| Basic Information | |
|---|---|
| Species | Fragaria vesca |
| Cazyme ID | mrna00757.1-v1.0-hybrid |
| Family | GT31 |
| Protein Properties | Length: 613 Molecular Weight: 70003.3 Isoelectric Point: 8.7211 |
| Chromosome | Chromosome/Scaffold: 4 Start: 27193568 End: 27196721 |
| Description | Galactosyltransferase family protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT31 | 415 | 599 | 0 |
| ERMAVRKSWMQHKLVKSSRVVARFFVALHGRKEVNVELMKEVEYFGDIVIVPYMDNYDLVVLKTIAICEYGVRTAPAKYIMKCDDDTFVRVDAVLKEARK ARKHRSLYIGNLNYHHKPLRFGKWAVTYELQEWPEEDYPTYANGPGYIISSDVAKFILSEFEKNKLRLFKMEDVSMGMWVEQFNN | |||
| Full Sequence |
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| Protein Sequence Length: 613 Download |
| MKRRKFDPVS LSHTRLRLLQ MLMATLLVYF LITSFDTHWD SGDENDAPFE LLSDTSLPTQ 60 GPLRDSPRIM RESKRVSGLV FEEKKKKKKT GFDGNASKAG GVHALHEAAV EAWRAGKKLW 120 AEIESGKVEL DNNNKYENRS DPCPHSFSVS GSEFRARNRV MVIPCGLTLW SHVTVVGTPR 180 WAHPEYDPKI AVLKEGAGAL MVSQFMMELQ GLKNVEGEDP PRILHFNPRL KGDWSNKPVI 240 EQNTCYRMQW GLSLRCEGWR SRADEETVDG QVKCEKWIRD DDDQSEESKA IWWLNRLIGR 300 TKKATVDWPY PFVEGRMFVL TLSAGLEGYH ISVDGRHVTS FPYRTGFVLE DATGLYVNGD 360 VDVHSVFAAS LPTSHPSFAP QMHLEMVTKW KAPPLPYGRV ELFLGILSAG NHFAERMAVR 420 KSWMQHKLVK SSRVVARFFV ALHGRKEVNV ELMKEVEYFG DIVIVPYMDN YDLVVLKTIA 480 ICEYGVRTAP AKYIMKCDDD TFVRVDAVLK EARKARKHRS LYIGNLNYHH KPLRFGKWAV 540 TYELQEWPEE DYPTYANGPG YIISSDVAKF ILSEFEKNKL RLFKMEDVSM GMWVEQFNNS 600 RPVKTGNPNA AI* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00908 | Gal-bind_lectin | 2.0e-15 | 164 | 366 | 203 | + 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 | 3.0e-18 | 163 | 367 | 205 | + 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. | ||
| pfam00337 | Gal-bind_lectin | 3.0e-23 | 158 | 366 | 209 | + Galactoside-binding lectin. This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5). | ||
| pfam01762 | Galactosyl_T | 3.0e-27 | 414 | 595 | 193 | + 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. | ||
| PLN03133 | PLN03133 | 4.0e-109 | 101 | 594 | 507 | + beta-1,3-galactosyltransferase; Provisional | ||
| Gene Ontology | |
|---|---|
| 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 |
| Hydropathy |
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| Sequence Alignments (This image is cropped. Click for full image.) |
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