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Conserved domains on  [gi|1625929997|ref|WP_136573919|]
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glycosyltransferase [Lampropedia puyangensis]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 7-369 9.73e-46

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member cd03818:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 396  Bit Score: 162.53  E-value: 9.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997   7 IVFVSAVCPAQYSLLCSYL-RQTGlaQSWYMTTPGNAQKFA--NTYDHLLPFKPDGKIVGPqsyYYTSKLERSARIGRGV 83
Cdd:cd03818     2 ILFVHQNFPGQFKHLARHLaRQPG--NEVTFLTRRNDQGIPgvRPVRYRPFRGVASPLEGH---RYVRDFEEGVLRGQAV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997  84 LKAIQAFEKK-QPIDLIVAHSLWGAPHFLYD-ETDAAIVSYIEFPsYRAHGWDAAY-PPDQAQRMGDRNMEMLHFHQVLN 160
Cdd:cd03818    77 LRALLALKREgFRPDVVVGHPGWGEALFVKDvFPDVPLIGYCEYY-YRAEGADVGFdPEFPLDLMIRCRLRNRNIALLLS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 161 ---SDLTIVPSQHARNLFPESLRSQIEVQFEGFDIAPLASSPQRQ-----DQRFT-----IGFSARDLSSAKGLETYIRL 227
Cdd:cd03818   156 leqADLGVTPTRWQRSLFPAAYRDRISVIHDGVDTDRLAPDPAARlrllnGTELKagdpvITYVARNLEPYRGFHVFMRA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 228 VDRLVREGDgqHMRFVALGDpQATTYGYEQqwverRYEGqfkSFRDHLLQQYPAAKQAIEFPGKLPYDVFSATLSSIDLF 307
Cdd:cd03818   236 LPRIQARRP--DARVVVVGG-DGVSYGSPP-----PDGG---SWKQKMLAELGVDLERVHFVGKVPYDQYVRLLQLSDAH 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1625929997 308 LYPLRYGVANWGLMEILARGGCVIGSNWGFVPELIRHDVNGMLMP-DSDDAWLGAIRQLRDDP 369
Cdd:cd03818   305 VYLTYPFVLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDfFDPDALAAAVLELLEDP 367
 
Name Accession Description Interval E-value
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 7-369 9.73e-46

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 162.53  E-value: 9.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997   7 IVFVSAVCPAQYSLLCSYL-RQTGlaQSWYMTTPGNAQKFA--NTYDHLLPFKPDGKIVGPqsyYYTSKLERSARIGRGV 83
Cdd:cd03818     2 ILFVHQNFPGQFKHLARHLaRQPG--NEVTFLTRRNDQGIPgvRPVRYRPFRGVASPLEGH---RYVRDFEEGVLRGQAV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997  84 LKAIQAFEKK-QPIDLIVAHSLWGAPHFLYD-ETDAAIVSYIEFPsYRAHGWDAAY-PPDQAQRMGDRNMEMLHFHQVLN 160
Cdd:cd03818    77 LRALLALKREgFRPDVVVGHPGWGEALFVKDvFPDVPLIGYCEYY-YRAEGADVGFdPEFPLDLMIRCRLRNRNIALLLS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 161 ---SDLTIVPSQHARNLFPESLRSQIEVQFEGFDIAPLASSPQRQ-----DQRFT-----IGFSARDLSSAKGLETYIRL 227
Cdd:cd03818   156 leqADLGVTPTRWQRSLFPAAYRDRISVIHDGVDTDRLAPDPAARlrllnGTELKagdpvITYVARNLEPYRGFHVFMRA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 228 VDRLVREGDgqHMRFVALGDpQATTYGYEQqwverRYEGqfkSFRDHLLQQYPAAKQAIEFPGKLPYDVFSATLSSIDLF 307
Cdd:cd03818   236 LPRIQARRP--DARVVVVGG-DGVSYGSPP-----PDGG---SWKQKMLAELGVDLERVHFVGKVPYDQYVRLLQLSDAH 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1625929997 308 LYPLRYGVANWGLMEILARGGCVIGSNWGFVPELIRHDVNGMLMP-DSDDAWLGAIRQLRDDP 369
Cdd:cd03818   305 VYLTYPFVLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDfFDPDALAAAVLELLEDP 367
Glyco_trans_4_3 pfam12000
Glycosyl transferase family 4 group; This domain is found associated with pfam00534.
 51-195 7.37e-34

Glycosyl transferase family 4 group; This domain is found associated with pfam00534.


Pssm-ID: 432252  Cd Length: 168  Bit Score: 124.20  E-value: 7.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997  51 HLLPFKPDGKiVGPQSYYYTSKLERSARIGRGVLKAIQAFEKK-QPIDLIVAHSLWGAPHFLYDE-TDAAIVSYIEFpSY 128
Cdd:pfam12000  20 RKVRYRPPRG-PTPGAHPYVREFEAAVRRGQAVARAAQALRAEgFVPDVIVGHSGWGETLFLKDVfPDAPLLGYFEF-FY 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1625929997 129 RAHGWDA----AYPPDQAQRMGDRNMEMLHFHQVLNSDLTIVPSQHARNLFPESLRSQIEVQFEGFDIAPL 195
Cdd:pfam12000  98 RAHGADVgfdpEFPLSLDDRARLRLKNAPILLALASCDAGLSPTAWQRSQFPAEFRSKISVIHDGIDTDAF 168
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 295-400 3.06e-12

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 63.09  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 295 DVFSATLSSIDLFLYPLRYGVANWGLMEILARGGCVIGSNWGFVPELIRHDVNGMLMPDSD-DAWLGAIRQLRDDPARRA 373
Cdd:COG0438    12 LLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDpEALAEAILRLLEDPELRR 91

                          90       100
                  ....*....|....*....|....*...
gi 1625929997 374 RYAAAARQTGEA-FHISKIAPRYMRLFE 400
Cdd:COG0438    92 RLGEAARERAEErFSWEAIAERLLALYE 119
 
Name Accession Description Interval E-value
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 7-369 9.73e-46

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 162.53  E-value: 9.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997   7 IVFVSAVCPAQYSLLCSYL-RQTGlaQSWYMTTPGNAQKFA--NTYDHLLPFKPDGKIVGPqsyYYTSKLERSARIGRGV 83
Cdd:cd03818     2 ILFVHQNFPGQFKHLARHLaRQPG--NEVTFLTRRNDQGIPgvRPVRYRPFRGVASPLEGH---RYVRDFEEGVLRGQAV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997  84 LKAIQAFEKK-QPIDLIVAHSLWGAPHFLYD-ETDAAIVSYIEFPsYRAHGWDAAY-PPDQAQRMGDRNMEMLHFHQVLN 160
Cdd:cd03818    77 LRALLALKREgFRPDVVVGHPGWGEALFVKDvFPDVPLIGYCEYY-YRAEGADVGFdPEFPLDLMIRCRLRNRNIALLLS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 161 ---SDLTIVPSQHARNLFPESLRSQIEVQFEGFDIAPLASSPQRQ-----DQRFT-----IGFSARDLSSAKGLETYIRL 227
Cdd:cd03818   156 leqADLGVTPTRWQRSLFPAAYRDRISVIHDGVDTDRLAPDPAARlrllnGTELKagdpvITYVARNLEPYRGFHVFMRA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 228 VDRLVREGDgqHMRFVALGDpQATTYGYEQqwverRYEGqfkSFRDHLLQQYPAAKQAIEFPGKLPYDVFSATLSSIDLF 307
Cdd:cd03818   236 LPRIQARRP--DARVVVVGG-DGVSYGSPP-----PDGG---SWKQKMLAELGVDLERVHFVGKVPYDQYVRLLQLSDAH 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1625929997 308 LYPLRYGVANWGLMEILARGGCVIGSNWGFVPELIRHDVNGMLMP-DSDDAWLGAIRQLRDDP 369
Cdd:cd03818   305 VYLTYPFVLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDfFDPDALAAAVLELLEDP 367
Glyco_trans_4_3 pfam12000
Glycosyl transferase family 4 group; This domain is found associated with pfam00534.
 51-195 7.37e-34

Glycosyl transferase family 4 group; This domain is found associated with pfam00534.


