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Conserved domains on  [gi|15221657|ref|NP_173818|]
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cellulose synthase-like A10 [Arabidopsis thaliana]

Protein Classification

cellulose synthase family protein( domain architecture ID 10157716)

cellulose synthase family protein similar to plant glucomannan 4-beta-mannosyltransferases that is involved in the synthesis of beta-1,4-mannan, the backbone for the synthesis of the storage polysaccharide galactomannan

CAZY:  GT2
EC:  2.4.1.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
122-358 1.13e-136

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: 395.53  E-value: 1.13e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 122 PMVLVQIPMYNEKEVLQLSIGAACRLIWPLDRLIVQVLDDSTDQTIKELVNTECAKWeSKGVNIKCERRDNRNGYKAGAL 201
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYA-AQGVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 202 KEGMKHNYvklCNYVVIFDADFQPEPDYLQhSVPFLVHNPEVALVQARWRFMNANKCLMTRMQEMSLNYHFMAEQESGST 281
Cdd:cd06437  80 AEGMKVAK---GEYVAIFDADFVPPPDFLQ-KTPPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221657 282 RHAFFSFNGTAGVWRMAAMEEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRWSCGP 358
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 ...
122-358 1.13e-136

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: 395.53  E-value: 1.13e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 122 PMVLVQIPMYNEKEVLQLSIGAACRLIWPLDRLIVQVLDDSTDQTIKELVNTECAKWeSKGVNIKCERRDNRNGYKAGAL 201
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYA-AQGVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 202 KEGMKHNYvklCNYVVIFDADFQPEPDYLQhSVPFLVHNPEVALVQARWRFMNANKCLMTRMQEMSLNYHFMAEQESGST 281
Cdd:cd06437  80 AEGMKVAK---GEYVAIFDADFVPPPDFLQ-KTPPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221657 282 RHAFFSFNGTAGVWRMAAMEEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRWSCGP 358
Cdd:cd06437 156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
119-481 9.97e-36

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: 135.64  E-value: 9.97e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 119 ETYPMVLVQIPMYNEKEVLQLSIGAACRLIWPLDRLIVQVLDD-STDQTIKElvnteCAKWESKGVNIKCERRDNRNGyK 197
Cdd:COG1215  26 ADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDgSTDETAEI-----ARELAAEYPRVRVIERPENGG-K 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 198 AGALKEGMKHnyVKlCNYVVIFDADFQPEPDYLQHSVPFLvHNPEVAlvqarwrfmnankclmtrmqemslnyhfmaeqe 277
Cdd:COG1215 100 AAALNAGLKA--AR-GDIVVFLDADTVLDPDWLRRLVAAF-ADPGVG--------------------------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 278 sgstrhaffsFNGTAGVWRMAAMEEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRWSCG 357
Cdd:COG1215 143 ----------ASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARG 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 358 panlfrkmIMEIIRNKRVTIWKKLYLVYSFFFLRKIIVHCFTFIFYCVILptsvffpevnipawstFYIPSMITLCIVIA 437
Cdd:COG1215 213 --------GLQLLLKHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLL----------------LLLPALLLALLLAL 268
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15221657 438 TPRSFYLVIFWILFENVMSMHRTKGtfigilerqRVNEWVVTEK 481
Cdd:COG1215 269 RRRRLLLPLLHLLYGLLLLLAALRG---------KKVVWKKTPR 303
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
215-413 3.18e-18

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: 82.77  E-value: 3.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657   215 YVVIFDADFQPEPDYLQHSVPFLVHnPEVALVQARWRFMNANKcLMTRMQEMSLNYHFMAEQESGSTRHAFFSFNGTAGV 294
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMAS-PEVAIIQGPILPMNVGN-YLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657   295 WRMAAMEEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRWSCGpanlfrkmIMEIIRNKR 374
Cdd:pfam13632  79 LRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYG--------CLLILLIRL 150
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 15221657   375 VTIWKKLYLVYSFFFLRKIIVHCFTFIFYCVILPTSVFF 413
Cdd:pfam13632 151 LGYLGTLLWSGLPLALLLLLLFSISSLALVLLLLALLAG 189
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
89-363 5.97e-09

