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Conserved domains on  [gi|15231448|ref|NP_187389|]
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Cellulose-synthase-like C6 [Arabidopsis thaliana]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

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
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
221-457 1.80e-116

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.


The actual alignment was detected with superfamily member cd06437:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 232  Bit Score: 348.53  E-value: 1.80e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 221 PMVIVQIPMCNEKEVYQQSIGAVCMLDWPRERMLVQVLDDSSELDVQQLIKAEVQKWQQrGVRIVYRHRLIRTGYKAGNL 300
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 301 KAAMNceyVKDYEFVAIFDADFQPPADFLKKTVPHFKgNEELALVQTRWAFVNKDENLLTRLQNINLSFHFEVEQQVNGV 380
Cdd:cd06437  80 AEGMK---VAKGEYVAIFDADFVPPPDFLQKTPPYFA-DPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231448 381 FINFFGFNGTAGVWRIKALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRWHSGP 457
Cdd:cd06437 156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
221-457 1.80e-116

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 348.53  E-value: 1.80e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 221 PMVIVQIPMCNEKEVYQQSIGAVCMLDWPRERMLVQVLDDSSELDVQQLIKAEVQKWQQrGVRIVYRHRLIRTGYKAGNL 300
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 301 KAAMNceyVKDYEFVAIFDADFQPPADFLKKTVPHFKgNEELALVQTRWAFVNKDENLLTRLQNINLSFHFEVEQQVNGV 380
Cdd:cd06437  80 AEGMK---VAKGEYVAIFDADFVPPPDFLQKTPPYFA-DPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231448 381 FINFFGFNGTAGVWRIKALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRWHSGP 457
Cdd:cd06437 156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
218-579 6.39e-39

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: 146.04  E-value: 6.39e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 218 EDYPMVIVQIPMCNEKEVYQQSIGAVCMLDWPRERMLVQVLDDSSELDVQQLikaeVQKWQQRGVRIVYRHRLIRTGyKA 297
Cdd:COG1215  26 ADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEI----ARELAAEYPRVRVIERPENGG-KA 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 298 GNLKAAMNceyVKDYEFVAIFDADFQPPADFLKKTVPHFKgneelalvqtrwafvnkDENLltrlqninlsfhfeveqqv 377
Cdd:COG1215 101 AALNAGLK---AARGDIVVFLDADTVLDPDWLRRLVAAFA-----------------DPGV------------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 378 ngvfinffGFNGTAGVWRIKALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRWHSGP 457
Cdd:COG1215 142 --------GASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGG 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 458 MQLFRlcffdilRSKVSAAKKANMIFLFFLLRKLILPFYSFTLFCVILPLTMFFpeanlpswvvcyipgIMSILNIIPAP 537
Cdd:COG1215 214 LQLLL-------KHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPAL---------------LLALLLALRRR 271
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15231448 538 RSFPFIVPYLlfentmsvtkFGAMISGLFKFDSSYEWVVTKK 579
Cdd:COG1215 272 RLLLPLLHLL----------YGLLLLLAALRGKKVVWKKTPR 303
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
171-463 2.09e-19

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 93.16  E-value: 2.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448  171 VC-IVLFLIQSVDRLVLVLGCF---WiKLRRiKPVaSMEYPTKLvgegvrledYPMVIVQIPMCNEK-EVYQQSIGAVCM 245
Cdd:PRK11498 218 VCgLILLFAETYAWIVLVLGYFqvvW-PLNR-QPV-PLPKDMSL---------WPTVDIFVPTYNEDlNVVKNTIYASLG 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448  246 LDWPRERMLVQVLDDSSELDVQQLIkaevqkwQQRGVrivyrHRLIRTGY---KAGNLKAAMNceyVKDYEFVAIFDADF 322
Cdd:PRK11498 286 IDWPKDKLNIWILDDGGREEFRQFA-------QEVGV-----KYIARPTHehaKAGNINNALK---YAKGEFVAIFDCDH 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448  323 QPPADFLKKTVPHFKGNEELALVQTRWAFVNKD---ENL--LTRLQNINLSFHFEVeQQVNGVFINFFgFNGTAGVWRIK 397
Cdd:PRK11498 351 VPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDpfeRNLgrFRKTPNEGTLFYGLV-QDGNDMWDATF-FCGSCAVIRRK 428
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231448  398 ALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRWHSGPMQLFRL 463
Cdd:PRK11498 429 PLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRL 494
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
314-511 8.05e-13

