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Conserved domains on  [gi|750095919|ref|WP_040400602|]
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glycosyltransferase family 2 protein [Amorphus coralli]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135280)

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
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
16-191 3.12e-50

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: 162.74  E-value: 3.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  16 VVIPAKDEAGNLPGLISEIGTALADRP-FEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQACGQSASIRTGVRYARG 94
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYdYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  95 DVILTIDGDGQNDPAFMPAMLARMEEGGdpVEMVAGEREGRKA----SWAKRHASRGANRLRRWLLKDGTRDTGCGLKAI 170
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPKLLEKLLEGG--ADVVIGSRFVRGGgagmPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLF 158
                        170       180
                 ....*....|....*....|.
gi 750095919 171 RRDVFLELPYFDGWHRYLPAL 191
Cdd:cd04179  159 RREVLEALLSLLESNGFEFGL 179
 
Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
16-191 3.12e-50

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: 162.74  E-value: 3.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  16 VVIPAKDEAGNLPGLISEIGTALADRP-FEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQACGQSASIRTGVRYARG 94
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYdYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  95 DVILTIDGDGQNDPAFMPAMLARMEEGGdpVEMVAGEREGRKA----SWAKRHASRGANRLRRWLLKDGTRDTGCGLKAI 170
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPKLLEKLLEGG--ADVVIGSRFVRGGgagmPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLF 158
                        170       180
                 ....*....|....*....|.
gi 750095919 171 RRDVFLELPYFDGWHRYLPAL 191
Cdd:cd04179  159 RREVLEALLSLLESNGFEFGL 179
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
11-224 1.25e-47

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 156.79  E-value: 1.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  11 RPSVSVVIPAKDEAGNLPGLISEIgTALADRPFEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQACGQSASIRTGVR 90
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESL-LAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  91 YARGDVILTIDGDGQNDPAFMPAMLARMEEGgdPVEMVAGEREGRKASWAKRHASRGANRLRRWLLKdgTRDTGCGLKAI 170
Cdd:COG0463   80 AARGDYIAFLDADDQLDPEKLEELVAALEEG--PADLVYGSRLIREGESDLRRLGSRLFNLVRLLTN--LPDSTSGFRLF 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 750095919 171 RRDVFLELPYFDGW-HRYLPALVQREGGRVRYVDVvdrERRFGASHYGVWDRAAV 224
Cdd:COG0463  156 RREVLEELGFDEGFlEDTELLRALRHGFRIAEVPV---RYRAGESKLNLRDLLRL 207
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
15-175 3.38e-27

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: 102.86  E-value: 3.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   15 SVVIPAKDEAGNLPGLISEIgTALADRPFEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQACGQSASIRTGVRYARG 94
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESL-LNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   95 DVILTIDGDGQNDPAFMPAMLARMEEggDPVEMVAGEREGRKASWAKRHASRGANRLRRW------LLKDGTRDTGCGLK 168
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEE--DGADVVVGSRYVIFGETGEYRRASRITLSRLPfflglrLLGLNLPFLIGGFA 157

                  ....*..
gi 750095919  169 AIRRDVF 175
Cdd:pfam00535 158 LYRREAL 164
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
14-216 7.86e-26

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 102.89  E-value: 7.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  14 VSVVIPAKDEAGNLPGLISEIGTALA--DRPFEVVVVDDGSTDETATVLAEIASASPwlRHVRH---DQACGQSASIRTG 88
Cdd:PRK10714   8 VSVVIPVYNEQESLPELIRRTTAACEslGKEYEILLIDDGSSDNSAEMLVEAAQAPD--SHIVAillNRNYGQHSAIMAG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  89 VRYARGDVILTIDGDGQNDPAFMPAMLARMEEGGDPVEMVageREGRKASWAKRHASRGANRLRRWLLKDGTRDTGCGLK 168
Cdd:PRK10714  86 FSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTV---RQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCMLR 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 750095919 169 AIRRDVFLELPYFDGWHRYLPALVQREGGRVRYVDVVDRERRFGASHY 216
Cdd:PRK10714 163 AYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKY 210
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
14-98 2.85e-08

