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
//