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 67.36  E-value: 8.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448   314 FVAIFDADFQPPADFLKKTVPHFKGNEeLALVQTrWAFVNKDENLLTRLQNINLSFHFEVEQQVNGVFINFFGFNGTAGV 393
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASPE-VAIIQG-PILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448   394 WRIKALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRWHSGPMQLFRLCFFDILRSKV 473
Cdd:pfam13632  79 LRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRLLGYLGTLL 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 15231448   474 SAAkkanmifLFFLLRKLILPFYSFTLFCVILPLTMFF 511
Cdd:pfam13632 159 WSG-------LPLALLLLLLFSISSLALVLLLLALLAG 189
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
221-457 1.80e-116

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 348.53  E-value: 1.80e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 221 PMVIVQIPMCNEKEVYQQSIGAVCMLDWPRERMLVQVLDDSSELDVQQLIKAEVQKWQQrGVRIVYRHRLIRTGYKAGNL 300
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 301 KAAMNceyVKDYEFVAIFDADFQPPADFLKKTVPHFKgNEELALVQTRWAFVNKDENLLTRLQNINLSFHFEVEQQVNGV 380
Cdd:cd06437  80 AEGMK---VAKGEYVAIFDADFVPPPDFLQKTPPYFA-DPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231448 381 FINFFGFNGTAGVWRIKALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRWHSGP 457
Cdd:cd06437 156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
221-461 4.54e-49

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 171.60  E-value: 4.54e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 221 PMVIVQIPMCNEK-EVYQQSIGAVCMLDWPRERMLVQVLDDSSELDVQQLIKAEvqkwqQRGVRIVYRHRLIRTGYKAGN 299
Cdd:cd06421   1 PTVDVFIPTYNEPlEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAEL-----GVEYGYRYLTRPDNRHAKAGN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 300 LKAAMncEYVkDYEFVAIFDADFQPPADFLKKTVPHFKGNEELALVQTRWAFVNKDENLLT--RLQNINLSFHFEVEQQV 377
Cdd:cd06421  76 LNNAL--AHT-TGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWLadGAPNEQELFYGVIQPGR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 378 NGVFINFFGfnGTAGVWRIKALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRWHSGP 457
Cdd:cd06421 153 DRWGAAFCC--GSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGM 230

                ....
gi 15231448 458 MQLF 461
Cdd:cd06421 231 LQIL 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
218-579 6.39e-39

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: 146.04  E-value: 6.39e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 218 EDYPMVIVQIPMCNEKEVYQQSIGAVCMLDWPRERMLVQVLDDSSELDVQQLikaeVQKWQQRGVRIVYRHRLIRTGyKA 297
Cdd:COG1215  26 ADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEI----ARELAAEYPRVRVIERPENGG-KA 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 298 GNLKAAMNceyVKDYEFVAIFDADFQPPADFLKKTVPHFKgneelalvqtrwafvnkDENLltrlqninlsfhfeveqqv 377
Cdd:COG1215 101 AALNAGLK---AARGDIVVFLDADTVLDPDWLRRLVAAFA-----------------DPGV------------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 378 ngvfinffGFNGTAGVWRIKALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRWHSGP 457
Cdd:COG1215 142 --------GASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGG 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 458 MQLFRlcffdilRSKVSAAKKANMIFLFFLLRKLILPFYSFTLFCVILPLTMFFpeanlpswvvcyipgIMSILNIIPAP 537
Cdd:COG1215 214 LQLLL-------KHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPAL---------------LLALLLALRRR 271
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15231448 538 RSFPFIVPYLlfentmsvtkFGAMISGLFKFDSSYEWVVTKK 579
Cdd:COG1215 272 RLLLPLLHLL----------YGLLLLLAALRGKKVVWKKTPR 303
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
225-462 2.81e-33

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 127.90  E-value: 2.81e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 225 VQIPMCNEK-EVYQQSIGAVCMLDWPRERMLVqvLDDSSEldvQQLIKAEVQKW-QQRGVRIVYRHRLIRTGYKAGNLKA 302
Cdd:cd06435   2 IHVPCYEEPpEMVKETLDSLAALDYPNFEVIV--IDNNTK---DEALWKPVEAHcAQLGERFRFFHVEPLPGAKAGALNY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 303 AMNcEYVKDYEFVAIFDADFQPPADFLKKTVPHFKgNEELALVQTRWAFVNKDENLLTRLQNINLSFHFEVEQ----QVN 378
Cdd:cd06435  77 ALE-RTAPDAEIIAVIDADYQVEPDWLKRLVPIFD-DPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMvsrnERN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 379 GVFinffgFNGTAGVWRIKALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRWHSGPM 458
Cdd:cd06435 155 AII-----QHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAV 229

