ID K1XMB6_MARBU Unreviewed; 1240 AA.
AC K1XMB6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Peroxisomal ATPase PEX1 {ECO:0000256|ARBA:ARBA00034532};
DE AltName: Full=Peroxin-1 {ECO:0000256|ARBA:ARBA00032509};
GN ORFNames=MBM_08322 {ECO:0000313|EMBL:EKD13604.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD13604.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD13604.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD13604.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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; JH921449; EKD13604.1; -; Genomic_DNA.
DR RefSeq; XP_007296211.1; XM_007296149.1.
DR AlphaFoldDB; K1XMB6; -.
DR STRING; 1072389.K1XMB6; -.
DR GeneID; 18764257; -.
DR KEGG; mbe:MBM_08322; -.
DR eggNOG; KOG0735; Eukaryota.
DR HOGENOM; CLU_000688_1_0_1; -.
DR InParanoid; K1XMB6; -.
DR OMA; LSASWCA; -.
DR OrthoDB; 544017at2759; -.
DR Proteomes; UP000006753; 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 Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 561..716
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 895..1031
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 239..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1240 AA; 133707 MW; 607768640B7569D0 CRC64;
MAHDRRRGSQ ATSAEISLIH LKNCFVNLPS SLCALLVNVN TLAQNVIIEL NYRAPQPAGS
GQTGSPPTRS IFVGWTGMQS QRKLAPIVSR DGISGTRGST SGREQDVPLI EIDATFARGL
GLSDGQKVTA SIHLDPPVAH TINIEPLTPE DWEIIELHAN FLELNAVSQL RALPNPNYTP
PNGPKPPPHP LTLHLSPTST ASIIVTSLAP EPPASSPFAK LSPDAEVIVA PKSRSKPLRS
FGEARSVTSR KSAGARSGTS TARRKSAREE ARPAIFFRGL DRSLCGEWFD DNKESKDQGL
KIWVDRDMLL SKALKGITWA CVTVVKPASL QTPIGPQKQQ QETDRLGEAG KVATKVVAKL
VAWDDPPDSQ HAALSSALCA AMAAERIVGG VVKLEPAPQQ VSLKELSQPA STPNSLTVRV
FPFSTSAAKS SEGLKFGGES KTEREEANRR IMKMYSSEGS SDALLDGPIT DGLILGAHHT
NDQVSGWEGG IIRFGHPPSE SAKITCNWFL GSELKFNIEV QPAIPRPSSV SRIVGDPLQS
QAPVLVGIDN LIDQLQSHLS HMSSVLLTGA LGSGKSNLAQ LLAHRLRSEY LFHTTYFSCR
QMVTDETRIS TIKETLTRIF MGAAWGARLG GKSLVILDDL DRLCPAETEL EVGSENGRSR
QISEGVCTVA TQYCGRDSGV VLLATAQAKE SLHSVIVGGH VVREIVSLKA PNKEGRRRVV
EMVVKQNATE TKHEPQALRS SGSRPTTADG SAGEDEDGGW MDSSSAASRP KSSGQSDGFN
ISPDLDFLDL AGETDGYMPG DLVLLAARAR SEALIRSVSQ TAKATDSSGV QLSREDFDRA
LKGFTPASLR NVTLQTSTTT FASIGGLHET RKILLETLQY PTTYAPIFAQ CPLRLRSGLL
LYGYPGCGKT MLASAVAGEC GLNFISVKGP EILNKYIGAS EKSVRDLFDR AEAARPCVLF
FDEFDSIAPK RGHDSTGVTD RVVNQLLTQM DGAEGLSGVY VLAATSRPDL IDPALLRPGR
LDKSLICDLP SSDDRIDILR ALGTKLMLSE EVLDSLPEIA DRTEGYSGAD LQALVYNAHL
DAIHDVLGDQ GHAEILGSKR TNKATASGPR DFIQFLYGED AHRLEAEARA KAGHNKSKLL
ADRAAISLKL AEIKNAKRRA KIGRRGEPDE KGEAKEEKEQ QEVVIEWKHV ESSLKSTRAS
ISAQERGRLE KIYREFVVGR NGEMKNGEGG REVGGRTSLM
//
