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Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna30397.1-v1.0-hybrid |
Family | GT31 |
Protein Properties | Length: 680 Molecular Weight: 77562.1 Isoelectric Point: 8.8948 |
Chromosome | Chromosome/Scaffold: 3 Start: 2167887 End: 2172822 |
Description | Galactosyltransferase family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT31 | 446 | 630 | 0 |
ERMAVRKTWMQSSAIKSSRVVVRFFVALNARKEVNAVLKKEAAYFGDIVILPFMDRYELVVLKTISICEFGVQNVTAAYIMKCDDDTFVRLDTVLKEIEG ISSKKSLYMGNLNLLHRPLRSGKWAVTYEEWPEEVYPPYANGPGYIISIDIAKFIASEHGNRSLRLFKMEDVSMGMWVEQFNSSR |
Full Sequence |
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Protein Sequence Length: 680 Download |
MKRLKGEPPV TRRFKLQHLL IGMAALYLVF ISFKFPQFLE IAKALSGDDG YDDMANEDSD 60 LSKPMFNSVY KDTLHRKLED DQHQDAPVRP RKEPLEEKRN GSKTIKPLQH RYGRITGEIM 120 KRRNRTNELS VFERMADEAW TLGLRAWEEL DKLDVKETGD SSIVEGKPES CPSWLSMSGE 180 ELATGDRLMF LPCGLAAGSS ITLVGTSHNA HQEYVPQLAK LRRSNGMVMV SQFMVELQGL 240 KSVDGEDPPK ILHLNPRLRG DWSQRPVIEH NTCYRMQWGS AQRCDGSPSK NSEEMLVDGY 300 ARCEKWMGND MVAAKESKTK TTSWFKRFIG REQKPEVTWP FPFVEGRLFI LTIRAGVDGF 360 HMSVGGRHVT SFPYRTGFTL EDATGLAIKG DVDVHSVYVT SLPASHPSFS PQRVLELSEK 420 WKAHPLPKTP IRLFVGVLSA TNHFAERMAV RKTWMQSSAI KSSRVVVRFF VALNARKEVN 480 AVLKKEAAYF GDIVILPFMD RYELVVLKTI SICEFGVQNV TAAYIMKCDD DTFVRLDTVL 540 KEIEGISSKK SLYMGNLNLL HRPLRSGKWA VTYEEWPEEV YPPYANGPGY IISIDIAKFI 600 ASEHGNRSLR LFKMEDVSMG MWVEQFNSSR VAVQYSHNWK FCQYGCMENY YTAHYQSPRQ 660 MVCLWDKLAR GRAQCCNFR* 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00908 | Gal-bind_lectin | 5.0e-18 | 192 | 397 | 206 | + Galactoside-binding lectin. Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction. | ||
cd00070 | GLECT | 2.0e-19 | 190 | 397 | 208 | + Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation. | ||
pfam01762 | Galactosyl_T | 6.0e-21 | 445 | 631 | 197 | + Galactosyltransferase. This family includes the galactosyltransferases UDP-galactose:2-acetamido-2-deoxy-D-glucose3beta-galactosyltransferase and UDP-Gal:beta-GlcNAc beta 1,3-galactosyltranferase. Specific galactosyltransferases transfer galactose to GlcNAc terminal chains in the synthesis of the lacto-series oligosaccharides types 1 and 2. | ||
pfam00337 | Gal-bind_lectin | 4.0e-23 | 191 | 397 | 207 | + Galactoside-binding lectin. This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5). | ||
PLN03133 | PLN03133 | 1.0e-119 | 134 | 676 | 558 | + beta-1,3-galactosyltransferase; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0005529 | Interacting selectively and non-covalently with any carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates." [CHEBI:16646, GOC:mah] |
GO:0006486 | protein glycosylation |
GO:0008378 | galactosyltransferase activity |
GO:0016020 | membrane |
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 | 4agv_D | 0.002 | 291 | 378 | 36 | 117 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 4agv_C | 0.002 | 291 | 378 | 36 | 117 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 4agv_B | 0.002 | 291 | 378 | 36 | 117 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 4agv_A | 0.002 | 291 | 378 | 36 | 117 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 4agr_D | 0.002 | 291 | 378 | 36 | 117 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |