ID G4U5B8_NEUT9 Unreviewed; 1338 AA.
AC G4U5B8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Peroxisomal ATPase PEX6 {ECO:0000256|ARBA:ARBA00034811};
DE AltName: Full=Peroxin-6 {ECO:0000256|ARBA:ARBA00034920};
GN ORFNames=NEUTE2DRAFT_78493 {ECO:0000313|EMBL:EGZ77244.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ77244.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ77244.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(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; GL890999; EGZ77244.1; -; Genomic_DNA.
DR STRING; 510952.G4U5B8; -.
DR eggNOG; KOG0736; Eukaryota.
DR HOGENOM; CLU_000688_0_2_1; -.
DR Proteomes; UP000008513; 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; 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; 1.
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:UP000008513}.
FT DOMAIN 707..835
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 980..1122
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..318
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1338 AA; 143584 MW; A56E2421FF3A1018 CRC64;
MTAPNSAPAS SRKRVRRRRQ DKPALSAKLV LDAHVKGDVG VIATDLFADL FPHLWANGDS
QDTVHVAIAP WAPSQTPEAN NWSIVPVIRS STVAPSTVQF SPSSLALQSF ATHLQQAAPS
KLSGHNKGGI EILILDVSPI ELDTVFVNLD GELAKRLEDG EGTFFREHPV NGKGKARADA
TPEEHLTAAL RTALSSLKIV HSGDLFPLPL PPHPITHQPP NPGRITLCEP VAQGILAPTT
KIIVSRGRTT SKTKRSSASG QQQGRKLNGV AEDDEDAYFS AAEEDRDSKT DAQTAETDAD
DTEFEPQAGE DEDNLSDDSL DGIISLQVPT LPTTVTGQST IGTGTPTMLR GRKTNGPGSV
ISSYTATTAR PDRPRGRLFK AQGLMKPIPP DLLHPKPTSE DDEEACIYVD MRDLTRVGCF
SGDWVRVEAA SEPPSNGLGA FGLGSFVEQE ADEINWRPAR VFGLPEGYSS RSATRSHHSR
HDSRNSSFFE AQSQNSSLKP PFAREVILQH VRTPTAVERD VQSAVMAGLK HYFERRLRVL
KTGDLIAVPI DTQLGKALQE STIPGEDSAI DEVLGLIAAT RPGQSLHYDD VAWFRVGHVQ
AMKQDITEAV GGEEAEDLWG GIACVDISLT HLERKGSVTG RVPGTISNSW QYYLGIRKLP
KHQQSPGLPA QLQILEPEKQ YVSSLRRKLR ELMAAATSKP ALHLNLPPLA ILLVSTQRHI
GKAATAMQAC SDIGLHTFAI DAYDIVNDGG GGGGSDVKTA GFLTSRAERA MSCGPESCVL
LVRHIEALTA DRMVSSIKEI LADARVLIAT TTEVEKVPDG IRALFTHELE MSAPDEQERE
GILSSILADR GIGLDHGVDL SGIALKTAAL VAGDLVDVVD RALVAQRSRL EKLTAKTTGS
ITFRDVQLAG GPAASGLTKQ DFELAVDAAR KNFADSIGAP KIPNVTWDDV GGLGNVKDAI
TETIQLPLER PELFAKGMKK RSGILFYGPP GTGKTLLAKA IATEYSLNFF SVKGPELLNM
YIGESEANVR RVFQRARDAR PCVVFFDELD SVAPKRGNQG DSGGVMDRIV SQLLAELDGM
SGGEGGGGGV FVIGATNRPD LLDPALLRPG RFDKMLYLGV SDTHDKQVTI MEALTRKFTL
HPTVSLRSVA ERLPFTYTGA DFYALCSDAM LKAVTRQATL VDTKIRELNA AAGPEGKHIS
TAYFFDHYAT KEDISVMVTE QDFLDAHREL VPSVSAGELE HYEQVRAMFE GAKDKDKKKE
GADGDGNGVD GLESGNGNGM LAITMGDDGA GAESTKKDGK GKGKAADNEV NGAGKGKGKE
GVSPFQESGG DEDEGLYD
//
