ID C1GUD5_PARBA Unreviewed; 926 AA.
AC C1GUD5;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE SubName: Full=Heat shock protein HSP98 {ECO:0000313|EMBL:EEH39941.1};
GN ORFNames=PAAG_02130 {ECO:0000313|EMBL:EEH39941.1};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH39941.1, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH39941.1, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; KN293995; EEH39941.1; -; Genomic_DNA.
DR RefSeq; XP_002796242.1; XM_002796196.2.
DR AlphaFoldDB; C1GUD5; -.
DR STRING; 502779.C1GUD5; -.
DR GeneID; 9099387; -.
DR KEGG; pbl:PAAG_02130; -.
DR VEuPathDB; FungiDB:PAAG_02130; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_2_1; -.
DR OMA; ERMKAVM; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000002059; Partially assembled 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; 2.
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:UP000002059};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:EEH39941.1}.
FT DOMAIN 1..165
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 44..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..548
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 46..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 102870 MW; 5C7F135C7A2D7F19 CRC64;
MNGTQLTDRA NQALVDAHAL AEQHAHPQLL PIHLAVSLLD PPVDESKDQQ VTTHPSHQAS
SGSLFKRVVE KAHGDPQQLR RALNKSLVRL ASQDPPPETI SPSPAFAKVL RAASNLSKTQ
KDTYVAIDHL IAALAQDPTI QRALADANIP NVKMIDSAIQ QIRGMKRVDS KTADTEEESE
NLKKFTVDMT AMAREGKIDP VIGREEEIRR VIRILSRRTK NNPVLIGEPG VGKTTVVEGL
ARRIVNADVP ANLANCKLLS LDVGSLVAGS KYRGEFEERM KGVLKEIEES KETIVLFVDE
IHLLMGAGSS GEGGMDAANL LKPMLARGQL HCIGATTLGE YRKYIEKDQA FERRFQQVLV
KEPTVGETIS ILRGLKERYE VHHGVNILDG AIVSAANLAS RYLTARRLPD SAVDLIDEAA
AAVRVTRESQ PEALDTLERR ARQLQIEIHA LAREKDAASK ARLEAAKQEA ANVNEELRPL
REKYESEKQR SKDIQDAKIK LDLLKVKRDE ATRSGDTQTA SDLIYYAIPD VEKRIEQLEA
ERARQDAELS AQPGAGETLM ADAVGPEQIN EIVARWTGIP VTRLRTTEKD RLLHMESHLS
KIVVGQKEAV QSVSNAIRLQ RSGLSNPNSP PSFLFCGPSG TGKTLLTKAL AEFLFDDPKA
MIRFDMSEYQ ERHSLSRMIG APPGYVGHDA GGQLTESLRR RPFSILLFDE VEKAAKEVLT
VLLQLMDDGR ITDGQGRIVD AKNCIVVMTS NLGAEFLQRP TASNGQIDPT TKELVMGALR
NYFLPEFLNR ISSIIIFNRL TRREIRKIVD VRLQEIQRRL EQNDRTVTID CTDEVKDYLG
NAGYSPVYGA RPLSRLIEKE VLNRLAVLIL RGAIKDGETA RVVMQEGRIT VLPNHVETES
EDEEMIDESD TLAEMEEDMG ERDLYE
//