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Conserved domains on  [gi|1276704822|gb|ATV55380|]
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glycosyl transferase family 2 [Prevotella intermedia]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11421525)

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

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  16037492|18518825

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-217 3.64e-44

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 150.24  E-value: 3.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   1 MAKISILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNAGIAKARNAGLSI 80
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822  81 STGEYIAFVDSDDWLSEDACEKVFDVFKRYPstdtvlfhVKSVYGDKEVDFTMPPFTTLDGFTAFRESLTWNIH----GI 156
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP--------ADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPdstsGF 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276704822 157 YVIRRELHLRFPYDESAIAysDENVTRL--HYLKSREIRtcegiYYYRQHLGSVTHKVSLRRF 217
Cdd:COG0463   153 RLFRREVLEELGFDEGFLE--DTELLRAlrHGFRIAEVP-----VRYRAGESKLNLRDLLRLL 208
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-217 3.64e-44

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 150.24  E-value: 3.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   1 MAKISILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNAGIAKARNAGLSI 80
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822  81 STGEYIAFVDSDDWLSEDACEKVFDVFKRYPstdtvlfhVKSVYGDKEVDFTMPPFTTLDGFTAFRESLTWNIH----GI 156
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP--------ADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPdstsGF 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276704822 157 YVIRRELHLRFPYDESAIAysDENVTRL--HYLKSREIRtcegiYYYRQHLGSVTHKVSLRRF 217
Cdd:COG0463   153 RLFRREVLEELGFDEGFLE--DTELLRAlrHGFRIAEVP-----VRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-164 4.64e-39

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: 135.60  E-value: 4.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   5 SILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNAGIAKARNAGLSISTGE 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822  85 YIAFVDSDDWLSEDACEKVFDVFKRYPSTDTVLFHVKSVYGDKEVDFTMPPFTTLDGFTAFRESLTWNIHGIY----VIR 160
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIggfaLYR 160

                  ....
gi 1276704822 161 RELH 164
Cdd:pfam00535 161 REAL 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-114 7.25e-33

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: 119.15  E-value: 7.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   6 ILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNAGIAKARNAGLSISTGEY 85
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80
                          90       100
                  ....*....|....*....|....*....
gi 1276704822  86 IAFVDSDDWLSEDACEKVFDVFKRYPSTD 114
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADPEAD 109
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-295 7.12e-29

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 113.22  E-value: 7.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   3 KISILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHlPQNAGIAKARNAGLSIST 82
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVAT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822  83 GEYIAFVDSDDWLSEDACEKVFDVfKRYPSTDTVLFHVKSVYGDKevDFTMPPFTT--------LDGFTAFRESL----- 149
Cdd:PRK10073   86 GKYVAFPDADDVVYPTMYETLMTM-ALEDDLDVAQCNADWCFRDT--GETWQSIPSdrlrstgvLSGPDWLRMALssrrw 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822 150 ---TWniHGIYviRREL----HLRFP--YDESAIAYSDE---NVTRLHYlksreirTCEGIYYYRQHLGSVTHkvsLRRF 217
Cdd:PRK10073  163 thvVW--LGVY--RRDFivknNIKFEpgLHHQDIPWTTEvmfNALRVRY-------TEQSLYKYYLHDTSVSR---LPRQ 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822 218 DYLLANKS---MK--QQLEAL--KVPDKIlDIYEEVRWRnvIGLYMFYFLH--RKELDKSSRKQGL-EIIKSS-WQSIEQ 286
Cdd:PRK10073  229 GNKNLNYQrhyIKitRMLEKLnrRYADKI-KIYPAFHQQ--ITKEALRVCHavRKEPDILTRQRMIaEIFTSGmYKRIWK 305
                         330
                  ....*....|....*..
gi 1276704822 287 N--------RLPRWLIR 295
Cdd:PRK10073  306 NarsvklgyQLLLWSFR 322
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
4-92 8.65e-11

