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Database: UniProt
Entry: A0A2I2G5T5_9EURO
LinkDB: A0A2I2G5T5_9EURO
Original site: A0A2I2G5T5_9EURO 
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
//
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