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Conserved domains on  [gi|1002819308|ref|NP_001307671|]
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queuosine-tRNA galactosyltransferase isoform b [Homo sapiens]

Protein Classification

queuosine-tRNA galactosyltransferase( domain architecture ID 10161044)

queuosine-tRNA galactosyltransferase (QTGAL) specifically catalyzes galactosylation of cytoplasmic tRNA(Tyr) modified with queuosine at position 34 (queuosine(34)). Galactosylates the cyclopentene hydroxyl group of queuosine(34) in tRNA(Tyr) to form galactosyl-queuosine(34)

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0141125|GO:0006417|GO:0006400
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
8-226 2.82e-167

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: 464.62  E-value: 2.82e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   8 IILPVHNAEPWLDECLRSVLQQDFEGTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHVIIGGHDSPSPRGVGYAKNQAV 87
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  88 AQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSIIGCRVRRDPPNSTERYTRWINQLTPEQLLTQVFTSNGPTVIMPT 167
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002819308 168 WFCSRAWFSHVGPFNEGGQGVPEDLLFFYEHLRKGGGVIRVDQSLLLYRHHPQAATHCV 226
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
 
Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
8-226 2.82e-167

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: 464.62  E-value: 2.82e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   8 IILPVHNAEPWLDECLRSVLQQDFEGTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHVIIGGHDSPSPRGVGYAKNQAV 87
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  88 AQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSIIGCRVRRDPPNSTERYTRWINQLTPEQLLTQVFTSNGPTVIMPT 167
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002819308 168 WFCSRAWFSHVGPFNEGGQGVPEDLLFFYEHLRKGGGVIRVDQSLLLYRHHPQAATHCV 226
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
7-220 4.29e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 103.24  E-value: 4.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKleDSGVHVIigghDSPSPRGVGYAKNQA 86
Cdd:COG0463     5 SVVIPTYNEEEYLEEALESLLAQTYP-DFEIIVVDDGSTDGTAEILRELAAK--DPRIRVI----RLERNRGKGAARNAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSII-GCRVRRDPPNSTERYTRWInqLTPEQLLTQVFTSNGPTVIM 165
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVyGSRLIREGESDLRRLGSRL--FNLVRLLTNLPDSTSGFRLF 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002819308 166 PTWFCSRAWFSHvgpfneggqGVPEDLLFFYeHLRKGGGVIRVDQsllLYRHHPQ 220
Cdd:COG0463   156 RREVLEELGFDE---------GFLEDTELLR-ALRHGFRIAEVPV---RYRAGES 197
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
7-177 5.73e-25

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: 99.01  E-value: 5.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKleDSGVHVIIgghdSPSPRGVGYAKNQA 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYAKK--DPRVRVIR----LPENRGKAGARNAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSIIGCRVRR--DPPNSTERYTRWINQLTPEQLLTQVFTSNGPTVI 164
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVifGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
                         170
                  ....*....|...
gi 1002819308 165 MPTWFCSRAWFSH 177
Cdd:pfam00535 154 GGFALYRREALEE 166
PRK10073 PRK10073
putative glycosyl transferase; Provisional
7-107 9.06e-14

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 71.23  E-value: 9.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKLEDsgVHVIigghDSPSpRGVGYAKNQA 86
Cdd:PRK10073    9 SIIIPLYNAGKDFRAFMESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYPH--VRLL----HQAN-AGVSVARNTG 80
                          90       100
                  ....*....|....*....|.
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMPQ 107
Cdd:PRK10073   81 LAVATGKYVAFPDADDVVYPT 101
 
Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
8-226 2.82e-167

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: 464.62  E-value: 2.82e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   8 IILPVHNAEPWLDECLRSVLQQDFEGTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHVIIGGHDSPSPRGVGYAKNQAV 87
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  88 AQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSIIGCRVRRDPPNSTERYTRWINQLTPEQLLTQVFTSNGPTVIMPT 167
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002819308 168 WFCSRAWFSHVGPFNEGGQGVPEDLLFFYEHLRKGGGVIRVDQSLLLYRHHPQAATHCV 226
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
7-220 4.29e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 103.24  E-value: 4.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKleDSGVHVIigghDSPSPRGVGYAKNQA 86
Cdd:COG0463     5 SVVIPTYNEEEYLEEALESLLAQTYP-DFEIIVVDDGSTDGTAEILRELAAK--DPRIRVI----RLERNRGKGAARNAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSII-GCRVRRDPPNSTERYTRWInqLTPEQLLTQVFTSNGPTVIM 165
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVyGSRLIREGESDLRRLGSRL--FNLVRLLTNLPDSTSGFRLF 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002819308 166 PTWFCSRAWFSHvgpfneggqGVPEDLLFFYeHLRKGGGVIRVDQsllLYRHHPQ 220
Cdd:COG0463   156 RREVLEELGFDE---------GFLEDTELLR-ALRHGFRIAEVPV---RYRAGES 197
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
7-177 5.73e-25