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 62.47  E-value: 8.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   4 ISILVAVYNAEKYLYQCLSS--SLSQTLQDIEIICVDDASTDSSLSIlnAYAAKDERIKVVHLPQNAGIAKARNAGLSIS 81
Cdd:TIGR03965  76 VTVVVPVRNRPAGLARLLAAllALDYPRDRLEVIVVDDGSEDPVPTR--AARGARLPVRVIRHPRRQGPAAARNAGARAA 153
                          90
                  ....*....|.
gi 1276704822  82 TGEYIAFVDSD 92
Cdd:TIGR03965 154 RTEFVAFTDSD 164
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
8-97 1.37e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 45.94  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   8 VAV--YNAEKYLYQCLSSSLSQT-LQDI--EIICVDDASTDSSLSILNAYAA---KDERIKVVHLPQNaGIAKARNAGLS 79
Cdd:NF038302    5 VAIptYNGANRLPEVLERLRSQIgTESLswEIIVVDNNSTDNTAQVVQEYQKnwpSPYPLRYCFEPQQ-GAAFARQRAIQ 83
                          90       100
                  ....*....|....*....|...
gi 1276704822  80 ISTGEYIAFVDSD-----DWLSE 97
Cdd:NF038302   84 EAKGELIGFLDDDnlpapNWVAA 106
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-217 3.64e-44

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 150.24  E-value: 3.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   1 MAKISILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNAGIAKARNAGLSI 80
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822  81 STGEYIAFVDSDDWLSEDACEKVFDVFKRYPstdtvlfhVKSVYGDKEVDFTMPPFTTLDGFTAFRESLTWNIH----GI 156
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP--------ADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPdstsGF 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276704822 157 YVIRRELHLRFPYDESAIAysDENVTRL--HYLKSREIRtcegiYYYRQHLGSVTHKVSLRRF 217
Cdd:COG0463   153 RLFRREVLEELGFDEGFLE--DTELLRAlrHGFRIAEVP-----VRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-164 4.64e-39

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: 135.60  E-value: 4.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   5 SILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNAGIAKARNAGLSISTGE 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822  85 YIAFVDSDDWLSEDACEKVFDVFKRYPSTDTVLFHVKSVYGDKEVDFTMPPFTTLDGFTAFRESLTWNIHGIY----VIR 160
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIggfaLYR 160

                  ....
gi 1276704822 161 RELH 164
Cdd:pfam00535 161 REAL 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-114 7.25e-33

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: 119.15  E-value: 7.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   6 ILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNAGIAKARNAGLSISTGEY 85
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80
                          90       100
                  ....*....|....*....|....*....
gi 1276704822  86 IAFVDSDDWLSEDACEKVFDVFKRYPSTD 114
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADPEAD 109
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
3-114 3.17e-30

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 113.84  E-value: 3.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   3 KISILVAVYNA-EKYLYQCLSSSLSQTLQDIEIICVDDASTDSSL-SILNAYAAKDERIKVVHLPQNAGIAKARNAGLSI 80
Cdd:cd04184     2 LISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDPEVkRVLKKYAAQDPRIKVVFREENGGISAATNSALEL 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1276704822  81 STGEYIAFVDSDDWLSEDACEKVFDVFKRYPSTD 114
Cdd:cd04184    82 ATGEFVALLDHDDELAPHALYEVVKALNEHPDAD 115
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-295 7.12e-29

