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Database: UniProt
Entry: A0A0C9X7C4_9AGAR
LinkDB: A0A0C9X7C4_9AGAR
Original site: A0A0C9X7C4_9AGAR 
ID   A0A0C9X7C4_9AGAR        Unreviewed;      1139 AA.
AC   A0A0C9X7C4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Peroxisomal ATPase PEX6 {ECO:0000256|ARBA:ARBA00034811};
DE   AltName: Full=Peroxin-6 {ECO:0000256|ARBA:ARBA00034920};
GN   ORFNames=K443DRAFT_1654 {ECO:0000313|EMBL:KIK08110.1};
OS   Laccaria amethystina LaAM-08-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK08110.1, ECO:0000313|Proteomes:UP000054477};
RN   [1] {ECO:0000313|EMBL:KIK08110.1, ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK08110.1,
RC   ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) 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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Peroxisome membrane
CC       {ECO:0000256|ARBA:ARBA00034691}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00034691}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00034691}.
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DR   EMBL; KN838543; KIK08110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9X7C4; -.
DR   STRING; 1095629.A0A0C9X7C4; -.
DR   HOGENOM; CLU_000688_0_0_1; -.
DR   OrthoDB; 7477at2759; -.
DR   Proteomes; UP000054477; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR   CDD; cd19527; RecA-like_PEX6_r2; 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; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047533; RecA-like_PEX6_r2.
DR   PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR   PANTHER; PTHR23077:SF9; PEROXISOME ASSEMBLY FACTOR 2; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Peroxisome biogenesis {ECO:0000256|ARBA:ARBA00022593};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054477}.
FT   DOMAIN          862..1003
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   1139 AA;  125255 MW;  1630E1B351E4B23F CRC64;
     MSLLFNRPAP VHCTFTVKPE QRAQAGALGH VDEETVFLGS KLWTKFASND VTRACISIAP
     IRPYPTNPSL LSSVSCWAIL SQTVNEDALA IPPAWLTTYS HIFSRDALEN SANREFLSVL
     SVRPVPLKEV IVTALSQEAY LAASRRDTVL ESWFSDARPI LRYGDVHSFG STVNEHLAPA
     TLDNVQYRLT MLQPVLQGYA ERNTTKLIVT LLEPVNQQPS EFLKTTCGDS DGIEIDESFL
     ANSFLRPSFI TSLKGLDGRS PQDIHHIFQV GWLSERHSFK PVSSATGLLE DNCTVYLRTA
     DLARIGILNG DWAVAGAHSS RLRLVRVMAN DILVTSIGRM AISPVLLHNM YPDSDAIFEP
     PTTIHLLPSP FGPYQPPIPT ARTLTVARVA SPLSINRAYQ GLFLSSLKGY FEVTQRLIKR
     GDVIGVPIDT DLSRSARKID SGDHQIETDH DYPGSVLRPN EVVYFVVTNV EYDVMGKDLS
     SQPEDMYLGS TLGELGCWVD TAATRVVQTG LEHMRIPDIG GYLDWDQTNP RAIFSALLKQ
     SSFLLRPSAP FGKIFSLSSA ALARSAIDYD LQLSLLLKGA RGIGKFTTAS WVAQRLGMHL
     FEIDCYDILG ESKAETEGFL RTRFDQAKAC TPCIVVLRRL EALSQTTQAL EPNKESAVLT
     ILREGIDGVR KSWAVTGYPA IVLGTTCEPA SVPLGILACF KHEINFEASP DWYTKTVRKL
     TYHSKAPNER ERLEILRCLL QNSSLAPDVS LVNLATQTAA LVPADLTDLV TRAKSGSIER
     IMRAIECEED HLDLAEISLT AGDFETALGK ARESYSESIG APKIPNVSWD DIGGLAHVKS
     DILDTIQLPF DHPELFSDGL KKRSGILLYG PPGTGKTLIA KAVATSCSLN FFSVKGPELL
     NMYIGESEAN VRRVFQRARD AKPCVIFFDE LDSVAPKRGN QGDSGGVMDR IVSQLLAELD
     GMSGSKAGAD VFVIGATNRP DLLDPALLRP GRFDRLLYLG VSESHQAQVN ILEALTRNFR
     LDRDVDLCRI AEQCPFNYTG ADFYALCSDA MLNAMSRKAD FLESKIADIN KLPESLGQHP
     YPMTPQYFLS ELASADDLLV AVSQVDFDNA LVTLVPSVTQ AEMEHYARVQ HHFSQGANI
//
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