ID A0A2I2G5T5_9EURO Unreviewed; 927 AA.
AC A0A2I2G5T5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Putative heat shock protein Hsp98/Hsp104/ClpA {ECO:0000313|EMBL:PLB48237.1};
GN ORFNames=P170DRAFT_410932 {ECO:0000313|EMBL:PLB48237.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB48237.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB48237.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB48237.1,
RC ECO:0000313|Proteomes:UP000234275};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLB48237.1}.
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DR EMBL; MSFO01000005; PLB48237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2G5T5; -.
DR STRING; 1392250.A0A2I2G5T5; -.
DR VEuPathDB; FungiDB:P170DRAFT_410932; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000234275; 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; 1.10.1780.10; Clp, N-terminal domain; 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; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
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 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000234275};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:PLB48237.1}.
FT DOMAIN 1..165
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 42..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..548
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 897..927
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 103000 MW; 7C990CA36643E64E CRC64;
MNGASFTDRA NKALLDSSSL AEQYAHLQIL PLHLAVALLN PSPDESKDQE APAHPSHEGA
SAPLFRQVVE RAHGDPQLLD RALMKMLVRL PSQDPPPETV SVSPALAKVI RSATDLSKTQ
KDSFVAIDHL ILAIAQDSQV QRALADSNIP NVKLIDNAVQ QIRGSKRVDS KTADSESENE
NLKKFTIDMT SMAREGKIDP VIGREEEIRR VIRILSRRTK NNPVLIGEPG VGKTTVVEGL
ARRIVNADVP ANLAQCRLLS LDVGSLVAGS KYRGEFEERM KGVLKEIEES KETIVLFVDE
IHLLMGAGSS GEGGMDAANL LKPMLARGQL HCIGATTLGE YRKYIEKDQA FERRFQQVLV
KEPSINETIS ILRGLKEKYE VHHNVNILDG AIVSAASLAA RYLTARRLPD SAVDLIDEAA
AAVRVTRESE PEALDNLERK HRQLQIEIHA LERETDEASK TRLEAAKQEA ANVTEELRPM
REKYESEKAR SKSIQDAKIK LDSLKVKRDE AERMGDTQTA ADLEYYAIPE TKTLIDRLET
ERAKADAEQR ARGGDNGEAL LADSVGPDQI NEIVARWTGI PVTRLKTTEK DKLLKMEKYL
GKLVVGQKEA VTSVSNAIRL QRSGLSNPNS PPSFLFCGPS GTGKTLLTKA LAEFLFDDPR
AMIRFDMSEY QERHSLSRMI GAPPGYVGHD AGGQLTESLR RRPFSILLFD EVEKAAKEVL
TVMLQLMDDG RITDGQGRIV DARNCIVVMT SNLGAEYLAR PATKDGRIDP QTRELVMDAL
RGYFLPEFLN RISSTVIFNR LTRREIRKIV DLRLAEVQKR LDENNRKVTI ECSEDVKDYL
GESGYSPAYG ARPLGRIIER EVLNRLAVLI LRGGIRDGEV ARVVMRNGHI DVLPNHESSD
DEDEDMVDSD DALAEMEDEN GDMDLYE
//