ID   A0A135TRL7_9PEZI        Unreviewed;      1211 AA.
AC   A0A135TRL7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Peroxisomal ATPase PEX1 {ECO:0000256|ARBA:ARBA00034532};
DE   AltName: Full=Peroxin-1 {ECO:0000256|ARBA:ARBA00032509};
GN   ORFNames=CSIM01_01658 {ECO:0000313|EMBL:KXH50809.1};
OS   Colletotrichum simmondsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH50809.1, ECO:0000313|Proteomes:UP000070328};
RN   [1] {ECO:0000313|EMBL:KXH50809.1, ECO:0000313|Proteomes:UP000070328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS122122 {ECO:0000313|EMBL:KXH50809.1,
RC   ECO:0000313|Proteomes:UP000070328};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH50809.1}.
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DR   EMBL; JFBX01000081; KXH50809.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135TRL7; -.
DR   OrthoDB; 544017at2759; -.
DR   Proteomes; UP000070328; 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; -; 2.
DR   Gene3D; 2.40.40.20; -; 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; IPR009010; Asp_de-COase-like_dom_sf.
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; SSF50692; ADC-like; 1.
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          543..694
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          873..1008
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          235..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1211 AA;  130368 MW;  80BB11360C73A92E CRC64;
     MSSRRNAQST PAEISLAHLK NCLVNLPASL VSLLVNVNTP AQNVVVELSY RPSAGASGSG
     ASQQRSVFVG WTGMPSKRKV APIVGRDGIN GGRPGASGRD QEVAQVEIDA TLANTLGLTD
     GQKVTASIHV DPPVAHTINI EPLTPEDWEM IELHATFLEL NLLSQVRALP NPAFTSSSGS
     LVAPHALTLH LSPTSTANVK VVSLDPAPGA EVPFVKISPD AEVIVAPKVR AKTAHSLGEN
     RSVASTSKSK RSGASTVRRR SAREDRKPAL CLRGIAHSAC REWFDEDLTT QDFSVWVDRD
     ILYTKDFRGV NYVSVNILRP TPQASSTQKP QDAEQSASTS KVATKVVAHL RAWDDPPDSK
     TIALSPALCA TLGFTNSVGG IVKIEPAPQQ WPLDAVTKLI VQPFAASKKS SDGLKFGGES
     KAGKEEAAKQ FRHLYARKDI APLITGPLTD GSVIGLFEGL EAPQGWEGGV IKFDPPAINS
     DPLRSSTRWV LGLSEKIPVD IRDPVPRPSW MNDDSITELQ PSYDGQLVGI DKLLQDLRSH
     LSHLSSTLLT GAMGSGKTAV ARSLAQELGK DLLFHTTYFP CRKLVNDETR IATIKDTLTQ
     VFMSASWGAR LGGKALVVLD DLDKLCPVET ELQVGNDNGR SRQISEIIGS MVRQYCNVDT
     GVVLLAVAEG KDSLNSVIIG GHVVREIVDL KAPNKEARRK VMESIVRRDA ISAEDFPRPL
     QNGSRPPTAD GSAGGEDSAW MDAGSQGSRE NQNGTSGGFV ISPDLDFLDV AGLIDGYMPG
     DITLLVARAR NEAIIRSVND TDSEGGAVHL SRVDFDNAFK GFTPASLRNV SLQHSTTTFS
     SIGGLQETRK VLLETLQYPT KYAPIFEQCP LRLRSGLLLY GYPGCGKTLL ASAVAGECGL
     NFISVKGPEI LNKYIGASEK SVRDLFERAS AAKPCVLFFD EFDSIAPKRG HDSTGVTDRV
     VNQLLTQMDG AEGLSGVYVL AATSRPDLID PALLRPGRLD KSLLCDMPLL EDRVDILKSL
     SSKVKLGEEL TESDDAWTDL ARRTEGFSGA DLQALVSNSQ LEAIHDVLDD VSHALTTNGK
     VNGKSSSQGS VPSFVQFRYG QDAALAAKPI SRQKELVENA AILAKLESIK LARKRVKQSQ
     RPEGDGKPVN DKEVVVKLEH LMKALENTRS SISTQERARL QRIYREFVVG RSGDMKDGQG
     SMEIGGRSSL M
//