ID A0A2S4L9K5_9HYPO Unreviewed; 926 AA.
AC A0A2S4L9K5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Heat shock protein hsp98 {ECO:0000313|EMBL:POR39134.1};
GN ORFNames=TPAR_00666 {ECO:0000313|EMBL:POR39134.1};
OS Tolypocladium paradoxum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=94208 {ECO:0000313|EMBL:POR39134.1, ECO:0000313|Proteomes:UP000237481};
RN [1] {ECO:0000313|EMBL:POR39134.1, ECO:0000313|Proteomes:UP000237481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRBC 100945 {ECO:0000313|EMBL:POR39134.1,
RC ECO:0000313|Proteomes:UP000237481};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (JAN-2018) 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:POR39134.1}.
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DR EMBL; PKSG01000069; POR39134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4L9K5; -.
DR STRING; 94208.A0A2S4L9K5; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000237481; 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; 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:UP000237481};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:POR39134.1}.
FT DOMAIN 3..162
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 893..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 431..518
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 898..926
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 103302 MW; A853F2B56521DD56 CRC64;
MTARMDFTDR AQKAVEDAMA LAEQYAHSQL VPVHLAVSLL DPPVDQSKDQ QNGPPQPTFT
LFRQVVERAH GDSQLFDRAL KKMLVRLPSQ DPPPEQVSLS PSFHGVLRKA MELQKVQKDT
FIGVDHLITA LSEDGNIQTA LREGNIPKAK LVQDAVAAIR GTKRVDSKTA DTEQENENLA
KFTIDMTAMA RDKKVDPVIG REEEIRRVVR ILSRRTKNNP VLIGEPGVGK TTVVEGLAQR
IVNRDVPDNL KNCKLLSLDI GALVAGSKYR GEFEERMKGV LKEIQDSKEM IVLFVDEIHL
LMGAGSSGEG GMDAANLLKP MLARGQLHCI GATTLAEYRK YVEKDAAFER RFQQVLVKEP
TIPETVSILR GLKERYDRHH RVTILDSALV AAANLAARYL TSRRMPDSAI DLVDEAAAAV
RVARESQPEI IDSLDRKLRQ LMIEIAALEK EHDEASKTRL QQARKDAQNV EEELEPLRAK
YRNEIKRSEE IHQAKVKLDD LEKRLEEAMD NMEHAKAADL QYGAIPEQKA VIKELEARKA
AADAALSATG ADIGGSMVTD IVTADHINEI VARWTGIPVT RLRTSEKEKL LHMEKVLGKV
VVGQKEAVQS VANSIRLQRS GLSNPNQPPS FLFCGPSGTG KTLLTKALAE FLFDDPKAMI
RFDMSEYQER HALSRMIGAP PGYVGHDAGG QLTEALRRKP FSILLFDEVE KAAKEVLTVL
LQLMDDGRIT DGQGRVVDAK NCIVVMTSNL GAEYLTRPGA KEGRVDATTR ELIMTSLRNY
FLPEFLNRIN SVVIFNRLTR REIRKIVDLR IIEIQKRLED NGRKVYIDVS EEAKDYLGNS
GYSPAYGARP LARLIEKEVL NRLAILILRN NICDGEIARV ELVEGKIVVL SNHPDSEMGE
DEDMDEDEDD AVDELVGDNM DEDIYD
//