Pssm-ID: 432252  Cd Length: 168  Bit Score: 124.20  E-value: 7.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997  51 HLLPFKPDGKiVGPQSYYYTSKLERSARIGRGVLKAIQAFEKK-QPIDLIVAHSLWGAPHFLYDE-TDAAIVSYIEFpSY 128
Cdd:pfam12000  20 RKVRYRPPRG-PTPGAHPYVREFEAAVRRGQAVARAAQALRAEgFVPDVIVGHSGWGETLFLKDVfPDAPLLGYFEF-FY 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1625929997 129 RAHGWDA----AYPPDQAQRMGDRNMEMLHFHQVLNSDLTIVPSQHARNLFPESLRSQIEVQFEGFDIAPL 195
Cdd:pfam12000  98 RAHGADVgfdpEFPLSLDDRARLRLKNAPILLALASCDAGLSPTAWQRSQFPAEFRSKISVIHDGIDTDAF 168
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 83-400 4.13e-18

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 85.28  E-value: 4.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997  83 VLKAIQAFEKKQPIDLIVAHSlWGAPHFLYDETDAAIVSYIefpsYRAHGWDAAYPPDQAQRMgdrnMEMLH--FHQVLN 160
Cdd:cd03801    70 LLRELRPLLRLRKFDVVHAHG-LLAALLAALLALLLGAPLV----VTLHGAEPGRLLLLLAAE----RRLLAraEALLRR 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 161 SDLTIVPSQHARNLF---PESLRSQIEVQFEGFDIA----PLASSPQRQDQRFTIGFSARdLSSAKGLETYIRLVDRLVR 233
Cdd:cd03801   141 ADAVIAVSEALRDELralGGIPPEKIVVIPNGVDLErfspPLRRKLGIPPDRPVLLFVGR-LSPRKGVDLLLEALAKLLR 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 234 EGDGQHMRFVALGDPQattygyeqqwverryegqfksfRDHLLQQYPAAKQAIEFPGKLPYDVFSATLSSIDLFLYPLRY 313
Cdd:cd03801   220 RGPDVRLVIVGGDGPL----------------------RAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRY 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 314 GvaNWGL--MEILARGGCVIGSNWGFVPELIRHDVNGMLMPDSD-DAWLGAIRQLRDDPARRARYAAAARQTGEA-FHIS 389
Cdd:cd03801   278 E--GFGLvvLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDvEALADALLRLLADPELRARLGRAARERVAErFSWE 355

                         330
                  ....*....|.
gi 1625929997 390 KIAPRYMRLFE 400
Cdd:cd03801   356 RVAERLLDLYR 366
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 295-400 3.06e-12

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 63.09  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 295 DVFSATLSSIDLFLYPLRYGVANWGLMEILARGGCVIGSNWGFVPELIRHDVNGMLMPDSD-DAWLGAIRQLRDDPARRA 373
Cdd:COG0438    12 LLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDpEALAEAILRLLEDPELRR 91

                          90       100
                  ....*....|....*....|....*...
gi 1625929997 374 RYAAAARQTGEA-FHISKIAPRYMRLFE 400
Cdd:COG0438    92 RLGEAARERAEErFSWEAIAERLLALYE 119
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 160-369 4.59e-12

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 66.97  E-value: 4.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 160 NSDLTIVPSQ-----HARNLFPESLRSQIEVQFEgFDIAPLASsPQRQDQRFTIGFSARdLSSAKGLETYIRLVDRLVRE 234
Cdd:cd03823   143 GGDAVLAPSRftanlHEANGLFSARISVIPNAVE-PDLAPPPR-RRPGTERLRFGYIGR-LTEEKGIDLLVEAFKRLPRE 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 235 GdgqhMRFVALGDPQATtyGYEQQWVERRyegqfksfrdhllqqypaakqaIEFPGKLPYDVFSATLSSIDLFLYPLRYG 314
Cdd:cd03823   220 D----IELVIAGHGPLS--DERQIEGGRR----------------------IAFLGRVPTDDIKDFYEKIDVLVVPSIWP 271

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1625929997 315 vANWGL--MEILARGGCVIGSNWGFVPELIRHDVNGMLM-PDSDDAWLGAIRQLRDDP 369
Cdd:cd03823   272 -EPFGLvvREAIAAGLPVIASDLGGIAELIQPGVNGLLFaPGDAEDLAAAMRRLLTDP 328
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 205-369 5.54e-11

