ID B2WKJ3_PYRTR Unreviewed; 920 AA.
AC B2WKJ3;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE SubName: Full=Heat shock protein 104 {ECO:0000313|EMBL:EDU43553.1};
GN ORFNames=PTRG_10503 {ECO:0000313|EMBL:EDU43553.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU43553.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; DS231628; EDU43553.1; -; Genomic_DNA.
DR RefSeq; XP_001940834.1; XM_001940799.1.
DR AlphaFoldDB; B2WKJ3; -.
DR STRING; 426418.B2WKJ3; -.
DR EnsemblFungi; EDU43553; EDU43553; PTRG_10503.
DR GeneID; 6348809; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_0_1; -.
DR InParanoid; B2WKJ3; -.
DR OMA; ERMKAVM; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
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; IEA:InterPro.
DR GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0070370; P:cellular heat acclimation; IEA:EnsemblFungi.
DR GO; GO:0071218; P:cellular response to misfolded protein; IEA:EnsemblFungi.
DR GO; GO:0042026; P:protein refolding; 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; 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; 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|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:UP000001471};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:EDU43553.1}.
FT DOMAIN 4..158
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 889..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 427..541
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 895..920
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 102300 MW; 279EF09224DAA212 CRC64;
MTSFDAYTDR AAKALADSFD LAKGYAHSQL TPLHLAVSLI DPPKDLANTV DVPPPPLFKQ
VLERANGDPQ LFERNLKKAM VRLPSQDPPP ERTSPSPAMA KVLRSAEELS KTQKDSFIAV
DHLIQSLCQD AQLQRILADS NVPNTKQIDN AIQALRGTKR VDSKTADAEE ENENLKKFTI
DMTAMAREGK IDPVIGREDE TRRVIRILTR RTKNNPVLIG EPGVGKTTVV EGLARRIVDA
DVPANLAACK LLSLDVGALV AGSKYRGEFE DRMKGVLKEI EDSKEMIVLF VDEIHLLMGA
GSSGEGGMDA ANLLKPMLAR GQLHCIGATT LGEYRKYIEK DAAFERRFQQ VLVKEPSIPE
TISILRGLKE RYETHHGVTI MDGAIVAAAT LAARYLTQRR LPDSAVDLID EAAAAVRVTR
ESQPEALDNL ERRHRQLQIE IHALSREKDE ASQVRLKDAR AEAANIEEEL KPLREMYERE
KGRSKDIQEQ KLKLEGLKTK LAEAERMRDI QTASDLKYYA IPDVEQRIAE LERDKARADA
EMWAHQASGG GEALMSDSVG PDQINEIVAR WTGIPVTRLK TTEKDKLLNM ERHLQEVVVG
QREAVVSVSN AIRLQRSGLA NPNQPPSFLF CGPSGTGKTL LTKALAEFLF DDAKAMIRFD
MSEYQERHSL SRMIGAPPGY VGHDAGGQLT EALRRKPFSI LLFDEVEKAA KEVLTVLLQL
MDDGRITDGQ GRVVDAKNCI VVMTSNLGAE HLSRPNAPDG KIDPTTKEMV MGALRNWFLP
EFLNRISSIV IFNRLTKREI RKIVDVRLGE IQKRLNQNGR NVRIEMTPEV RDYLGSAGYS
PAYGARPLAR LIEKEVLNRL AVLILRGSIK EGEVARVVLE DGHILVLPNH TDSEDDSEMY
DESDAVAELD DDGGDMDLYD
//