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 52.51  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   14 VSVVIPAKDEAGNLPGLISEIgTALADrPFEVVVVDDGSTDETATVlaeiasASPWLRHVRHDQAcGQSASIRTGVRYAR 93
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADL-QALRG-DAEVIVVDGGSTDGTVEI------ARSLGAKVIHSPK-GRARQMNAGAALAK 71

                  ....*
gi 750095919   94 GDVIL 98
Cdd:TIGR04283  72 GDILL 76
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
15-109 7.44e-03

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 37.08  E-value: 7.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  15 SVVIPAKDEAGNLP----GLISEIGT-ALAdrpFEVVVVDDGSTDETATVLAEIASAspW-----LRHVRHDQacgQSAS 84
Cdd:NF038302   4 TVAIPTYNGANRLPevleRLRSQIGTeSLS---WEIIVVDNNSTDNTAQVVQEYQKN--WpspypLRYCFEPQ---QGAA 75
                         90       100
                 ....*....|....*....|....*..
gi 750095919  85 I--RTGVRYARGDVILTIDGDgqNDPA 109
Cdd:NF038302  76 FarQRAIQEAKGELIGFLDDD--NLPA 100
 
Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
16-191 3.12e-50

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: 162.74  E-value: 3.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  16 VVIPAKDEAGNLPGLISEIGTALADRP-FEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQACGQSASIRTGVRYARG 94
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYdYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  95 DVILTIDGDGQNDPAFMPAMLARMEEGGdpVEMVAGEREGRKA----SWAKRHASRGANRLRRWLLKDGTRDTGCGLKAI 170
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPKLLEKLLEGG--ADVVIGSRFVRGGgagmPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLF 158
                        170       180
                 ....*....|....*....|.
gi 750095919 171 RRDVFLELPYFDGWHRYLPAL 191
Cdd:cd04179  159 RREVLEALLSLLESNGFEFGL 179
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
16-196 4.73e-49

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: 159.56  E-value: 4.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  16 VVIPAKDEAGNLPGLISEIGTALADRP--FEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQACGQSASIRTGVRYAR 93
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGydYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  94 GDVILTIDGDGQNDPAFMPAMLARMEEGgdpVEMVAGEREGRKASWAKRHASRGANRLRRWLLKDGTRDTGCGLKAIRRD 173
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEG---YDVVYGVRKNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRK 157
                        170       180
                 ....*....|....*....|...
gi 750095919 174 VFLELPYFDGWHRYLPALVQREG 196
Cdd:cd04187  158 VVDALLLLPERHRFLRGLIAWVG 180
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
11-224 1.25e-47

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 156.79  E-value: 1.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  11 RPSVSVVIPAKDEAGNLPGLISEIgTALADRPFEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQACGQSASIRTGVR 90
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESL-LAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  91 YARGDVILTIDGDGQNDPAFMPAMLARMEEGgdPVEMVAGEREGRKASWAKRHASRGANRLRRWLLKdgTRDTGCGLKAI 170
Cdd:COG0463   80 AARGDYIAFLDADDQLDPEKLEELVAALEEG--PADLVYGSRLIREGESDLRRLGSRLFNLVRLLTN--LPDSTSGFRLF 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 750095919 171 RRDVFLELPYFDGW-HRYLPALVQREGGRVRYVDVvdrERRFGASHYGVWDRAAV 224
Cdd:COG0463  156 RREVLEELGFDEGFlEDTELLRALRHGFRIAEVPV---RYRAGESKLNLRDLLRL 207
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
16-235 7.37e-35

