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Conserved domains on  [gi|1897071367|ref|WP_186990064|]
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glycosyltransferase family 2 protein [Synechococcus sp. MIT S9220]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11440388)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
14-123 1.18e-17

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: 77.93  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  14 IPTYGRKRELARLLDSLSKQSSLPEQIIIIDQN-EPGFLNsIIKEWIDKLP--IQHGSVAFRSASKARNYGAQKLTTDII 90
Cdd:cd00761     3 IPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGsTDGTLE-ILEEYAKKDPrvIRVINEENQGLAAARNAGLKAARGEYI 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1897071367  91 AFPDDDCIFIERTIELVKQTFFNNPSFDVIIGQ 123
Cdd:cd00761    82 LFLDADDLLLPDWLERLVAELLADPEADAVGGP 114
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
9-256 1.89e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.80  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367   9 SVGLCIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQNEPGFLNSIIKEWidklpiQHGSVAF------RSASKARNYGA 82
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL------AFPRVRVirnpenLGFAAARNLGL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  83 QKLTTDIIAFPDDDCIFIERTIE-LVkqtffnnpsfdviigqkpirqakfstktikpkhlttvlnlfnakaETSNIFCRK 161
Cdd:COG1216    78 RAAGGDYLLFLDDDTVVEPDWLErLL---------------------------------------------AAACLLIRR 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367 162 SFVIKMPtLFNEHIGpgdqtsiISNEETDLLIRMLRENAKIVHCKGILIEHH--SSQVSFKRSLKYAEGRYELIRRQKLG 239
Cdd:COG1216   113 EVFEEVG-GFDERFF-------LYGEDVDLCLRLRKAGYRIVYVPDAVVYHLggASSGPLLRAYYLGRNRLLFLRKHGPR 184
                         250
                  ....*....|....*..
gi 1897071367 240 LFYYLINLVQPLIRLAK 256
Cdd:COG1216   185 PLLRLALLRGLRLRLRG 201
 
Name Accession Description Interval E-value
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
14-123 1.18e-17

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: 77.93  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  14 IPTYGRKRELARLLDSLSKQSSLPEQIIIIDQN-EPGFLNsIIKEWIDKLP--IQHGSVAFRSASKARNYGAQKLTTDII 90
Cdd:cd00761     3 IPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGsTDGTLE-ILEEYAKKDPrvIRVINEENQGLAAARNAGLKAARGEYI 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1897071367  91 AFPDDDCIFIERTIELVKQTFFNNPSFDVIIGQ 123
Cdd:cd00761    82 LFLDADDLLLPDWLERLVAELLADPEADAVGGP 114
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
8-226 1.28e-17

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 78.98  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367   8 LSVglCIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQnepgflNS------IIKEWIDKLP----IQHgsVAFRSASKA 77
Cdd:COG0463     4 VSV--VIPTYNEEEYLEEALESLLAQTYPDFEIIVVDD------GStdgtaeILRELAAKDPrirvIRL--ERNRGKGAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  78 RNYGAQKLTTDIIAFPDDDCIFIERTIELVKQTFFNNPsFDVIIGQKPIRQAKFSTKTIKPKHLTTVLNLFNAKAETSNI 157
Cdd:COG0463    74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGF 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367 158 FC-RKSFVIKMPtlFNEHIGpgdqtsiisnEETDLLiRMLRENAKIVHCKgILIEHHSSQVSFKRSLKYA 226
Cdd:COG0463   153 RLfRREVLEELG--FDEGFL----------EDTELL-RALRHGFRIAEVP-VRYRAGESKLNLRDLLRLL 208
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
9-256 1.89e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.80  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367   9 SVGLCIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQNEPGFLNSIIKEWidklpiQHGSVAF------RSASKARNYGA 82
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL------AFPRVRVirnpenLGFAAARNLGL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  83 QKLTTDIIAFPDDDCIFIERTIE-LVkqtffnnpsfdviigqkpirqakfstktikpkhlttvlnlfnakaETSNIFCRK 161
Cdd:COG1216    78 RAAGGDYLLFLDDDTVVEPDWLErLL---------------------------------------------AAACLLIRR 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367 162 SFVIKMPtLFNEHIGpgdqtsiISNEETDLLIRMLRENAKIVHCKGILIEHH--SSQVSFKRSLKYAEGRYELIRRQKLG 239
Cdd:COG1216   113 EVFEEVG-GFDERFF-------LYGEDVDLCLRLRKAGYRIVYVPDAVVYHLggASSGPLLRAYYLGRNRLLFLRKHGPR 184
                         250
                  ....*....|....*..
gi 1897071367 240 LFYYLINLVQPLIRLAK 256
Cdd:COG1216   185 PLLRLALLRGLRLRLRG 201
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
12-165 1.87e-13

