y
Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_499839g0010 |
Family | GT4 |
Protein Properties | Length: 151 Molecular Weight: 16828.2 Isoelectric Point: 5.2916 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT4 | 10 | 119 | 1.6e-30 |
REYLEELKDMASREGVSDKVVFLPSCSTAQRDALLSECLCVVYTPKDEHFGIVPLEAMAAQKPVIACNSGGPLESIKHDVTGFLCEPSPQNFSSAMLMLI KDADKAEKMG |
Full Sequence |
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Protein Sequence Length: 151 Download |
GFDKRLKENR EYLEELKDMA SREGVSDKVV FLPSCSTAQR DALLSECLCV VYTPKDEHFG 60 IVPLEAMAAQ KPVIACNSGG PLESIKHDVT GFLCEPSPQN FSSAMLMLIK DADKAEKMGR 120 EARDHVEKTF SRHVLGESLN RIIFDVVDTT H 180 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd03795 | GT1_like_4 | 7.0e-24 | 14 | 136 | 129 | + This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes. | ||
pfam00534 | Glycos_transf_1 | 4.0e-27 | 11 | 125 | 116 | + Glycosyl transferases group 1. Mutations in this domain of human PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family. | ||
COG0438 | RfaG | 3.0e-27 | 11 | 147 | 138 | + Glycosyltransferase [Cell envelope biogenesis, outer membrane] | ||
cd03801 | GT1_YqgM_like | 4.0e-29 | 11 | 131 | 122 | + This family is most closely related to the GT1 family of glycosyltransferases and named after YqgM in Bacillus licheniformis about which little is known. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea. | ||
cd03805 | GT1_ALG2_like | 3.0e-69 | 1 | 139 | 140 | + This family is most closely related to the GT1 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAC83030.1 | 0 | 1 | 149 | 253 | 401 | Similar to gene pi010 glycosyltransferase gi |
GenBank | AAM26674.1 | 0 | 1 | 149 | 251 | 399 | At1g78800/F9K20_16 [Arabidopsis thaliana] |
GenBank | ACU21459.1 | 0 | 1 | 146 | 256 | 401 | unknown [Glycine max] |
RefSeq | NP_178001.2 | 0 | 1 | 149 | 251 | 399 | glycosyl transferase family 1 protein [Arabidopsis thaliana] |
RefSeq | XP_001778889.1 | 0 | 1 | 147 | 262 | 408 | predicted protein [Physcomitrella patens subsp. patens] |
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 | 2f9f_A | 0.00000000000005 | 27 | 117 | 78 | 168 | A Chain A, Crystal Structure Of The Putative Mannosyl Transferase (Wbaz-1)from Archaeoglobus Fulgidus, Northeast Structural Genomics Target Gr29a |
PDB | 2jjm_L | 0.0000000003 | 25 | 147 | 265 | 386 | A Chain A, Crystal Structure Of A Family Gt4 Glycosyltransferase From Bacillus Anthracis Orf Ba1558. |
PDB | 2jjm_K | 0.0000000003 | 25 | 147 | 265 | 386 | A Chain A, Crystal Structure Of A Family Gt4 Glycosyltransferase From Bacillus Anthracis Orf Ba1558. |
PDB | 2jjm_J | 0.0000000003 | 25 | 147 | 265 | 386 | A Chain A, Crystal Structure Of A Family Gt4 Glycosyltransferase From Bacillus Anthracis Orf Ba1558. |
PDB | 2jjm_I | 0.0000000003 | 25 | 147 | 265 | 386 | A Chain A, Crystal Structure Of A Family Gt4 Glycosyltransferase From Bacillus Anthracis Orf Ba1558. |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DR568816 | 151 | 1 | 151 | 0 |
DR561666 | 151 | 1 | 151 | 0 |
DR559195 | 151 | 1 | 151 | 0 |
DR687818 | 151 | 1 | 151 | 0 |
DT634293 | 151 | 1 | 151 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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