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 60.75  E-value: 5.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 205 RFTIGFSARdLSSAKGLETYIRLVDRLVREGDGQHMRFValGDpqattygyeqqwverryeGQFKSFRDHLLQQYPAAKQ 284
Cdd:pfam00534   2 KKIILFVGR-LEPEKGLDLLIKAFALLKEKNPNLKLVIA--GD------------------GEEEKRLKKLAEKLGLGDN 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 285 aIEFPGKLPYDVFSATLSSIDLFLYPLRY---GVAnwgLMEILARGGCVIGSNWGFVPELIRHDVNGMLM-PDSDDAWLG 360
Cdd:pfam00534  61 -VIFLGFVSDEDLPELLKIADVFVLPSRYegfGIV---LLEAMACGLPVIASDVGGPPEVVKDGETGFLVkPNNAEALAE 136


                  ....*....
gi 1625929997 361 AIRQLRDDP 369
Cdd:pfam00534 137 AIDKLLEDE 145
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 75-369 1.78e-08

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 55.85  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997  75 RSARIGRGVLKAIQAFEKKQPiDLIVAHSLWGAPhFLydetdAAIVSYIEFPSY--RAHGWDAA-YPPDQAQRmgdrnme 151
Cdd:cd03798    76 LAPLRAPSLAKLLKRRRRGPP-DLIHAHFAYPAG-FA-----AALLARLYGVPYvvTEHGSDINvFPPRSLLR------- 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 152 MLHFHQVLNSDLTIVPS----QHARNLFPEslRSQIEVQFEGFDIA---PLASSPQRQDQRFTIGFSARdLSSAKGLETY 224
Cdd:cd03798   142 KLLRWALRRAARVIAVSkalaEELVALGVP--RDRVDVIPNGVDPArfqPEDRGLGLPLDAFVILFVGR-LIPRKGIDLL 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 225 IRLVDRLVREgdGQHMRFVALGDPQATTYgYEQQWVERRYEGQfksfrdhllqqypaakqaIEFPGKLPYDVFSATLSSI 304
Cdd:cd03798   219 LEAFARLAKA--RPDVVLLIVGDGPLREA-LRALAEDLGLGDR------------------VTFTGRLPHEQVPAYYRAC 277

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1625929997 305 DLFLYPLR---YGVAnwgLMEILARGGCVIGSNWGFVPELIRHDVNGMLMPDSD-DAWLGAIRQLRDDP 369
Cdd:cd03798   278 DVFVLPSRhegFGLV---LLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDaDALAAALRRALAEP 343
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 301-402 2.55e-07

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 52.35  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 301 LSSIDLFLYPLR---YGVAnwgLMEILARGGCVIGSNWGFVPELIRHDVNGMLMP--DSDDAWLGAIRQLRDDPARRARY 375
Cdd:cd04962   267 LSIADLFLLPSEkesFGLA---ALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDvgDVDAMAKSALSILEDDELYNRMG 343

                          90       100
                  ....*....|....*....|....*..
gi 1625929997 376 AAAARQTGEAFHISKIAPRYMRLFELA 402
Cdd:cd04962   344 RAARKRAAERFDPERIVPQYEAYYRRL 370
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
205-368 3.46e-07

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 49.05  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 205 RFTIGFSARDLSSAKGLETYIRLVDRLVREGDGQHMRFValGDpqattygYEQQWVERRYEGqfksfrdhllqqypaAKQ 284
Cdd:pfam13692   1 RPVILFVGRLHPNVKGVDYLLEAVPLLRKRDNDVRLVIV--GD-------GPEEELEELAAG---------------LED 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 285 AIEFPGKLPyDVFSAtLSSIDLFLYPLRY---GVAnwgLMEILARGGCVIGSNWGFVPELIrHDVNGMLMPDSD-DAWLG 360
Cdd:pfam13692  57 RVIFTGFVE-DLAEL-LAAADVFVLPSLYegfGLK---LLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDpEALAE 130


                  ....*...
gi 1625929997 361 AIRQLRDD 368
Cdd:pfam13692 131 AILRLLED 138
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 197-369 5.33e-07

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 51.44  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 197 SSPQRQDQRFTIGFSARdLSSAKGLETYIRLVDRLVREGDgqHMRFVALGDPqATTYGYEQQWVERRYEGQfksfrdhll 276
Cdd:cd03808   181 SPESLPSEKVVFLFVAR-LLKDKGIDELIEAAKILKKKGP--NVRFLLVGDG-ELENPSEILIEKLGLEGR--------- 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 277 qqypaakqaIEFPGKlPYDVFsATLSSIDLFLYPLRY-GVANwGLMEILARGGCVIGSNWGFVPELIRHDVNGMLMPDSD 355
Cdd:cd03808   248 ---------IEFLGF-RSDVP-ELLAESDVFVLPSYReGLPR-SLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGD 315