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: 124.18  E-value: 7.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  16 VVIPAKDEAGNLPGLISEIGTALADRPFEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQACGQSASIRTGVRYARGD 95
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  96 VILTIDGDGQNDPAFMPAMLARMEEGGdpVEMVAGER---EGRKASWA-KRH-ASRGANRLRRWLLKDGTRDTGCGLKAI 170
Cdd:cd06442   81 VIVVMDADLSHPPEYIPELLEAQLEGG--ADLVIGSRyveGGGVEGWGlKRKlISRGANLLARLLLGRKVSDPTSGFRAY 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 750095919 171 RRDVFLELPY---FDGWHRYLPALVQ--REGGRVRYVDVVDRERRFGAS--HYGVWDRAavgvldLFGVWWL 235
Cdd:cd06442  159 RREVLEKLIDslvSKGYKFQLELLVRarRLGYRIVEVPITFVDREHGESklGGKEIVEY------LKGLLRL 224
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
16-178 4.68e-28

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: 106.11  E-value: 4.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  16 VVIPAKDEAGNLPGLISEIGTALADRP---FEVVVVDDGSTDETATVLAEIASASPWL-RHVRHDQACGQSASIRTGVRY 91
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYLEERPsfsYEIIVVDDGSKDGTAEVARKLARKNPALiRVLTLPKNRGKGGAVRAGMLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  92 ARGDVILTIDGDGQNDPAFMPAMLARMEEGGdpVEMVAGER------EGRKASWAKRHASRGANRLRRWLLKDGTRDTGC 165
Cdd:cd04188   81 ARGDYILFADADLATPFEELEKLEEALKTSG--YDIAIGSRahlasaAVVKRSWLRNLLGRGFNFLVRLLLGLGIKDTQC 158
                        170
                 ....*....|...
gi 750095919 166 GLKAIRRDVFLEL 178
Cdd:cd04188  159 GFKLFTRDAARRL 171
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
15-175 3.38e-27

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: 102.86  E-value: 3.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   15 SVVIPAKDEAGNLPGLISEIgTALADRPFEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQACGQSASIRTGVRYARG 94
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESL-LNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   95 DVILTIDGDGQNDPAFMPAMLARMEEggDPVEMVAGEREGRKASWAKRHASRGANRLRRW------LLKDGTRDTGCGLK 168
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEE--DGADVVVGSRYVIFGETGEYRRASRITLSRLPfflglrLLGLNLPFLIGGFA 157

                  ....*..
gi 750095919  169 AIRRDVF 175
Cdd:pfam00535 158 LYRREAL 164
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
14-216 7.86e-26

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 102.89  E-value: 7.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  14 VSVVIPAKDEAGNLPGLISEIGTALA--DRPFEVVVVDDGSTDETATVLAEIASASPwlRHVRH---DQACGQSASIRTG 88
Cdd:PRK10714   8 VSVVIPVYNEQESLPELIRRTTAACEslGKEYEILLIDDGSSDNSAEMLVEAAQAPD--SHIVAillNRNYGQHSAIMAG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  89 VRYARGDVILTIDGDGQNDPAFMPAMLARMEEGGDPVEMVageREGRKASWAKRHASRGANRLRRWLLKDGTRDTGCGLK 168
Cdd:PRK10714  86 FSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTV---RQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCMLR 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 750095919 169 AIRRDVFLELPYFDGWHRYLPALVQREGGRVRYVDVVDRERRFGASHY 216
Cdd:PRK10714 163 AYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKY 210
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-242 2.89e-24

