesis protein pex6;
GN   Name=pex6; ORFNames=SPAC17A5.01;
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 pex1, 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|UniProtKB:P33760}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:P33760}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P33760}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB11501.1; -; Genomic_DNA.
DR   PIR; T37816; T37816.
DR   RefSeq; NP_593468.1; NM_001018901.2.
DR   AlphaFoldDB; O13764; -.
DR   SMR; O13764; -.
DR   BioGRID; 278899; 20.
DR   STRING; 4896.SPAC17A5.01.1; -.
DR   MaxQB; O13764; -.
DR   PaxDb; O13764; -.
DR   EnsemblFungi; SPAC17A5.01.1; SPAC17A5.01.1:pep; SPAC17A5.01.
DR   GeneID; 2542437; -.
DR   KEGG; spo:SPAC17A5.01; -.
DR   PomBase; SPAC17A5.01; pex6.
DR   VEuPathDB; FungiDB:SPAC17A5.01; -.
DR   eggNOG; KOG0736; Eukaryota.
DR   HOGENOM; CLU_310384_0_0_1; -.
DR   InParanoid; O13764; -.
DR   OMA; RTITRKF; -.
DR   PhylomeDB; O13764; -.
DR   PRO; PR:O13764; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
DR   GO; GO:0016558; P:protein import into peroxisome matrix; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015415; Vps4_C.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF09336; Vps4_C; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Membrane; Nucleotide-binding; Peroxisome;
KW   Peroxisome biogenesis; Reference proteome.
FT   CHAIN           1..948
FT                   /note="Peroxisomal ATPase pex6"
FT                   /id="PRO_0000084619"
FT   BINDING         695..702
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   948 AA;  106506 MW;  F41DFD7DE6D391B5 CRC64;
     MENRICTLAK PLPKLDESKQ AWVSYLWLKK ALPGFEEHSA YVYMTTNPTI AGRIFLPINN
     EDLEDGTVEI SGYDNLLADA LYISTIAPVK LDFVQLIVID DNSQDQDAII ERIKGRNAIL
     MESDFINQNI LVQVCQPVRH GVVDSETKFV IERKDSFTFL ASNEKNISSF KRGKTETDAE
     LVIRPSKVHT EIQWCLQNCS LIHVPFELLF NVGKKNGCPI SLRLSDGKNV YGIASIKSDT
     EHDSVQLSPS LHYFDEFNES VISEEGTEAF LVARGPSVGI ASRISLRTIP TQSCFSEKLL
     KAANLCVVQQ VKQKVFLQSK QIFCVPINSL MANSDSVDIL ELTRNTDAYI WYSVEEIDPL
     NTYNIYYTNE DTSIVLDTQL SHRLLPSLRK PLLNFVKVHP PSQKLLRFCR AFFDPQQVPG
     FNPFFLLHGN PFTGKTKAVE EVASLFSAPV FTISSYEFAD ATADHLEAKL DMFVQNVVKS
     PCAIIFVKDL DVLSISSDEG NIVPGSKSIQ ILLSKIDLVK SPQGRYIVIG TCHSIEKIPY
     EILSESFFEL KFSELEMDER LELLKIYANN VIIDKRISLK DVALKTNSMS FGELECLPDH
     MTKAAVDRIK RTGYDNDSII LSGPIITEQD VDVSINRIRK EKSNTIFTVP KVNWDDIGGL
     EEAKTVLRDT LQLPLQFPEL FSQGLKPRSG VLLYGPPGTG KTLLAKAVAT ELSLEFVSIK
     GPELLNMYVG ESEANVRNVF EKARNSSPCV IFFDELDSIA PHRGNSSDSG NVMDRVVSQL
     LAELDSISKD NNKYVFVIGA TNRPDLLDPS LLRPGRFDKL VYLGINKSEE SKASMLRALT
     KTFKLDETID LNEIAKNCHP NFTGADMYAL CSDAVLSAIK RKTNEIDLLI QASGTDLSTE
     EFFKRNENQD SLELRITKED FLTSLKKLRP SISEQELHRY EMVRHQFS