                         170
                  ....*....|....*
gi 1625929997 356 -DAWLGAIRQLRDDP 369
Cdd:cd03808   316 vEALADAIEKLIEDP 330
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 152-376 3.81e-05

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 45.36  E-value: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 152 MLHFHQvlNSDLTIVPSQHARNLFPESLRSQIEVQFEGFDIAplASSPQRQDQRFTIGFSARD---------LSSAKGLE 222
Cdd:cd03814   139 LRWFHN--PFDTTLVPSPSIARELEGHGFERVRLWPRGVDTE--LFHPSRRDAALRRRLGPPGrplllyvgrLAPEKNLE 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 223 TYIRLVDRLVREGDgqhMRFVALGDpqattyGYEQQWVERRYegqfksfrdhllqqyPaakQAIeFPGKLPYDVFSATLS 302
Cdd:cd03814   215 ALLDADLPLAASPP---VRLVVVGD------GPARAELEARG---------------P---DVI-FTGFLTGEELARAYA 266

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625929997 303 SIDLFLYPLR---YGVAnwgLMEILARGGCVIGSNWGFVPELIRHDVNGMLMPDSD-DAWLGAIRQLRDDPARRARYA 376
Cdd:cd03814   267 SADVFVFPSRtetFGLV---VLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDaAAFAAALRALLEDPELRRRMA 341
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 56-369 5.40e-05

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 45.04  E-value: 5.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997  56 KPDGKIVGPQSYYYTSKLERSARIGRGVLKaIQAFEKKQPIDLIVAHsLWGAPHFlydetdAAIVSYIEFPS-YRAHGwd 134
Cdd:cd03811    45 KQLNGDVKLIRLLIRVLKLIKLGLLKAILK-LKRILKRAKPDVVISF-LGFATYI------VAKLAAARSKViAWIHS-- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 135 aaYPPdqaQRMGDRNMEMLHFHQVLNSDLTIVPSQHARNLFPE---SLRSQIEV-----QFEGFDIAPLASSPQRQDQRF 206
Cdd:cd03811   115 --SLS---KLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRlgpSPPEKIEViynpiDIDRIRALAKEPILNEPEDGP 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 207 TIGFSARdLSSAKGLETYIRLVDRLVREGDGQHMRFValGDpqattyGYEqqwverryegqfksfRDHLLQQypAAKQAI 286
Cdd:cd03811   190 VILAVGR-LDPQKGHDLLIEAFAKLRKKYPDVKLVIL--GD------GPL---------------REELEKL--AKELGL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 287 E----FPG--KLPYDVFSATlssiDLFLYPLRY---GVAnwgLMEILARGGCVIGSNWGFVPELIRHDVNGMLMPDSDDA 357
Cdd:cd03811   244 AerviFLGfqSNPYPYLKKA----DLFVLSSRYegfPNV---LLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAA 316

                         330
                  ....*....|..
gi 1625929997 358 WLGAIRQLRDDP 369
Cdd:cd03811   317 ALAGILAALLQK 328
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 215-350 3.06e-04

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 42.01  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 215 LSSAKGLETYIRLVDRLVREGDGqhMRFVALGDPqattygyeqqwVERRYEGQFKSFRDHLlqqypaaKQAIEFPGKLPY 294
Cdd:cd01635   119 LVPEKGIDLLLEALALLKARLPD--LVLVLVGGG-----------GEREEEEALAAALGLL-------ERVVIIGGLVDD 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1625929997 295 DVFSATLSSIDLFLYPLRYGVANWGLMEILARGGCVIGSNWGFVPELIRHDVNGML 350
Cdd:cd01635   179 EVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLL 234
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 45-400 8.18e-04