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: 98.28  E-value: 2.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   1 MTVSDPAAGVRPSVSVVIPAKDEAGNLPGLISEIgtALADRP---FEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQ 77
Cdd:COG1215   18 LARRRRAPADLPRVSVIIPAYNEEAVIEETLRSL--LAQDYPkekLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  78 ACGQSASIRTGVRYARGDVILTIDGDGQNDPAFMPAMLARMEEGGdpVEMvageregrkaswakrhasrganrlrrwllk 157
Cdd:COG1215   96 NGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG--VGA------------------------------ 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919 158 dgtrdTGCGLkAIRRDVFLELPYFDGWH----RYLPALVQREGGRVRYVD---VVDRERRFGASHYGVWDRAAVGVLDLF 230
Cdd:COG1215  144 -----SGANL-AFRREALEEVGGFDEDTlgedLDLSLRLLRAGYRIVYVPdavVYEEAPETLRALFRQRRRWARGGLQLL 217
                        250
                 ....*....|..
gi 750095919 231 GVWWLMRRRRRV 242
Cdd:COG1215  218 LKHRPLLRPRRL 229
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
4-217 1.22e-17

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 79.36  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   4 SDPAAGVRPSVSVVIPAKDEAGNLPGLISEIGTALAD-RPFEVVVVDDGSTDETATVLAEIASA--SPWLRHVRHDQACG 80
Cdd:PLN02726   1 MEAPGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDvKDFEIIVVDDGSPDGTQDVVKQLQKVygEDRILLRPRPGKLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  81 QSASIRTGVRYARGDVILTIDGDGQNDPAFMPAMLARMEEGGdpVEMVAGER---EGRKASWAKRH--ASRGANRLRRWL 155
Cdd:PLN02726  81 LGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETG--ADIVTGTRyvkGGGVHGWDLRRklTSRGANVLAQTL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 750095919 156 LKDGTRDTGCGLKAIRRDVFLELpyfdgwhryLPALV--------------QREGGRVRYVDVVDRERRFGASHYG 217
Cdd:PLN02726 159 LWPGVSDLTGSFRLYKRSALEDL---------VSSVVskgyvfqmeiivraSRKGYRIEEVPITFVDRVYGESKLG 225
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
13-182 2.78e-17

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: 78.43  E-value: 2.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  13 SVSVVIPAKDEAGNLPGLI-SEIGTALADRPFEVVVVDDGSTDETATVLAEIASASPWLRhVRHDQACGQSASIRTGVRY 91
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLeSLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIR-LIDNPKRIQSAGLNIGIRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  92 ARGDVILTIDGDGQNDPAFMPAMLARMEEG-----GDPVEMVAGEREGRKASWAKRHASRGANRLRRWLLKDGTR-DTGC 165
Cdd:cd02525   80 SRGDIIIRVDAHAVYPKDYILELVEALKRTgadnvGGPMETIGESKFQKAIAVAQSSPLGSGGSAYRGGAVKIGYvDTVH 159
                        170
                 ....*....|....*..
gi 750095919 166 GLkAIRRDVFLELPYFD 182
Cdd:cd02525  160 HG-AYRREVFEKVGGFD 175
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
16-184 7.08e-17

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: 75.73  E-value: 7.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  16 VVIPAKDEAGNLPGLISEIgTALADRPFEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQA-CGQSASIRTGVRYARG 94
Cdd:cd06423    1 IIVPAYNEEAVIERTIESL-LALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEnGGKAGALNAGLRHAKG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  95 DVILTIDGDGQNDPAFMPAMLARMEEGGDpVEMVAGE---REGRKASWAKRHA-----SRGANRLRRWLLKD-----GTr 161
Cdd:cd06423   80 DIVVVLDADTILEPDALKRLVVPFFADPK-VGAVQGRvrvRNGSENLLTRLQAieylsIFRLGRRAQSALGGvlvlsGA- 157
                        170       180
                 ....*....|....*....|...
gi 750095919 162 dtgCGlkAIRRDVFLELPYFDGW 184
Cdd:cd06423  158 ---FG--AFRREALREVGGWDED 175
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
16-202 1.10e-16

