ID   PEX6_ARTOA              Reviewed;        1183 AA.
AC   G1X4S3;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Peroxisomal biogenesis factor 6 {ECO:0000303|PubMed:35323036};
DE   AltName: Full=Peroxin-6 {ECO:0000250|UniProtKB:P24004};
GN   Name=PEX6 {ECO:0000303|PubMed:35323036}; ORFNames=AOL_s00043g697;
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491;
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=35323036; DOI=10.1128/spectrum.00275-22;
RA   Liu Q., Li D., Jiang K., Zhang K.Q., Yang J.;
RT   "AoPEX1 and AoPEX6 are required for mycelial growth, conidiation, stress
RT   Response, fatty acid utilization, and trap formation in Arthrobotrys
RT   oligospora.";
RL   Microbiol. Spectr. 10:e0027522-e0027522(2022).
CC   -!- FUNCTION: Peroxisomal biogenesis factor that has pleiotropic roles in
CC       various cellular processes (PubMed:35323036). Regulates autophagy and
CC       biogenesis of peroxisomes and Woronin bodies (PubMed:35323036). Plays
CC       important roles in mycelial growth and development and stress response
CC       (PubMed:35323036). Is also essential for conidiation and fatty acid
CC       utilization (PubMed:35323036). Required for nematode predation via trap
CC       formation (PubMed:35323036). {ECO:0000269|PubMed:35323036}.
CC   -!- SUBUNIT: Interacts with PEX1 to form a high-molecular-mass
CC       heterooligomer in the cytosol (By similarity). The PEX1-PEX6
CC       heterooligomers associate with the peroxisomal importomer via
CC       interaction of PEX6 with the peroxisomal membrane anchor PEX15 (By
CC       similarity). {ECO:0000250|UniProtKB:P24004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P24004}.
CC       Peroxisome membrane {ECO:0000250|UniProtKB:P24004}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:P24004}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P24004}. Note=Shuttles between the cytoplasm and
CC       the peroxisomal membrane. {ECO:0000250|UniProtKB:P24004}.
CC   -!- DOMAIN: AAA-cassette D1 is required for interaction with PEX1 (By
CC       similarity). ATP-binding in AAA-cassette D1 is required for attachment
CC       to PEX15 (By similarity). ATP-binding and hydrolysis in AAA-cassette D2
CC       is required for release from PEX15 and proper function in PEX5
CC       dislocation (By similarity). {ECO:0000250|UniProtKB:P24004}.
CC   -!- DISRUPTION PHENOTYPE: Leads to growth defects with sparse aerial
CC       hyphae, and reduced number of nuclei in hyphal cells (PubMed:35323036).
CC       Results also in complete elimination of sporulation and trap formation
CC       and a remarkable decrease in the ability to trap nematodes
CC       (PubMed:35323036). Leads to defective cell wall biosynthesis and
CC       increased stress susceptibility (PubMed:35323036). Results in the up-
CC       regulation of the proteasome, membranes, ribosomes, DNA replication,
CC       and cell cycle functions, and the down-regulation of MAPK signaling and
CC       nitrogen metabolism (PubMed:35323036). {ECO:0000269|PubMed:35323036}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; ADOT01000060; EGX51963.1; -; Genomic_DNA.
DR   RefSeq; XP_011119485.1; XM_011121183.1.
DR   STRING; 13349.G1X4S3; -.
DR   EnsemblFungi; EGX51963; EGX51963; AOL_s00043g697.
DR   GeneID; 22890437; -.
DR   eggNOG; KOG0736; Eukaryota.
DR   HOGENOM; CLU_000688_0_2_1; -.
DR   InParanoid; G1X4S3; -.
DR   OMA; MVQAGSE; -.
DR   OrthoDB; 233419at2759; -.
DR   Proteomes; UP000008784; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 2.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Membrane; Nucleotide-binding; Peroxisome;
KW   Reference proteome; Virulence.
FT   CHAIN           1..1183
FT                   /note="Peroxisomal biogenesis factor 6"
FT                   /id="PRO_0000456238"
FT   REGION          576..785
FT                   /note="AAA-cassette D1"
FT                   /evidence="ECO:0000250|UniProtKB:P33760"
FT   REGION          878..1070
FT                   /note="AAA-cassette D2"
FT                   /evidence="ECO:0000250|UniProtKB:P33760"
FT   BINDING         883..890
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1183 AA;  126938 MW;  301554555062C344 CRC64;
     MPITHVALSP SPIPAPTSCA SPWIVIPTTI PPLNSSQFPT IPLSTILLPA SGAPHPLWEA
     FANQPSLRAE NGIKFPIQLT ATTPIALTSV VVGFFSTGEE GLFDEETIEE MITKGLDDMR
     VVHTGDIVRV QWMSVLARVR LCEPVDQGVI TEDTKVIVVK ESRGKKTGEP EDGPLANGID
     LNGVDDSDSD EDVLSQGDDD DENNVDLPGV STFMDIATTL GTPSISTPLR NGPGASISGL
     SDAPKVVKFT AKPLSQKIPT TLLLPTPPAA DDAEARVYVR VNELMGLGCF SGDWIGVASD
     HGLFGDRLPN GSRAWRPAKV YSLPELYAGK EKVKVLMKGC VYMSPLLHAN LGSPSSVVLT
     KSPFMNPSNI QQGALLSPVT TAPPSSATPQ IPPTAKEVTL LRISTPISTD RALQPSLLAG
     LKTYFETSRK MVKVGDLIPV LIDESLGRNL FSPAALLPPD AENAEEIPGA GDELLYGSHG
     GAGIGVNNTG KLCAAWFRVG TIAPTDEATN AFSNGMTSQQ WGGVAIVDPG STRMVQAGSE
     RGRIPPTLNS PWEYYLNIVP PPIPNNPPPI HPALELPNNY ISPVHRRLRE LISAATSLRS
     IKLGLAPLAV LLTSTQRSIG KRLLAYRAAS DVGVHIFHID AYDIIGEGGQ ASDVKTEAYL
     RARSERAASC GIENCVLLIS HIEAFTAERM AEALRDIVAD MRIVIATTTD VDKVPEPVRN
     VFTHELEVGA PDEGERTGLL RQITQERGVR LAKEIDLSTI ALKTAALVAG DLVDVVERAM
     TACSERMEGL AAEMEGVTVR DIQLAGGDAS CLNKQDFEAA VDAARKNFAD SIGAPKIPNV
     SWDDVGGLAN VKSAVMETIQ LPLERPELFA KGMKKRSGIL FYGPPGTGKT LLAKAIATEF
     SLNFFSVKGP ELLNMYIGES EANVRRVFQR ARDARPCVVF FDELDSVAPK RGNQGDSGGV
     MDRIVSQLLA ELDGMSEGKE GSGGVFVIGA TNRPDLLDPA LLRPGRFDKM LFLGVSDTHH
     KQLTILEALT RKFTLHNSLS LAKISETLPF TYTGADLYAL CSDAMLKAIT RQASKVDQKI
     KEMENPVSTA YFFDYLATPD DVAVAVTEDD FMEAKKELIG SVSQKELEHY DRVRQMFETV
     DEKKGDATVD KKGKGRAIEI MVDGPGTGGE GAFGDDGDEE GLY