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
LXL04_017781	LXL04_017781	function	LXL04_017781	Similar to HSC-2: Heat shock cognate 70 kDa protein 2 (Solanum lycopersicum OX%3D4081)		GFF-derived	GCA_047496595.1_OSU_TarKok_2.0	OH1004	OH1004	LXL04_017781	GCA_047496595.1_OSU_TarKok_2.0	annotation_conflict	False
LXL04_017781	LXL04_017781	GO	GO:0006950	response to stress	biological_process	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=69.325; coverage=48.802; evalue=1.22e-150; UniProt GO evidence=IEA:UniProtKB-ARBA	UniProtKB/Swiss-Prot DAT 2026 current_release	OH1004	OH1004	LXL04_017781	GCA_047496595.1_OSU_TarKok_2.0	annotation_conflict	False
LXL04_017781	LXL04_017781	GO	GO:0042026	protein refolding	biological_process	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=69.325; coverage=48.802; evalue=1.22e-150; UniProt GO evidence=IBA:GO_Central	UniProtKB/Swiss-Prot DAT 2026 current_release	OH1004	OH1004	LXL04_017781	GCA_047496595.1_OSU_TarKok_2.0	annotation_conflict	False
LXL04_017781	LXL04_017781	GO	GO:0005737	cytoplasm	cellular_component	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=69.325; coverage=48.802; evalue=1.22e-150; UniProt GO evidence=IBA:GO_Central	UniProtKB/Swiss-Prot DAT 2026 current_release	OH1004	OH1004	LXL04_017781	GCA_047496595.1_OSU_TarKok_2.0	annotation_conflict	False
LXL04_017781	LXL04_017781	GO	GO:0005524	ATP binding	molecular_function	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=69.325; coverage=48.802; evalue=1.22e-150; UniProt GO evidence=IEA:UniProtKB-KW	UniProtKB/Swiss-Prot DAT 2026 current_release	OH1004	OH1004	LXL04_017781	GCA_047496595.1_OSU_TarKok_2.0	annotation_conflict	False
LXL04_017781	LXL04_017781	GO	GO:0016887	ATP hydrolysis activity	molecular_function	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=69.325; coverage=48.802; evalue=1.22e-150; UniProt GO evidence=IBA:GO_Central	UniProtKB/Swiss-Prot DAT 2026 current_release	OH1004	OH1004	LXL04_017781	GCA_047496595.1_OSU_TarKok_2.0	annotation_conflict	False
LXL04_017781	LXL04_017781	GO	GO:0031072	heat shock protein binding	molecular_function	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=69.325; coverage=48.802; evalue=1.22e-150; UniProt GO evidence=IBA:GO_Central	UniProtKB/Swiss-Prot DAT 2026 current_release	OH1004	OH1004	LXL04_017781	GCA_047496595.1_OSU_TarKok_2.0	annotation_conflict	False
LXL04_017781	LXL04_017781	GO	GO:0044183	protein folding chaperone	molecular_function	Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=69.325; coverage=48.802; evalue=1.22e-150; UniProt GO evidence=IBA:GO_Central	UniProtKB/Swiss-Prot DAT 2026 current_release	OH1004	OH1004	LXL04_017781	GCA_047496595.1_OSU_TarKok_2.0	annotation_conflict	False
LXL04_017781	LXL04_017781	KEGG	sly:101247772	KEGG gene cross-reference from reviewed UniProt hit; pathway name pending		Swiss-Prot reviewed homolog transfer; hit_rank=1; identity=69.325; coverage=48.802; evalue=1.22e-150	UniProtKB/Swiss-Prot DAT 2026 current_release	OH1004	OH1004	LXL04_017781	GCA_047496595.1_OSU_TarKok_2.0	annotation_conflict	False
LXL04_017781	LXL04_017781	organism_homology	P22953	Heat shock 70 kDa protein 1 OS=Arabidopsis thaliana OX=3702 GN=HSP70-1 PE=1 SV=3	Arabidopsis thaliana	identity=66.871; coverage=44.611; evalue=1.53e-144; rank=7	OH-1004 Swiss-Prot homology; source_gene=LXL04_017781; source_db=UniProt Swiss-Prot current_release 2026-06-10	OH1004	OH1004	LXL04_017781			False
LXL04_017781	LXL04_017781	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			OH1004	OH1004	LXL04_017781			False
LXL04_017781	LXL04_017781	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/						
LXL04_017781	LXL04_017781	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/						
LXL04_017781	LXL04_017781	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/						
LXL04_017781	LXL04_017781	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/						
LXL04_017781	LXL04_017781	reference_gene_function	At1g56410	Heat shock 70 kDa protein 18.	Arabidopsis	No verified direct reference in this release