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
LXL04_012377	gene-LXL04_012377	KAL4576285.1	OH-1004	1	O22283	RHC2A_ARATH	Swiss-Prot		Probable E3 ubiquitin-protein ligase RHC2A OS=Arabidopsis thaliana OX=3702 GN=RHC2A PE=2 SV=1	Arabidopsis thaliana	RHC2A	51.198	334	78.765	1.71e-96	297.0	strong_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At2g39720	可能的 E3 泛素蛋白连接酶，在体外可能具有 E3 泛素连接酶活性。	Probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro.	[]
LXL04_012377	gene-LXL04_012377	KAL4576285.1	OH-1004	2	Q9SNB6	RDUF1_ARATH	Swiss-Prot		E3 ubiquitin-protein ligase RDUF1 OS=Arabidopsis thaliana OX=3702 GN=RDUF1 PE=1 SV=1	Arabidopsis thaliana	RDUF1	48.083	339	78.272	1.07e-92	287.0	moderate_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At3g46620	参与正向调控脱落酸依赖干旱胁迫响应的E3泛素蛋白连接酶。	E3 ubiquitin-protein ligase involved in the positive regulation of abscisic acid-dependent drought stress responses.	"[{""pmid"":""22405823"",""title"":""Suppression of Arabidopsis RING-DUF1117 E3 ubiquitin ligases, AtRDUF1 and AtRDUF2, reduces tolerance to ABA-mediated drought stress."",""doi"":""10.1016/j.bbrc.2012.02.131"",""url"":""https://pubmed.ncbi.nlm.nih.gov/22405823/"",""year"":""2012"",""journal"":""Biochemical and biophysical research communications"",""authors"":""Kim SJ; Ryu MY; Kim WT"",""matched_aliases"":[""At3g46620"",""AtRDUF1""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed""],""fulltext_reviewed"":false},{""pmid"":""23951086"",""title"":""The E3 ligase AtRDUF1 positively regulates salt stress responses in Arabidopsis thaliana."",""doi"":""10.1371/journal.pone.0071078"",""url"":""https://pubmed.ncbi.nlm.nih.gov/23951086/"",""year"":""2013"",""journal"":""PloS one"",""authors"":""Li J; Han Y; Zhao Q; Li C; Xie Q; Chong K; Xu Y"",""matched_aliases"":[""AtRDUF1""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed""],""fulltext_reviewed"":false}]"
LXL04_012377	gene-LXL04_012377	KAL4576285.1	OH-1004	3	Q940T5	RDUF2_ARATH	Swiss-Prot		E3 ubiquitin-protein ligase RDUF2 OS=Arabidopsis thaliana OX=3702 GN=DURF2 PE=1 SV=1	Arabidopsis thaliana	DURF2	49.541	327	78.519	2.61e-89	278.0	moderate_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At5g59550	参与正向调控脱落酸依赖干旱胁迫响应的E3泛素蛋白连接酶。	E3 ubiquitin-protein ligase involved in the positive regulation of abscisic acid-dependent drought stress responses.	"[{""pmid"":""22405823"",""title"":""Suppression of Arabidopsis RING-DUF1117 E3 ubiquitin ligases, AtRDUF1 and AtRDUF2, reduces tolerance to ABA-mediated drought stress."",""doi"":""10.1016/j.bbrc.2012.02.131"",""url"":""https://pubmed.ncbi.nlm.nih.gov/22405823/"",""year"":""2012"",""journal"":""Biochemical and biophysical research communications"",""authors"":""Kim SJ; Ryu MY; Kim WT"",""matched_aliases"":[""At5g59550""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed""],""fulltext_reviewed"":false}]"
LXL04_012377	gene-LXL04_012377	KAL4576285.1	OH-1004	5	Q8LPN7	RNG1L_ARATH	Swiss-Prot		E3 ubiquitin-protein ligase RING1-like OS=Arabidopsis thaliana OX=3702 GN=At3g19950 PE=1 SV=1	Arabidopsis thaliana	At3g19950	31.66	259	60.247	1.74e-38	144.0	moderate_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At3g19950	E3 泛素蛋白连接酶以硫酯的形式接受来自 E2 泛素结合酶的泛素，然后将泛素直接转移至目标底物。	E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.	[]