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Database: UniProt
Entry: A0A1V6RE18_9EURO
LinkDB: A0A1V6RE18_9EURO
Original site: A0A1V6RE18_9EURO 
ID   A0A1V6RE18_9EURO        Unreviewed;       789 AA.
AC   A0A1V6RE18;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENSOL_c006G05141 {ECO:0000313|EMBL:OQD99497.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD99497.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQD99497.1}.
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DR   EMBL; MDYO01000006; OQD99497.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6RE18; -.
DR   STRING; 60172.A0A1V6RE18; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000191612; 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:UP000191612}.
FT   DOMAIN          117..261
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          516..663
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          694..785
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          330..410
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   789 AA;  87462 MW;  BDE770680A1DA4C1 CRC64;
     MAARLSLNAR SRLLRTPHLS STRVLSPIPR SIILPCASII LPAVNHNPVY VRHYANGGRP
     HPPGGTHRMD MSGEDEKPAL EKYGVELTEK AKAGKLDPVI GRDAEIHRTI QILSRRTKNN
     PVLIGAAGTG KTAVLEGLAQ RIVQGDVPES IKDKRVVALD LGSLIAGAKF RGDFEERLKA
     VLKEVEDAQG GVILFIDELH TLLGLGKAEG SIDASNLLKP ALSRGELQCC GATTLNEYRL
     IEKDVALARR FQPILVNEPS VASTISILRG IKNKYEVHHG VRITDGALVA AATYSNRYIT
     DRFLPDKAID LVDEAASALR LQQESKPDSI RELERDITTI QIELESLRKE TDVASRERRE
     KLQEDLKTKQ AEADKLTEAW EEEKAEIDAI KRTKEDLERA RFELEQAQRE GNFARAGELR
     YSTIPDLEAK LPKEGAEQDP QNQTLIHDSV TADDIGNVVS RTTGIPVNKL MAGDVEKLIH
     MEDTLRKSVR GQDEALSAVA NAVRMQRAGL SGDNRPMASF MFLGPTGVGK TELCKKMAEF
     LFSTETAVLR FDMSEFQEKH TISRLIGSPA GYVGYDDAGQ LTEAVRRKPY AVLLFDEFEK
     AHRDISALLL QVLDEGFLTD AQGHKVDFRN TLIVLTSNLG ASILVGADPL HPIKDSCDAE
     LPEKVKAAVM DVVQSAYPPE FMNRIDEFII FRRLSKDALR DIVDIRIKEL QARLDDRRMT
     LQVDDETKNW LCEKGYDPRF GARPLNRLIA KEIGNRLADK IIRGEVVSGQ TVQVSLDEAK
     SGLVVTTQE
//
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