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Basic Information | |
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Species | Oryza sativa |
Cazyme ID | LOC_Os02g58590.1 |
Family | GT13 |
Protein Properties | Length: 449 Molecular Weight: 51547.9 Isoelectric Point: 7.8356 |
Chromosome | Chromosome/Scaffold: 2 Start: 35812497 End: 35817776 |
Description | alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase, putative |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT13 | 22 | 283 | 0 |
IQVRLFSTQSHYADRLAQAEKSENQCTSQLRSLIDQVSSQQEKIVALEEMKIRQDEERVHLKILIQDLEKRSVQTLVNNNVAPVAAVVVMACNRPDYLQR TVESILKYQTSVASKFPLFISQDGINGEVKKKALSYNEITYMQIHESYQGNSRSNGYKLSSEKQGHNHTPNLWMYCLKGKLDATVLYFPPPHNIGMQQSD ICKKHGKYFSAKTLSEHYKWALDELFIKHNFARVIILEDDMEIAPDFFDYFEAAAKLLDNDN | |||
GT13 | 304 | 426 | 0 |
VGSSMGQFFRQYLEPIKLNDAHIKWNSEDLSYLKEDKFLIQFGKDVASATPLHGSDAALKAHNMDADVRIQYNDQEDFERIARQFGIFEEWKDGIPRTAY KGVVVFRYKSSRRRIYLVGPDSL |
Full Sequence |
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Protein Sequence Length: 449 Download |
MARSPCDLRI LLVAAAAAFI YIQVRLFSTQ SHYADRLAQA EKSENQCTSQ LRSLIDQVSS 60 QQEKIVALEE MKIRQDEERV HLKILIQDLE KRSVQTLVNN NVAPVAAVVV MACNRPDYLQ 120 RTVESILKYQ TSVASKFPLF ISQDGINGEV KKKALSYNEI TYMQIHESYQ GNSRSNGYKL 180 SSEKQGHNHT PNLWMYCLKG KLDATVLYFP PPHNIGMQQS DICKKHGKYF SAKTLSEHYK 240 WALDELFIKH NFARVIILED DMEIAPDFFD YFEAAAKLLD NDNWKAKDFI CNVSNCFAAI 300 PVTVGSSMGQ FFRQYLEPIK LNDAHIKWNS EDLSYLKEDK FLIQFGKDVA SATPLHGSDA 360 ALKAHNMDAD VRIQYNDQED FERIARQFGI FEEWKDGIPR TAYKGVVVFR YKSSRRRIYL 420 VGPDSLSQLR FLNWTYARMK GNEILIDI* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd02514 | GT13_GLCNAC-TI | 1.0e-29 | 115 | 282 | 170 | + GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13. | ||
cd02514 | GT13_GLCNAC-TI | 3.0e-37 | 304 | 425 | 125 | + GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13. | ||
pfam03071 | GNT-I | 4.0e-48 | 305 | 429 | 125 | + GNT-I family. Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, GLCNAC-T I) EC:2.4.1.101 transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide. This is an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localised to the Golgi apparatus, and is probably distributed in all tissues. The catalytic domain is located at the C-terminus. | ||
pfam03071 | GNT-I | 2.0e-61 | 15 | 282 | 270 | + GNT-I family. Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, GLCNAC-T I) EC:2.4.1.101 transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide. This is an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localised to the Golgi apparatus, and is probably distributed in all tissues. The catalytic domain is located at the C-terminus. |
Gene Ontology | |
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GO Term | Description |
GO:0000139 | Golgi membrane |
GO:0003827 | alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity |
GO:0005794 | Golgi apparatus |
GO:0005975 | carbohydrate metabolic process |
GO:0006464 | cellular protein modification process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAB37480.1 | 0 | 1 | 429 | 1 | 452 | glycosyltransferase like protein (fragment) [Arabidopsis thaliana] |
EMBL | CAB37564.1 | 0 | 1 | 433 | 1 | 456 | glycosyltransferase like protein [Arabidopsis thaliana] |
EMBL | CAC80700.1 | 0 | 1 | 433 | 1 | 443 | N-acetylglucosaminyltransferase I [Arabidopsis thaliana] |
EMBL | CBI29533.1 | 0 | 1 | 429 | 1 | 436 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_195537.2 | 0 | 1 | 433 | 1 | 443 | CGL1 (COMPLEX GLYCAN LESS 1); alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase/ protein N-acetylglucosaminyltransferase/ transferase, transferring glycosyl groups [Arabidopsis thaliana] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1foa_A | 0.00000000000001 | 305 | 425 | 221 | 339 | A Chain A, Crystal Structure Of N-acetylglucosaminyltransferase I |
PDB | 1foa_A | 0.000000000003 | 105 | 282 | 8 | 135 | A Chain A, Crystal Structure Of N-acetylglucosaminyltransferase I |
PDB | 1fo9_A | 0.00000000000001 | 305 | 425 | 221 | 339 | A Chain A, Crystal Structure Of N-acetylglucosaminyltransferase I |
PDB | 1fo9_A | 0.000000000003 | 105 | 282 | 8 | 135 | A Chain A, Crystal Structure Of N-acetylglucosaminyltransferase I |
PDB | 1fo8_A | 0.00000000000001 | 305 | 425 | 216 | 334 | A Chain A, Crystal Structure Of N-Acetylglucosaminyltransferase I |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FL718546 | 290 | 1 | 290 | 0 |
CB631083 | 276 | 7 | 282 | 0 |
DT652345 | 282 | 1 | 282 | 0 |
GR324011 | 282 | 1 | 282 | 0 |
EE030388 | 279 | 1 | 279 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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