y
Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29813.m001496 |
Family | GT31 |
Protein Properties | Length: 631 Molecular Weight: 71156.2 Isoelectric Point: 7.4271 |
Chromosome | Chromosome/Scaffold: 29813 Start: 297011 End: 300352 |
Description | galactosyltransferase1 |
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 | 395 | 579 | 0 |
KRRMAVRRTWMQYAAVRAGTAAVRFFVGLHKNQLVNEELWNEARTYGDIQLMPFVDYYNLITWKTLAICMFGTEVASAKYVMKTDDDAFVRVDEVLASLK RTKVNHGLLYGLINSDSQPHRNPDSKWYISLEEWSEENYPPWAHGPGYVVSQDVAKEVYRRYKEGRLKIFKLEDVAMGIWIAEMK |
Full Sequence |
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Protein Sequence Length: 631 Download |
MKMKRWYGGV LIASLFMLLI LRYSLMKNPI GDSYLMNAFS NGTNPLQWVQ STLPPTVKIP 60 ENSAKVISTE TIVFSLFAQR NISNEEQVSL QTWNLLKHLI DQAHLLPNGV EAIKEAGSAW 120 NNLMASIEEE RHGYTNESSR AREKQCPHFL NKVNATAVKS SGFKLRLPCG LTQGSSITII 180 GIPDGLLGNF RIELTGEALP GEPDPPIILH YNVRLHGDKI TEDPVIVQNT WTVAHDWGDE 240 ERCPSPTPEK NKKVDDLDQC NNIVGRNDTR AIRHSEGARS SAMVQEGFKN RRYFPFRQGY 300 LSVATLRVGT EGIQTTVDGK HITSFAYRET LEPWLVSEVR ISGDLKLISA VASGLPTSEE 360 LEHAIDLEAL KSVPLSAKRP PHLFVGVFST ANNFKRRMAV RRTWMQYAAV RAGTAAVRFF 420 VGLHKNQLVN EELWNEARTY GDIQLMPFVD YYNLITWKTL AICMFGTEVA SAKYVMKTDD 480 DAFVRVDEVL ASLKRTKVNH GLLYGLINSD SQPHRNPDSK WYISLEEWSE ENYPPWAHGP 540 GYVVSQDVAK EVYRRYKEGR LKIFKLEDVA MGIWIAEMKK EGLAVSYVKD EKIHNEGCSD 600 GYTVAHYQGP REMLCLWQKL QDGIGAKCCG D 660 |
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 | 168 | 349 | 182 | + 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 | 8.0e-21 | 162 | 349 | 188 | + 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 | 6.0e-23 | 163 | 349 | 187 | + 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-38 | 395 | 579 | 191 | + 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 | 3 | 631 | 635 | + 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 |