ID A2QQR8_ASPNC Unreviewed; 798 AA.
AC A2QQR8;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Contig An08c0100, genomic contig {ECO:0000313|EMBL:CAK45384.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:CAK45384.1};
GN ORFNames=An08g03480 {ECO:0000313|EMBL:CAK45384.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK45384.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK45384.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; AM270165; CAK45384.1; -; Genomic_DNA.
DR RefSeq; XP_001392464.1; XM_001392427.2.
DR AlphaFoldDB; A2QQR8; -.
DR EnsemblFungi; CAK45384; CAK45384; An08g03480.
DR GeneID; 4982662; -.
DR KEGG; ang:An08g03480; -.
DR VEuPathDB; FungiDB:An08g03480; -.
DR HOGENOM; CLU_005070_4_0_1; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000006706; Chromosome 8R.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0034605; P:cellular response to heat; IEA:EnsemblFungi.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR GO; GO:0043335; P:protein unfolding; IEA:EnsemblFungi.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:CAK45384.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 116..260
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 516..709
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 694..785
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 329..409
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 798 AA; 88274 MW; 5562EB786BBFBEBD CRC64;
MSSRLQLARG RLLRPSSLPS SNRVLQPSQA LRLLARTRIA NLARHPSVLP IRTYANGRPH
PPGGTHRMNL GGEPEKSALE QFGVDLTARA KAGKLDPVIG RDAEIHRTIQ VLSRRTKNNP
VLIGAAGTGK TAVLEGLAQR IVQGDVPESI KDKRVIALDL GSLIAGAKFR GDFEERLKSV
LKEVEDAQGG VILFIDELHT LLGLGKAEGS IDASNLLKPA LSRGELQCCG ATTLNEYRLI
EKDVALARRF QPIQVGEPSV AATISILRGI KNKYEVHHGV RITDGALVAA ATYSNRYITD
RFLPDKAIDL VDEAASALRL QQESKPDVIR ELDRDITTIQ IELESLRKET DVSSRERRDK
LQEDLKVKQE EARKLTEVWE KEKAEIEELK RAKEELERAR FELEKAQREG NFAKAGELRY
ATIPSLEAKL PKEGEEQATK AQTSLIHDSV TADDIGNVVS RTTGIPVNKL MAGEVEKLIK
MEDTLRKSVR GQDEALSAVA NAVRMQRAGL SGENRPLASF MFLGPTGVGK TELCKKMAEF
LFSTETAVVR FDMSEFQEKH TISRLIGSPA GYVGYDDAGQ LTEAVRRKPY AVLLFDEFEK
AHRDISALLL QVLDEGFLTD SQGHKVDFRN TLIVLTSNLG ADILVGADPL HPYKEGGDNE
LSPETKKSVM DVVQSAYPPE FLNRIDEFII FKRLSRDALR DIVDIRVKEL QSRLDDRRMT
LQVDDEIKDW LCDKGYDPKY GARPLNRLIA KEIGNKLADK IIRGEVTSGQ TARVTFNADK
SGLAVAAEAP VATETESS
//
