"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PF13844"	"{'subfamilies': 0, 'domain_architectures': 2863, 'interactions': 0, 'matches': 23550, 'pathways': 0, 'proteins': 13844, 'proteomes': 4945, 'sets': 1, 'structural_models': {'alphafold': 10349, 'bfvd': 0}, 'structures': 55, 'taxa': 13916}"	"{}"	"[{'text': '<p>This family of glycosyltransferases includes O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase, an enzyme which catalyses the addition of O-GlcNAc to serine and threonine residues [[cite:PUB00047969],[cite:PUB00049883]]. In addition to its function as an O-GlcNAc transferase, human OGT, [swissprot:O15294], also appears to proteolytically cleave the epigenetic cell-cycle regulator HCF-1 [[cite:PUB00070115]].</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	"IPR029489"	False	False	False	"{'PUB00049883': {'PMID': 18536723, 'ISBN': None, 'volume': '15', 'issue': '7', 'year': 2008, 'title': 'Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation.', 'URL': None, 'raw_pages': '764-5', 'medline_journal': 'Nat Struct Mol Biol', 'ISO_journal': 'Nat. Struct. Mol. Biol.', 'authors': ['Martinez-Fleites C', 'Macauley MS', 'He Y', 'Shen DL', 'Vocadlo DJ', 'Davies GJ.'], 'DOI_URL': 'http://dx.doi.org/10.1038/nsmb.1443'}, 'PUB00070115': {'PMID': 21295698, 'ISBN': None, 'volume': '144', 'issue': '3', 'year': 2011, 'title': 'O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1.', 'URL': None, 'raw_pages': '376-88', 'medline_journal': 'Cell', 'ISO_journal': 'Cell', 'authors': ['Capotosti F', 'Guernier S', 'Lammers F', 'Waridel P', 'Cai Y', 'Jin J', 'Conaway JW', 'Conaway RC', 'Herr W.'], 'DOI_URL': 'http://dx.doi.org/10.1016/j.cell.2010.12.030'}, 'PUB00047969': {'PMID': 18818698, 'ISBN': None, 'volume': '27', 'issue': '20', 'year': 2008, 'title': 'Structural insights into mechanism and specificity of O-GlcNAc transferase.', 'URL': None, 'raw_pages': '2780-8', 'medline_journal': 'EMBO J', 'ISO_journal': 'EMBO J.', 'authors': ['Clarke AJ', 'Hurtado-Guerrero R', 'Pathak S', 'Schuttelkopf AW', 'Borodkin V', 'Shepherd SM', 'Ibrahim AF', 'van Aalten DM.'], 'DOI_URL': 'http://dx.doi.org/10.1038/emboj.2008.186'}}"	""	"{'name': 'Glycosyl transferase family 41', 'short': 'Glyco_transf_41'}"	""	"{'accession': '5npr', 'name': 'The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor'}"	"{'accession': 'CL0113', 'name': 'GT-B'}"	"pfam"	"family"	"[{'title': 'N-glycosyltransferase', 'extract': '<p><b><i>N</i>-glycosyltransferase</b> is an enzyme in prokaryotes which transfers individual hexoses onto asparagine sidechains in substrate proteins, using a nucleotide-bound intermediary, within the cytoplasm. They are distinct from regular <span><i>N</i>-glycosylating enzymes</span>, which are oligosaccharyltransferases that transfer pre-assembled oligosaccharides. Both enzyme families however target a shared amino acid sequence asparagine—-any amino acid except proline—serine or threonine (N–x–S/T), with some variations.</p>', 'thumbnail': None}]"