query	gene_id	record_type	id	name	namespace_or_position	evidence	source	query_reference	annotation_reference	annotation_gene_id	annotation_assembly	mapping_category	mapped_annotation
TkA01G300300	TkA01G300300	function	TkA01G300300	Similar to HSC-2: Heat shock cognate 70 kDa protein 2 (Solanum lycopersicum OX%3D4081)		GFF-derived	GCA_047496595.1_OSU_TarKok_2.0	TK1151	OH1004	LXL04_037426	GCA_047496595.1_OSU_TarKok_2.0	many_to_one	True
TkA01G300300	TkA01G300300	GO	GO:0006950	response to stress	biological_process	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=67.327; coverage=42.259; evalue=5.99e-41; UniProt GO evidence=IEA:UniProtKB-ARBA	UniProtKB/Swiss-Prot DAT 2026 current_release	TK1151	OH1004	LXL04_037426	GCA_047496595.1_OSU_TarKok_2.0	many_to_one	True
TkA01G300300	TkA01G300300	GO	GO:0042026	protein refolding	biological_process	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=67.327; coverage=42.259; evalue=5.99e-41; UniProt GO evidence=IBA:GO_Central	UniProtKB/Swiss-Prot DAT 2026 current_release	TK1151	OH1004	LXL04_037426	GCA_047496595.1_OSU_TarKok_2.0	many_to_one	True
TkA01G300300	TkA01G300300	GO	GO:0005737	cytoplasm	cellular_component	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=67.327; coverage=42.259; evalue=5.99e-41; UniProt GO evidence=IBA:GO_Central	UniProtKB/Swiss-Prot DAT 2026 current_release	TK1151	OH1004	LXL04_037426	GCA_047496595.1_OSU_TarKok_2.0	many_to_one	True
TkA01G300300	TkA01G300300	GO	GO:0005524	ATP binding	molecular_function	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=67.327; coverage=42.259; evalue=5.99e-41; UniProt GO evidence=IEA:UniProtKB-KW	UniProtKB/Swiss-Prot DAT 2026 current_release	TK1151	OH1004	LXL04_037426	GCA_047496595.1_OSU_TarKok_2.0	many_to_one	True
TkA01G300300	TkA01G300300	GO	GO:0016887	ATP hydrolysis activity	molecular_function	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=67.327; coverage=42.259; evalue=5.99e-41; UniProt GO evidence=IBA:GO_Central	UniProtKB/Swiss-Prot DAT 2026 current_release	TK1151	OH1004	LXL04_037426	GCA_047496595.1_OSU_TarKok_2.0	many_to_one	True
TkA01G300300	TkA01G300300	GO	GO:0031072	heat shock protein binding	molecular_function	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=67.327; coverage=42.259; evalue=5.99e-41; UniProt GO evidence=IBA:GO_Central	UniProtKB/Swiss-Prot DAT 2026 current_release	TK1151	OH1004	LXL04_037426	GCA_047496595.1_OSU_TarKok_2.0	many_to_one	True
TkA01G300300	TkA01G300300	GO	GO:0044183	protein folding chaperone	molecular_function	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=67.327; coverage=42.259; evalue=5.99e-41; UniProt GO evidence=IBA:GO_Central	UniProtKB/Swiss-Prot DAT 2026 current_release	TK1151	OH1004	LXL04_037426	GCA_047496595.1_OSU_TarKok_2.0	many_to_one	True
TkA01G300300	TkA01G300300	KEGG	sly:101247772	KEGG gene cross-reference from reviewed UniProt hit; pathway name pending		Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=67.327; coverage=42.259; evalue=5.99e-41	UniProtKB/Swiss-Prot DAT 2026 current_release	TK1151	OH1004	LXL04_037426	GCA_047496595.1_OSU_TarKok_2.0	many_to_one	True
TkA01G300300	TkA01G300300	organism_homology	O65719	sp|O65719|HSP7C_ARATH Heat shock 70 kDa protein 3	Arabidopsis thaliana	identity=65.5; coverage=44.845; evalue=5.01e-30; rank=2	TK1151 Swiss-Prot homology; source_gene=TkA01G300300; source_db=UniProt Swiss-Prot local database (DIAMOND)	TK1151	TK1151	TkA01G300300			False
TkA01G300300	TkA01G300300	organism_homology_status	Oryza sativa	当前查询蛋白的来源表暂无该物种命中；不能据此判断不存在同源。	no_species_hit			TK1151	TK1151	TkA01G300300			False
TkA01G300300	TkA01G300300	reference_gene_function	At3g09440	In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions.	Arabidopsis	No verified direct reference in this release							
TkA01G300300	TkA01G300300	reference_gene_literature	At5g02500	In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable).	Arabidopsis	Physiological and molecular assessment of altered expression of Hsc70-1 in Arabidopsis. Evidence for pleiotropic consequences.; PMID=12805626; DOI=10.1104/pp.102.019398	https://pubmed.ncbi.nlm.nih.gov/12805626/						
TkA01G300300	TkA01G300300	reference_gene_literature	At5g02500	In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable).	Arabidopsis	Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones regulates Arabidopsis immune responses.; PMID=18065690; DOI=10.1105/tpc.107.051896	https://pubmed.ncbi.nlm.nih.gov/18065690/						
TkA01G300300	TkA01G300300	reference_gene_literature	At5g02500	In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable).	Arabidopsis	WPP-domain proteins mimic the activity of the HSC70-1 chaperone in preventing mistargeting of RanGAP1-anchoring protein WIT1.; PMID=19617588; DOI=10.1104/pp.109.143404	https://pubmed.ncbi.nlm.nih.gov/19617588/						
TkA01G300300	TkA01G300300	reference_gene_literature	At5g02500	In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable).	Arabidopsis	The cytosolic/nuclear HSC70 and HSP90 molecular chaperones are important for stomatal closure and modulate abscisic acid-dependent physiological responses in Arabidopsis.; PMID=21586649; DOI=10.1104/pp.111.174425	https://pubmed.ncbi.nlm.nih.gov/21586649/