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Database: UniProt
Entry: G2XQL1_BOTF4
LinkDB: G2XQL1_BOTF4
Original site: G2XQL1_BOTF4 
ID   G2XQL1_BOTF4            Unreviewed;      1245 AA.
AC   G2XQL1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Peroxisomal ATPase PEX1 {ECO:0000256|ARBA:ARBA00034532};
DE   AltName: Full=Peroxin-1 {ECO:0000256|ARBA:ARBA00032509};
GN   ORFNames=BofuT4_P069560.1 {ECO:0000313|EMBL:CCD43116.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD43116.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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}.
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DR   EMBL; FQ790252; CCD43116.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2XQL1; -.
DR   STRING; 999810.G2XQL1; -.
DR   eggNOG; KOG0735; Eukaryota.
DR   HOGENOM; CLU_000688_1_0_1; -.
DR   InParanoid; G2XQL1; -.
DR   Proteomes; UP000008177; Unplaced contigs.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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   CDD; cd00009; AAA; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          561..713
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          891..1027
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          233..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1094..1114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1121..1140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1225..1245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..761
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1245 AA;  134778 MW;  50CFB5A45580655C CRC64;
     MASNLKGRGS QATPAEISLI HLKNCLVNLP SSLSSLLVNI NALAQNVIVE LNYRLPPPQS
     PNQTNGAPTQ RSIFVGWTGM QSKRKLAPIV GRDGISGTRG SGREQEVQVV EIDATFARTL
     GISDGQKITA TIHVDPPVAH TINIEPLTPE DWEIIELHAN FLELNFINQI RALPNPSFTS
     PSGSSHLPHP LTLHLSPTST ANIIVTSLLP APPSNIAFTK LAPDAEVIVA PKTRSKPSRS
     LGENVSVSSR KSVGGRSVSS AVRRKSGRSE ETKPAMYYRG IDRALCGEWF EEEKDADDGG
     LKIWVDGDFI LGDSLKGLTW VTVTVVKPAT LQEPIDPQRQ QQEDENTGVA GKPASKVVAR
     LMTWDEPPDQ YHVALSSSLC ASMGCKNMVG GVIRVAPAPS QTSKPTFQPT SKSGTPHIKV
     FPYTSSTGKA NEGLKFGGES KAEREEAAKS IMKMYSKNGS NSGILEGPLT DGLVLGKPSG
     SDFPSSWEGG MIRLEQGPQE SGKQPCNWFL GSEKKFNLEV QAAIPKPLTL AANAIDGLGS
     QPPVLVGIDN LMEQLYSHLS HLSSVLLTGA LGSGKTAVVQ HLAHRLRQDS RYHTTYLSCR
     KFVTDEARVS TIRETFDRIF LAASWGARIG GKSIVILDDL DKLCPAETEL EVGNDNLRSD
     LISEKIIAIA REYLIGHRSN VVLLATAQAK ESLHKNIIGC HCVREIVALK APNKEGRRRV
     MEKVAMQNAI SEIATKPVAS GSRPSTADNS ERQNDNDWMG GSSLEGTKKL EGDGYVIDQD
     LDFLDLAGQT DGYMPGDLVL LVARARSEAM IRTVSSSLQN ADSGSIRLTR EDFDSALKGF
     TPASLRNVTL QTSTTTFDSI GGLQETRKIL LETLQYPTTY APIFAQCPLR LRSGLLLYGF
     PGCGKTLLAS AVAGECGLNF ISVKGPEILN KYIGASEKSV RDLFERAEAA RPCVLFFDEF
     DSIAPKRGHD STGVTDRVVN QLLTQMDGAE GLSGVYVLAA TSRPDLIDPA LLRPGRLDKS
     LICDLPNVDD RFDILKALGK KLKLSEEVRD SPEGGLFEIA RRTEGYSGAD LQALISNAQL
     EAIHDVLGDH EQVEVGGKRN GPKTNGASGG PQSFVQFRYG EDEDRTEAET RAKAGNNRSK
     QLAEKAAITA KLEEIKKAKK KEKLRAKGID VSSEDRGEQK EVKSQQEVTI LWKHLVKSLE
     GTRPSISADE RRRLQGIYRE FVVGRSGDMP NGQGGTEVGG RSSLM
//
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