ID N1J9D9_BLUG1 Unreviewed; 802 AA.
AC N1J9D9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative heat shock protein/chaperonin HSP78 {ECO:0000313|EMBL:CCU76776.1};
GN ORFNames=BGHDH14_bgh04944 {ECO:0000313|EMBL:CCU76776.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU76776.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU76776.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU76776.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, 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:CCU76776.1}.
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DR EMBL; CAUH01003024; CCU76776.1; -; Genomic_DNA.
DR AlphaFoldDB; N1J9D9; -.
DR STRING; 546991.N1J9D9; -.
DR EnsemblFungi; BLGH_03326-mRNA-1; BLGH_03326-mRNA-1; BLGH_03326.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_0_1; -.
DR InParanoid; N1J9D9; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000015441; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0034605; P:cellular response to heat; IEA:EnsemblFungi.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR GO; GO:0043335; P:protein unfolding; IEA:EnsemblFungi.
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:SF18; 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|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:UP000015441};
KW Stress response {ECO:0000313|EMBL:CCU76776.1}.
FT DOMAIN 120..264
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 527..670
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 705..795
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 56..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..420
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 802 AA; 89623 MW; 3D032B28758A8C32 CRC64;
MMLRRRVFTL QGIHSTFIAQ TCSKSFVQNF RFPSSFTRNR ISDAISVSTS RKPCFRRISS
GRPSQPGGTH RMNLGGEKEK SPLETYGIDL TARARDGKLD PVIGRSAEIQ RTIQVLSRRT
KNNPVLIGSA GTGKTAILEG LAQRIVQGDV PESMKDKRVI SLDLGQLIAG AKFRGDFEER
LKAVLKEVQD GNGKIVLFID ELHILLGLGK AEGSIDASNL LKPALSRGEL QCCGATTLNE
YRAIEKDVAL ARRFQPIQVD EPNLQDTISI LRGIKGKYEL HHGVQIMDSA LVAAATYSNR
YITDRFLPDK AIDLMDEAAS ALRLQQESKP EDIMRLDQRI MTLQIEIESL RKEKDVASLE
RREKLELDLS ECQKEAAKLL EIWEREKAGI EEVKRVKQDL EKAQFELEQA QRENNFARAG
ELRYSVIPQL ESKIPKDGSS TTGNLNSGEN GDPFPLIHEA VTADDIAMVV SRITGIPITK
LNSGTADRLI RMEEILRESV RGQDEALTAV ANAVRMQRAG LNGENRPLAS FFFLGPTGVG
KTELCKKMAN FLFSTDTAVI RFDMSEFQEK HTISRLIGSP AGYVGYDDAG QLTEAVRRKP
YAVLLFDEFE KAHRDISALL LQVLDEGFLT DSQGHKIDFR NTLIVFTSNL GAEVLVGNYL
DSASQHDVDG EIPGTVRNEV MNIVQNSYAP EFLNRIDEFI IFRRLSPKAL REIVDIRLLE
LQAQLDDRRI KLEVRDEVRS WLADRGYDPK YGARPLNRLI SKKIGNRLAE KIIKGEIKGG
DIASIVLNED GDDIIAQRIH CG
//