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: 74.85  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  16 VVIPAKDEAGNLPGLISEIgTALADRPFEVVVVDDGSTDETATVLAEIASASPWLRHVRHDQACGQSASIRTGVRYARGD 95
Cdd:cd00761    1 VIIPAYNEEPYLERCLESL-LAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  96 VILTIDGDGQNDPAFMPAMLARMEEGGDpVEMVageregrkaswakrhasrganrlrrwllkdgtrdTGCGLKAIRRDVF 175
Cdd:cd00761   80 YILFLDADDLLLPDWLERLVAELLADPE-ADAV----------------------------------GGPGNLLFRRELL 124
                        170       180       190
                 ....*....|....*....|....*....|..
gi 750095919 176 LELPYFDGWHR-----YLPALVQREGGRVRYV 202
Cdd:cd00761  125 EEIGGFDEALLsgeedDDFLLRLLRGGKVAFR 156
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
11-116 5.25e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 73.87  E-value: 5.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  11 RPSVSVVIPAKDEAGNLPGLISEIgTALADRPFEVVVVDDGSTDETATVLAEIasASPWLRHVRHDQACGQSASIRTGVR 90
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESL-LAQTYPPFEVIVVDNGSTDGTAELLAAL--AFPRVRVIRNPENLGFAAARNLGLR 78
                         90       100
                 ....*....|....*....|....*.
gi 750095919  91 YARGDVILTIDGDGQNDPAFMPAMLA 116
Cdd:COG1216   79 AAGGDYLLFLDDDTVVEPDWLERLLA 104
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
16-130 1.64e-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: 65.00  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  16 VVIPAKDEAGNLPGLISEIgTAL--ADRPFEVVVVDDGSTDETATVLAEIAS-ASPWLRHVRHDQ--ACGQSASIRTGVR 90
Cdd:cd04192    1 VVIAARNEAENLPRLLQSL-SALdyPKEKFEVILVDDHSTDGTVQILEFAAAkPNFQLKILNNSRvsISGKKNALTTAIK 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 750095919  91 YARGDVILTIDGDGQNDPAFMPAMLARMEEggDPVEMVAG 130
Cdd:cd04192   80 AAKGDWIVTTDADCVVPSNWLLTFVAFIQK--EQIGLVAG 117
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
15-173 4.56e-12

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 64.79  E-value: 4.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  15 SVVIPAKDEAGNLPGLISEIGTALADRP-------FEVVVVDDGSTDETATVLAEIA----SASPWLRHVRHDQACGQSA 83
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKMLKETIKYLESRSrkdpkfkYEIIIVNDGSKDKTLKVAKDFWrqniNPNIDIRLLSLLRNKGKGG 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  84 SIRTGVRYARGDVILTIDGDGQ---NDPAFMPAMLARMEEGGdpVEMVAGERE-------GRKASWAKRHASRGANRLRR 153
Cdd:PTZ00260 153 AVRIGMLASRGKYILMVDADGAtdiDDFDKLEDIMLKIEQNG--LGIVFGSRNhlvdsdvVAKRKWYRNILMYGFHFIVN 230
                        170       180
                 ....*....|....*....|
gi 750095919 154 WLLKDGTRDTGCGLKAIRRD 173
Cdd:PTZ00260 231 TICGTNLKDTQCGFKLFTRE 250
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
40-103 1.94e-11

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: 61.05  E-value: 1.94e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 750095919  40 DRPFEVVVVDDGSTDETATVLAEIASASPW-LRHVRHDQACGQSASIRT-GVRYARGDVILTIDGD 103
Cdd:cd06420   24 ILPFEVIIADDGSTEETKELIEEFKSQFPIpIKHVWQEDEGFRKAKIRNkAIAAAKGDYLIFIDGD 89
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
14-98 2.05e-10

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: 58.74  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  14 VSVVIPAKDEAGNLPGLISEIgTALADRPFEVVVVDDGSTDETatvlAEIASASPWlrHVRHDQAcGQSASIRTGVRYAR 93
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASL-RRLNPLPLEIIVVDGGSTDGT----VAIARSAGV--VVISSPK-GRARQMNAGAAAAR 72

