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Database: UniProt
Entry: A0A1V6QJL1_9EURO
LinkDB: A0A1V6QJL1_9EURO
Original site: A0A1V6QJL1_9EURO 
ID   A0A1V6QJL1_9EURO        Unreviewed;       790 AA.
AC   A0A1V6QJL1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENANT_c002G09435 {ECO:0000313|EMBL:OQD89385.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD89385.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
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:OQD89385.1}.
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DR   EMBL; MDYN01000002; OQD89385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QJL1; -.
DR   STRING; 416450.A0A1V6QJL1; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000191672; 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:UP000191672}.
FT   DOMAIN          117..261
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          516..660
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   790 AA;  87445 MW;  97BCA50FF2BCE857 CRC64;
     MAARLSITAR SRLLRAPNLA SARLLTPIAR STLLPRASSV LLPVASVTPI SVRHYAKGRP
     HPPGGTHRMD MSGGEEKSAL EQYGVDLTDK AKAGKLDPVI GRDSEIHRTI QILSRRTKNN
     PVLIGAAGTG KTAVLEGLAQ RIVQGDVPES IKNKRVVSLD LGSLIAGAKF RGDFEERLKS
     VLKEVEDAHG GVILFIDELH TLLGLGKAEG SIDASNLLKP ALSRGELQCC GATTLNEYRL
     IEKDVALARR FQPILVGEPS VPSTISILRG IKNKYEVHHG VRITDGALVA AATYSNRYIT
     DRYLPDKAID LVDEAASALR LQQESKPDSI RELERDITTI QIELESLRKE TDVSSRERRD
     KLQEDLKTKQ AEVGELTEAW EKEKAEIDTI KRTKEELERA RFELEQAQRE GNFAKAGELR
     YSTIPELEGK LPKEGAEQDA RQQTLIHDSV TADDIGNVVS RTTGIPVSKL MAGEVEKLIH
     MEDTLRKSVR GQDEALSAVA NAVRMQRAGL SGENRPLASF MFLGPTGVGK TELCKKMAEF
     LFSTETAVVR FDMSEFQEKH TISRLIGSPA GYVGYDDAGQ LTEAVRRKPY AVLLFDEFEK
     AHRDISALLL QVLDEGFLTD AQGHKIDFKN TLIVLTSNLG ADILVGADPI HSRKEFGDAE
     LSPDIKAAVM DVVQRAYAPE FLNRIDEFII FKRLSREALR DIVDIRLKEL QARLDDRRMT
     LQVDNEIKDW LCARGYDPRF GARPLNRLIS KEIGNRLADK IIRGEIVSGQ TARVSLDETK
     SGLVVTTQEE
//
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