ID   PEX1_DICDI              Reviewed;        1227 AA.
AC   Q54GX5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Peroxisome biogenesis factor 1;
DE   AltName: Full=Peroxin-1;
GN   Name=pex1; ORFNames=DDB_G0289867;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Involved in peroxisome biosynthesis. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; AAFI02000149; EAL62534.1; -; Genomic_DNA.
DR   RefSeq; XP_636032.1; XM_630940.1.
DR   AlphaFoldDB; Q54GX5; -.
DR   SMR; Q54GX5; -.
DR   STRING; 44689.DDB0238022; -.
DR   PaxDb; Q54GX5; -.
DR   EnsemblProtists; EAL62534; EAL62534; DDB_G0289867.
DR   GeneID; 8627359; -.
DR   KEGG; ddi:DDB_G0289867; -.
DR   dictyBase; DDB_G0289867; pex1.
DR   eggNOG; KOG0735; Eukaryota.
DR   HOGENOM; CLU_000688_1_1_1; -.
DR   InParanoid; Q54GX5; -.
DR   OMA; LSPCQFK; -.
DR   PhylomeDB; Q54GX5; -.
DR   PRO; PR:Q54GX5; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; ISS:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0007031; P:peroxisome organization; ISS:dictyBase.
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; 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; PEX-N_psi_beta-barrel.
DR   InterPro; IPR025653; Pex1.
DR   PANTHER; PTHR23077:SF12; PTHR23077:SF12; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF09262; PEX-1N; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54585; SSF54585; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; Nucleotide-binding;
KW   Peroxisome biogenesis; Reference proteome.
FT   CHAIN           1..1227
FT                   /note="Peroxisome biogenesis factor 1"
FT                   /id="PRO_0000371402"
FT   REGION          251..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1096..1132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          282..315
FT                   /evidence="ECO:0000255"
FT   COILED          454..519
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        264..287
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1096..1110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1111..1132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         609..616
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         907..914
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1227 AA;  138952 MW;  12FD971DCA1700C7 CRC64;
     MELHVQLKHS TDCFVSLPPK IVHSLLLLSE KQSKSLGTLG LEITWYDKIN KKENKGYVGW
     AGGSTDPRFT DSIEMSQEMA QCLGGIKNEQ KLKLKALNNI ELAHSVQVEP LTSDDWEIME
     VHQQYLEEQL LNQVNILYSG QIVPIWIHHK TIIKLKVTET LPTPVVKLSS NSEIIVAPKP
     RNLPTTTTSS QQQQISKETL KPRFLQIKDF KIDYNNNNTF INEIYINKEL LNQFQWNIGD
     IIEISKVSKN NNKNNKKEKN NNGGDEEEDD DDNEEFDDDD DDDNNNNEDD TSKLQKQLDN
     KNNNNKKNKK NNKTIYARVF INDKSNNQQV LIHRNIRTIG NFYINTIVRL KYTTSHSLPI
     CPIGSILVKQ VIWKQNSLSN LIKQQSSQKI YSVEQIKEQI KVWSNNNLSN NQRYPLLNGS
     IVSINSNLDL SFNFNNLTSS IIPPTSSSSS SPSNNLDSQR SNNNNNNINN DQLNDITNNM
     NNPYLSSIQQ IGDIMSNLNT NNNQNNQNNN SNKLMNQFQM NNGIFMLSLE ILSNDKLLKI
     ESGGNNSIEK KKSLEDYNEI GDRLFQRIGG MEKQIKQAKE FLSLYMYKDL SVIREQLNTP
     GVNGMIIAGS HGSGKSLLAT SLGGYYSTDS RSNAFIIKLD CNQLKELKVE NIRKQFNKLF
     YKSCKESGNT LSATTSTNTT PPPIIIILES LDLILGTPND QDPGSKIRCE QLVSHIKSLC
     FKYQNRSSPI VMIATVISSQ SLCQSIQIPE LFGLTIELQA PTREERVEIL ERYLKYQGKQ
     LKDQQSLNLM KFSASMEGYL GCDVEQIVDR SIHLSSIKEI ENNNNNNDDN DDDNIIEFSI
     IEKAKEGYTP ITLKGIKLHS SEIKWQDIGG LDSVRAMLKE TIEWPTKYPK LFQSSPLRLR
     SGILLYGPTG CGKTLLASAI AGECGLNFIS VKGPELLNKY IGSSEQGVRD VFSRASSAKP
     CVLFFDEFDS IAPRRGHDNS GVTDRVVNQF LTQLDGVEGL TGVYVLAATS RPDLIDPALL
     RPGRLDKSLY CNIPEFNERL DILTCLKSKM NLSPSISLEQ LSTNTQYYTG ADLRALMYNA
     QLKSIHEWMN HLEEEKKRKR KEKEDQSNKN SSQQQDDFII FQPKNNDNSI SKSNLTFEEK
     TNLQKQIDTI KSQFINSNTS TLNKSNLSNE QPPLITQSHI DLALKESSPS ISESERKKYE
     RIYNNFLKER GSVTGNKKEG VPKQTLA