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 113.22  E-value: 7.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   3 KISILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHlPQNAGIAKARNAGLSIST 82
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVAT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822  83 GEYIAFVDSDDWLSEDACEKVFDVfKRYPSTDTVLFHVKSVYGDKevDFTMPPFTT--------LDGFTAFRESL----- 149
Cdd:PRK10073   86 GKYVAFPDADDVVYPTMYETLMTM-ALEDDLDVAQCNADWCFRDT--GETWQSIPSdrlrstgvLSGPDWLRMALssrrw 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822 150 ---TWniHGIYviRREL----HLRFP--YDESAIAYSDE---NVTRLHYlksreirTCEGIYYYRQHLGSVTHkvsLRRF 217
Cdd:PRK10073  163 thvVW--LGVY--RRDFivknNIKFEpgLHHQDIPWTTEvmfNALRVRY-------TEQSLYKYYLHDTSVSR---LPRQ 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822 218 DYLLANKS---MK--QQLEAL--KVPDKIlDIYEEVRWRnvIGLYMFYFLH--RKELDKSSRKQGL-EIIKSS-WQSIEQ 286
Cdd:PRK10073  229 GNKNLNYQrhyIKitRMLEKLnrRYADKI-KIYPAFHQQ--ITKEALRVCHavRKEPDILTRQRMIaEIFTSGmYKRIWK 305
                         330
                  ....*....|....*..
gi 1276704822 287 N--------RLPRWLIR 295
Cdd:PRK10073  306 NarsvklgyQLLLWSFR 322
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-109 1.21e-28

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: 112.14  E-value: 1.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   1 MAKISILVAVYNAEKYLYQCLSSSLSQT--LQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNAGIAKARNAGL 78
Cdd:COG1215    28 LPRVSVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGL 107
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1276704822  79 SISTGEYIAFVDSDDWLSEDACEKVFDVFKR 109
Cdd:COG1215   108 KAARGDIVVFLDADTVLDPDWLRRLVAAFAD 138
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-133 2.69e-27

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 105.85  E-value: 2.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   1 MAKISILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYaaKDERIKVVHLPQNAGIAKARNAGLSI 80
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL--AFPRVRVIRNPENLGFAAARNLGLRA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276704822  81 STGEYIAFVDSDDWLSEDACEKVF---------DVFKRYPSTDTVLFHvksvYGDkEVDFTM 133
Cdd:COG1216    80 AGGDYLLFLDDDTVVEPDWLERLLaaacllirrEVFEEVGGFDERFFL----YGE-DVDLCL 136
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
5-172 1.68e-25

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 101.08  E-value: 1.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   5 SILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAakDERIKVVHLPQNaGIAKARNAGLSISTGE 84
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYE--DKITYWISEPDK-GIYDAMNKGIALATGD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822  85 YIAFVDSDDWLSEDACEKVFDVFKRYPSTDTVLFHVKSVYGDKEVDFTMPPFTTLDGFTAFResltWNIH--GIYViRRE 162
Cdd:cd06433    78 IIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYG----MPIChqATFF-RRS 152
                         170
                  ....*....|.
gi 1276704822 163 LHLRFP-YDES 172
Cdd:cd06433   153 LFEKYGgFDES 163
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-97 1.52e-22

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: 93.46  E-value: 1.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   5 SILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHL-PQNAGIAKARNAGLSISTG 83
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRnGKNLGVARNFESLLQAADG 80
                          90
                  ....*....|....*
gi 1276704822  84 EYIAFVDSDD-WLSE 97
Cdd:cd04196    81 DYVFFCDQDDiWLPD 95
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
3-109 3.76e-19

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: 84.98  E-value: 3.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   3 KISILVAVYNAEKYLYQCLSSSLSQT--LQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQnAGIAKARNAGLSI 80
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSypKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPK-RIQSAGLNIGIRN 79
                          90       100
                  ....*....|....*....|....*....
gi 1276704822  81 STGEYIAFVDSDDWLSEDACEKVFDVFKR 109
Cdd:cd02525    80 SRGDIIIRVDAHAVYPKDYILELVEALKR 108
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
6-111 4.40e-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: 4.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   6 ILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQ-NAGIAKARNAGLSISTGE 84
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKeNGGKAGALNAGLRHAKGD 80
                          90       100
                  ....*....|....*....|....*..
gi 1276704822  85 YIAFVDSDDWLSEDACEKVFDVFKRYP 111
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADP 107
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
6-92 4.27e-18

