query	query_gene_id	query_protein_id	source_reference	hit_rank	swissprot_acc	swissprot_entry	database_section	target_gene_id	description	organism	homolog_gene_name	percent_identity	alignment_length	query_coverage	evalue	bitscore	confidence	evidence_type	source_db	reference_gene_id	reference_function_zh	reference_function_en	reference_papers_json
TkA03G413650	TkA03G413650	TkA03G413650.1	TK1151	1	P42762	CLPD_ARATH	Swiss-Prot		sp|P42762|CLPD_ARATH Chaperone protein ClpD, chloroplastic	Arabidopsis thaliana	CLPD	70.5	899	93.114	0.0	1196.0	High	TK1151 direct protein BLASTP	UniProt Swiss-Prot local database (DIAMOND)	At5g51070	与 ClpP 样蛋白酶相互作用的分子伴侣，参与叶绿体中变性蛋白质的降解。	Molecular chaperone that interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast.	"[{""pmid"":""21737456"",""title"":""Insights into the Clp/HSP100 chaperone system from chloroplasts of Arabidopsis thaliana."",""doi"":""10.1074/jbc.m110.211946"",""url"":""https://pubmed.ncbi.nlm.nih.gov/21737456/"",""year"":""2011"",""journal"":""The Journal of biological chemistry"",""authors"":""Rosano GL, Bruch EM, Ceccarelli EA."",""matched_aliases"":[""AtCLPD"",""CLPD""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed"",""EuropePMC""],""fulltext_reviewed"":false},{""pmid"":""22545953"",""title"":""Chloroplastic Hsp100 chaperones ClpC2 and ClpD interact in vitro with a transit peptide only when it is located at the N-terminus of a protein."",""doi"":""10.1186/1471-2229-12-57"",""url"":""https://pubmed.ncbi.nlm.nih.gov/22545953/"",""year"":""2012"",""journal"":""BMC plant biology"",""authors"":""Bruch EM, Rosano GL, Ceccarelli EA."",""matched_aliases"":[""AtCLPD"",""CLPD""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed"",""EuropePMC""],""fulltext_reviewed"":false},{""pmid"":""25149061"",""title"":""Characterization of the accessory protein ClpT1 from Arabidopsis thaliana: oligomerization status and interaction with Hsp100 chaperones."",""doi"":""10.1186/s12870-014-0228-0"",""url"":""https://pubmed.ncbi.nlm.nih.gov/25149061/"",""year"":""2014"",""journal"":""BMC plant biology"",""authors"":""Colombo CV, Ceccarelli EA, Rosano GL."",""matched_aliases"":[""CLPD""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed"",""EuropePMC""],""fulltext_reviewed"":false}]"
TkA03G413650	TkA03G413650	TkA03G413650.1	TK1151	2	Q7XL03	CLPD2_ORYSJ	Swiss-Prot		sp|Q7XL03|CLPD2_ORYSJ Chaperone protein ClpD2, chloroplastic	Oryza sativa subsp. japonica	CLPD2	65.4	882	90.89	0.0	1084.0	High	TK1151 direct protein BLASTP	UniProt Swiss-Prot local database (DIAMOND)	Os04g0405000	分子伴侣蛋白，可能与参与叶绿体中变性蛋白降解的ClpP样蛋白酶相互作用。	Molecular chaperone that may interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast.	[]
TkA03G413650	TkA03G413650	TkA03G413650.1	TK1151	3	Q6H795	CLPD1_ORYSJ	Swiss-Prot		sp|Q6H795|CLPD1_ORYSJ Chaperone protein ClpD1, chloroplastic	Oryza sativa subsp. japonica	CLPD1	66.4	880	90.784	0.0	1083.0	High	TK1151 direct protein BLASTP	UniProt Swiss-Prot local database (DIAMOND)	Os02g0526400	可能在热应激反应中发挥作用的分子伴侣。	Molecular chaperone that may function in heat stress response.	"[{""pmid"":""20141629"",""title"":""Genome-wide analysis of rice ClpB/HSP100, ClpC and ClpD genes."",""doi"":""10.1186/1471-2164-11-95"",""url"":""https://pubmed.ncbi.nlm.nih.gov/20141629/"",""year"":""2010"",""journal"":""BMC genomics"",""authors"":""Singh A, Singh U, Mittal D, Grover A."",""matched_aliases"":[""CLPD1"",""OsCLPD1""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed"",""EuropePMC""],""fulltext_reviewed"":false},{""pmid"":""27457985"",""title"":""Constitutive over-expression of rice ClpD1 protein enhances tolerance to salt and desiccation stresses in transgenic Arabidopsis plants."",""doi"":""10.1016/j.plantsci.2016.06.004"",""url"":""https://pubmed.ncbi.nlm.nih.gov/27457985/"",""year"":""2016"",""journal"":""Plant science : an international journal of experimental plant biology"",""authors"":""Mishra RC, Richa, Grover A."",""matched_aliases"":[""CLPD1"",""OsCLPD1""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed"",""EuropePMC""],""fulltext_reviewed"":false}]"
TkA03G413650	TkA03G413650	TkA03G413650.1	TK1151	4	Q2QVG9	CLPC2_ORYSJ	Swiss-Prot		sp|Q2QVG9|CLPC2_ORYSJ Chaperone protein ClpC2, chloroplastic	Oryza sativa subsp. japonica	CLPC2	47.8	859	90.042	1.62e-253	737.0	Medium	TK1151 direct protein BLASTP	UniProt Swiss-Prot local database (DIAMOND)	Os12g0230100	分子伴侣蛋白，可能与参与叶绿体中变性蛋白降解的ClpP样蛋白酶相互作用。	Molecular chaperone that may interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast.	[]