                 ....*
gi 750095919  94 GDVIL 98
Cdd:cd02522   73 GDWLL 77
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
3-179 1.25e-09

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: 56.82  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   3 VSDPAAGVRPSVSVVIPAKDEAGNLPGLISEIgTALaDRP---FEVVVVDDGSTDETATVLAEIASASpwLRHVRHDQAC 79
Cdd:cd06439   20 PSLPDPAYLPTVTIIIPAYNEEAVIEAKLENL-LAL-DYPrdrLEIIVVSDGSTDGTAEIAREYADKG--VKLLRFPERR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  80 GQSASIRTGVRYARGDVILTIDGDGQNDPAFMPAMLARMEeggDP-VEMVAGE---REGRKASWAKRHASRGANRLRRWL 155
Cdd:cd06439   96 GKAAALNRALALATGEIVVFTDANALLDPDALRLLVRHFA---DPsVGAVSGElviVDGGGSGSGEGLYWKYENWLKRAE 172
                        170       180
                 ....*....|....*....|....*
gi 750095919 156 LKDGTRDTGCG-LKAIRRDVFLELP 179
Cdd:cd06439  173 SRLGSTVGANGaIYAIRRELFRPLP 197
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
13-116 2.26e-08

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 53.77  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  13 SVSVVIPAKDEAGNLPGLISEIGTALADR-PFEVVVVDDGSTDETATVlAEIASAspwlRHVRHDQAC-------GQSAS 84
Cdd:PRK13915  32 TVSVVLPALNEEETVGKVVDSIRPLLMEPlVDELIVIDSGSTDATAER-AAAAGA----RVVSREEILpelpprpGKGEA 106
                         90       100       110
                 ....*....|....*....|....*....|...
gi 750095919  85 IRTGVRYARGDVILTIDGDGQN-DPAFMPAMLA 116
Cdd:PRK13915 107 LWRSLAATTGDIVVFVDADLINfDPMFVPGLLG 139
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
14-98 2.85e-08

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 52.51  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   14 VSVVIPAKDEAGNLPGLISEIgTALADrPFEVVVVDDGSTDETATVlaeiasASPWLRHVRHDQAcGQSASIRTGVRYAR 93
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADL-QALRG-DAEVIVVDGGSTDGTVEI------ARSLGAKVIHSPK-GRARQMNAGAALAK 71

                  ....*
gi 750095919   94 GDVIL 98
Cdd:TIGR04283  72 GDILL 76
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
16-125 9.87e-08

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 50.68  E-value: 9.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  16 VVIPAKDEAGNLPGLISEIGTALADRP-FEVVVVDDGSTDETatvlAEIASASPWLRHVRHDQAC-GQSASIRTGVRYAR 93
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQDYPRElYRIFVVADNCTDDT----AQVARAAGATVLERHDPERrGKGYALDFGFRHLL 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 750095919  94 G-----DVILTIDGDGQNDPAFMPAMLARMEEGGDPV 125
Cdd:cd06438   77 NladdpDAVVVFDADNLVDPNALEELNARFAAGARVV 113
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
13-130 2.36e-07

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 50.33  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  13 SVSVVIPAKDEAGNLpgLISEIGTALADRPFEVVVVDDGSTDETATVLAEIASASPwlRHVRHDQACGQSASIRTGVRYA 92
Cdd:cd06434    1 DVTVIIPVYDEDPDV--FRECLRSILRQKPLEIIVVTDGDDEPYLSILSQTVKYGG--IFVITVPHPGKRRALAEGIRHV 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 750095919  93 RGDVILTIDGDGQNDPAFMPAMLARMEEggdpvEMVAG 130
Cdd:cd06434   77 TTDIVVLLDSDTVWPPNALPEMLKPFED-----PKVGG 109
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
14-103 2.44e-07

