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
//