                ....
gi 15231448 459 QLFR 462
Cdd:cd06435 230 QILK 233
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
225-413 6.93e-32

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: 121.95  E-value: 6.93e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 225 VQIPMCNEKEVYQQSIGAVCMLDWPRERmlVQVLDDSSELDVQQLIKAEvqkwQQRGVRIVYRHRLIRTGYKAGNLKAAM 304
Cdd:cd06423   1 IIVPAYNEEAVIERTIESLLALDYPKLE--VIVVDDGSTDDTLEILEEL----AALYIRRVLVVRDKENGGKAGALNAGL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 305 NceyVKDYEFVAIFDADFQPPADFLKKTVPHFKGNEELALVQTRWAFVNKDENLLTRLQNINLSFHFEVEQQVNGVFINF 384
Cdd:cd06423  75 R---HAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGV 151
                       170       180
                ....*....|....*....|....*....
gi 15231448 385 FGFNGTAGVWRIKALEDCGGWLERTTVED 413
Cdd:cd06423 152 LVLSGAFGAFRREALREVGGWDEDTLTED 180
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
221-459 1.65e-25

CESA_like_2 is a member of 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: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 105.80  E-value: 1.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 221 PMVIVQIPMCNEKEVYQQSIGAVCMLDWPRERMLVQ-VLDDSSELDVQQLIKAEVQKWQQRgvrIVYRHRLIRTGYKAGN 299
Cdd:cd06427   1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKlLLEEDDEETIAAARALRLPSIFRV---VVVPPSQPRTKPKACN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 300 --LKAAMNceyvkdyEFVAIFDADFQPPADFLKKTVPHF-KGNEELALVQTRWAFVNKDENLLTRLQNINLSFHFEveqq 376
Cdd:cd06427  78 yaLAFARG-------EYVVIYDAEDAPDPDQLKKAVAAFaRLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFD---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 377 vngVFINFFG-------FNGTAGVWRIKALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKcLCELPESYEAYKKQ 449
Cdd:cd06427 147 ---YLLPGLArlglpipLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTT-LEEANNALGNWIRQ 222
                       250
                ....*....|
gi 15231448 450 QYRWHSGPMQ 459
Cdd:cd06427 223 RSRWIKGYMQ 232
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
171-463 2.09e-19

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 93.16  E-value: 2.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448  171 VC-IVLFLIQSVDRLVLVLGCF---WiKLRRiKPVaSMEYPTKLvgegvrledYPMVIVQIPMCNEK-EVYQQSIGAVCM 245
Cdd:PRK11498 218 VCgLILLFAETYAWIVLVLGYFqvvW-PLNR-QPV-PLPKDMSL---------WPTVDIFVPTYNEDlNVVKNTIYASLG 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448  246 LDWPRERMLVQVLDDSSELDVQQLIkaevqkwQQRGVrivyrHRLIRTGY---KAGNLKAAMNceyVKDYEFVAIFDADF 322
Cdd:PRK11498 286 IDWPKDKLNIWILDDGGREEFRQFA-------QEVGV-----KYIARPTHehaKAGNINNALK---YAKGEFVAIFDCDH 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448  323 QPPADFLKKTVPHFKGNEELALVQTRWAFVNKD---ENL--LTRLQNINLSFHFEVeQQVNGVFINFFgFNGTAGVWRIK 397
Cdd:PRK11498 351 VPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDpfeRNLgrFRKTPNEGTLFYGLV-QDGNDMWDATF-FCGSCAVIRRK 428
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231448  398 ALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRWHSGPMQLFRL 463
Cdd:PRK11498 429 PLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRL 494
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
314-511 8.05e-13

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 67.36  E-value: 8.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448   314 FVAIFDADFQPPADFLKKTVPHFKGNEeLALVQTrWAFVNKDENLLTRLQNINLSFHFEVEQQVNGVFINFFGFNGTAGV 393
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASPE-VAIIQG-PILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448   394 WRIKALEDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRWHSGPMQLFRLCFFDILRSKV 473
Cdd:pfam13632  79 LRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRLLGYLGTLL 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 15231448   474 SAAkkanmifLFFLLRKLILPFYSFTLFCVILPLTMFF 511
Cdd:pfam13632 159 WSG-------LPLALLLLLLFSISSLALVLLLLALLAG 189
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
227-401 3.40e-12

