PubMed:9451011
Annnotations
sentences
{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":85},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":86,"end":193},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":194,"end":404},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":405,"end":554},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":555,"end":678},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":679,"end":786},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":787,"end":951},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":952,"end":1223},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1224,"end":1407},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":85},"obj":"Sentence"},{"id":"T2","span":{"begin":86,"end":193},"obj":"Sentence"},{"id":"T3","span":{"begin":194,"end":404},"obj":"Sentence"},{"id":"T4","span":{"begin":405,"end":554},"obj":"Sentence"},{"id":"T5","span":{"begin":555,"end":678},"obj":"Sentence"},{"id":"T6","span":{"begin":679,"end":786},"obj":"Sentence"},{"id":"T7","span":{"begin":787,"end":951},"obj":"Sentence"},{"id":"T8","span":{"begin":952,"end":1223},"obj":"Sentence"},{"id":"T9","span":{"begin":1224,"end":1407},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":85},"obj":"Sentence"},{"id":"T2","span":{"begin":86,"end":193},"obj":"Sentence"},{"id":"T3","span":{"begin":194,"end":404},"obj":"Sentence"},{"id":"T4","span":{"begin":405,"end":554},"obj":"Sentence"},{"id":"T5","span":{"begin":555,"end":678},"obj":"Sentence"},{"id":"T6","span":{"begin":679,"end":786},"obj":"Sentence"},{"id":"T7","span":{"begin":787,"end":951},"obj":"Sentence"},{"id":"T8","span":{"begin":952,"end":1223},"obj":"Sentence"},{"id":"T9","span":{"begin":1224,"end":1407},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}
GlycoBiology-GDGDB
{"project":"GlycoBiology-GDGDB","denotations":[{"id":"_T1","span":{"begin":41,"end":58},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00008"},{"id":"_T2","span":{"begin":96,"end":113},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00008"},{"id":"_T3","span":{"begin":1126,"end":1144},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00008"},{"id":"_T4","span":{"begin":1347,"end":1365},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00008"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}
GlycoBiology-PACDB
{"project":"GlycoBiology-PACDB","denotations":[{"id":"_T1","span":{"begin":323,"end":347},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC297"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}
GlycoBiology-FMA
{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":114,"end":118},"obj":"FMAID:198663"},{"id":"_T2","span":{"begin":211,"end":215},"obj":"FMAID:198663"},{"id":"_T3","span":{"begin":386,"end":393},"obj":"FMAID:165447"},{"id":"_T4","span":{"begin":386,"end":393},"obj":"FMAID:67257"},{"id":"_T5","span":{"begin":471,"end":475},"obj":"FMAID:198663"},{"id":"_T6","span":{"begin":546,"end":553},"obj":"FMAID:84121"},{"id":"_T7","span":{"begin":546,"end":553},"obj":"FMAID:198075"},{"id":"_T8","span":{"begin":574,"end":584},"obj":"FMAID:82739"},{"id":"_T9","span":{"begin":574,"end":584},"obj":"FMAID:196728"},{"id":"_T10","span":{"begin":659,"end":666},"obj":"FMAID:165447"},{"id":"_T11","span":{"begin":659,"end":666},"obj":"FMAID:67257"},{"id":"_T12","span":{"begin":683,"end":690},"obj":"FMAID:67257"},{"id":"_T13","span":{"begin":683,"end":690},"obj":"FMAID:165447"},{"id":"_T14","span":{"begin":761,"end":778},"obj":"FMAID:167608"},{"id":"_T15","span":{"begin":761,"end":778},"obj":"FMAID:30322"},{"id":"_T16","span":{"begin":941,"end":950},"obj":"FMAID:63832"},{"id":"_T17","span":{"begin":941,"end":950},"obj":"FMAID:162296"},{"id":"_T18","span":{"begin":941,"end":950},"obj":"FMAID:226763"},{"id":"_T19","span":{"begin":1022,"end":1029},"obj":"FMAID:67257"},{"id":"_T20","span":{"begin":1022,"end":1029},"obj":"FMAID:165447"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}
uniprot-human
{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":39,"end":58},"obj":"http://www.uniprot.org/uniprot/Q16706"},{"id":"T2","span":{"begin":94,"end":113},"obj":"http://www.uniprot.org/uniprot/Q16706"},{"id":"T3","span":{"begin":1345,"end":1365},"obj":"http://www.uniprot.org/uniprot/Q16706"},{"id":"T4","span":{"begin":365,"end":367},"obj":"http://www.uniprot.org/uniprot/P03372"},{"id":"T5","span":{"begin":1074,"end":1076},"obj":"http://www.uniprot.org/uniprot/P03372"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}
uniprot-mouse
{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":39,"end":58},"obj":"http://www.uniprot.org/uniprot/P27046"},{"id":"T2","span":{"begin":94,"end":113},"obj":"http://www.uniprot.org/uniprot/P27046"},{"id":"T3","span":{"begin":1345,"end":1365},"obj":"http://www.uniprot.org/uniprot/P27046"},{"id":"T4","span":{"begin":365,"end":367},"obj":"http://www.uniprot.org/uniprot/P19785"},{"id":"T5","span":{"begin":1074,"end":1076},"obj":"http://www.uniprot.org/uniprot/P19785"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}
GlycoBiology-NCBITAXON
