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Database: UniProt
Entry: A0A4Z0Z7A7_9PEZI
LinkDB: A0A4Z0Z7A7_9PEZI
Original site: A0A4Z0Z7A7_9PEZI 
ID   A0A4Z0Z7A7_9PEZI        Unreviewed;       809 AA.
AC   A0A4Z0Z7A7;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=E0Z10_g3492 {ECO:0000313|EMBL:TGJ85256.1};
OS   Xylaria hypoxylon.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX   NCBI_TaxID=37992 {ECO:0000313|EMBL:TGJ85256.1, ECO:0000313|Proteomes:UP000297716};
RN   [1] {ECO:0000313|EMBL:TGJ85256.1, ECO:0000313|Proteomes:UP000297716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 108379 {ECO:0000313|EMBL:TGJ85256.1,
RC   ECO:0000313|Proteomes:UP000297716};
RA   Buettner E., Leonhardt S., Gebauer A.M., Liers C., Hofrichter M.,
RA   Kellner H.;
RT   "Draft genome sequence of Xylaria hypoxylon DSM 108379, a ubiquitous
RT   saprotrophic-parasitic fungi on hardwood.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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:TGJ85256.1}.
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DR   EMBL; SKBN01000049; TGJ85256.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Z0Z7A7; -.
DR   STRING; 37992.A0A4Z0Z7A7; -.
DR   Proteomes; UP000297716; 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: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:UP000297716}.
FT   DOMAIN          117..261
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          518..658
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          696..787
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          53..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          330..410
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        795..809
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  89826 MW;  7E233C3AF2DEEF05 CRC64;
     MLAKRNIVSS SRQSLAAVSR GLGRSDGRLS IHARAALLAT IPKTSRASLP IIRTYSNGRP
     HPPGGTHRMN LGGEPEKPAL EQYGVDLTAK ARDGKLDPVI GRDDEIQRTI QVLSRRTKNN
     PVLIGSAGTG KTAVLEGLAS RIVRGDVPES IKNKRVISLD LGSLIAGAKF RGDFEERLKK
     VLTEVEQAQG EVVLFIDELH VLLGLGKAEG SIDASNLLKP ALSRGELQCC GATTLTEYRL
     IEKDVALARR FQPILVNEPS VPDTISILRG IKEKYEVHHG VRITDGALVA AATYSNRYIT
     DRFLPDKAID LMDEAASSLR LQQESKPEDI MRLDQKIMTI QIELESLRKE KDVASRERRE
     KLESDLKKLQ EEEKTLTGRW EKERSQIEAL KKVQEDLDKA RIELEHAQRS GNFARASELR
     FGVIPTLENK LPKDGETGPD AQGPDTLIHD SVTADDIAAV VSRVTGIPVT KLTSGHIEKL
     IHMEDTLRKS VRGQDEALKA VADAVRIQRA GLNRDNRPLA TFFFLGPTGV GKTELCKKLA
     SFLFSTEQAV VRFDMSEFQE KHTISRLIGA PSGYVGYEDA GQLTEAVRRK PYAVLLFDEF
     EKAHRDISSL LLQVLDEGYL TDSQGRKVDF RNVITIFTSN LGADILVGSN PIHHYSETPE
     GDVSPDVRKA VMDVVSANYA PEFLNRIDSF IIFKRLKLDA LRDIVDIRLR ELQQRLDDRR
     IKLNVDDEVR KWLAEHGYDP RFGARPLNRL ITTEISNNLA DKIIRGEVRG GDTASVRIKE
     DKSGLEIFPE KSTVEPASKS DSGSHDSSI
//
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