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: 99.01  E-value: 5.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKleDSGVHVIIgghdSPSPRGVGYAKNQA 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYAKK--DPRVRVIR----LPENRGKAGARNAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSIIGCRVRR--DPPNSTERYTRWINQLTPEQLLTQVFTSNGPTVI 164
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVifGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
                         170
                  ....*....|...
gi 1002819308 165 MPTWFCSRAWFSH 177
Cdd:pfam00535 154 GGFALYRREALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
8-207 8.76e-25

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: 98.35  E-value: 8.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   8 IILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKledsGVHVIIggHDSPSPRGVGYAKNQAV 87
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYP-NFEVIVVDDGSTDGTLEILEEYAKK----DPRVIR--VINEENQGLAAARNAGL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  88 AQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSIIGCRVrrdppnsterytrwinqltpeqlltqvftsngptvimPT 167
Cdd:cd00761    74 KAARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGP-------------------------------------GN 116
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1002819308 168 WFCSRAWFSHVGPFNEGGQGVPEDLLFFYEHLRKGGGVIR 207
Cdd:cd00761   117 LLFRRELLEEIGGFDEALLSGEEDDDFLLRLLRGGKVAFR 156
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
7-110 2.07e-18

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 84.41  E-value: 2.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDF-EGTMELSVFNDASKDKSGAIIEKWrvKLEDSGVHVIigghDSPSPRGVGYAKNQ 85
Cdd:COG1215    32 SVIIPAYNEEAVIEETLRSLLAQDYpKEKLEVIVVDDGSTDETAEIAREL--AAEYPRVRVI----ERPENGGKAAALNA 105
                          90       100
                  ....*....|....*....|....*
gi 1002819308  86 AVAQSSGSYLCFLDSDDVMMPQRVR 110
Cdd:COG1215   106 GLKAARGDIVVFLDADTVLDPDWLR 130
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
7-224 2.00e-17

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: 79.51  E-value: 2.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWrvklEDSGVHVIigghdSPSPRGVGYAKNQA 86
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYP-NIEYIVIDGGSTDGTVDIIKKY----EDKITYWI-----SEPDKGIYDAMNKG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSS--IIGCRVRRDPPNsterytRWINQLTPEQLLTQVFTSNGPTVI 164
Cdd:cd06433    71 IALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVdvVYGDVLLVDENG------RVIGRRRPPPFLDKFLLYGMPICH 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002819308 165 mPTWFCSRAWFSHVGPFNE----GGqgvpeDLLFFYEHLRKGGGVIRVDQSLLLYRHHPQAATH 224
Cdd:cd06433   145 -QATFFRRSLFEKYGGFDEsyriAA-----DYDLLLRLLLAGKIFKYLPEVLAAFRLGGVSSTS 202
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
7-106 1.07e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 74.64  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEGtMELSVFNDASKDKSGAIIEKWRvkleDSGVHVIigghDSPSPRGVGYAKNQA 86
Cdd:COG1216     6 SVVIPTYNRPELLRRCLESLLAQTYPP-FEVIVVDNGSTDGTAELLAALA----FPRVRVI----RNPENLGFAAARNLG 76
                          90       100
                  ....*....|....*....|
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMP 106
Cdd:COG1216    77 LRAAGGDYLLFLDDDTVVEP 96
PRK10073 PRK10073
putative glycosyl transferase; Provisional
7-107 9.06e-14

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 71.23  E-value: 9.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKLEDsgVHVIigghDSPSpRGVGYAKNQA 86
Cdd:PRK10073    9 SIIIPLYNAGKDFRAFMESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYPH--VRLL----HQAN-AGVSVARNTG 80
                          90       100
                  ....*....|....*....|.
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMPQ 107
Cdd:PRK10073   81 LAVATGKYVAFPDADDVVYPT 101
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
7-223 5.10e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 64.57  E-value: 5.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEGTmELSVFNDASKDKSGAIIEKWrVKLEDSGVHVIIGGHdspsprGVGYAKN-- 84
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKND-ELIISDDGSTDGTVEIIKEY-IDKDPFIIILIRNGK------NLGVARNfe 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  85 QAVAQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPS--------SIIgcrvrrDPPNSTERYTRWINQ-LTPEQLLTQV 155
Cdd:cd04196    73 SLLQAADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKpllvysdlELV------DENGNPIGESFFEYQkIKPGTSFNNL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002819308 156 FTSN---GPTVIMptwfcSRAWFSHVGPFneggqgvPEDLL-----FFYEHLRKGGGVIRVDQSLLLYRHHPQAAT 223
Cdd:cd04196   147 LFQNvvtGCTMAF-----NRELLELALPF-------PDADVimhdwWLALLASAFGKVVFLDEPLILYRQHGNNVV 210
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
8-144 1.49e-11

