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Database: UniProt
Entry: A0A4Z1PA49_9PEZI
LinkDB: A0A4Z1PA49_9PEZI
Original site: A0A4Z1PA49_9PEZI 
ID   A0A4Z1PA49_9PEZI        Unreviewed;       933 AA.
AC   A0A4Z1PA49;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Heat shock protein Hsp98/Hsp104/ClpA {ECO:0000313|EMBL:TID17787.1};
GN   ORFNames=E6O75_ATG10432 {ECO:0000313|EMBL:TID17787.1};
OS   Venturia nashicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Venturiaceae; Venturia.
OX   NCBI_TaxID=86259 {ECO:0000313|EMBL:TID17787.1, ECO:0000313|Proteomes:UP000298493};
RN   [1] {ECO:0000313|EMBL:TID17787.1, ECO:0000313|Proteomes:UP000298493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRI2 {ECO:0000313|EMBL:TID17787.1,
RC   ECO:0000313|Proteomes:UP000298493};
RA   Prokchorchik M., Won K., Lee Y., Choi E.D., Segonzac C., Sohn K.H.;
RT   "High contiguity whole genome sequence and gene annotation resource for two
RT   Venturia nashicola isolates.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {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:TID17787.1}.
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DR   EMBL; SNSC02000015; TID17787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Z1PA49; -.
DR   STRING; 86259.A0A4Z1PA49; -.
DR   Proteomes; UP000298493; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000298493};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:TID17787.1}.
FT   DOMAIN          3..167
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          41..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          896..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..933
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   933 AA;  103814 MW;  53074702D3312F06 CRC64;
     MASGMQFTDK AQASLVDANQ LAVTYQHTQM MPLHLAVSLI DPPPDLSKDQ QNPQGHASHA
     GSSVPLFKQI IERANGDPQA FDRSLKKALV RLPSQDPPPE SVPLSPQLSK VLRSANELQK
     TQKDSFIAVD HLIQALVQDP TIQKCLAEAN IPRPNLVDQA IQTIRGTKRV DSKTADAEEE
     NENLKKFTID MTAMAREGKI DPVIGREEEI RRVVRILSRR TKNNPVLIGE PGVGKTTVVE
     GLALRIVNAD VPTNLAQCKL LSLDVGSLVA GSKYRGEFEE RMKGVLKEVE ESKDMIVLFV
     DEMHLLMGAG SSGEGGMDAA NLLKPMLARG QLHCIGATTL SEYRKYIEKD QAFERRFQQV
     LVKEPTIPET ISILRGLKEK YETHHGVTIL DGAIVAAATL APRYLTQRRL PDSAVDLIDE
     AAAAVRVARD SQPEIIDHYE RRLRQLQIEI HALSRETDEA SATRLREAKA EAANLEEELK
     PLREKYESEK GRSSEIQELK QRLDNLKVKL AEADRNRDFA TASDLQYYAI PDLQARIDKL
     EREKEQQDAE ANQRRGSFGE APLITDSVGP DQINEIVARW TGIPITRLRT SEKDKLLNME
     KVLGQIVVGQ REAVNSVSNA IRLQRSGLAN PNQPPSFLFC GPSGTGKTLL TKALAEFLFD
     DPKSMVRFDM SEYQERHSLS RMIGSPPGYV GHDAGGQLTE ALRRKPFSIL LFDEVEKAAK
     EVLTVLLQLM DDGRITDGQG RVVDAKNCIV VMTSNLGAEY LARPTAPSGK IDPTTKELVM
     NALRNYFLPE FLNRINSIVI FNRLTKKEIR SIVDVRMQEI QKRLKANGRD VKIEMTKDVL
     DYLGSAGYSP AYGARPLARL IEKEVLNRMA VLILRGAIKD GETAKVVLED GHIHVLPNHS
     DTDESEDSEM YEAEGEDALH DLEDADGDME LYN
//
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