ID A0A8E2JSZ2_9PEZI Unreviewed; 1472 AA.
AC A0A8E2JSZ2;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 08-OCT-2025, entry version 17.
DE RecName: Full=Peroxisomal ATPase PEX6 {ECO:0000256|ARBA:ARBA00034811};
DE AltName: Full=Peroxin-6 {ECO:0000256|ARBA:ARBA00034920};
GN ORFNames=AOQ84DRAFT_389115 {ECO:0000313|EMBL:OCL08044.1};
OS Glonium stellatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Gloniales; Gloniaceae; Glonium.
OX NCBI_TaxID=574774 {ECO:0000313|EMBL:OCL08044.1, ECO:0000313|Proteomes:UP000250140};
RN [1] {ECO:0000313|EMBL:OCL08044.1, ECO:0000313|Proteomes:UP000250140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 207.34 {ECO:0000313|EMBL:OCL08044.1,
RC ECO:0000313|Proteomes:UP000250140};
RX PubMed=27601008; DOI=10.1038/ncomms12662;
RG DOE Joint Genome Institute;
RA Peter M., Kohler A., Ohm R.A., Kuo A., Krutzmann J., Morin E., Arend M.,
RA Barry K.W., Binder M., Choi C., Clum A., Copeland A., Grisel N.,
RA Haridas S., Kipfer T., LaButti K., Lindquist E., Lipzen A., Maire R.,
RA Meier B., Mihaltcheva S., Molinier V., Murat C., Poggeler S., Quandt C.A.,
RA Sperisen C., Tritt A., Tisserant E., Crous P.W., Henrissat B., Nehls U.,
RA Egli S., Spatafora J.W., Grigoriev I.V., Martin F.M.;
RT "Ectomycorrhizal ecology is imprinted in the genome of the dominant
RT symbiotic fungus Cenococcum geophilum.";
RL Nat. Commun. 7:12662-12662(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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:ARBA00048778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00048778};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914}.
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DR EMBL; KV749724; OCL08044.1; -; Genomic_DNA.
DR OrthoDB; 5553750at2759; -.
DR Proteomes; UP000250140; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IEA:TreeGrafter.
DR CDD; cd19527; RecA-like_PEX6_r2; 1.
DR FunFam; 1.10.8.60:FF:000108; Peroxisomal biogenesis factor 6; 1.
DR FunFam; 3.40.50.300:FF:000109; Peroxisomal biogenesis factor 6; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR050168; AAA_ATPase_domain.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR056995; PEX6_4th_dom.
DR InterPro; IPR047533; RecA-like_PEX6_r2.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF9; PEROXISOMAL ATPASE PEX6; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF23315; PEX6_4th; 1.
DR Pfam; PF23120; PEX6_N; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peroxisome biogenesis {ECO:0000256|ARBA:ARBA00022593};
KW Reference proteome {ECO:0000313|Proteomes:UP000250140}.
FT DOMAIN 790..917
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1067..1206
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..19
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1449
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1472 AA; 157277 MW; 0539118868395D0A CRC64;
MEASVSPFNP RKRRRRRRAD RPAISARLLL DERMKGEIGV LSDDLFTDLF PGLNREPAGQ
QNCVYHVAIT PWLPSSVVAP HSTTWTILPV QVAEKNDTST ARPHSSLQFP AASLALQSFV
HTLHSVSPNK VQKRDAPIEI RIFDAVPLGL ETIFVNLDTE ALRKLDEVHA KFGGGFGFSR
PNGAAKGPGG RLLEVNGTGG KAKNTVDIAS QEQGWKNAVR DALKAPTIVH TGDLLPLPIP
SHPITHVPPP PAKITACEPV SQGLLLPTTK IVVLKSHGYS KPSKALPPVH PPMIPNGAGD
DDDDTSNETF YSAAEERTPP SQAATPPEED PGHSITDNLD SEMSGTDAGD LSDDSEDMIS
LSAPMLPPQS SGVLSSFSSA TPRPGIFQAN GAATPGSVFS SFTATTARGH APKSKLFKAQ
GLLESIPDEL VHPKPGSDDD EEARVFVDTS ALVKVGCFSG DWVRLEAAAE PPQHSLGSWG
LGAFGNEDED SSEWRAVKIY GLPENLTKKS HRYPVHKAMD RRSSFSGMIQ PSTNSHAYLS
PALLANLGDP THLRIVSLTP HQGSHLSRTS IHKPRITSSS LPPSAKEVTL LKLSTPLSTD
RLLQPSLFAA LKEYFEQKRR LVKSGDLVGI AIDESLGKAV FQGPNAEEGS GSDELLFKSR
HSGSEESSNG QDWNAKAVAW FKVGNVVASA SAELRDDEES DIWGGVVSVD AASTKMVQAG
SEQGKVPATM NSSWQYYLGV KRSPATPGVS TSKPVGISEL PKPHISPLRR RLRELMSAAT
SPRAIHLSLP PLAILITSTQ RGIGKSTVAT RACEDLGLHT FSIDAFDILT EGGAGGGDVK
TEAFLKARAE RALTCGAEYT ALLLKHVEAL NADRMTTALK EVLADSRVLI ATTTEVDKVP
EGIRGLFTHE LEMTAPDEKE REGILRGIVE DTGIRLSPDV ELSNIAIKTA ALVAGDLVDV
VDRAVVAKRT RLELLAQTAT KSSSTDPVTI KDIELAGGPS SNSLTKADFD TAVEAARKNF
ADAIGAPKIP NVSWSDVGGL THVKDAVMET IQLPLARPEL FAKGMKKRSG ILFYGPPGTG
KTLLAKAIAT EFSLNFFSVK GPELLNMYIG ESEANVRRVF QRARDARPCV VFFDELDSVA
PKRGNQGDSG GVMDRIVSQL LAELDGMSDG GEGVFVIGAT NRPDLLDQAL LRPGRFDKML
YLGVSDTHEK QLTILEALTR KFTLHPTLSL PRVASTLPFT YTGADLYALC SDAMLKAITR
QARAVDEKVK SYNSAHSPSN PKSPAQVGHV GPISIAYFFD HLANEEDTAV VVTEQDFVEA
GRELVPSVSV DELKHYERVR TTFEGEGARK QEEQKAVGPA LGASASFSRP PGSRVPSYDR
SKGKGKGKVD AASSFDDSQA DGEAGGNEDS EDDFIIRTDH LKLNGSAGGG GVGFDSAKGK
GKVKTKGKGK GSVEIAEGGF GDAAEGDEEL YA
//
