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Database: UniProt
Entry: HSP98_NEUCR
LinkDB: HSP98_NEUCR
Original site: HSP98_NEUCR 
ID   HSP98_NEUCR             Reviewed;         927 AA.
AC   P31540; Q7RYM4;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   24-JAN-2024, entry version 139.
DE   RecName: Full=Heat shock protein hsp98;
DE   AltName: Full=Protein aggregation-remodeling factor hsp98;
GN   Name=hsp98; ORFNames=NCU00104;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 312-340.
RC   STRAIN=74A;
RX   PubMed=1472534; DOI=10.1016/0304-4165(92)90087-b;
RA   Vassilev A.O., Plesofsky-Vig N., Brambl R.;
RT   "Isolation, partial amino acid sequence, and cellular distribution of heat-
RT   shock protein hsp98 from Neurospora crassa.";
RL   Biochim. Biophys. Acta 1156:1-6(1992).
CC   -!- FUNCTION: Required, in concert with Hsp40 and Hsp70 and small Hsps, for
CC       the dissociation, resolubilization and refolding of aggregates of
CC       damaged proteins after heat or other environmental stresses. Extracts
CC       proteins from aggregates by unfolding and threading them in an ATP-
CC       dependent process through the axial channel of the protein hexamer,
CC       after which they can be refolded by components of the Hsp70/Hsp40
CC       chaperone system (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer, forming a ring with a central pore.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Note=More
CC       concentrated in polyribosomes than in monoribosomes, and preferentially
CC       localized in the large subunit.
CC   -!- DOMAIN: Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per
CC       monomer. ATP binding to NBD1 triggers binding of polypeptides and
CC       stimulates ATP hydrolysis at NBD2. Nucleotide binding to NBD2 is
CC       crucial for oligomerization (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal extension is involved in oligomerization.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR   EMBL; CM002238; EAA27992.1; -; Genomic_DNA.
DR   PIR; S28174; S28174.
DR   RefSeq; XP_957228.1; XM_952135.3.
DR   AlphaFoldDB; P31540; -.
DR   SMR; P31540; -.
DR   STRING; 367110.P31540; -.
DR   PaxDb; 5141-EFNCRP00000000125; -.
DR   EnsemblFungi; EAA27992; EAA27992; NCU00104.
DR   GeneID; 3873391; -.
DR   KEGG; ncr:NCU00104; -.
DR   VEuPathDB; FungiDB:NCU00104; -.
DR   HOGENOM; CLU_005070_4_2_1; -.
DR   InParanoid; P31540; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0140602; C:nucleolar peripheral inclusion body; IEA:EnsemblFungi.
DR   GO; GO:0140453; C:protein aggregate center; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0070370; P:cellular heat acclimation; IBA:GO_Central.
DR   GO; GO:0071218; P:cellular response to misfolded protein; IEA:EnsemblFungi.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0043335; P:protein unfolding; IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repeat; Stress response.
FT   CHAIN           1..927
FT                   /note="Heat shock protein hsp98"
FT                   /id="PRO_0000191213"
FT   DOMAIN          2..162
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          7..87
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          99..162
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          179..428
FT                   /note="NBD1"
FT   REGION          454..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..752
FT                   /note="NBD2"
FT   REGION          908..927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          429..553
FT                   /evidence="ECO:0000255"
FT   BINDING         224..231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         635..642
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   927 AA;  103182 MW;  46F263181BBD9D18 CRC64;
     MTSKMEFTDR AKKALEDAMA LAEQYAHSQL LPVHLAVALL DPLPDPSKDQ QNAPAGATSS
     LFRQVIERAH GDPQLFDRAL KKALVRLPSQ DPPPDHVSMA PSFHTVLRKA NELQKTQKDT
     YIAVDHLITA LAEEPSIMNA LKEANIPKPK LVTDAIQAIR GTKRVDSRNA DTEEEHENLA
     KFTIDMTAMA REGKIDPVIG REEEIRRVIR ILSRRTKNNP VLIGEPGVGK TTVVEGLAQR
     IVNADVPDNL ANCKLLSLDV GALVAGSKYR GEFEERMKGV LKEISESKEM IILFIDEIHL
     LMGAGASGEG GMDAANLLKP MLARGQLHCI GATTLAEYRK YIEKDAAFER RFQQVIVKEP
     SVSETISILR GLKEKYEVHH GVTISDAAIV AAANLAARYL TSRRLPDSAI DLIDEAAAAV
     RVARESQPEI IDSLERKLRQ LKIEIHALSR EKDEASKARL EQAKKDAENV EEELRPLREK
     YEQEKQRAKA LQEARMKLES LRQKAEEASR MGDHSRAADL QYYAIPEQEA VIKRLEKEKA
     AADAALNAAA AETGGAMITD VVGPDQINEI VARWTGIPVT RLKTSEKEKL LHMEKHLSKI
     VVGQKEAVQS VSNAIRLQRS GLSNPNQPPS FLFCGPSGTG KTLLTKALAE FLFDDPKAMI
     RFDMSEYQER HSLSRMIGAP PGYVGHDSGG QLTEALRRKP FSILLFDEVE KAAKEVLTVL
     LQLMDDGRIT DGQGRVVDAR NCIVVMTSNL GAEYLSRPNA KDGKIDPTTR ELVMNALRNY
     FLPEFLNRIS SIVIFNRLTR REIRKIVELR IAEIQKRLQD NDRNVKIEVS EEAKDKLGAL
     GYSPAYGARP LQRVLEKEVL NRLAVLILRG SIRDGEVARV VVQDGKITVL PNHPEVNDED
     DEMMLDEEDA VDEVAPESEM DEDLYDD
//
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