ID A0A4V5N3I6_9PEZI Unreviewed; 933 AA.
AC A0A4V5N3I6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Heat shock protein hsp98 {ECO:0000313|EMBL:TKA23799.1};
GN ORFNames=B0A50_07081 {ECO:0000313|EMBL:TKA23799.1};
OS Salinomyces thailandica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Salinomyces.
OX NCBI_TaxID=706561 {ECO:0000313|EMBL:TKA23799.1, ECO:0000313|Proteomes:UP000308549};
RN [1] {ECO:0000313|EMBL:TKA23799.1, ECO:0000313|Proteomes:UP000308549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 6315 {ECO:0000313|EMBL:TKA23799.1,
RC ECO:0000313|Proteomes:UP000308549};
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:TKA23799.1}.
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DR EMBL; NAJL01000051; TKA23799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V5N3I6; -.
DR Proteomes; UP000308549; 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; 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|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:UP000308549};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:TKA23799.1}.
FT DOMAIN 1..166
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 44..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 435..549
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 45..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..933
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 933 AA; 103700 MW; 2F62D5DBD375F176 CRC64;
MTSGFQFTDK ATQALAEAQD LCQQYAHSQM LPLHLAVALF DPQPDLSKDQ QNTGHASHAG
SSTPLFKQVV ERAHGDPQLL DRAMKKALVR LPSQDPPPEQ VAVSPAFSKV LRAANELSKT
QKDSYIAVDH LIQCLVQDTS IQRCLAESNI PNPKLIDNAV QQIRGTKRVD SKTADADEES
ENLKKFTIDM TAMAREGKID PVIGREEEIR RVIRILSRRT KNNPVLIGEP GVGKTTVVEG
LALRIVNADV PAGLAACRLL SLDVGALVAG SKYRGEFEER MKGVLKEIED SKEMIVLFVD
EIHLLMGAGS SGEGGMDAAN LLKPMLARGQ LHCIGATTLA EYRKYIEKDQ AFERRFQQVL
VKEPSIPETI SILRGLKEKY EVHHGVTILD GAIVAAATLA ARYLTQRRLP DSAVDLIDEA
AAAVRVTRES QPEVLDNMER KQRQLEIEIH ALDREKDDAS KARLREARAE KANVEEELKP
LREKYESEKA RSKEIQEQKI KLDQLKVKQQ EAERTRDLQT ASDLKYYAIP DVEARIEQLE
HQKHLQEQDE AGRRGSMGET LITDAVGPDQ INEIVGRWTG IPVTRLKTTE KEKLLQMEKV
LGNQVVGQKE AVTSVANAIR LQRSGLSNPG QPPSFLFCGP SGTGKTLLTK ALAEFLFDDS
KSMIRFDMSE YQERHSLSRM IGAPPGYVGH DAGGQLTEAL RRRPFSILLF DEVEKAAKEV
LTVLLQLMDD GRITDGQGRV IDARNCIVVM TSNLGAEYLA RPNAPDGKID PTTKELVMTA
LRNYFLPEFL NRISSIVIFN RLAKKEIRKI VDVRLDEIQK RLTGNGRNVS IQLSADVKDY
LGSAGYSPAY GARPLQRLIE KEVLNRLAVL ILRGSVRDGE VARVVLEDGH IVVLPNHGES
DLEDGSEDEE MWDEEDAAEE LNGADGEMDL YDE
//
