| Basic Information | |
|---|---|
| Species | Ricinus communis |
| Cazyme ID | 28838.m000256 |
| Family | GT31 |
| Protein Properties | Length: 612 Molecular Weight: 69233.1 Isoelectric Point: 8.3018 |
| Chromosome | Chromosome/Scaffold: 28838 Start: 100714 End: 104559 |
| Description | galactosyltransferase1 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT31 | 399 | 562 | 0 |
| ERRMAVRRTWMQYPAVKTGEVAVRFFVGLHKNQMVNEQLWVELQTYGDIQLMPFVDYYSLITWKTIAICTFGVKVVSAKNVMKTDDDAFVRVDEVLSSLK RTTVSHGLLYGLINYNAQPHRNPFSKWYISLEEWPESFYPPWAHGPGYVVSHDIAKAVYNRHKM | |||
| Full Sequence |
|---|
| Protein Sequence Length: 612 Download |
| MKKWLSGVLI GSFFMLLILR KVFMKNPLKE SPPMRLPIPV NLTTPLECIY SEGNLPATHS 60 PEFSNQIISA ETLLSSLFVD RNFSNQVQSS LLTWNHMKYL VNYSQPLPNG MGAIREAQVA 120 WESLLESVKK REQGGAKESL LNKLKGKQCP YFVNIMNATK FGDNGYRLWV PCGLVQGSTI 180 TIIGIPNGLL GNFRIDLLGE QLPGEPEPST ILHYNVRLLG DKITEDSVIL QNTWTADHGW 240 SEEERCPASV PGDDKKVDEL SQCNKMVGKD NSQKFAANGS SNNFSTMSRN RTGARWYFPF 300 KQGFLSVMTL RMGEEGIQMT VDGKHVTSFA YRENLEPWLV SEVRISGGLK LISVLASGLP 360 SSEESEHIID LESLKSAQLP LHHPLDLFIG VFSTANNFER RMAVRRTWMQ YPAVKTGEVA 420 VRFFVGLHKN QMVNEQLWVE LQTYGDIQLM PFVDYYSLIT WKTIAICTFG VKVVSAKNVM 480 KTDDDAFVRV DEVLSSLKRT TVSHGLLYGL INYNAQPHRN PFSKWYISLE EWPESFYPPW 540 AHGPGYVVSH DIAKAVYNRH KMGRLKVRVH APMMRADVQX XYIVAHYQSP REMLCLWQNL 600 QEGNEPGCCS GK 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00070 | GLECT | 3.0e-17 | 165 | 354 | 190 | + 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. | ||
| smart00908 | Gal-bind_lectin | 2.0e-17 | 171 | 354 | 184 | + 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. | ||
| pfam00337 | Gal-bind_lectin | 3.0e-20 | 166 | 354 | 189 | + 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 | 5.0e-33 | 399 | 577 | 184 | + 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 | 1 | 612 | 638 | + 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 |