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: 49.98  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  14 VSVVIPAKDEAGNLPG-LISEIGtaLADrpfEVVVVDDGSTDETatvlAEIASASPWlrHVrHDQACGQSASIRT-GVRY 91
Cdd:cd02511    2 LSVVIITKNEERNIERcLESVKW--AVD---EIIVVDSGSTDRT----VEIAKEYGA--KV-YQRWWDGFGAQRNfALEL 69
                         90
                 ....*....|..
gi 750095919  92 ARGDVILTIDGD 103
Cdd:cd02511   70 ATNDWVLSLDAD 81
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
37-202 4.19e-07

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: 48.71  E-value: 4.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  37 ALADRPFEVVVVDDGSTDETAtvlAEIASASPWLRHVRHDQACGQSASIRTGVRYARGDVILTIDGDGQNDPAFMPAMLA 116
Cdd:cd04186   21 AQTYPDFEVIVVDNASTDGSV---ELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYVLLLNPDTVVEPGALLELLD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919 117 RMEEGGDpVEMVageregrkaswakrhasrganrlrrwllkdGTRDTGCGLkAIRRDVFLELPYFDgwHRYLPAL----- 191
Cdd:cd04186   98 AAEQDPD-VGIV------------------------------GPKVSGAFL-LVRREVFEEVGGFD--EDFFLYYedvdl 143
                        170
                 ....*....|....
gi 750095919 192 ---VQREGGRVRYV 202
Cdd:cd04186  144 clrARLAGYRVLYV 157
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
12-184 1.07e-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: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   12 PSVSVVIPAKDEAGNLPGLISEIGtALADRPFEVVVVDDGSTDETATVLAEIASASP--WLRHVRHDQACG---QSASIR 86
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAIL-AQPYPPVEVVVVVNPSDAETLDVAEEIAARFPdvRLRVIRNARLLGptgKSRGLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   87 TGVRYARGDVILTIDGDGQNDPAFMPAMLARMEegGDPVEMVAGERE--GRKASWAKRHAS----RGANRLRRWLLKDGT 160
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFD--SPKVGAVGTPVFslNRSTMLSALGALefalRHLRMMSLRLALGVL 158
                         170       180
                  ....*....|....*....|....
gi 750095919  161 RDTGCGLkAIRRDVFLELPYFDGW 184
Cdd:pfam13641 159 PLSGAGS-AIRREVLKELGLFDPF 181
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
15-115 6.27e-06

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: 46.12  E-value: 6.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919   15 SVVIPAKDEAGNlPGLISEI--GTALADRPFEVVVVDDGSTDETATVLAEIASAS--PWLRHVrHDQACGQSASIRTGVR 90
Cdd:pfam10111   1 SVVIPVYNGEKT-HWIQERIlnQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNlqVYYPNA-PDTTYSLAASRNRGTS 78
                          90       100
                  ....*....|....*....|....*
gi 750095919   91 YARGDVILTIDGDGQNDPAFMPAML 115
Cdd:pfam10111  79 HAIGEYISFIDGDCLWSPDKFEKQL 103
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
40-203 7.48e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 45.70  E-value: 7.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  40 DRPFEVVVVDDGSTDETATVLAEIASASPWLRHV-RHDQACGQSASIRTGVRYARGDVILTIDgdgQNDpAFMP---AML 115
Cdd:cd04196   25 YKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILiRNGKNLGVARNFESLLQAADGDYVFFCD---QDD-IWLPdklERL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919 116 ARMEEGGDPVEMV---------AGEREGRKASwaKRHASRGANRLRRWLLKDGTrdTGCGLkAIRRDV---FLELPYFDG 183
Cdd:cd04196  101 LKAFLKDDKPLLVysdlelvdeNGNPIGESFF--EYQKIKPGTSFNNLLFQNVV--TGCTM-AFNRELlelALPFPDADV 175
                        170       180
                 ....*....|....*....|.
gi 750095919 184 W-HRYLPALVQREGGRVRYVD 203
Cdd:cd04196  176 ImHDWWLALLASAFGKVVFLD 196
PRK10073 PRK10073
putative glycosyl transferase; Provisional
12-115 7.24e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 43.11  E-value: 7.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  12 PSVSVVIPAKDEAGNLPGLISEIGTALADRpFEVVVVDDGSTDETATVLAEIASASPWLRHVrHDQACGQSASIRTGVRY 91
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTA-LEIIIVNDGSTDNSVEIAKHYAENYPHVRLL-HQANAGVSVARNTGLAV 83
                         90       100
                 ....*....|....*....|....
gi 750095919  92 ARGDVILTIDGDGQNDPAFMPAML 115
Cdd:PRK10073  84 ATGKYVAFPDADDVVYPTMYETLM 107
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
15-102 3.29e-04

