| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_029083m |
| Family | GT43 |
| Protein Properties | Length: 357 Molecular Weight: 40174.9 Isoelectric Point: 7.0208 |
| Chromosome | Chromosome/Scaffold: 05133 Start: 132601 End: 134221 |
| Description | Nucleotide-diphospho-sugar transferases superfamily protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| GT43 | 132 | 335 | 0 |
| LANTIRLVPPPLLWIVVEGQTESDEVSEILRKTGIMYRHFVSKENFTDPQAELDHQRNVALRHIEQHRLSGIVHFAGLSNTYDLAFFDELREIEVFGTWP MALLTANKNKVIIEGPVCDSSQVIGWHLKKINNQTDSTPPIHISSFGFNSSILWDPERWGRPSSVPQTSQNSIKFVKQVALEDETKLKGIPPEECSKIML WQLK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 357 Download |
| MGSLERSKKK VQLWKKAVVH FALCFVMGFF TGFAPTGKAS IFSSQIISSN KSYFSPQPIE 60 VLHSAVTPPA QDPKNDSLAA ETPMQIPAES ERAKFLEEVE EREAKLNPRR LIIIITPMSS 120 KDAYEGVFLR RLANTIRLVP PPLLWIVVEG QTESDEVSEI LRKTGIMYRH FVSKENFTDP 180 QAELDHQRNV ALRHIEQHRL SGIVHFAGLS NTYDLAFFDE LREIEVFGTW PMALLTANKN 240 KVIIEGPVCD SSQVIGWHLK KINNQTDSTP PIHISSFGFN SSILWDPERW GRPSSVPQTS 300 QNSIKFVKQV ALEDETKLKG IPPEECSKIM LWQLKFPIEN SSSDSLSNTA VDSNQR* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03360 | Glyco_transf_43 | 2.0e-61 | 132 | 337 | 221 | + Glycosyltransferase family 43. | ||
| cd00218 | GlcAT-I | 4.0e-81 | 110 | 337 | 234 | + Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan synthesis. Beta1,3-glucuronyltransferase I (GlcAT-I) domain; GlcAT-I is a Key enzyme involved in the initial steps of proteoglycan synthesis. GlcAT-I catalyzes the transfer of a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region of trisaccharide Gal-beta-(1-3)-Gal-beta-(1-4)-Xyl of proteoglycans. The enzyme has two subdomains that bind the donor and acceptor substrate separately. The active site is located at the cleft between both subdomains in which the trisaccharide molecule is oriented perpendicular to the UDP. This family has been classified as Glycosyltransferase family 43 (GT-43). | ||
| PLN02458 | PLN02458 | 0 | 1 | 343 | 346 | + transferase, transferring glycosyl groups | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0015018 | galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity |
| GO:0016020 | membrane |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAX33319.1 | 0 | 1 | 343 | 1 | 346 | secondary cell wall-related glycosyltransferase family 43 [Populus tremula x Populus tremuloides] |
| GenBank | ABP65661.1 | 0 | 1 | 343 | 1 | 346 | secondary wall-associated glycosyltransferase family 43B [Populus tremula x Populus alba] |
| EMBL | CAI93178.1 | 0 | 1 | 356 | 1 | 361 | glycosyltransferase [Populus balsamifera] |
| RefSeq | XP_002323456.1 | 0 | 1 | 343 | 1 | 347 | glycosyl transferase [Populus trichocarpa] |
| RefSeq | XP_002326337.1 | 0 | 1 | 356 | 1 | 357 | glycosyl transferase [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2d0j_D | 0.000000000000004 | 112 | 335 | 5 | 225 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
| PDB | 2d0j_C | 0.000000000000004 | 112 | 335 | 5 | 225 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
| PDB | 2d0j_B | 0.000000000000004 | 112 | 335 | 5 | 225 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
| PDB | 2d0j_A | 0.000000000000004 | 112 | 335 | 5 | 225 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
| PDB | 1v84_B | 0.0000000001 | 112 | 335 | 5 | 232 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