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 80.60  E-value: 4.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   6 ILVAVYNAEKY---LYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNAGIAKARNAGLSIST 82
Cdd:cd04187     1 IVVPVYNEEENlpeLYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                          90
                  ....*....|
gi 1276704822  83 GEYIAFVDSD 92
Cdd:cd04187    81 GDAVITMDAD 90
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
5-116 7.56e-18

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: 80.44  E-value: 7.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   5 SILVAVYNAEK--YLYQCLSSSLSQTLQDIEIICVDD-ASTDSSLSILNAYAaKDERIKVVHLPQNAGIAKARNAGLSIS 81
Cdd:cd04195     1 SVLMSVYIKEKpeFLREALESILKQTLPPDEVVLVKDgPVTQSLNEVLEEFK-RKLPLKVVPLEKNRGLGKALNEGLKHC 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1276704822  82 TGEYIAFVDSDDWLSEDACEKVFDVFKRYPSTDTV 116
Cdd:cd04195    80 TYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIV 114
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
3-199 1.81e-17

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: 80.32  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   3 KISILVAVYNAEKYLYQCLSSSLSQT--LQDIEIICVDDASTDSSLSILNAYAakDERIKVVHLPQNAGIAKARNAGLSI 80
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLLALDypRDRLEIIVVSDGSTDGTAEIAREYA--DKGVKLLRFPERRGKAAALNRALAL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822  81 STGEYIAFVDSDDWLSEDACEKVFDVFKRyPSTDTVLfHVKSVYGDKEVDFTMPPFTTLDGFTAFRESLTWNI---HG-I 156
Cdd:cd06439   108 ATGEIVVFTDANALLDPDALRLLVRHFAD-PSVGAVS-GELVIVDGGGSGSGEGLYWKYENWLKRAESRLGSTvgaNGaI 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276704822 157 YVIRRELHLRFP----------------------YDESAIAYsDENVTRLHYLKSREIRTCEGIY 199
Cdd:cd06439   186 YAIRRELFRPLPadtinddfvlplriarqgyrvvYEPDAVAY-EEVAEDGSEEFRRRVRIAAGNL 249
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
6-92 2.46e-17

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 78.38  E-value: 2.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   6 ILVAVYNAEKYLYQCLSSsLSQTLQ---DIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNAGIAKARNAGLSIST 82
Cdd:cd04179     1 VVIPAYNEEENIPELVER-LLAVLEegyDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79
                          90
                  ....*....|
gi 1276704822  83 GEYIAFVDSD 92
Cdd:cd04179    80 GDIVVTMDAD 89
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-111 9.36e-15

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: 71.05  E-value: 9.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   6 ILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILnayAAKDERIKVVHLPQNAGIAKARNAGLSISTGEY 85
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELL---RELFPEVRLIRNGENLGFGAGNNQGIREAKGDY 77
                          90       100
                  ....*....|....*....|....*.
gi 1276704822  86 IAFVDSDDWLSEDACEKVFDVFKRYP 111
Cdd:cd04186    78 VLLLNPDTVVEPGALLELLDAAEQDP 103
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
6-93 7.18e-14

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 69.79  E-value: 7.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   6 ILVAVYNAEKYLYQCLSSSLSQT-LQDIEIICVDDASTDSSLSILNAYAAKDERIKVV------HLPQNAGIAKARNAGL 78
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDfEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIvlvgshNSPSPKGVGYAKNQAI 80
                          90
                  ....*....|....*
gi 1276704822  79 SISTGEYIAFVDSDD 93
Cdd:cd06913    81 AQSSGRYLCFLDSDD 95
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-97 1.53e-12