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: 65.11  E-value: 3.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448   227 IPMCNEKEVYQQSIGAVCMLDWPRERMLVqvLDDSSELDVQQLIKaevqKWQQRGVRIVYRHRLIRTGyKAGNLKAAMnc 306
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLNQTYPNFEIIV--VDDGSTDGTVEIAE----EYAKKDPRVRVIRLPENRG-KAGARNAGL-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448   307 EYVKDyEFVAIFDADFQPPADFLKKTVPHFKgNEELALVQTRWAFVNKDENLLTRLQNINLSFHFEVEQQVNGVFINFFG 386
Cdd:pfam00535  75 RAATG-DYIAFLDADDEVPPDWLEKLVEALE-EDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFL 152
                         170
                  ....*....|....*
gi 15231448   387 FNGTAGVWRiKALED 401
Cdd:pfam00535 153 IGGFALYRR-EALEE 166
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
221-453 1.04e-10

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: 62.39  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448   221 PMVIVQIPMCNEKEVYQQSIGAVcmLDWPRERMLVQVLDDSSELDVQQLIKAEVQKWQQRGVRIVYRHRLIRTGYKAGNL 300
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAI--LAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTGKSRGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448   301 KAAmnCEYVKDyEFVAIFDADFQPPADFLKKTVPHFKGnEELALVQTRwAFVNKDENLLTRLQNinlsFHFEVEQQVNGV 380
Cdd:pfam13641  80 NHG--FRAVKS-DLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTP-VFSLNRSTMLSALGA----LEFALRHLRMMS 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231448   381 FINFFGF---NGTAGVWRIKALEDCGGWLERTTV-EDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYRW 453
Cdd:pfam13641 151 LRLALGVlplSGAGSAIRREVLKELGLFDPFFLLgDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARW 227
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
220-452 1.84e-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: 58.75  E-value: 1.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 220 YPMVIVQIPMCNEKEVYQQSIGAVCMLDWPRERMLVQVLDDSSELDVQQLikaeVQKWQQRGVRIVYRHRliRTGyKAGN 299
Cdd:cd06439  28 LPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLEIIVVSDGSTDGTAEI----AREYADKGVKLLRFPE--RRG-KAAA 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 300 LKAAMncEYVKDyEFVAIFDADFQPPADFLKKTVPHFKgNEELALVQTRWAFVNKD-----ENLLTRLQNiNLSFHfevE 374
Cdd:cd06439 101 LNRAL--ALATG-EIVVFTDANALLDPDALRLLVRHFA-DPSVGAVSGELVIVDGGgsgsgEGLYWKYEN-WLKRA---E 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 375 QQVNGVfinfFGFNGTagvwrIKAL--EDCGGWLERTTVEDMDIAVRAHLCGWKFIYLNDVKCLCELPESYEAYKKQQYR 452
Cdd:cd06439 173 SRLGST----VGANGA-----IYAIrrELFRPLPADTINDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDGSEEFRRRVR 243
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
257-363 4.03e-07

Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic Glucan Biosynthesis protein MdoH is a glucosyltransferase that catalyzes the elongation of beta-1,2 polyglucose chains of glucan, requiring a beta-glucoside as a primer and UDP-glucose as a substrate. Glucans are composed of 5 to 10 units of glucose forming a highly branched structure, where beta-1,2-linked glucose constitutes a linear backbone to which branches are attached by beta-1,6 linkages. In Escherichia coli, glucans are located in the periplasmic space, functioning as regulator of osmolarity. It is synthesized at a maximum when cells are grown in a medium with low osmolarity. It has been shown to span the cytoplasmic membrane.


Pssm-ID: 133034 [Multi-domain]  Cd Length: 254  Bit Score: 51.89  E-value: 4.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 257 VLDDSSELDV---QQLIKAEVQKWQQRGVRIVYRHRLIRTGYKAGNLkaAMNCE-YVKDYEFVAIFDADFQPPADFLKKT 332
Cdd:cd04191  39 ILSDTRDPDIwlaEEAAWLDLCEELGAQGRIYYRRRRENTGRKAGNI--ADFCRrWGSRYDYMVVLDADSLMSGDTIVRL 116
                        90       100       110
                ....*....|....*....|....*....|.
gi 15231448 333 VPHFKGNEELALVQTRWAFVNKdENLLTRLQ 363
Cdd:cd04191 117 VRRMEANPRAGIIQTAPKLIGA-ETLFARLQ 146
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
294-453 2.58e-06

