NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2041620524|gb|KAG6384618|]
View 

hypothetical protein SASPL_155558 [Salvia splendens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 97-227 2.11e-65

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: 202.93  E-value: 2.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  97 PIVLVQIPMFNEKEVYKISIGAACNLSWPADRLVIQVLDDSTDPIVKDMVERECIRWAnKGINITYQIRETRGGYKAGAL 176
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAA-QGVNIKHVRRADRTGYKAGAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2041620524 177 KEGLKrdyVKPCEYVVIFDADFRPEPDFLRRsVPFLIHNPNIALVQARWRF 227
Cdd:cd06437    80 AEGMK---VAKGEYVAIFDADFVPPPDFLQK-TPPYFADPKLGFVQTRWGH 126
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 97-227 2.11e-65

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: 202.93  E-value: 2.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  97 PIVLVQIPMFNEKEVYKISIGAACNLSWPADRLVIQVLDDSTDPIVKDMVERECIRWAnKGINITYQIRETRGGYKAGAL 176
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAA-QGVNIKHVRRADRTGYKAGAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2041620524 177 KEGLKrdyVKPCEYVVIFDADFRPEPDFLRRsVPFLIHNPNIALVQARWRF 227
Cdd:cd06437    80 AEGMK---VAKGEYVAIFDADFVPPPDFLQK-TPPYFADPKLGFVQTRWGH 126
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 60-221 2.00e-18

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: 82.48  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  60 LYMGVVIVLVHLFWKKPEKRYRYEPMkddlesgnagyPIVLVQIPMFNEKEVYKISIGAACNLSWPADRLVIQVLDD-ST 138
Cdd:COG1215     3 LLLALLALLYLLLLALARRRRAPADL-----------PRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDgST 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 139 DPiVKDMVERecirWANKGINITYQIRETRGGyKAGALKEGLKRDyvkPCEYVVIFDADFRPEPDFLRRSVPFLiHNPNI 218
Cdd:COG1215    72 DE-TAEIARE----LAAEYPRVRVIERPENGG-KAAALNAGLKAA---RGDIVVFLDADTVLDPDWLRRLVAAF-ADPGV 141


                  ...
gi 2041620524 219 ALV 221
Cdd:COG1215   142 GAS 144
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 103-242 2.71e-12

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 62.80  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 103 IPMFNEKEVYKISIGAACNLSWPADRLVIqVLDDSTDPIVkDMVERecirWANKGINITYqIRETRGGYKAGALKEGLKr 182
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLNQTYPNFEIIV-VDDGSTDGTV-EIAEE----YAKKDPRVRV-IRLPENRGKAGARNAGLR- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 183 dYVKpCEYVVIFDADFRPEPDFLRRSVPFLIHNPNIALVQARWRFGKPRYLDYMLNCFCW 242
Cdd:pfam00535  76 -AAT-GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITL 133
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
 36-222 4.68e-10

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 59.27  E-value: 4.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  36 LIVPLLTV-CVYI--------------CLAMSIMVFIERLYMGVVIVL--VHLFW---KKPEkryryePMKDDLESgnag 95
Cdd:PRK11498  189 LIVLSLTVsCRYIwwrytstlnwddpvSLVCGLILLFAETYAWIVLVLgyFQVVWplnRQPV------PLPKDMSL---- 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  96 YPIVLVQIPMFNEK-EVYKISIGAACNLSWPADRLVIQVLDDStdpivkdmvERECIRWANKGINITYQIRETRGGYKAG 174
Cdd:PRK11498  259 WPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDG---------GREEFRQFAQEVGVKYIARPTHEHAKAG 329

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2041620524 175 ALKEGLKrdYVKPcEYVVIFDADFRPEPDFLRRSVPFLIHNPNIALVQ 222
Cdd:PRK11498  330 NINNALK--YAKG-EFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQ 374
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 97-227 2.11e-65

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: 202.93  E-value: 2.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  97 PIVLVQIPMFNEKEVYKISIGAACNLSWPADRLVIQVLDDSTDPIVKDMVERECIRWAnKGINITYQIRETRGGYKAGAL 176
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAA-QGVNIKHVRRADRTGYKAGAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2041620524 177 KEGLKrdyVKPCEYVVIFDADFRPEPDFLRRsVPFLIHNPNIALVQARWRF 227
Cdd:cd06437    80 AEGMK---VAKGEYVAIFDADFVPPPDFLQK-TPPYFADPKLGFVQTRWGH 126
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 97-231 8.59e-32

