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Database: UniProt
Entry: A0A2B7XU65_9EURO
LinkDB: A0A2B7XU65_9EURO
Original site: A0A2B7XU65_9EURO 
ID   A0A2B7XU65_9EURO        Unreviewed;       928 AA.
AC   A0A2B7XU65;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Hsp98-like protein {ECO:0000313|EMBL:PGH12027.1};
GN   ORFNames=AJ79_04536 {ECO:0000313|EMBL:PGH12027.1};
OS   Helicocarpus griseus UAMH5409.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX   NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH12027.1, ECO:0000313|Proteomes:UP000223968};
RN   [1] {ECO:0000313|EMBL:PGH12027.1, ECO:0000313|Proteomes:UP000223968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH12027.1,
RC   ECO:0000313|Proteomes:UP000223968};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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:PGH12027.1}.
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DR   EMBL; PDNB01000064; PGH12027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7XU65; -.
DR   STRING; 1447875.A0A2B7XU65; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000223968; 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:UP000223968};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..165
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          434..555
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   928 AA;  103011 MW;  2B6428A04DA112C3 CRC64;
     MNGAQLTDRA TQALSDAQAL AEQHAHPQLL PIHLAVSLFD PPADESKDQQ VTAHPSHQAS
     SISLFRRVVE KAHGDPQQLG RALNKSLVRL PSQDPPPEHI ALSPAMAKVI RSASNLAKTQ
     KDSYVAIDHL ITALAQDPTI QRALADANVP NVKLIDSAIQ QIRGMKRVDS KTADTEEESE
     NLKKFTIDMT SMAREGKIDP VIGREEEIRR VIRILSRRTK NNPVLIGEPG VGKTTVVEGL
     ARRIVNADVP ANLSNCKLLS LDVGSLVAGS KYRGEFEERM KGVLKEIEDS KETIVLFVDE
     IHLLMGAGSS GEGGMDAANL LKPMLARGQL HCIGATTLGE YRKYIEKDQA FERRFQQVLV
     KEPSVSETIS ILRGLKERYE VHHGVNILDG AIVAAANLAS RYLTARKLPD SAVDLIDEAA
     AAVRVTRESQ PEALDTLERR ARQLQIEIHA LEREKDAASK ARLDAAKQEA ANVNEELRPL
     REKYESEKQR SKDVQDAKIK LDLLKVKRDE ATRSGDTQTA SDLIYYAIPD VEKRIEQLEA
     ERARADAEQS AQQGEEGETL MADAVGIEQI NEIVARWTGI PVTRLRTSEK DRLLHMESHL
     GKIVVGQKEA VQSVSNAIRL QRSGLSNPNC PPSFLFCGPS GTGKTLLTKA LAEFLFDDAK
     SMIRFDMSEY QERHSLSRMI GAPPGYVGHD AGGQLTEALR RRPFSILLFD EVEKAAKEVL
     TVLLQLMDDG RITDGQGRIV DAKNCIVVMT SNLGAEYLQR PTGSNGQIDP TTKELVMGAL
     RNYFLPEFLN RISSIIIFNR LTRREIRKIV DVRLQEIQRR LEQNDRSVEI ECTDEVKDYL
     GSAGYSPVYG ARPLSRLIEK EVLNRLAVLI LRGAIRDGEK ARVVMEEGRV TVLPNHVDGE
     SEDEEMIDED EAIAEMEEDA MGEQDLYE
//
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