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 48.05  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448   294 GYKAGNLKAAMncEYVKdYEFVAIFDADFQPPADFLKKTVPHFKGnEELALVqTRWAFVNKDENLLTRLQNINLSFHfev 373
Cdd:pfam13506  16 NPKVNNLLQGL--EAAK-YDLLVISDSDIRVPPDYLRDLLAPLAD-PKVGLV-TSPPVGSDPKGLAAALEAAFFNTL--- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448   374 eqqvNGVFINFFGFNGTA-G---VWRIKALEDCGGW--LERTTVEDMDIAVRAHLCGWKFIYLNDVKC--LCELPESYEA 445
Cdd:pfam13506  88 ----AGVLQAALSGIGFAvGmsmAFRRADLERIGGFeaLADYLAEDYALGKLLRAAGLKVVLSPRPILqtSGPRRTSFRA 163

                  ....*...
gi 15231448   446 YKKQQYRW 453
Cdd:pfam13506 164 FMARQLRW 171
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
221-431 4.75e-06

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 48.16  E-value: 4.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 221 PMVIVQIPMCNEKEVYQQSIGAVCMLDWPRERMLVqvLDDSSELDVQQLIkaevQKWQQRGVRIVYRHRLIRTGyKAGNL 300
Cdd:COG0463   2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIV--VDDGSTDGTAEIL----RELAAKDPRIRVIRLERNRG-KGAAR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 301 KAAMncEYVKdYEFVAIFDADFQPPADFLKKTVPHFKGNEELALVQTRWafVNKDENLLTRLQNINLSFHfeveqqvnGV 380
Cdd:COG0463  75 NAGL--AAAR-GDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRL--IREGESDLRRLGSRLFNLV--------RL 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15231448 381 FINFFGFNGTAGVWRIKALEDCGgwLERTTVEDMDIaVRAHLCGWKFIYLN 431
Cdd:COG0463 142 LTNLPDSTSGFRLFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVP 189
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
225-365 5.61e-06

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: 47.38  E-value: 5.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 225 VQIPMCNEKEVYQQSIGAVCMLdwpRERMLVQVLDDSSELDVQQLIKAEVQKWQqrgVRIVYRHRL-IRTGyKAGNLKAA 303
Cdd:cd06436   1 VLVPCLNEEAVIQRTLASLLRN---KPNFLVLVIDDASDDDTAGIVRLAITDSR---VHLLRRHLPnARTG-KGDALNAA 73
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 304 MN--CEYVK----DYE--FVAIFDADFQPPADFLKKTVPHFkGNEELALVQTRWAFVNKDENLLTRLQNI 365
Cdd:cd06436  74 YDqiRQILIeegaDPErvIIAVIDADGRLDPNALEAVAPYF-SDPRVAGTQSRVRMYNRHKNLLTILQDL 142
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
227-352 1.22e-05

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: 45.96  E-value: 1.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231448 227 IPMCNEKEVYQQSIGAVCMLDWPRERmlVQVLDDSSELDvqqlIKAEVQKWQQRGVRIVYRHRLIRTGyKAGNLKAAmnC 306
Cdd:cd00761   3 IPAYNEEPYLERCLESLLAQTYPNFE--VIVVDDGSTDG----TLEILEEYAKKDPRVIRVINEENQG-LAAARNAG--L 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15231448 307 EYVKdYEFVAIFDADFQPPADFLKKTVPHFKGNEELALVQTRWAFV 352
Cdd:cd00761  74 KAAR-GEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLL 118
MdoH COG2943
Membrane glycosyltransferase [Cell wall/membrane/envelope biogenesis, Carbohydrate transport ...
257-321 3.37e-04

Membrane glycosyltransferase [Cell wall/membrane/envelope biogenesis, Carbohydrate transport and metabolism];


Pssm-ID: 442186 [Multi-domain]  Cd Length: 661  Bit Score: 43.71  E-value: 3.37e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231448 257 VLDDSSELDVqqlIKAEVQKWQQ------RGVRIVYRHRLIRTGYKAGNLKaamncEYV----KDYEFVAIFDAD 321
Cdd:COG2943 136 ILSDTTDPDI---WAAEEAAWAAlrarlgGGGRIFYRRRRRNTGRKAGNIA-----DFCrrwgGAYDYMLVLDAD 202
PRK05454 PRK05454
glucans biosynthesis glucosyltransferase MdoH;
257-321 2.22e-03

glucans biosynthesis glucosyltransferase MdoH;


Pssm-ID: 235476 [Multi-domain]  Cd Length: 605  Bit Score: 41.02  E-value: 2.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231448  257 VLDDSSELDVQQLIKAEVQKWQQR---GVRIVYRHRLIRTGYKAGNLKaamncEYV----KDYEFVAIFDAD 321
Cdd:PRK05454 164 ILSDTRDPDIAAAEEAAWLELRAElggEGRIFYRRRRRNVGRKAGNIA-----DFCrrwgGAYDYMVVLDAD 230
 
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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