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: 116.52  E-value: 8.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  97 PIVLVQIPMFNEK-EVYKISIGAACNLSWPADRLVIQVLDDSTDPIVKDMVERECIRWankgiNITYQIRETRGGYKAGA 175
Cdd:cd06421     1 PTVDVFIPTYNEPlEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEY-----GYRYLTRPDNRHAKAGN 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2041620524 176 LKEGLKR-DYvkpcEYVVIFDADFRPEPDFLRRSVPFLIHNPNIALVQARWRFGKPR 231
Cdd:cd06421    76 LNNALAHtTG----DFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPD 128
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 101-231 1.27e-19

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 83.05  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 101 VQIPMFNEKEVYKISIGAACNLSWPADRLVIqVLDDSTDPIVkdmveRECIRWANKGINITYQIRETRGGYKAGALKEGL 180
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIV-VDDGSTDDTL-----EILEELAALYIRRVLVVRDKENGGKAGALNAGL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2041620524 181 KR-DYvkpcEYVVIFDADFRPEPDFLRRSVPFLIHNPNIALVQARWRFGKPR 231
Cdd:cd06423    75 RHaKG----DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGS 122
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 60-221 2.00e-18

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: 82.48  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  60 LYMGVVIVLVHLFWKKPEKRYRYEPMkddlesgnagyPIVLVQIPMFNEKEVYKISIGAACNLSWPADRLVIQVLDD-ST 138
Cdd:COG1215     3 LLLALLALLYLLLLALARRRRAPADL-----------PRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDgST 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 139 DPiVKDMVERecirWANKGINITYQIRETRGGyKAGALKEGLKRDyvkPCEYVVIFDADFRPEPDFLRRSVPFLiHNPNI 218
Cdd:COG1215    72 DE-TAEIARE----LAAEYPRVRVIERPENGG-KAAALNAGLKAA---RGDIVVFLDADTVLDPDWLRRLVAAF-ADPGV 141


                  ...
gi 2041620524 219 ALV 221
Cdd:COG1215   142 GAS 144
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 103-227 1.13e-12

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.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 63.68  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 103 IPMFNEKEVYKISIGAACNLSWPADRLVIqVLDDSTDpivkdMVERECIRWANKGINITYQIRETRGGyKAGALKEGLKr 182
Cdd:cd00761     3 IPAYNEEPYLERCLESLLAQTYPNFEVIV-VDDGSTD-----GTLEILEEYAKKDPRVIRVINEENQG-LAAARNAGLK- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2041620524 183 dYVKpCEYVVIFDADFRPEPDFLRRSVPFLIHNPNIALVQARWRF 227
Cdd:cd00761    75 -AAR-GEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNL 117
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 103-242 2.71e-12

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 62.80  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 103 IPMFNEKEVYKISIGAACNLSWPADRLVIqVLDDSTDPIVkDMVERecirWANKGINITYqIRETRGGYKAGALKEGLKr 182
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLNQTYPNFEIIV-VDDGSTDGTV-EIAEE----YAKKDPRVRV-IRLPENRGKAGARNAGLR- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 183 dYVKpCEYVVIFDADFRPEPDFLRRSVPFLIHNPNIALVQARWRFGKPRYLDYMLNCFCW 242
Cdd:pfam00535  76 -AAT-GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITL 133
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 101-223 4.63e-11

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 60.88  E-value: 4.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 101 VQIPMFNEK-EVYKISIGAACNLSWPaDRLVIQVLDDSTDPIVKDMVERECirwANKGINITYQIRETRGGYKAGALKEG 179
Cdd:cd06435     2 IHVPCYEEPpEMVKETLDSLAALDYP-NFEVIVIDNNTKDEALWKPVEAHC---AQLGERFRFFHVEPLPGAKAGALNYA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2041620524 180 LKRDYVKpCEYVVIFDADFRPEPDFLRRSVPfLIHNPNIALVQA 223
Cdd:cd06435    78 LERTAPD-AEIIAVIDADYQVEPDWLKRLVP-IFDDPRVGFVQA 119
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
 36-222 4.68e-10