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: 62.24  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   8 IILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHVIIGGHdspspRGVGYAKNQAV 87
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYP-KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN-----GGKAGALNAGL 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  88 AQSSGSYLCFLDSDDVM---MPQRVRLQHEA-----AVQhpssiIGCRVRRDPPN-----STERYTRWIN 144
Cdd:cd06423    75 RHAKGDIVVVLDADTILepdALKRLVVPFFAdpkvgAVQ-----GRVRVRNGSENlltrlQAIEYLSIFR 139
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
7-119 4.69e-11

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: 62.21  E-value: 4.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEG-TMELSVFNDASKDKSGAIIEKWRvkleDSGVHVIIgghdSPSPRGVGYAKNQ 85
Cdd:cd06439    32 TIIIPAYNEEAVIEAKLENLLALDYPRdRLEIIVVSDGSTDGTAEIAREYA----DKGVKLLR----FPERRGKAAALNR 103
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1002819308  86 AVAQSSGSYLCFLDSDDVMMPQRVRLqheaAVQH 119
Cdd:cd06439   104 ALALATGEIVVFTDANALLDPDALRL----LVRH 133
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
7-106 2.06e-10

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: 59.52  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNA-EPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKlEDSGVHVIIgghdSPSPRGVGYAKNQ 85
Cdd:cd04184     4 SIVMPVYNTpEKYLREAIESVRAQTYP-NWELCIADDASTDPEVKRVLKKYAA-QDPRIKVVF----REENGGISAATNS 77
                          90       100
                  ....*....|....*....|.
gi 1002819308  86 AVAQSSGSYLCFLDSDDVMMP 106
Cdd:cd04184    78 ALELATGEFVALLDHDDELAP 98
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-128 2.24e-10

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: 58.72  E-value: 2.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   8 IILPVHNAEPWLDECLRSVLQQDFEGTmELSVFNDASKDKSgaiIEKWRVKLEDsgVHVIIgghdSPSPRGVGYAKNQAV 87
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDF-EVIVVDNASTDGS---VELLRELFPE--VRLIR----NGENLGFGAGNNQGI 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1002819308  88 AQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPS-SIIGCRV 128
Cdd:cd04186    71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDvGIVGPKV 112
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
7-101 3.38e-09

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: 56.86  E-value: 3.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEGT-MELSVFNDASKDKSGAIIEKWRVKleDSGVHVIigghDSPSpRGVGYAKNQ 85
Cdd:cd02525     3 SIIIPVRNEEKYIEELLESLLNQSYPKDlIEIIVVDGGSTDGTREIVQEYAAK--DPRIRLI----DNPK-RIQSAGLNI 75
                          90
                  ....*....|....*.
gi 1002819308  86 AVAQSSGSYLCFLDSD 101
Cdd:cd02525    76 GIRNSRGDIIIRVDAH 91
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
8-146 1.10e-08

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: 54.12  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   8 IILPVHNAEPWLDECLRSVLQQDFEG-TMELSVFNDASKDKSGAIIEKWRVKleDSGVHVIigghDSPSPRGVGYAKNQA 86
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGyDYEIIVVDDGSTDGTAEIARELAAR--VPRVRVI----RLSRNFGKGAAVRAG 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  87 VAQSSGSYLCFLDSDdvmmpqrvrLQH---------EAAVQHPSSI-IGCRVRRDPPNSTERYTRWINQL 146
Cdd:cd04179    75 FKAARGDIVVTMDAD---------LQHppedipkllEKLLEGGADVvIGSRFVRGGGAGMPLLRRLGSRL 135
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
8-127 2.89e-08

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: 53.34  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   8 IILPVHNAE----PWLDEcLRSVLQQDFEGTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHViigghDSPSPRGVGYAK 83
Cdd:cd04188     1 VVIPAYNEEkrlpPTLEE-AVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVL-----TLPKNRGKGGAV 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002819308  84 NQAVAQSSGSYLCFLDSD------DVMmpqrvRLQHEAAVQHPSSIIGCR 127
Cdd:cd04188    75 RAGMLAARGDYILFADADlatpfeELE-----KLEEALKTSGYDIAIGSR 119
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
7-209 3.70e-07