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 41.50  E-value: 8.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997  45 FANTYDHLLPFKPDGKIVgpqsyYYTSKLERSARIG--RGVLKAIQAFEKKQPIDLIVAHS-------------LWGAP- 108
Cdd:cd03817    37 ITPSDPGAEDEEEVVRYR-----SFSIPIRKYHRQHipFPFKKAVIDRIKELGPDIIHTHTpfslgklglriarKLKIPi 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 109 ----HFLYDEtdaaIVSYIEFPSYRAHGwdaayppdqaqrmGDRNMEMLHFHQVlnsDLTIVPSQHARNLFPES-LRSQI 183
Cdd:cd03817   112 vhtyHTMYED----YLHYIPKGKLLVKA-------------VVRKLVRRFYNHT---DAVIAPSEKIKDTLREYgVKGPI 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 184 EVQFEGFDIAPLASSPQ---------RQDQrFTIGFSARdLSSAKGLETYIRLVDRLVREgdgQHMRFVALGDpqattyG 254
Cdd:cd03817   172 EVIPNGIDLDKFEKPLNteerrklglPPDE-PILLYVGR-LAKEKNIDFLLRAFAELKKE---PNIKLVIVGD------G 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 255 YEQQWVERryegqfksfrdhlLQQYPAAKQAIEFPGKLPYDVFSATLSSIDLFLYPLRYGVANWGLMEILARGGCVIGSN 334
Cdd:cd03817   241 PEREELKE-------------LARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAK 307

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1625929997 335 WGFVPELIRHDVNGMLMPDSDDAWLGAIRQLRDDPARRARYAAAARQTGEAFHISKiapRYMRLFE 400
Cdd:cd03817   308 DPAASELVEDGENGFLFEPNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAK---SVEKLYE 370
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 301-400 2.40e-03

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 40.01  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 301 LSSIDLFLYPLRygVANWGLM--EILARGGCVIGSNWGFVPELIRHDVNGMLMPDSDDAWLG-AIRQLRDDPARRARYAA 377
Cdd:cd03825   261 YSAADLFVHPSL--ADNLPNTllEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAeAIEWLLANPKERESLGE 338

                          90       100
                  ....*....|....*....|....
gi 1625929997 378 AARQTGEA-FHISKIAPRYMRLFE 400
Cdd:cd03825   339 RARALAENhFDQRVQAQRYLELYK 362
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 183-368 2.83e-03

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 39.74  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 183 IEVQFEGFDIAPLASSPQRQDQRfTIGFSARdLSSAKGLETYIRLVDRLvrEGDGQHMRFVALGDPQATTygyeqqwver 262
Cdd:cd05844   168 IHVHYIGIDPAKFAPRDPAERAP-TILFVGR-LVEKKGCDVLIEAFRRL--AARHPTARLVIAGDGPLRP---------- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 263 ryegqfksfrdhLLQQYPAAKQAIEFPGKLPYDVFSATLSSIDLFLYPLRygVANWG--------LMEILARGGCVIGSN 334
Cdd:cd05844   234 ------------ALQALAAALGRVRFLGALPHAEVQDWMRRAEIFCLPSV--TAASGdseglgivLLEAAACGVPVVSSR 299

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1625929997 335 WGFVPELIRHDVNGMLMPDSDDAWLGA--IRQLRDD 368
Cdd:cd05844   300 HGGIPEAILDGETGFLVPEGDVDALADalQALLADR 335
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 205-369 3.19e-03

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 39.26  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 205 RFTIGFSARdLSSAKGLETYIRLVDRLVREGDgqhMRFVALGDPqattygyeqqwvERRYEgqfksfrDHLLQQYPAAKQ 284
Cdd:cd03819   182 KPVVGYVGR-LSPEKGWLLLVDAAAELKDEPD---FRLLVAGDG------------PERDE-------IRRLVERLGLRD 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 285 AIEFPGkLPYDVfSATLSSIDLFLYPLRYGVANWGLMEILARGGCVIGSNWGFVPELIRHDVNGMLMPDSDDAWL-GAIR 363
Cdd:cd03819   239 RVTFTG-FREDV-PAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALaDAIR 316


                  ....*.
gi 1625929997 364 QLRDDP 369
Cdd:cd03819   317 AAKLLP 322
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 272-369 6.41e-03

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 38.38  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625929997 272 RDHLLQQYPAAKQaIEFPGKLPYDVFSATLSSIDLFLYPLRYgvANWGL--MEILARGGCVIGSNWGFVPELIRHDVNGM 349
Cdd:cd03800   272 LAELAEELGLIDR-VRFPGRVSRDDLPELYRAADVFVVPSLY--EPFGLtaIEAMACGTPVVATAVGGLQDIVRDGRTGL 348

                          90       100
                  ....*....|....*....|.
gi 1625929997 350 LMPDSD-DAWLGAIRQLRDDP 369
Cdd:cd03800   349 LVDPHDpEALAAALRRLLDDP 369
 
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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