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 59.27  E-value: 4.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  36 LIVPLLTV-CVYI--------------CLAMSIMVFIERLYMGVVIVL--VHLFW---KKPEkryryePMKDDLESgnag 95
Cdd:PRK11498  189 LIVLSLTVsCRYIwwrytstlnwddpvSLVCGLILLFAETYAWIVLVLgyFQVVWplnRQPV------PLPKDMSL---- 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  96 YPIVLVQIPMFNEK-EVYKISIGAACNLSWPADRLVIQVLDDStdpivkdmvERECIRWANKGINITYQIRETRGGYKAG 174
Cdd:PRK11498  259 WPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDG---------GREEFRQFAQEVGVKYIARPTHEHAKAG 329

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2041620524 175 ALKEGLKrdYVKPcEYVVIFDADFRPEPDFLRRSVPFLIHNPNIALVQ 222
Cdd:PRK11498  330 NINNALK--YAKG-EFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQ 374
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
 97-232 2.60e-09

CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, Glucan Biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of glucan.


Pssm-ID: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 55.72  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  97 PIVLVQIPMFNEKEVYKISIGAACNLSWPADRLVIQVLDDSTDPIVKDMVERECIRWANKGINITYQIRETrggyKAGAL 176
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRVVVVPPSQPRT----KPKAC 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2041620524 177 KEGLKRdyvkpC--EYVVIFDADFRPEPDFLRRSV-PFLIHNPNIALVQARWRFGKPRY 232
Cdd:cd06427    77 NYALAF-----ArgEYVVIYDAEDAPDPDQLKKAVaAFARLDDKLACVQAPLNYYNARE 130
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 97-239 1.73e-08

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 53.53  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  97 PIVLVQIPMFNEKEVYKISIGAACNLSWPADRLVIQVL--DDSTDPIVKDMVEREcirwanKGINITYQIRETRGGY--K 172
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNpsDAETLDVAEEIAARF------PDVRLRVIRNARLLGPtgK 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041620524 173 AGALKEGLKRdyVKPcEYVVIFDADFRPEPDFLRRSVPFLIHnPNIALVQARWRFgkpRYLDYMLNC 239
Cdd:pfam13641  76 SRGLNHGFRA--VKS-DLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTPVFS---LNRSTMLSA 135
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 61-221 1.42e-07

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 51.04  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  61 YMG---VVIVLVHLFWKKPekryryePMKDDlesgnAGYPIVLVQIPMFNEKEVykisIGAACN----LSWPADRL-VIQ 132
Cdd:cd06439     2 YFGyplLLKLLARLRPKPP-------SLPDP-----AYLPTVTIIIPAYNEEAV----IEAKLEnllaLDYPRDRLeIIV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 133 VLDDSTD---PIVKdmvereciRWANKGINITYQirETRGGyKAGALKEGLKRdyVKPcEYVVIFDADFRPEPDFLRRSV 209
Cdd:cd06439    66 VSDGSTDgtaEIAR--------EYADKGVKLLRF--PERRG-KAAALNRALAL--ATG-EIVVFTDANALLDPDALRLLV 131

                         170
                  ....*....|...
gi 2041620524 210 -PFLihNPNIALV 221
Cdd:cd06439   132 rHFA--DPSVGAV 142
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 97-243 2.00e-06

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 47.00  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  97 PIVLVQIPMFNEKEVYKISIGAACNLSWPADRLVIqVLDDSTDPIVkDMVERecirWANKGINITYqIRETRGGYKAGAL 176
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIV-VDDGSTDGTA-EILRE----LAAKDPRIRV-IRLERNRGKGAAR 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041620524 177 KEGLKrdYVKpCEYVVIFDADFRPEPDFLRRSVPFLIHNPNIALVQARW-RFGKPRYLDYMLNCFCWT 243
Cdd:COG0463    75 NAGLA--AAR-GDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLiREGESDLRRLGSRLFNLV 139
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
 125-223 1.41e-05

Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic Glucan Biosynthesis protein MdoH is a glucosyltransferase that catalyzes the elongation of beta-1,2 polyglucose chains of glucan, requiring a beta-glucoside as a primer and UDP-glucose as a substrate. Glucans are composed of 5 to 10 units of glucose forming a highly branched structure, where beta-1,2-linked glucose constitutes a linear backbone to which branches are attached by beta-1,6 linkages. In Escherichia coli, glucans are located in the periplasmic space, functioning as regulator of osmolarity. It is synthesized at a maximum when cells are grown in a medium with low osmolarity. It has been shown to span the cytoplasmic membrane.