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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 66.16  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   6 ILVAVYNAEKYLYQCLSSSLSQTLQD--IEIICVDDASTDSSLSILNAYAAKDE-RIKVVHLPQ--NAGIAKARNAGLSI 80
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPKekFEVILVDDHSTDGTVQILEFAAAKPNfQLKILNNSRvsISGKKNALTTAIKA 80
                          90       100
                  ....*....|....*....|..
gi 1276704822  81 STGEYIAFVDSD-----DWLSE 97
Cdd:cd04192    81 AKGDWIVTTDADcvvpsNWLLT 102
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
3-99 1.91e-12

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 65.77  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   3 KISILVAVYNAEKYLYQCLSSslsqtLQDI--EIICVDDASTDSSLSIlnayaAKDERIKVVHLPQNaGIAKARNAGLSI 80
Cdd:cd02511     1 TLSVVIITKNEERNIERCLES-----VKWAvdEIIVVDSGSTDRTVEI-----AKEYGAKVYQRWWD-GFGAQRNFALEL 69
                          90
                  ....*....|....*....
gi 1276704822  81 STGEYIAFVDSDDWLSEDA 99
Cdd:cd02511    70 ATNDWVLSLDADERLTPEL 88
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
6-92 7.50e-11

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 60.66  E-value: 7.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   6 ILVAVYNAEKYLYQCLSS----SLSQTLQDIEIICVDDASTDSSLSILNAYAAK-DERIKVVHLPQNAGIAKARNAGLSI 80
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEaveyLEERPSFSYEIIVVDDGSKDGTAEVARKLARKnPALIRVLTLPKNRGKGGAVRAGMLA 80
                          90
                  ....*....|..
gi 1276704822  81 STGEYIAFVDSD 92
Cdd:cd04188    81 ARGDYILFADAD 92
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
4-92 8.65e-11

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 62.47  E-value: 8.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   4 ISILVAVYNAEKYLYQCLSS--SLSQTLQDIEIICVDDASTDSSLSIlnAYAAKDERIKVVHLPQNAGIAKARNAGLSIS 81
Cdd:TIGR03965  76 VTVVVPVRNRPAGLARLLAAllALDYPRDRLEVIVVDDGSEDPVPTR--AARGARLPVRVIRHPRRQGPAAARNAGARAA 153
                          90
                  ....*....|.
gi 1276704822  82 TGEYIAFVDSD 92
Cdd:TIGR03965 154 RTEFVAFTDSD 164
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
6-92 2.92e-09

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: 55.66  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   6 ILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDErIKVVHLPQ-NAG--IAKARNAGLSIST 82
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFP-IPIKHVWQeDEGfrKAKIRNKAIAAAK 79
                          90
                  ....*....|
gi 1276704822  83 GEYIAFVDSD 92
Cdd:cd06420    80 GDYLIFIDGD 89
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
5-91 4.76e-09

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 56.44  E-value: 4.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   5 SILVAVYN-AEKYLYQCLSSSLSQTLQD--IEIICVDDASTDSSLSILNA--YAAKDERIKVVHLPQNAGIAKARNAGLS 79
Cdd:cd02510     1 SVIIIFHNeALSTLLRTVHSVINRTPPEllKEIILVDDFSDKPELKLLLEeyYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                          90
                  ....*....|..
gi 1276704822  80 ISTGEYIAFVDS 91
Cdd:cd02510    81 AATGDVLVFLDS 92
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
4-104 1.08e-08

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily 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: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 54.50  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   4 ISILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSlsilnayAAKDERIKVVHLPQNAGIAKARNAGLSISTG 83
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGT-------VAIARSAGVVVISSPKGRARQMNAGAAAARG 73
                          90       100
                  ....*....|....*....|.
gi 1276704822  84 EYIAFVDSDDWLSEDACEKVF 104
Cdd:cd02522    74 DWLLFLHADTRLPPDWDAAII 94
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
5-222 2.38e-08