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: 50.26  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSvLQQDFEGTMELSVFNDASKDKSGAIIEkwrvkleDSGVHVIigghdsPSPRGVGYAKNQA 86
Cdd:cd02522     2 SIIIPTLNEAENLPRLLAS-LRRLNPLPLEIIVVDGGSTDGTVAIAR-------SAGVVVI------SSPKGRARQMNAG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSIIGCRVRRDPPNSTER--------YTRWINQLTPEQLLtqvfts 158
Cdd:cd02522    68 AAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAFRLRFDDPGPRLRllelganlRSRLFGLPYGDQGL------ 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002819308 159 ngptvimptwFCSRAWFSHVGPFNEggqgVP--EDLLFFyEHLRKGGGVIRVD 209
Cdd:cd02522   142 ----------FIRRELFEELGGFPE----LPlmEDVELV-RRLRRRGRPALLP 179
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
8-203 9.12e-07

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: 48.34  E-value: 9.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   8 IILPVHNAEPWLDECLRSVLQQ---DFEgtmeLSVFNDASKDKSGAIIEKWRvkledsgvhviiggHDSPSP------RG 78
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQsilPFE----VIIADDGSTEETKELIEEFK--------------SQFPIPikhvwqED 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  79 VGYAK----NQAVAQSSGSYLCFLDSDDVMMPQRVRlQHEAAVQHPSSIIGCRVRRDpPNSTERYTRWINqltpeqlltq 154
Cdd:cd06420    63 EGFRKakirNKAIAAAKGDYLIFIDGDCIPHPDFIA-DHIELAEPGVFLSGSRVLLN-EKLTERGIRGCN---------- 130
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002819308 155 vftsngptviMPTWfcsRAWFSHVGPFNEGGQG-VPEDLLFFYEHLRKGG 203
Cdd:cd06420   131 ----------MSFW---KKDLLAVNGFDEEFTGwGGEDSELVARLLNSGI 167
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
7-119 5.84e-06

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 47.29  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKdkSGAIIEKWRVKLEDSGVHVIIGGHDSpsprGVGYAKNQA 86
Cdd:PRK10018    8 SIYMPTWNRQQLAIRAIKSVLRQDYS-NWEMIIVDDCST--SWEQLQQYVTALNDPRITYIHNDINS----GACAVRNQA 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMPQR--VRLQH-EAAVQH 119
Cdd:PRK10018   81 IMLAQGEYITGIDDDDEWTPNRlsVFLAHkQQLVTH 116
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-124 1.40e-05

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: 45.74  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   8 IILPVHNAEPWLDECLRSVLQQDF-EGTMELSVFNDASKDKSGAIIEKWRvklEDSGVHVIIGGHDSPSPRGVGYAKNQA 86
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYpKEKFEVILVDDHSTDGTVQILEFAA---AKPNFQLKILNNSRVSISGKKNALTTA 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSII 124
Cdd:cd04192    78 IKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLV 115
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
7-167 1.79e-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: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQQDFeGTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHVIIGGHDsPSPRGVGYAKNQA 86
Cdd:pfam13641   5 SVVVPAFNEDSVLGRVLEAILAQPY-PPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARL-LGPTGKSRGLNHG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308  87 VAQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSIIGCRVRRDPPNST------ERYTRWINQLTPEQLLTQVFTSNG 160
Cdd:pfam13641  83 FRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTMlsalgaLEFALRHLRMMSLRLALGVLPLSG 162

                  ....*..
gi 1002819308 161 PTVIMPT 167
Cdd:pfam13641 163 AGSAIRR 169
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
8-67 3.67e-04

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: 40.92  E-value: 3.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002819308   8 IILPVHNAEPWLDEC---LRSVLQQDFEgTMELsVF-NDASKDKSGAIIEKWRvkLEDSGVHVI 67
Cdd:cd04187     1 IVVPVYNEEENLPELyerLKAVLESLGY-DYEI-IFvDDGSTDRTLEILRELA--ARDPRVKVI 60
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
7-124 6.57e-04

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: 40.38  E-value: 6.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEP--WLDECLRSVLQQDFEGTMELSVFNDASKDKSGAIIEKWRVKLedsGVHVIIgghdSPSPRGVGYAKN 84
Cdd:cd04195     1 SVLMSVYIKEKpeFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKL---PLKVVP----LEKNRGLGKALN 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002819308  85 QAVAQSSGSYLCFLDSDDVMMPQRVRLQHEAAVQHPSSII 124
Cdd:cd04195    74 EGLKHCTYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDI 113
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
7-101 9.45e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 40.52  E-value: 9.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819308   7 SIILPVHNAEPWLDECLRSVLQ-----QDFEGTM--ELSVFNDASKDKSGAIIEK-WRVKL-EDSGVHVIigghDSPSPR 77
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKMLKETIKylesrSRKDPKFkyEIIIVNDGSKDKTLKVAKDfWRQNInPNIDIRLL----SLLRNK 148
                          90       100
                  ....*....|....*....|....
gi 1002819308  78 GVGYAKNQAVAQSSGSYLCFLDSD 101
Cdd:PTZ00260  149 GKGGAVRIGMLASRGKYILMVDAD 172
 
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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