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: 66.65  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  12 LCIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQNEPGFLNSIIKEWIDKLPiqHGSVAFRS----ASKARNYGAQKLTT 87
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDP--RVRVIRLPenrgKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897071367  88 DIIAFPDDDCIFIERTIE-LVKqtFFNNPSFDVIIGQkpiRQAKFSTKTIKPKHLTTVLNLFNAKAETSNIFCRKSFVI 165
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEkLVE--ALEEDGADVVVGS---RYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
PRK10073 PRK10073
putative glycosyl transferase; Provisional
1-99 1.57e-06

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 48.50  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367   1 MKSGVSALSVglCIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQNEPGFLNSIIKEWIDKLP-IQHGSVAFRSASKARN 79
Cdd:PRK10073    1 MMNSTPKLSI--IIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhVRLLHQANAGVSVARN 78
                          90       100
                  ....*....|....*....|.
gi 1897071367  80 YGAQKLTTDIIAFPD-DDCIF 99
Cdd:PRK10073   79 TGLAVATGKYVAFPDaDDVVY 99
 
Name Accession Description Interval E-value
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
14-123 1.18e-17

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: 77.93  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  14 IPTYGRKRELARLLDSLSKQSSLPEQIIIIDQN-EPGFLNsIIKEWIDKLP--IQHGSVAFRSASKARNYGAQKLTTDII 90
Cdd:cd00761     3 IPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGsTDGTLE-ILEEYAKKDPrvIRVINEENQGLAAARNAGLKAARGEYI 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1897071367  91 AFPDDDCIFIERTIELVKQTFFNNPSFDVIIGQ 123
Cdd:cd00761    82 LFLDADDLLLPDWLERLVAELLADPEADAVGGP 114
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
8-226 1.28e-17

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 78.98  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367   8 LSVglCIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQnepgflNS------IIKEWIDKLP----IQHgsVAFRSASKA 77
Cdd:COG0463     4 VSV--VIPTYNEEEYLEEALESLLAQTYPDFEIIVVDD------GStdgtaeILRELAAKDPrirvIRL--ERNRGKGAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  78 RNYGAQKLTTDIIAFPDDDCIFIERTIELVKQTFFNNPsFDVIIGQKPIRQAKFSTKTIKPKHLTTVLNLFNAKAETSNI 157
Cdd:COG0463    74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGF 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367 158 FC-RKSFVIKMPtlFNEHIGpgdqtsiisnEETDLLiRMLRENAKIVHCKgILIEHHSSQVSFKRSLKYA 226
Cdd:COG0463   153 RLfRREVLEELG--FDEGFL----------EDTELL-RALRHGFRIAEVP-VRYRAGESKLNLRDLLRLL 208
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
9-256 1.89e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.80  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367   9 SVGLCIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQNEPGFLNSIIKEWidklpiQHGSVAF------RSASKARNYGA 82
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL------AFPRVRVirnpenLGFAAARNLGL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  83 QKLTTDIIAFPDDDCIFIERTIE-LVkqtffnnpsfdviigqkpirqakfstktikpkhlttvlnlfnakaETSNIFCRK 161
Cdd:COG1216    78 RAAGGDYLLFLDDDTVVEPDWLErLL---------------------------------------------AAACLLIRR 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367 162 SFVIKMPtLFNEHIGpgdqtsiISNEETDLLIRMLRENAKIVHCKGILIEHH--SSQVSFKRSLKYAEGRYELIRRQKLG 239
Cdd:COG1216   113 EVFEEVG-GFDERFF-------LYGEDVDLCLRLRKAGYRIVYVPDAVVYHLggASSGPLLRAYYLGRNRLLFLRKHGPR 184
                         250
                  ....*....|....*..
gi 1897071367 240 LFYYLINLVQPLIRLAK 256
Cdd:COG1216   185 PLLRLALLRGLRLRLRG 201
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
12-165 1.87e-13