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 54.21  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   5 SILVAVYNAEK--YLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNA-GIAKARNAGLSIS 81
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAPDTTySLAASRNRGTSHA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822  82 TGEYIAFVDSDDWLSEDACEKVFDV-----FKRYPSTDTVLFHVKSVYGDKEV-----DFTMPPFTTLDGFTAFReslTW 151
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDKFEKQLKIatslaLQENIQAAVVLPVTDLNDESSNFlrrggDLTASGDVLRDLLVFYS---PL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822 152 NIH-----GIYVIRRELHLRF-PYDESAIAYSDEN---VTRL-HYLKSREIRTCEgiYYYRQHLGSVTHKVSLRRFDYLL 221
Cdd:pfam10111 158 AIFfapnsSNALINRQAFIEVgGFDESFRGHGAEDfdiFLRLaARYPFVAVMPPQ--LLYRLSAKSMSPYSGFRRFLGDL 235

                  .
gi 1276704822 222 A 222
Cdd:pfam10111 236 A 236
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-92 7.93e-08

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 53.20  E-value: 7.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   3 KISILVAVYNAEKYLYQCLSSSLS---QTLQDIEIICVDDASTDSSLSILNAYA-AKDERIKVVHLPQNAGIAKARNAGL 78
Cdd:PRK10714    7 KVSVVIPVYNEQESLPELIRRTTAaceSLGKEYEILLIDDGSSDNSAEMLVEAAqAPDSHIVAILLNRNYGQHSAIMAGF 86
                          90
                  ....*....|....
gi 1276704822  79 SISTGEYIAFVDSD 92
Cdd:PRK10714   87 SHVTGDLIITLDAD 100
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
6-92 3.40e-07

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 50.22  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   6 ILVAVYNaEK----YLYQCLSSSLSQTlqDIEIICVDDASTDSSLSILNAYAAKDERIKVVHLPQNAGIAKARNAGLSIS 81
Cdd:cd06442     1 IIIPTYN-ERenipELIERLDAALKGI--DYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAA 77
                          90
                  ....*....|.
gi 1276704822  82 TGEYIAFVDSD 92
Cdd:cd06442    78 RGDVIVVMDAD 88
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
4-106 7.51e-07

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 50.15  E-value: 7.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   4 ISILVAVYNAE-------KYLYQCLSSSLSQTLQDI-EIICVDDASTDSSLSILNAYAAKDER----IKVVHLPQNAGIA 71
Cdd:PTZ00260   72 LSIVIPAYNEEdrlpkmlKETIKYLESRSRKDPKFKyEIIIVNDGSKDKTLKVAKDFWRQNINpnidIRLLSLLRNKGKG 151
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1276704822  72 KARNAGLSISTGEYIAFVDSDDWLSEDACEKVFDV 106
Cdd:PTZ00260  152 GAVRIGMLASRGKYILMVDADGATDIDDFDKLEDI 186
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
4-93 1.46e-06

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 48.84  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   4 ISILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDAStdSSLSILNAY--AAKDERIKVVHLPQNAGIAKARNAGLSIS 81
Cdd:PRK10018    7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCS--TSWEQLQQYvtALNDPRITYIHNDINSGACAVRNQAIMLA 84
                          90
                  ....*....|..
gi 1276704822  82 TGEYIAFVDSDD 93
Cdd:PRK10018   85 QGEYITGIDDDD 96
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-205 1.90e-06

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: 48.14  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   4 ISILVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAA--KDERIKVVHLPQNAGI---AKARNAGL 78
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAArfPDVRLRVIRNARLLGPtgkSRGLNHGF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822  79 SISTGEYIAFVDSDDWLSEDACEKVFDVFKRYPstdtvlfhVKSVYGDKEVDF--TMPPFTTLDGFTA--FRESLTWNIH 154
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPK--------VGAVGTPVFSLNrsTMLSALGALEFALrhLRMMSLRLAL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822 155 GI-------YVIRRELHLRF--------PYDESAIAYS-DENVTRLHYLKSREIRTCEGIY---YYRQHL 205
Cdd:pfam13641 156 GVlplsgagSAIRREVLKELglfdpfflLGDDKSLGRRlRRHGWRVAYAPDAAVRTVFPTYlaaSIKQRA 225
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-92 3.50e-06

