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Database: UniProt
Entry: A0A423WEC8_9PEZI
LinkDB: A0A423WEC8_9PEZI
Original site: A0A423WEC8_9PEZI 
ID   A0A423WEC8_9PEZI        Unreviewed;       806 AA.
AC   A0A423WEC8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VSDG_02164 {ECO:0000313|EMBL:ROW01750.1};
OS   Valsa sordida.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW01750.1, ECO:0000313|Proteomes:UP000284375};
RN   [1] {ECO:0000313|EMBL:ROW01750.1, ECO:0000313|Proteomes:UP000284375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YSFL {ECO:0000313|EMBL:ROW01750.1,
RC   ECO:0000313|Proteomes:UP000284375};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) 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:ROW01750.1}.
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DR   EMBL; LJZO01000006; ROW01750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423WEC8; -.
DR   STRING; 252740.A0A423WEC8; -.
DR   Proteomes; UP000284375; 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; 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:UP000284375}.
FT   DOMAIN          131..276
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          529..676
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          707..798
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          28..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          344..424
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        28..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  89165 MW;  1121D5DC0F59027B CRC64;
     MLTRRQLLSS TRRIANAPAT IRTTVRAASS ALRPLATTGS PLTTTTTTPS ARPSPTTLLP
     SVSSIRHYAN GRPHPPGGTH RMDMGGGGEE KPALEQYGVD LTAKAKEGKL DPVIGRDAEI
     QRTIQVLSRR TKNNPVLIGQ AGTGKTAILE GLALRIVRGD VPESVKNKRV VSLDLGSLIA
     GAKFRGDFEE RLKKVLTEVE QAEGQVILFI DELHTLLGLG KAEGSIDASN LLKPALSRGE
     LQCCGATTLN EYRLIEKDVA LARRFQPILV NEPTVEDTIS ILRGIKDKYE VHHGVRITDG
     ALVAAATYSN RYITDRFLPD KAIDLMDEAA SSLRLQQESK PEDIMKLDQK IMTIQIELES
     LRKETDVASK ERREKLEGDL KKLQDEVGTL NERWEKERGE LEAIKNTQAD LDKARVELEM
     AQREGNFGRA SELRYSVIPA LEQKLPKEGE QPKTDGTLIH DSVTPDDIAQ VVARITGIPV
     SKLTSGHIEK LVHMEDTLRQ SVKGQDEALR AVANAVRMQR AGLSGENRPL ASFFFLGPTG
     VGKTELCKKL AGFLFSTESA VVRFDMSEFQ EKHTISRLIG APSGYVGYED AGQLTEAVRR
     KPYAVLLFDE FEKAHRDISA LLLQVLDEGY LTDAQGHKVD FKNTIIVLTS NLGADILVGA
     NPAHRYRETE DGDIAPESKK AVMDVVADNY PPEFLNRIDE FIIFKRLSRD ALRDIVDIRL
     RELQERLVDR RITLDVPDEV RRWLADRGYD PKFGARPLNR LITHQIGNKL ADKIIRGEMK
     MGDTAEVFIN ADGDALEVRA RGSGGD
//
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