ID G2WYM1_VERDV Unreviewed; 1369 AA.
AC G2WYM1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Peroxisomal ATPase PEX6 {ECO:0000256|ARBA:ARBA00034811};
DE AltName: Full=Peroxin-6 {ECO:0000256|ARBA:ARBA00034920};
GN ORFNames=VDAG_03113 {ECO:0000313|EMBL:EGY21673.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY21673.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(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 -!- 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; DS572699; EGY21673.1; -; Genomic_DNA.
DR RefSeq; XP_009655273.1; XM_009656978.1.
DR STRING; 498257.G2WYM1; -.
DR EnsemblFungi; EGY21673; EGY21673; VDAG_03113.
DR GeneID; 20704576; -.
DR KEGG; vda:VDAG_03113; -.
DR eggNOG; KOG0736; Eukaryota.
DR HOGENOM; CLU_000688_0_2_1; -.
DR InParanoid; G2WYM1; -.
DR OMA; KIMLCEP; -.
DR OrthoDB; 7477at2759; -.
DR Proteomes; UP000001611; Chromosome 6.
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; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 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 SMART; SM00382; AAA; 2.
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:UP000001611}.
FT DOMAIN 733..860
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1014..1156
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 128..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..314
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1369 AA; 146962 MW; 2E532950B0A60732 CRC64;
MASAILAKRR RRRRRADKPA AAATLLLDGN VKGDVGFLSD DLFADLFPQL SNSIAPWAPT
ASPTKTSWTL VPVLKNPELG PLYPAVFPEV PGPAVLPHGS AAPGPLQAHG QRPAVALRFS
SSMPLPCRST PSLSNLEKES IKASGNRARA ISSTATPTTT PRPRPKGKTA TSPEDHLTEA
LRVALGSVAV IHSGDQFLLP LPPHPVTHVP PNGGEIVMCE PYNQGILTPD TKIVLMRGNV
RAKSGRTPAA MAANRGLNGV PEDDEDTAND QFYSAAEERY KTDAQVTEME TVTETEESEA
SGLEQDDESS DDSMDDMISL QAPMLHTTNA SGVSTMQPGS PMTIGRGRRT NGIATPGSVF
SSYTATTARP DRPRGRLFKA QGLMEQIPQV LLHPKPTPED DEEARIFVDI SSLLKIGCFS
GDWVRVEAAE EPPAHGFGAF GLGGLNSLNA LEDGPEPNWR PVRVYSLPEG YTQKPVTRIP
SSRHLQRKPS FFESQTQKPT GPAAYISPIL LANLESPAYL RLSPLKPSTP QGKRTAAKFS
RASHPPFARD ITIHQVRSPI SVERAYQTVV LAGLKRYFAE KVRIAKAGDL IAVPIDTLLG
KMFQDAEVDN IISLSNDTSK ANQVAWFKVG HVQAQKRDED DDLIEDLWKG VACIDSETVG
MNLSGFVTAR PPASLSSTWE YYTGVKKAPI RSLAAPTPAL PSQDQRYISP LRHRLQALLA
AATSPAAIHG RMSPVAILLT STHRYIGKST VATAACADVG LHTYPIDAND LLSEAEGSGS
DVKTEGFLKA RAERGLSCGA DCTVLLFKHI EGLTADRMVS TMKGLLQESR VLIATTNDVD
KLPKGLRSLF TYELEMGAPD EVERAGILRS VVDDMGLDLD LDVEISGVAL KTAAFVAGGL
VDAVERARIA RNLRLEDMSR KASSDNRIVT VRDVEVSGGP QATGCPAARS VTKTDFDVAV
EKARKNFAGA IGAPKIPNVT WDDVGGLQYV KDAVKETIQL PLERPELFAK GLKKRSGILF
YGPPGTGKTL LAKAIATEYS LNFFSVKGPE LLNMYIGESE ANVRRVFQKA RDARPCVVFF
DELDSVAPKR GNQGDSGGVM DRIVSQLLAE LDGMSGGSDG GGGVFVIGAT NRPDLLDPAL
LRPGRFDKML YLSVADTRET QLKILEAVTR KFTLHPSLSL DRVASQLPYH YTGADYYALC
SDAMLKAITR QTSSVDAKVA AINAARGPDQ HPISTANFFD HHATAEDIAV VVTEEDFLAA
DRELVPSVSA GELARYETMR RSFEGPAQKE GQEAEVARPG GGAARAVSGE SVASSKGKGK
APARDKGKGK ALAVDSDDDD DRAPNGRVNK GKGKAAFQHG TADDDDELY
//