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 47.38  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   1 MAKISILVAVYNAEK---YLYQCLSSSLsQTLQDIEIICVDDASTDSSLSILNAYAA--KDERIKVVHLPQNAGIAKARN 75
Cdd:PLN02726    8 AMKYSIIVPTYNERLniaLIVYLIFKAL-QDVKDFEIIVVDDGSPDGTQDVVKQLQKvyGEDRILLRPRPGKLGLGTAYI 86
                          90
                  ....*....|....*..
gi 1276704822  76 AGLSISTGEYIAFVDSD 92
Cdd:PLN02726   87 HGLKHASGDFVVIMDAD 103
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
7-98 4.69e-06

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: 46.47  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   7 LVAVYNAEKYLYQCLSSSLSQTLQDIEIICVDDASTDSSLSILNAYAAKDErIKVVHLPQNAGIAKARNAGLSISTGEYI 86
Cdd:cd04185     2 VVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDN-IVYLRLPENLGGAGGFYEGVRRAYELGY 80
                          90
                  ....*....|..
gi 1276704822  87 AFVdsddWLSED 98
Cdd:cd04185    81 DWI----WLMDD 88
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
8-97 1.37e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 45.94  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   8 VAV--YNAEKYLYQCLSSSLSQT-LQDI--EIICVDDASTDSSLSILNAYAA---KDERIKVVHLPQNaGIAKARNAGLS 79
Cdd:NF038302    5 VAIptYNGANRLPEVLERLRSQIgTESLswEIIVVDNNSTDNTAQVVQEYQKnwpSPYPLRYCFEPQQ-GAAFARQRAIQ 83
                          90       100
                  ....*....|....*....|...
gi 1276704822  80 ISTGEYIAFVDSD-----DWLSE 97
Cdd:NF038302   84 EAKGELIGFLDDDnlpapNWVAA 106
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
33-104 3.24e-04

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: 41.50  E-value: 3.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276704822  33 EIICVDDaSTDSSLSILNAYAAkdERIKVVHLPQNAGIAKARNAGLSISTG---EYIAFVDSDDWLSEDACEKVF 104
Cdd:cd02526    26 KVVVVDN-SSGNDIELRLRLNS--EKIELIHLGENLGIAKALNIGIKAALEngaDYVLLFDQDSVPPPDMVEKLL 97
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
4-98 1.35e-03

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 39.12  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   4 ISILVAVYNAEKYLYQCLSSSLSQTLQDIEII-CVDDAsTDSSLSILNAYAAK--DERIK-VVHLPQNAGIAKARN--AG 77
Cdd:cd02520     3 VSILKPLCGVDPNLYENLESFFQQDYPKYEILfCVQDE-DDPAIPVVRKLIAKypNVDARlLIGGEKVGINPKVNNliKG 81
                          90       100
                  ....*....|....*....|.
gi 1276704822  78 LSISTGEYIAFVDSDDWLSED 98
Cdd:cd02520    82 YEEARYDILVISDSDISVPPD 102
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
4-97 2.24e-03

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: 38.83  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276704822   4 ISILVAVYNaEKYLYQCLSSS---LSQTLQDIEIICVDDaSTDSSLSIL----NAYAAKDERIKVVHLPQNAGI-AKARN 75
Cdd:cd06437     3 VTVQLPVFN-EKYVVERLIEAacaLDYPKDRLEIQVLDD-STDETVRLAreivEEYAAQGVNIKHVRRADRTGYkAGALA 80
                          90       100
                  ....*....|....*....|....*..
gi 1276704822  76 AGLSISTGEYIAFVDSD-----DWLSE 97
Cdd:cd06437    81 EGMKVAKGEYVAIFDADfvpppDFLQK 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.
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