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: 41.04  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  15 SVVIPAKDEAGN--LPGLISEIGTALADRPFEVVVVDDGSTDETATVLAE--IASASPWLRHVRHDQacgQSASIR---T 87
Cdd:cd02510    1 SVIIIFHNEALStlLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeyYKKYLPKVKVLRLKK---REGLIRariA 77
                         90
                 ....*....|....*
gi 750095919  88 GVRYARGDVILTIDG 102
Cdd:cd02510   78 GARAATGDVLVFLDS 92
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
41-205 4.23e-04

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: 40.22  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  41 RPFEVVVVDDGSTDETatvLAEIASASPWLRHV--RHDQacGQSASIRTGVRYARGDVILTIDGDGQ---NDPAFMPAML 115
Cdd:cd06433   26 PNIEYIVIDGGSTDGT---VDIIKKYEDKITYWisEPDK--GIYDAMNKGIALATGDIIGFLNSDDTllpGALLAVVAAF 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919 116 ARMEEggdpVEMVAGEREGRKASWAKRHASRGANRLRRWLLKdgtRDTGC--GLkAIRRDVFLELPYFD----------G 183
Cdd:cd06433  101 AEHPE----VDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLY---GMPIChqAT-FFRRSLFEKYGGFDesyriaadydL 172
                        170       180
                 ....*....|....*....|..
gi 750095919 184 WHRYLpalvqREGGRVRYVDVV 205
Cdd:cd06433  173 LLRLL-----LAGKIFKYLPEV 189
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
16-116 5.14e-03

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 36.98  E-value: 5.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  16 VVIPAKDEAGnlpgLISE-IGTALADRP-FEVVVVDDGSTDETAtVLAEIASASPWLRHVRH-------------DQACG 80
Cdd:cd06436    1 VLVPCLNEEA----VIQRtLASLLRNKPnFLVLVIDDASDDDTA-GIVRLAITDSRVHLLRRhlpnartgkgdalNAAYD 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 750095919  81 QSASIRTGVRYARGDVILT-IDGDGQNDPAFMPAMLA 116
Cdd:cd06436   76 QIRQILIEEGADPERVIIAvIDADGRLDPNALEAVAP 112
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
15-109 7.44e-03

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 37.08  E-value: 7.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750095919  15 SVVIPAKDEAGNLP----GLISEIGT-ALAdrpFEVVVVDDGSTDETATVLAEIASAspW-----LRHVRHDQacgQSAS 84
Cdd:NF038302   4 TVAIPTYNGANRLPevleRLRSQIGTeSLS---WEIIVVDNNSTDNTAQVVQEYQKN--WpspypLRYCFEPQ---QGAA 75
                         90       100
                 ....*....|....*....|....*..
gi 750095919  85 I--RTGVRYARGDVILTIDGDgqNDPA 109
Cdd:NF038302  76 FarQRAIQEAKGELIGFLDDD--NLPA 100
 
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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