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Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna09548.1-v1.0-hybrid |
Family | GT31 |
Protein Properties | Length: 660 Molecular Weight: 74636.5 Isoelectric Point: 6.9511 |
Chromosome | Chromosome/Scaffold: 5 Start: 10949422 End: 10952482 |
Description | Galactosyltransferase family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT31 | 419 | 601 | 0 |
ERMAVRKSWMQHNLIKSSKVVARFFVALHSKKEVNVELKKEAEFFGDIVIVPYMDNYDLVVLKTVAICEYGVRTMSAKYIMKCDDDTFVRVDAVISEASR VPKGRSLYVGNINYYHKPLRYGKWAVTYEEWPEEDYPPYANGPGYILSSDIAKFIISEFESRKLRLFKMEDVSMGMWVEKFNS |
Full Sequence |
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Protein Sequence Length: 660 Download |
MRRAKLDRFG AVLTRQRSVQ ILVGIGLLYL LLVTLEIPFV FKTGFSTISP DSLTRPDRLH 60 SREAVEEKEA PTRPLERVSQ NSNQPSQSRR PESNVVSGLV FDPKTFDSEL YKSAKIAWEV 120 GKKFWEELQA GKVRVVEERV AGNGSESCPH SITMTGSEFS EQGRVMVVPC GLTLGSYITM 180 VGRPRAAHEE SEPKIALVKE GQSVMVSQFK VELLGLKTVE GEDPPRLLHF NPRLKGDWSG 240 TPVIELNTCY RMQWGSAQRC EGWKSKADEE TVDGQVKCEK WIRDDDSRSE ETKATWWLSR 300 LVGRTKKVTV DWPYPFGEEK LFVLTLSAGL EGYHVNVDGR HITSFPYHNG FSLEDATGLS 360 LSGDVDLHSV FAASLPTSHP SFAPQKHLEM SPRWRAPPLP DGEIELFIGI LSAGNHFAER 420 MAVRKSWMQH NLIKSSKVVA RFFVALHSKK EVNVELKKEA EFFGDIVIVP YMDNYDLVVL 480 KTVAICEYGV RTMSAKYIMK CDDDTFVRVD AVISEASRVP KGRSLYVGNI NYYHKPLRYG 540 KWAVTYEEWP EEDYPPYANG PGYILSSDIA KFIISEFESR KLRLFKMEDV SMGMWVEKFN 600 SSKPVEYLHS LKFCQFGCIE EARKTPMLQH EIALTVVLVN SNLDNLGENK EVLLAVIAW* 660 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00908 | Gal-bind_lectin | 1.0e-13 | 169 | 370 | 202 | + 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 | 168 | 371 | 204 | + 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 | 9.0e-20 | 418 | 598 | 192 | + 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-21 | 164 | 370 | 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 | 5.0e-105 | 125 | 596 | 491 | + 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 |