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: 66.65  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  12 LCIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQNEPGFLNSIIKEWIDKLPiqHGSVAFRS----ASKARNYGAQKLTT 87
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDP--RVRVIRLPenrgKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897071367  88 DIIAFPDDDCIFIERTIE-LVKqtFFNNPSFDVIIGQkpiRQAKFSTKTIKPKHLTTVLNLFNAKAETSNIFCRKSFVI 165
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEkLVE--ALEEDGADVVVGS---RYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
12-201 4.13e-12

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 63.37  E-value: 4.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  12 LCIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQNEpgflNSIIKEWIDK------LPIQH---GSVAFRsASKARNYGA 82
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGS----TEETKELIEEfksqfpIPIKHvwqEDEGFR-KAKIRNKAI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  83 QKLTTDIIAFPDDDCI----FIERTIELVKQTFFnnpsfdvIIGQKPIRQAKFSTKTIKpkhlttvlnlfnakaeTSNIF 158
Cdd:cd06420    76 AAAKGDYLIFIDGDCIphpdFIADHIELAEPGVF-------LSGSRVLLNEKLTERGIR----------------GCNMS 132
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1897071367 159 CRKSFVIKMPTLFNEHIGPGdqtsiisNEETDLLIRMLRENAK 201
Cdd:cd06420   133 FWKKDLLAVNGFDEEFTGWG-------GEDSELVARLLNSGIK 168
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
9-255 7.43e-12

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: 64.38  E-value: 7.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367   9 SVGLCIPTYGRKRELARLLDSLSKQS--SLPEQIIIIDQNEPGFLNSIIKEWIDKLP---IQHGSVAfRSASKARNYGAQ 83
Cdd:COG1215    30 RVSVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPrvrVIERPEN-GGKAAALNAGLK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  84 KLTTDIIAFPDDDCI----FIERTIElvkqtFFNNPSFDVIigqkpirqakfstktikpkhlttvlnlfnakaeTSNIFC 159
Cdd:COG1215   109 AARGDIVVFLDADTVldpdWLRRLVA-----AFADPGVGAS---------------------------------GANLAF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367 160 RKSFVikmptlfnEHIGPGDQTSIisNEETDLLIRMLRENAKIVHCKGILIEHH---SSQVSFKRSLKYAEGRYELIRRQ 236
Cdd:COG1215   151 RREAL--------EEVGGFDEDTL--GEDLDLSLRLLRAGYRIVYVPDAVVYEEapeTLRALFRQRRRWARGGLQLLLKH 220
                         250       260
                  ....*....|....*....|....
gi 1897071367 237 KL-----GLFYYLINLVQPLIRLA 255
Cdd:COG1215   221 RPllrprRLLLFLLLLLLPLLLLL 244
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
9-244 8.42e-07

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: 49.15  E-value: 8.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367   9 SVGLCIPTYGRKRELARLLDSLSKQSSLPEQ--IIIIDQNEPGFLNSIIKEWIDKLPIqhgsVAF-----RSASKARNYG 81
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPKDLieIIVVDGGSTDGTREIVQEYAAKDPR----IRLidnpkRIQSAGLNIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  82 AQKLTTDIIAFPDDDCI----FIERTIELVKQTffnnpSFDVIIGqkpIRQAKFSTKTIKPKH--LTTVLNLFNAK---- 151
Cdd:cd02525    77 IRNSRGDIIIRVDAHAVypkdYILELVEALKRT-----GADNVGG---PMETIGESKFQKAIAvaQSSPLGSGGSAyrgg 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367 152 ------AETSNIFCRKSFVIKMPTLFNEhigpgdqtSIISNEETDLLIRMLRENAKIVHCKGILIEHH--SSQVS-FKRS 222
Cdd:cd02525   149 avkigyVDTVHHGAYRREVFEKVGGFDE--------SLVRNEDAELNYRLRKAGYKIWLSPDIRVYYYprSTLKKlARQY 220
                         250       260
                  ....*....|....*....|....
gi 1897071367 223 LKYAEGRYELIRRQK--LGLFYYL 244
Cdd:cd02525   221 FRYGKWRARTLRKHRksLSLRHLL 244
PRK10073 PRK10073
putative glycosyl transferase; Provisional
1-99 1.57e-06

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 48.50  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367   1 MKSGVSALSVglCIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQNEPGFLNSIIKEWIDKLP-IQHGSVAFRSASKARN 79
Cdd:PRK10073    1 MMNSTPKLSI--IIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhVRLLHQANAGVSVARN 78
                          90       100
                  ....*....|....*....|.
gi 1897071367  80 YGAQKLTTDIIAFPD-DDCIF 99
Cdd:PRK10073   79 TGLAVATGKYVAFPDaDDVVY 99
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
10-111 1.31e-05

