Basic Information | |
---|---|
Species | Gossypium raimondii |
Cazyme ID | Gorai.004G051000.1 |
Family | GT43 |
Protein Properties | Length: 348 Molecular Weight: 39594.7 Isoelectric Point: 9.7032 |
Chromosome | Chromosome/Scaffold: 04 Start: 4692999 End: 4694468 |
Description | Nucleotide-diphospho-sugar transferases superfamily protein |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GT43 | 28 | 263 | 0 |
MHSLMLVPYDLVWIVGEAGGVSNEKASLIAKPSLKIIHVGFNQRMPNSWEERHKLESKMRLRALRSIREKKSDGIVMFAGDSNMFSMELFDEIQNVKWFG AVSVGMLTHSVNTDEMADRKKDEKENPRMPIQCPACNASDMLAGWHTFKTLPFVGKSAVYIDDRATVLPKKLEWSGFVLNSRLLWKDSSDKSEWIKDIDM LNGDIESPLGLVNDPSVVEPLGNCDRQVLLWWLRVE |
Full Sequence |
---|
Protein Sequence Length: 348 Download |
MTKNPRIFIV VTSTYVRTFQ VLYLTGVMHS LMLVPYDLVW IVGEAGGVSN EKASLIAKPS 60 LKIIHVGFNQ RMPNSWEERH KLESKMRLRA LRSIREKKSD GIVMFAGDSN MFSMELFDEI 120 QNVKWFGAVS VGMLTHSVNT DEMADRKKDE KENPRMPIQC PACNASDMLA GWHTFKTLPF 180 VGKSAVYIDD RATVLPKKLE WSGFVLNSRL LWKDSSDKSE WIKDIDMLNG DIESPLGLVN 240 DPSVVEPLGN CDRQVLLWWL RVEARADSKF PPIWIIDPPL EITVSSKRTP WRDAPPELPA 300 NEKPTMGIQD PIVKHSTKRT SRSKHRSKRK PEPKTDTQVS TRHSEQN* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02458 | PLN02458 | 3.0e-14 | 6 | 221 | 218 | + transferase, transferring glycosyl groups | ||
pfam03360 | Glyco_transf_43 | 9.0e-47 | 27 | 264 | 247 | + Glycosyltransferase family 43. | ||
cd00218 | GlcAT-I | 1.0e-51 | 9 | 264 | 265 | + 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 | |
---|---|
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 |
EMBL | CAI93186.1 | 0 | 2 | 325 | 154 | 477 | glycosyltransferase [Gossypium raimondii] |
EMBL | CBI21374.1 | 0 | 3 | 322 | 124 | 443 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002283249.1 | 0 | 3 | 322 | 162 | 481 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002306485.1 | 0 | 3 | 347 | 153 | 503 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002310709.1 | 0 | 2 | 347 | 153 | 510 | glycosyl transferase, CAZy family GT43 [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1v84_B | 0.000009 | 10 | 282 | 7 | 253 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1v84_A | 0.000009 | 10 | 282 | 7 | 253 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1v83_B | 0.000009 | 10 | 282 | 7 | 253 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1v83_A | 0.000009 | 10 | 282 | 7 | 253 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1v82_B | 0.000009 | 10 | 282 | 7 | 253 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |