ID A0A5N5X249_9EURO Unreviewed; 810 AA.
AC A0A5N5X249;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KAB8074065.1};
GN ORFNames=BDV29DRAFT_174357 {ECO:0000313|EMBL:KAB8074065.1};
OS Aspergillus leporis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=41062 {ECO:0000313|EMBL:KAB8074065.1, ECO:0000313|Proteomes:UP000326565};
RN [1] {ECO:0000313|EMBL:KAB8074065.1, ECO:0000313|Proteomes:UP000326565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 151.66 {ECO:0000313|EMBL:KAB8074065.1,
RC ECO:0000313|Proteomes:UP000326565};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ML732216; KAB8074065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5X249; -.
DR Proteomes; UP000326565; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:SF176; 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|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:KAB8074065.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000326565}.
FT DOMAIN 120..264
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 519..712
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 697..788
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 333..413
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 810 AA; 89773 MW; 756A90740A30D079 CRC64;
MASRLFTRGR LLRSPALSSL NRTFRPTQQL RLPSQARIIP SLVTKTSLFQ PIYLVRNYAN
GRPHPPGGTH RMNLGGEPEK SALEQFGVDL TAKAKAGKLD PVIGRDSEIH RTIQILSRRT
KNNPVLIGAA GTGKTAVLEG LAQRIVQGDV PESIKDKRVI SLDLGSLIAG AKFRGDFEER
LKSVLKEVEE AQGGVILFID ELHILLGLGK AEGSIDASNL LKPALSRGDL QCCGATTLNE
YRLIEKDVAL ARRFQPIMVG EPSVAATISI LRGIKNKYEV HHGVRITDGA LVAAATYSNR
YITDRFLPDK AIDLVDEAAS ALRLQQESKP DVIRELDRDI TTIQIELESL RKETDVSSRE
RREKLQEDLK SKQEEAAKLT EVWEKEKAEI ETLKRTKEDL ELARFELEQA QREGNFAKAG
ELRYSKIPSL EAQLPKEGEE QATGPQALIH DSVTPDDIAN VVSRTTGIPV NKLMAGDVEK
LIRMEDTLRQ SVRGQDEALS AVANAVRMQR AGLSGENRPL ASFMFLGPTG VGKTELCKKM
AEFLFSTETA VVRFDMSEFQ EKHTISRLIG SPAGYVGYDD AGQLTEAVRR KPYAVLLFDE
FEKAHRDISA LLLQVLDEGF LTDAQGHKVD FRNTLIVLTS NLGADILVGS DPLHSHKLSE
GDEVSPQIKK AVMDVVQHAY PPEFLNRIDE FIIFKRLSRE ALRGIVDIRL KELQSRLDDR
RITLQVDSDI KDWLCERGYD PRYGARPLNR LIAKEIGNRL ADRIIRGEVI SGQSAHVSLN
ADKSGLEVTA QGTMAADATN STYPTEAENP
//