ID Q7SDI0_NEUCR Unreviewed; 810 AA.
AC Q7SDI0;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 24-JAN-2024, entry version 121.
DE SubName: Full=Heat shock protein 78 {ECO:0000313|EMBL:EAA34819.1};
GN Name=hsp78 {ECO:0000313|EMBL:EAA34819.1};
GN ORFNames=NCU02630 {ECO:0000313|EMBL:EAA34819.1};
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 {ECO:0000313|EMBL:EAA34819.1, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:EAA34819.1, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA 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 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., 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., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CM002236; EAA34819.1; -; Genomic_DNA.
DR RefSeq; XP_964055.1; XM_958962.3.
DR AlphaFoldDB; Q7SDI0; -.
DR SMR; Q7SDI0; -.
DR STRING; 367110.Q7SDI0; -.
DR PaxDb; 5141-EFNCRP00000002199; -.
DR EnsemblFungi; EAA34819; EAA34819; NCU02630.
DR GeneID; 3880204; -.
DR KEGG; ncr:NCU02630; -.
DR VEuPathDB; FungiDB:NCU02630; -.
DR HOGENOM; CLU_005070_4_0_1; -.
DR InParanoid; Q7SDI0; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
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; 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; 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:SF176; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000001805};
KW Stress response {ECO:0000313|EMBL:EAA34819.1}.
FT DOMAIN 125..270
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 523..663
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 701..790
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 338..418
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 810 AA; 89936 MW; 7AF9620FD8CC7DEC CRC64;
MQTRRQLLST ATRRISEASR ASLSRTTRQF PRAPALGVTV PALNATHLAS SLRLLPTIAT
RSYANGRPRP PGGTHRMNLG GEDEKPALEQ YGIDLTAKAR EGKLDPVIGR AAEIQRTIQI
LSRRTKNNPV LIGCAGVGKT AILEGLALEI VKGAVPESIK NRRVISLDLG SLIAGAKFRG
DFEERLKKVL GEVQEANGEV ILFIDELHTL LGLGKAEGSI DASNLLKPAL SRGELQCCGA
TTMTEYRQIE KDVALARRFQ PIIVSEPTVE DTISILRGIK EKYEVHHGVR ITDGALVAAA
TYSNRYITDR FLPDKAIDLM DEAASSLRLQ QESKPDDIQR LDQKIMTIQI ELESLRKEKD
VASVERREKL EADLKKYQDE VAVLTERWLK EKAEIDSIKQ TQAELDRARI ELEQAQRTGN
FARASELRFG VIPNLEKKLP KDGERPTRDL SLIHDSVTAD DIANVVSRIT GIPISKLSSG
HTERLIHMED ILRESVRGQD EALKAVADAV RMQRAGLSGE NRPLASFFFL GPTGVGKTEL
CKKLAGFLFS TETAVVRFDM SEFQEKHTIS RLIGAPSGYV GYEDAGQLTE AVRRKPYAVI
LLDEFEKAHR DISALLLQVL DEGYLTDAQG HKVDFKNTII VLTSNLGADI LVGANPMVPY
KETEDGDIHP DVKQAVMDVV ASQYPPEFLN RIDSFIIFKR LAMEALRDIV DIRLKELQER
LNDRRITLDV PEEVRQWLAE RGYDPKFGAR PLNRLITTEI GNGLADKIIR GQIKSGDKAV
VEIKEDRSGL NVYAEQQEQP PAAEEAEAEA
//