Pssm-ID: 133034 [Multi-domain]  Cd Length: 254  Bit Score: 44.96  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 125 PADRLVIQVLDDSTDPivkDMVERECIRWAN------KGINITYQIRETRGGYKAGALKEGLKRdYVKPCEYVVIFDADF 198
Cdd:cd04191    31 LADHFDFFILSDTRDP---DIWLAEEAAWLDlceelgAQGRIYYRRRRENTGRKAGNIADFCRR-WGSRYDYMVVLDADS 106

                          90       100
                  ....*....|....*....|....*
gi 2041620524 199 RPEPDFLRRSVPFLIHNPNIALVQA 223
Cdd:cd04191   107 LMSGDTIVRLVRRMEANPRAGIIQT 131
PRK05454 PRK05454
glucans biosynthesis glucosyltransferase MdoH;
133-222 9.38e-04

glucans biosynthesis glucosyltransferase MdoH;


Pssm-ID: 235476 [Multi-domain]  Cd Length: 605  Bit Score: 39.86  E-value: 9.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 133 VLDDSTDPivkDMVERE-------CiRWANKGINITYQIRETRGGYKAGALKEGLKR---DYvkpcEYVVIFDADFRPEP 202
Cdd:PRK05454  164 ILSDTRDP---DIAAAEeaawlelR-AELGGEGRIFYRRRRRNVGRKAGNIADFCRRwggAY----DYMVVLDADSLMSG 235

                          90       100
                  ....*....|....*....|
gi 2041620524 203 DFLRRSVPFLIHNPNIALVQ 222
Cdd:PRK05454  236 DTLVRLVRLMEANPRAGLIQ 255
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
99-207 1.92e-03

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 38.44  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  99 VLVQIPMFNEKEVYKISIGAACNLSWPADRLVIqVLDDSTDPivkdmvERECIRwANKGINITYQIRETRGGYkAGALKE 178
Cdd:COG1216     5 VSVVIPTYNRPELLRRCLESLLAQTYPPFEVIV-VDNGSTDG------TAELLA-ALAFPRVRVIRNPENLGF-AAARNL 75

                          90       100
                  ....*....|....*....|....*....
gi 2041620524 179 GLKrdYVKpCEYVVIFDADFRPEPDFLRR 207
Cdd:COG1216    76 GLR--AAG-GDYLLFLDDDTVVEPDWLER 101
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 121-221 8.13e-03

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 36.49  E-value: 8.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524 121 NLSWPADRLVIqvLDDSTDPIVKDMVE-----RECIR-WANKGInityqiretrggykAGALKEGLKRDYVKPCEYVVIF 194
Cdd:cd02526    19 ALAEQVDKVVV--VDNSSGNDIELRLRlnsekIELIHlGENLGI--------------AKALNIGIKAALENGADYVLLF 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 2041620524 195 DADFRPEPDFLRRSVPFLIH---NPNIALV 221
Cdd:cd02526    83 DQDSVPPPDMVEKLLAYKILsdkNSNIGAV 112
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 99-213 8.25e-03

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 36.44  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041620524  99 VLVQIPMFNEKEVYKISIGAACNLSWPADRLVIQVLD----DSTDPIVKDMVER-ECIRWAN-------KGINITyqIRE 166
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDggstDGTREIVQEYAAKdPRIRLIDnpkriqsAGLNIG--IRN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2041620524 167 TRGgykagalkeglkrdyvkpcEYVVIFDADFRPEPDFLRRSVPFLI 213
Cdd:cd02525    80 SRG-------------------DIIIRVDAHAVYPKDYILELVEALK 107
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH