ID A0A1V8SES1_9PEZI Unreviewed; 931 AA.
AC A0A1V8SES1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Heat shock protein hsp98 {ECO:0000313|EMBL:OQN97593.1};
GN ORFNames=B0A48_16457 {ECO:0000313|EMBL:OQN97593.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN97593.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-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:OQN97593.1}.
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DR EMBL; NAJO01000052; OQN97593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8SES1; -.
DR STRING; 1507870.A0A1V8SES1; -.
DR InParanoid; A0A1V8SES1; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000192596; 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; 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:UP000192596};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:OQN97593.1}.
FT DOMAIN 3..167
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 42..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 429..523
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 46..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..921
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 103304 MW; 8B7C6CF8AEE0EF98 CRC64;
MAAGMSFTDK ATQALSDAQD LAQQYAHSQM LPLHLAVALL DPPPDLSKDQ QTNNSHASHA
QSSSPLFKQV IERAHGDPQL LDRSLKKALV RLPSQDPPPE HVSVSPTFSK VLRSANDLSK
TQKDSYIAVD HLIQCLVQDP AIARCLADAN VPNVKLIDTA VQQIRGTKRV DSKTADAEEE
HENLKKFTID MTAMAREGKI DPVIGREDEI RRVVRILSRR TKNNPVLIGE PGVGKTTVVE
GLASRIVNAD VPASLAQCKL LSLDVGALVA GSKYRGEFEE RMKGVLKEIE DSSEMIVLFV
DEIHLLMGAG SSGEGGMDAA NLLKPMLARG QLHCIGATTL NEYRKYIEKD QAFERRFQQV
LVKEPSIPET ISILRGLKEK YEVHHGVTIT DAAIVAAATL AARYLTQRRL PDSAVDLIDE
AAAAVRVERE SQPEVLDQME RKLRQLEIEI HALDREKDDA SKTRLRDAKA EKANVEEELK
PMREKYESEK QRSHEIQDQK IKLDQLKVKL QEAERTRDLQ TASDLKYYAI PDVDARINEM
EREKFAAEQS GRRGSVGESI VTDSVGPDQI NEIVGRWTGI PVTRLKTTEK DKLLQMEKVL
GNLVVGQKEA VTSVANAIRL QRSGLSNPNQ PPSFLFCGPS GTGKTLLTKA LAEFLFDDEK
AMIRLDMSEY QERHSLSRMI GAPPGYVGHD AGGQLTEALR RRPFSILLFD EVEKAAKEVL
TVLLQLMDDG RITDGQGRVI DAKNCIVVMT SNLGAEHLSR PNAPDGRIDP TTRELIMGAL
RSWFLPEFLN RISSIVIFNR LSKKEIRRIV DVRLDEIQRR LNNNGRAVKI QLTADVKDYL
GSAGYSPAYG ARPLARLIEK EVLNRLAVLI LRGAVRDGET ARVVLEDGHI VVIPNHGESD
DEGEGDEEMW DSDEAGEEVL ANGDGEMDLY E
//