ID R0H8J0_9BRAS Unreviewed; 971 AA.
AC R0H8J0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN ORFNames=CARUB_v10000151mg {ECO:0000313|EMBL:EOA19903.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA19903.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; KB870810; EOA19903.1; -; Genomic_DNA.
DR RefSeq; XP_006287005.1; XM_006286943.1.
DR AlphaFoldDB; R0H8J0; -.
DR STRING; 81985.R0H8J0; -.
DR GeneID; 17884102; -.
DR KEGG; crb:17884102; -.
DR eggNOG; KOG1051; Eukaryota.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; 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; 1.10.1780.10; Clp, N-terminal domain; 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; IPR017730; Chaperonin_ClpB.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
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; PF02861; Clp_N; 2.
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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
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:UP000029121};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 78..222
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 488..602
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 971 AA; 109028 MW; 58F282673FE4BC6D CRC64;
MATATTAATA AFTGVVGVGT ETRRVPSFSH LQPSVAFPAN PNSFKALKLK QSARLTRRLE
HRPFVVRCEA SSSNGRLTQQ EFTEMAWQSI VSSPDVAKEN KQQIVETEHL MKALLEQKNG
LARRIFSKIG VDNTKVLEST EKFIQRQPKV YGDAAGSMLG RDLEGLFQRA RQFKKDLGDS
YVSVEHLVLA FADDKRFGKQ LFKDFQISEK SLKTAILSIR GKQSVIDQDP EGKYEALEKY
GKDLTAMARE GKLDPVIGRD DEIRRCIQIL SRRTKNNPVL IGEPGVGKTA ISEGLAQRIV
QGDVPQALMN RKLISLDMGA LIAGAKYRGE FEDRLKAVLK EVTDSEGQII LFIDEIHTVV
GAGATNGAMD AGNLLKPMLG RGELRCIGAT TLDEYRKYIE KDPALERRFQ QVYVDQPTVE
DTISILRGLR ERYELHHGVR ISDSALVEAA ILSDRYISGR FLPDKAIDLV DEAAAKLKME
ITSKPTALDE LDRAVIKLEM ERLSLTNDTD KASRERLNRI ETELVLLKEK QAELTEQWEH
ERSVMSRLQS IKEEIDRVNL EIQQAEREYD LNRAAELKYG SLNSLQRQLN DAEKELNEYL
SSGKSMFREE VLGSDIAEIV SKWTGIPVSK LQQSERDKLL HLEEELHKRV VGQNPAVTAV
AEAIQRSRAG LSDPGRPIAS FMFMGPTGVG KTELAKALAS YLFNTEEALV RIDMSEYMEK
HAVSRLIGAP PGYVGYEEGG QLTETVRRRP YSVILFDEIE KAHGDVFNVF LQILDDGRVT
DSQGRTVSFT NTVIIMTSNV GSQFILNNTD DDANELPYET IKERVMNAAR SVFRPEFMNR
VDEYIVFQPL DREQINRIVR LQLARVQKRI ADRKMKINIT DAAVDLLGSL GYDPNYGARP
VKRVIQQNIE NELAKGILRG DFKEEDGILI DTEVTAFSNG QLPQHKLIFK KIESETAGAE
QEEEAFSKQS S
//