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: 45.44  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  10 VGLCIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQNEPGFLNSIIKEWIDKLPIQHGSVA-------FRSASKARNYGA 82
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIrnarllgPTGKSRGLNHGF 83
                          90       100
                  ....*....|....*....|....*....
gi 1897071367  83 QKLTTDIIAFPDDDCIFIERTIELVKQTF 111
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYF 112
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
23-210 6.11e-05

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 43.07  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  23 LARLLDSLSKQSSLPEQIIII-DQNEPGFLNSIIKEWIDKLPIQ-HGSVAFRSASKARNYGAQKLTTDIIAFPDDDCIFI 100
Cdd:cd04195    15 LREALESILKQTLPPDEVVLVkDGPVTQSLNEVLEEFKRKLPLKvVPLEKNRGLGKALNEGLKHCTYDWVARMDTDDISL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367 101 ERTIELVKQTFFNNPSFDVIIGQkpIRQAKFSTKTIKPKHLTTVLNLFNAKAETSNIFC------RKSFVIKMptlfneh 174
Cdd:cd04195    95 PDRFEKQLDFIEKNPEIDIVGGG--VLEFDSDGNDIGKRRLPTSHDDILKFARRRSPFNhptvmfRKSKVLAV------- 165
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1897071367 175 igpGDQTSIISNEETDLLIRMLRENAKIVHCKGILI 210
Cdd:cd04195   166 ---GGYQDLPLVEDYALWARMLANGARFANLPEILV 198
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
16-117 5.44e-04

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 40.31  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  16 TYGRKRELARLLDSLSKQSSLPEQIIIIDqNepgflNSI--IKEWIDKlpiQHGSVAFRSASKARNYG-----------A 82
Cdd:cd04185     5 TYNRLDLLKECLDALLAQTRPPDHIIVID-N-----ASTdgTAEWLTS---LGDLDNIVYLRLPENLGgaggfyegvrrA 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1897071367  83 QKLTTDIIAFPDDDCIFIERTIE-LVKQTFFNNPSF 117
Cdd:cd04185    76 YELGYDWIWLMDDDAIPDPDALEkLLAYADKDNPQF 111
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
14-122 1.03e-03

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: 39.13  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  14 IPTYGRKRELARLLDSLSKQSSLPEQIIIIDQN-EPGFLNSIIKEWIDKLPIQHGSVAFRSASKAR--NYGAQKLTTDII 90
Cdd:cd06423     3 VPAYNEEAVIERTIESLLALDYPKLEVIVVDDGsTDDTLEILEELAALYIRRVLVVRDKENGGKAGalNAGLRHAKGDIV 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1897071367  91 AFPDDDCIFIERTIELVKQTFFNNPSFDVIIG 122
Cdd:cd06423    83 VVLDADTILEPDALKRLVVPFFADPKVGAVQG 114
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
14-115 1.49e-03

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 38.31  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  14 IPTYGRKRELARLLDSLSKQSSLPEQIIIIDQNEPGFLNSIIKEWIDKLPI--QHGSVAFrsaSKARNYGAQKLTTDIIA 91
Cdd:cd04186     3 IVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPEVRLirNGENLGF---GAGNNQGIREAKGDYVL 79
                          90       100
                  ....*....|....*....|....
gi 1897071367  92 FPDDDCIFIERTIELVKQTFFNNP 115
Cdd:cd04186    80 LLNPDTVVEPGALLELLDAAEQDP 103
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
13-149 4.19e-03

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 37.61  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897071367  13 CIPTYGRKRELARLLDSLSKQSSLPEQIIIIDQnepgflNS------IIKEWIDK------LPIQHGSVAFrsaskARNY 80
Cdd:cd04196     3 LMATYNGEKYLREQLDSILAQTYKNDELIISDD------GStdgtveIIKEYIDKdpfiiiLIRNGKNLGV-----ARNF 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897071367  81 --GAQKLTTDIIAFPDDDCIFIERTIELVKQTFFNNP-----SFDVII---GQKPIRQAKFSTKTIKPKHLTTVLNLFN 149
Cdd:cd04196    72 esLLQAADGDYVFFCDQDDIWLPDKLERLLKAFLKDDkpllvYSDLELvdeNGNPIGESFFEYQKIKPGTSFNNLLFQN 150
 
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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