ID W7HUI4_9PEZI Unreviewed; 928 AA.
AC W7HUI4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Heat shock protein hsp98 {ECO:0000313|EMBL:EWC47149.1};
GN ORFNames=DRE_03518 {ECO:0000313|EMBL:EWC47149.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC47149.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC47149.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC47149.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) 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; KI966412; EWC47149.1; -; Genomic_DNA.
DR AlphaFoldDB; W7HUI4; -.
DR HOGENOM; CLU_005070_1_0_1; -.
DR Proteomes; UP000024837; 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:SF194; 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; 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|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:UP000024837};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:EWC47149.1}.
FT DOMAIN 4..164
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 899..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 433..547
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 905..928
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 103773 MW; DF99A416D21BA518 CRC64;
MSGPGGHDYT DRALRAIQNS IELAQQYDHV EIRPINLAVS LLTPPPDDSK PGVTDAVPQG
PLLFRQAVER ANGDFQTLDR ELKKALVRSP SQNPPPDHVT FSPSMSKALR KAHDLQKLQK
DKFIGVDHLI MSVVEDATVQ TALKNANVPQ IKVLQDAIAA IRGDRRMDSK TADAESPNET
LSKYTIDMTA QAREGKLDPV IGREEEVRRV IRILSRRTKN NPVLIGEPGV GKTSVAEGLA
QRIVAADVPA NLAQCKLLSL DVGALVAGSK YRGEFEERMK SVLKEIEESK EMIVLFIDEI
HLLMGAGSSG EGGMDAANLL KPMLARGKLH CIGATTLAEY RKYIEKDAAF ERRFQQVIVK
EPSLPETISI LRGLKERYEV HHGTTILDSA LVTSATLAQR YLTSRKLPDS AIDLMDEACS
AVRVARESQP EALDHLERKL RQIEIEIHAL EREKDAASKE RLEIARKEAA NVQEELRPIR
EKYESEMRRS NELQDLKKRL EEKRHRREAL ERERRFGEVY DLDKHVIPEL EDRIQLLERQ
KVQAEVDQLS NLTGEGEAPL VTDVVGPDQI NEIVAKWTGI PVTRLKTTEK EKLLNMEKYL
SKAVVGQKEA VKGVSNAIRL SRSGLNNPNQ PIASFLFCGP SGTGKTLLAK SLAEFLFDDP
KSMIRFDMSE YMEKHSVSRL IGAPPGYVGH DSGGQLTEAL RRKPFSILLF DEVEKAAKEV
LTVLLQLLDE GRITDSQGRI VDGKNTVIIL TSNLGAEYLT SRRSSHGKID SETRELVMDA
IRRHFLPEFI NRLSSIVIFN QLDRHGIRKI VDLRLAEVQK RLADNGRNIH IVVNDPAKDY
LAQAGFSQAY GARVMQRVIE KEVLNPLAVL ILKGAVRDGE QAHVVLSTEG NREKVIVVPN
HESESDMEDD VEMDLSDVDD KMDDDLYD
//
