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Database: UniProt
Entry: A0A1B8GVK9_9PEZI
LinkDB: A0A1B8GVK9_9PEZI
Original site: A0A1B8GVK9_9PEZI 
ID   A0A1B8GVK9_9PEZI        Unreviewed;       931 AA.
AC   A0A1B8GVK9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Heat shock protein hsp98 {ECO:0000313|EMBL:OBT99848.1};
GN   Name=HSP98 {ECO:0000313|EMBL:OBT99848.1};
GN   ORFNames=VE01_02076 {ECO:0000313|EMBL:OBT99848.1};
OS   Pseudogymnoascus verrucosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=342668 {ECO:0000313|EMBL:OBT99848.1, ECO:0000313|Proteomes:UP000091956};
RN   [1] {ECO:0000313|EMBL:OBT99848.1, ECO:0000313|Proteomes:UP000091956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBT99848.1,
RC   ECO:0000313|Proteomes:UP000091956};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000091956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX   PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT   white-nose syndrome of bats.";
RL   Nat. Commun. 9:35-35(2018).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; KV460211; OBT99848.1; -; Genomic_DNA.
DR   RefSeq; XP_018133581.1; XM_018271587.1.
DR   AlphaFoldDB; A0A1B8GVK9; -.
DR   STRING; 342668.A0A1B8GVK9; -.
DR   GeneID; 28835462; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000091956; 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; 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:UP000091956};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:OBT99848.1}.
FT   DOMAIN          4..167
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          894..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          436..557
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        903..931
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   931 AA;  103291 MW;  5739A98C0C49B638 CRC64;
     MATSNMQFTD RAKKALEDSM ILAEQHAHSQ LLPIHLAVSL LDPLPDESKD QQQSFNASHG
     PAQSSFFRQV VERAHGDPQL FDRALKKALV RLPSQDPPPD QIAMSPAFSK ILRSANELQK
     TQKDSFIAVD HMISALAQDT TIQKALSDSN IPNSKLVQDA VQQIRGTKRV DSKTADAEEE
     SENLKKFTID MTAMAREGKI DPVIGREEEI RRVIRILSRR TKNNPVLIGE PGVGKTTVVE
     GLAQRIVNLD VPDNLAACKL LSLDVGGLVA GAKYRGEFEE RMKGVLKEIE DSKEMIVLFV
     DEMHLLMGAG ASGEGGMDAA NLLKPMLARG QLHCIGATTL SEYRKYIEKD AAFERRFQQV
     IVKEPTIPET ISILRGLKER YEVHHGVTIA DAAIVSSATL AARYLTARRL PDSAVDLIDE
     AAAAVRVARE SQPEIIDSLE RKLRQLKIEI HALSREKDEA SKVRLAQAKQ DASNVEEELR
     PLRDKYENER KRGKSIQEAK MKLDQLKFKQ EEASRIGDVG RAADLKYNAI PEQEDLIKSL
     EEEKRLADAR LNETSADTGG SMTSDVVGPD QINEIVARWT GIPVTRLRTT EKDKLLHMEK
     VLSKIVVGQK EAVGSVSNAI RLQRSGLSNP NQPPSFLFCG PSGTGKTLLT KALADFLFDD
     PKAMIRFDMS EYQERHSLSR MIGAPPGYVG HDAGGQLTEA LRRKPFSILL FDEVEKAAKE
     VLTVLLQLMD DGRITDGQGR VVDARNCIVV MTSNLGAEFL ARQNAPNGKI DPTTKEMVMQ
     ALRNYFLPEF LNRISSIVIF NRLTRHEIRK IVDVRLEEIQ KRLESNGRNV TIEISGPAKD
     YLGSAGYSPA YGARPLARLI EKEVLNRMAV LILRGSIKDG ETARVVLEDG RLDVLPNHGD
     SSEQESEEED MDLDDGDALD AITGEDMDLY D
//
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