Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s248_13V6.1 |
Family | GT43 |
Protein Properties | Length: 537 Molecular Weight: 61275.6 Isoelectric Point: 10.5077 |
Chromosome | Chromosome/Scaffold: 248 Start: 121005 End: 123787 |
Description | Nucleotide-diphospho-sugar transferases superfamily 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 |
GT43 | 174 | 434 | 0 |
LMHTLSLVRRPVTWIVIEASGISAETAELLRQVRVHKLVHLGASEHLPRTLQDRIILEARLRTEGLRYVREQNLEGVIVFADESNVYSMQFFDEVQKVKW VGALPVGTLGYAGFEDPALLRDKGFLKDSGARLFRRRLLEPLQEMPVSRNTVLQVQGPTCDSSENITGWRAFRPLSLDDVLINEYRDEQTNLEWSGFVLN ARTVWASAPDRPKWIREWVEWARPEQRRYIDPRSLLSDETKVETLGSCGNGKAVLVWWARI |
Full Sequence |
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Protein Sequence Length: 537 Download |
MRPGGTLRNP RVRVKPITVG GLTELTTVTT LCSKRVSILR ILTQCIFCIA ALILGFRVSY 60 EANLVRVLDV EETSRQNSQV PIQRVHESNL RVFKSQNARL TPRGKSSQVY VGRHPILKRP 120 WPHPDPIEMA QAYNMLARVQ LEQQRLYGIE NWKPIIAITP TYFRTFQSLH LSGLMHTLSL 180 VRRPVTWIVI EASGISAETA ELLRQVRVHK LVHLGASEHL PRTLQDRIIL EARLRTEGLR 240 YVREQNLEGV IVFADESNVY SMQFFDEVQK VKWVGALPVG TLGYAGFEDP ALLRDKGFLK 300 DSGARLFRRR LLEPLQEMPV SRNTVLQVQG PTCDSSENIT GWRAFRPLSL DDVLINEYRD 360 EQTNLEWSGF VLNARTVWAS APDRPKWIRE WVEWARPEQR RYIDPRSLLS DETKVETLGS 420 CGNGKAVLVW WARIEARSDS KYPPRWNLDL PLEVVVPARK TPWPEKIFPL SYPPPYVGKR 480 KVGNRSGGRG GRSRRGKRQP DSKISALVNQ REVNATKGHI GHVTTLGLTW DYEIPM* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02458 | PLN02458 | 2.0e-14 | 155 | 418 | 275 | + transferase, transferring glycosyl groups | ||
pfam03360 | Glyco_transf_43 | 9.0e-22 | 174 | 436 | 275 | + Glycosyltransferase family 43. | ||
cd00218 | GlcAT-I | 4.0e-39 | 153 | 436 | 295 | + 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). |
Gene Ontology | |
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GO Term | Description |
GO:0015018 | galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity |
GO:0016020 | membrane |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | NP_201524.1 | 0 | 37 | 506 | 35 | 490 | glycosyl transferase family 43 protein [Arabidopsis thaliana] |
RefSeq | XP_001755715.1 | 0 | 106 | 445 | 1 | 328 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001765650.1 | 0 | 1 | 445 | 1 | 417 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001778969.1 | 0 | 106 | 465 | 1 | 337 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002310709.1 | 0 | 37 | 495 | 38 | 477 | glycosyl transferase, CAZy family GT43 [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2d0j_D | 0.00000002 | 155 | 290 | 5 | 143 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
PDB | 2d0j_C | 0.00000002 | 155 | 290 | 5 | 143 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
PDB | 2d0j_B | 0.00000002 | 155 | 290 | 5 | 143 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
PDB | 2d0j_A | 0.00000002 | 155 | 290 | 5 | 143 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
PDB | 1kws_B | 0.00000007 | 155 | 290 | 3 | 155 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |