ID A0A4U0URU0_9PEZI Unreviewed; 940 AA.
AC A0A4U0URU0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Heat shock protein hsp98 {ECO:0000313|EMBL:TKA38122.1};
GN ORFNames=B0A54_11136 {ECO:0000313|EMBL:TKA38122.1};
OS Friedmanniomyces endolithicus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Friedmanniomyces.
OX NCBI_TaxID=329885 {ECO:0000313|EMBL:TKA38122.1, ECO:0000313|Proteomes:UP000310066};
RN [1] {ECO:0000313|EMBL:TKA38122.1, ECO:0000313|Proteomes:UP000310066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5311 {ECO:0000313|EMBL:TKA38122.1,
RC ECO:0000313|Proteomes:UP000310066};
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:TKA38122.1}.
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; NAJP01000047; TKA38122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U0URU0; -.
DR STRING; 329885.A0A4U0URU0; -.
DR Proteomes; UP000310066; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000310066};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:TKA38122.1}.
FT DOMAIN 3..167
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 36..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..920
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 104290 MW; 4D798DE6023C25ED CRC64;
MASGMQFTDK ASTALGDAQE LAQQYAHSQM LPIHLGVSLI DPPPDQSKDQ QTNHAHASHS
ASSVPLFKQV VERAHGDPQL FDRALKKALV RLPSQDPPPE QVSVSPSFTK ILRAANDLSK
TQKDTYIAVD HLIQCLVQDA TIQKCLADAN VPNTKLIDTA IQQIRGTKRV DSKTADAEQE
NENLKKFTID MTAMAREGKM DPVIGREEEI RRVIRILSRR TKNNPVLIGE PGVGKTTVVE
GLAQRIVNAD VPSGLAACKL LSLDVGSLVA GSKYRGEFEE RMKGVLKEIE DSKEMIVLFV
DEIHLLMGAG SSGEGGMDAA NLLKPMLARG QLHCIGATTL AEYRKYIEKD QAFERRFQQV
LVGEPSIPET ISILRGLKDK YEVHHGVTIL DGAIVAAATL ASRYLTQRRL PDSAVDLVDE
AAAAVRVTRE SQPEVLDNME RKLRQLEIEI HALDREKDDA SKARLGEARA EKANIEEELK
PLREKYESEK TRSKEIQEQK IKLDQLKVKQ QEAERTRDLQ TASDLKYYAI PDVEARIEQL
EHHKQQAEYQ DSGRRGSIGE KLTTDAVGPD QINEIVARWT GIPVTRLRTT EKEKLLQMEK
VLGAQVIGQK EAVTSVANAI RLQRSGLSNP GQPPSFLFCG PSGTGKTLLT KALAEFLFDD
PKSMIRFDMS EYQERHSLSR MIGAPPGYVG HDAGGQLTEA LRRRPFSILL FDEVEKAAKE
VLTVLLQLMD DGRITDGQGR VIDARNCIVV MTSNLGAEFL SRPNAPDGRI DPTTRELVMN
ALRNYFLPEF LNRISSIVIF NRLTKREIRR IVDVRLDEIQ KRLLTNGRMV TISLSPAVKD
YLGSAGYSPA YGARPLARLI EKEVLNRLAV LILRGSIRDG EVAKVVLEDG HVMVLPNHGD
SEGEGSEGGD SEMWDEEEEE EAVRGMVKEG NGGEMDLYDD
//
