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Conserved domains on  [gi|2041620523|gb|KAG6384617|]
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hypothetical protein SASPL_155557 [Salvia splendens]

Protein Classification

glycosyltransferase family 2 protein; glycosyltransferase family protein( domain architecture ID 1904475)

glycosyltransferase family 2 protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 95-143 5.82e-20

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd06437:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 232  Bit Score: 81.97  E-value: 5.82e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2041620523  95 PMVLVQIPIYNEIEVYKISIGAACRLSWPVDRLVVQVLDDSTDLVIKVL 143
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLA 49
BcsA super family cl43359
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 51-137 6.49e-03

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


The actual alignment was detected with superfamily member COG1215:

Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 35.49  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620523  51 FLLFVEWVHMMFLAALAKLMRRRHAERYkweplrddleggsldfPMVLVQIPIYNEIEVYKISIGAACRLSWPVDRLVVQ 130
Cdd:COG1215     1 LLLLLALLALLYLLLLALARRRRAPADL----------------PRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVI 64


                  ....*...
gi 2041620523 131 VLDD-STD 137
Cdd:COG1215    65 VVDDgSTD 72
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 95-143 5.82e-20

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 81.97  E-value: 5.82e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2041620523  95 PMVLVQIPIYNEIEVYKISIGAACRLSWPVDRLVVQVLDDSTDLVIKVL 143
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLA 49
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 51-137 6.49e-03

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 35.49  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620523  51 FLLFVEWVHMMFLAALAKLMRRRHAERYkweplrddleggsldfPMVLVQIPIYNEIEVYKISIGAACRLSWPVDRLVVQ 130
Cdd:COG1215     1 LLLLLALLALLYLLLLALARRRRAPADL----------------PRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVI 64


                  ....*...
gi 2041620523 131 VLDD-STD 137
Cdd:COG1215    65 VVDDgSTD 72
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
 95-134 6.94e-03

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 35.77  E-value: 6.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2041620523  95 PMVLVQIPIYNE-IEVYKISIGAACRLSWPVDRLVVQVLDD 134
Cdd:PRK11498  260 PTVDIFVPTYNEdLNVVKNTIYASLGIDWPKDKLNIWILDD 300
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 95-143 5.82e-20

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 81.97  E-value: 5.82e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2041620523  95 PMVLVQIPIYNEIEVYKISIGAACRLSWPVDRLVVQVLDDSTDLVIKVL 143
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLA 49
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 95-144 4.25e-04

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 38.71  E-value: 4.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2041620523  95 PMVLVQIPIYNE-IEVYKISIGAACRLSWPVDRLVVQVLDDSTDLVIKVLC 144
Cdd:cd06421     1 PTVDVFIPTYNEpLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALA 51
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 51-137 6.49e-03

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 35.49  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620523  51 FLLFVEWVHMMFLAALAKLMRRRHAERYkweplrddleggsldfPMVLVQIPIYNEIEVYKISIGAACRLSWPVDRLVVQ 130
Cdd:COG1215     1 LLLLLALLALLYLLLLALARRRRAPADL----------------PRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVI 64


                  ....*...
gi 2041620523 131 VLDD-STD 137
Cdd:COG1215    65 VVDDgSTD 72
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
 95-134 6.94e-03

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 35.77  E-value: 6.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2041620523  95 PMVLVQIPIYNE-IEVYKISIGAACRLSWPVDRLVVQVLDD 134
Cdd:PRK11498  260 PTVDIFVPTYNEdLNVVKNTIYASLGIDWPKDKLNIWILDD 300
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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