{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":64,"end":75},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/454240"},{"id":"T2","span":{"begin":64,"end":75},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/41750"},{"id":"T3","span":{"begin":64,"end":75},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/40382"},{"id":"T4","span":{"begin":64,"end":84},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/162425"},{"id":"T5","span":{"begin":165,"end":171},"obj":"http://purl.bioontology.org/ontology/STY/T004"},{"id":"T6","span":{"begin":172,"end":183},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/454240"},{"id":"T7","span":{"begin":172,"end":183},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/41750"},{"id":"T8","span":{"begin":172,"end":183},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/40382"},{"id":"T9","span":{"begin":172,"end":192},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/162425"},{"id":"T10","span":{"begin":323,"end":336},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4891"},{"id":"T11","span":{"begin":323,"end":336},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4930"},{"id":"T12","span":{"begin":323,"end":336},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4895"},{"id":"T13","span":{"begin":323,"end":336},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/36034"},{"id":"T14","span":{"begin":1271,"end":1278},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/353209"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}
GO-BP
{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":625,"end":638},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T2","span":{"begin":742,"end":748},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T3","span":{"begin":800,"end":808},"obj":"http://purl.obolibrary.org/obo/GO_0007349"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}
GO-CC
{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":365,"end":367},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T2","span":{"begin":1074,"end":1076},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T3","span":{"begin":368,"end":377},"obj":"http://purl.obolibrary.org/obo/GO_0005829"},{"id":"T4","span":{"begin":1077,"end":1086},"obj":"http://purl.obolibrary.org/obo/GO_0005829"},{"id":"T5","span":{"begin":761,"end":769},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T6","span":{"begin":941,"end":950},"obj":"http://purl.obolibrary.org/obo/GO_0043226"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}
GlycoBiology-Epitope
{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":670,"end":673},"obj":"http://www.glycoepitope.jp/epitopes/AN0571"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}
NCBITAXON
{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":64,"end":84},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":172,"end":192},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":323,"end":347},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":361,"end":364},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":1070,"end":1073},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":1167,"end":1170},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"162425"},{"id":"A2","pred":"db_id","subj":"T2","obj":"162425"},{"id":"A3","pred":"db_id","subj":"T3","obj":"4932"},{"id":"A4","pred":"db_id","subj":"T4","obj":"10114"},{"id":"A5","pred":"db_id","subj":"T4","obj":"10116"},{"id":"A6","pred":"db_id","subj":"T6","obj":"10114"},{"id":"A7","pred":"db_id","subj":"T6","obj":"10116"},{"id":"A8","pred":"db_id","subj":"T8","obj":"10114"},{"id":"A9","pred":"db_id","subj":"T8","obj":"10116"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}
Anatomy-UBERON
{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":761,"end":769},"obj":"Body_part"},{"id":"T4","span":{"begin":941,"end":950},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0043226"}],"text":"Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.\nA Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2 protein sequences. The PCR amplification product was used to isolate the full length gene, and DNA sequencing revealed a 3383 bp coding region containing three introns. The predicted 1049 amino acid reading frame contained six potential N-glycosylation sites and encoded a protein of 118 kDa. The protein sequence did not appear to encode a typical fungal signal sequence or membrane spanning domain. Although the cellular location of the A.nidulans mannosidase was not determined, experimental evidence suggested that it was located within a subcellular organelle. The Matchbox sequence similarity matrix indicated that the A.nidulans protein sequence was more highly similar to the rat ER/cytosolic (Rij = 0.33) and S.cerevisiae vacuolar alpha-mannosidases (Rij = 0.43) than the rat and yeast sequences were to each other (Rij = 0.29). These three enzymes were found to be distantly related to other Class 2 sequences, and compose a third subgroup of Class 2 alpha-mannosidases, as shown by ClustalW sequence alignment."}