| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb03g013300.1 |
| Family | GT31 |
| Protein Properties | Length: 594 Molecular Weight: 65539 Isoelectric Point: 6.0439 |
| Chromosome | Chromosome/Scaffold: 3 Start: 16270599 End: 16284323 |
| Description | Galactosyltransferase family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GT31 | 359 | 542 | 0 |
| KRRMALRRTWMQYEAVRSGDVVVRFFTGLHKNEHVNMELWREAQLYGDIQLMPFVDYYTLITLKTISICIFGTKIVPAKYIMKTDDDAFVRIDEVISSLK KSSSDGLLYGLISFQSSPHRDKDSKWFISRKEWPFDMYPPWAHGPGYIISRDIAKFVVRGHQELTLQLFKLEDVAMGIWIQQYK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 594 Download |
| MRKCSGVLFI LTLAIVLFLL SPSPSPTPPP TTAPNGPIAD LLPALPGLSD LYPPAPNSTA 60 QLSWGLLRPL LCRSDALPGT AAGVLEAAEA WRNLTLAVAA AAASEEEGRP QGPRCSSSVG 120 GDLRGGRARL PCGLAEGAAV TVVGVPREGA AKFWVEMLGA SGEVVLHVNV SLRAAGMVVE 180 QNSWTPEEGW GEWERCPLVG DVGSSNSSLQ RSPVDGLVRC NEKVGERIVQ ENNNTVVNVT 240 GNQPEDWQSS KGHGQLSGSF SIVEREPFTV ILWAGVEGFH MTVNGRHETS FAYRERSEPW 300 LVAEVKVSGD LELLSFLANG LPVSEDIDMA SVAVLKAPPL PKKRTFLLVG VFSTGNNFKR 360 RMALRRTWMQ YEAVRSGDVV VRFFTGLHKN EHVNMELWRE AQLYGDIQLM PFVDYYTLIT 420 LKTISICIFG TKIVPAKYIM KTDDDAFVRI DEVISSLKKS SSDGLLYGLI SFQSSPHRDK 480 DSKWFISRKE WPFDMYPPWA HGPGYIISRD IAKFVVRGHQ ELTLQLFKLE DVAMGIWIQQ 540 YKNSGQQVNI VTDDRFYNEG CDADYVLAHY QTPRLMMCLW EKLKTEYQAV CCE* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00908 | Gal-bind_lectin | 0.0001 | 131 | 197 | 68 | + 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. | ||
| smart00908 | Gal-bind_lectin | 2.0e-7 | 247 | 316 | 71 | + 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-7 | 127 | 197 | 71 | + 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 | 5.0e-34 | 359 | 542 | 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 | 0 | 62 | 592 | 563 | + 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 |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | NP_001042919.1 | 0 | 41 | 593 | 42 | 599 | Os01g0328900 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001150985.1 | 0 | 1 | 593 | 1 | 592 | beta 1, 3 galactosyltransferase [Zea mays] |
| RefSeq | XP_002274418.1 | 0 | 47 | 593 | 75 | 637 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002316064.1 | 0 | 47 | 593 | 54 | 611 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002457770.1 | 0 | 1 | 593 | 1 | 593 | hypothetical protein SORBIDRAFT_03g013300 [Sorghum bicolor] |
