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Database: UniProt
Entry: A0A0S3T7U2_PHAAN
LinkDB: A0A0S3T7U2_PHAAN
Original site: A0A0S3T7U2_PHAAN 
ID   A0A0S3T7U2_PHAAN        Unreviewed;       977 AA.
AC   A0A0S3T7U2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN   Name=Vigan.11G052300 {ECO:0000313|EMBL:BAU01314.1};
GN   ORFNames=VIGAN_11052300 {ECO:0000313|EMBL:BAU01314.1};
OS   Vigna angularis var. angularis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=157739 {ECO:0000313|EMBL:BAU01314.1, ECO:0000313|Proteomes:UP000291084};
RN   [1] {ECO:0000313|EMBL:BAU01314.1, ECO:0000313|Proteomes:UP000291084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX   PubMed=26616024; DOI=10.1038/srep16780;
RA   Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA   Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA   Tomooka N.;
RT   "The power of single molecule real-time sequencing technology in the de
RT   novo assembly of a eukaryotic genome.";
RL   Sci. Rep. 5:16780-16780(2015).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; AP015044; BAU01314.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S3T7U2; -.
DR   Proteomes; UP000291084; Chromosome 11.
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:SF187; CHAPERONE PROTEIN CLPB3; 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|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:UP000291084};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          81..225
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          520..605
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   977 AA;  109409 MW;  F31E366EE0BEBF06 CRC64;
     MASATSFPGV SLRPSVPIRS HARLAQCRVS FGFPPNLTSL KSLSSVPSKK REAFSNGSSR
     TGRILAPFSV RCSISSSGKI IQQEFTEMAW QAITTAPEVA KENKHQIVET EHLMKALLEQ
     KNGLARRIFS KVGVDNTRLL EATDKHIKRQ PKVLGESGGS MLGRDLEALI QKAKDIKKAY
     GDSFVSVEHF VLGFAQDKRF GKTLFRDFQI SEQGLKSAIE SIRGRQSVID QDPEGKYEAL
     EKYGKDLTAM AKAGKLDPVI GRDDEIRRCI QILSRRTKNN PVLIGEPGVG KTAISEGLAQ
     RIVQGDVPQA LMNRRLISLD MGALIAGAKY RGEFEDRLKA VLKEVTESDG QIILFIDEIH
     TVVGAGATNG ALDAGNLLKP MLGRGELRCI GATTLDEYRK YIEKDPALER RFQQVFVDQP
     SVENTISILR GLRERYELHH GVRISDSALV DAAILSDRYI SGRFLPDKAI DLVDEAAAKL
     KMEITSKPTA LDEINRSVLK LEMERLSLMN DTDKASKDRL NRLETELSLL KGKQDELNGQ
     WEHEKSVMTR LQSIKEEIDR VNLEIQQAER EYDLNRAAEL KYGSLNSLQR QLESVEKELH
     EYMNSGKSML REEVIGSDIA EIVSKWTGIP ISKLQQSERE KLLYLEEELH KRVVGQDPAV
     KAVAEAIQRS RAGLSDPHRP IASFMFMGPT GVGKTELAKA LASYLFNTEE ALVRIDMSEY
     MDKHTVSRLI GAPPGYVGYE EGGQLTETVR RRPYAVILFD EIEKAHSDVF NVFLQILDDG
     RVTDSQGRTV SFTNTVIIMT SNVGSQYILN TDNDTVPKES AYETIKQKVM DAARSIFRPE
     FMNRVDEYIV FRPLDRDQIG SIVRLQLERV QKRIADRKMK IQVTEAAIQL LGSLGYDPNY
     GARPVKRVIQ QNVENELAKG ILRGEFRDED TILVDTEVTV FANGQLPQQK LVFKRVGTDA
     ESSSTVKENW EGSPQIL
//
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