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 58.88  E-value: 5.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657   89 LVVLYVKV---FERKPEkvyrweAMQEDIElgheTYPMVLVQIPMYNEK-EVLQLSIGAACRLIWPLDRLIVQVLDDSTD 164
Cdd:PRK11498 234 LVLGYFQVvwpLNRQPV------PLPKDMS----LWPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDGGR 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657  165 QTIKELvntecakweSKGVNIKCERRDNRNGYKAGALKEGMKHNYVKlcnYVVIFDADFQPEPDYLQHSVPFLVHNPEVA 244
Cdd:PRK11498 304 EEFRQF---------AQEVGVKYIARPTHEHAKAGNINNALKYAKGE---FVAIFDCDHVPTRSFLQMTMGWFLKDKKLA 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657  245 LVQARWRFM-------NANKCLMTRmQEMSLNYHFMaeQESGSTRHAFFsFNGTAGVWRMAAMEEAGGWHDRTTVEDMDL 317
Cdd:PRK11498 372 MMQTPHHFFspdpferNLGRFRKTP-NEGTLFYGLV--QDGNDMWDATF-FCGSCAVIRRKPLDEIGGIAVETVTEDAHT 447
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15221657  318 AVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRWSCGPANLFR 363
Cdd:PRK11498 448 SLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFR 493
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
122-358 1.13e-136

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: 395.53  E-value: 1.13e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 122 PMVLVQIPMYNEKEVLQLSIGAACRLIWPLDRLIVQVLDDSTDQTIKELVNTECAKWeSKGVNIKCERRDNRNGYKAGAL 201
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYA-AQGVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 202 KEGMKHNYvklCNYVVIFDADFQPEPDYLQhSVPFLVHNPEVALVQARWRFMNANKCLMTRMQEMSLNYHFMAEQESGST 281
Cdd:cd06437  80 AEGMKVAK---GEYVAIFDADFVPPPDFLQ-KTPPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221657 282 RHAFFSFNGTAGVWRMAAMEEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRWSCGP 358
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 ...
122-362 1.73e-38

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: 141.17  E-value: 1.73e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 122 PMVLVQIPMYNEK-EVLQLSIGAACRLIWPLDRLIVQVLDDSTDQTIKELVNTECAKWESKGVnikceRRDNRNGYKAGA 200
Cdd:cd06421   1 PTVDVFIPTYNEPlEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEYGYRYL-----TRPDNRHAKAGN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 201 LKEGMKH-NYvklcNYVVIFDADFQPEPDYLQHSVPFLVHNPEVALVQARWRFMNANKCLMTRMQEMSLNYHFMAEQESG 279
Cdd:cd06421  76 LNNALAHtTG----DFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWLADGAPNEQELFYGVIQPG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 280 --STRHAFFSfnGTAGVWRMAAMEEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRWSCG 357
Cdd:cd06421 152 rdRWGAAFCC--GSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARG 229

                ....*
gi 15221657 358 PANLF 362
Cdd:cd06421 230 MLQIL 234
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
126-314 4.33e-37

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: 135.43  E-value: 4.33e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 126 VQIPMYNEKEVLQLSIGAACRLIWPLDRLIVqVLDDSTDQTIKELvntecAKWESKGVNIKCERRDNRNGYKAGALKEGM 205
Cdd:cd06423   1 IIVPAYNEEAVIERTIESLLALDYPKLEVIV-VDDGSTDDTLEIL-----EELAALYIRRVLVVRDKENGGKAGALNAGL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 206 KH-NYvklcNYVVIFDADFQPEPDYLQHSVPFLVHNPEVALVQARWRFMNANKCLMTRMQEMSLNYHFMAEQESGSTRHA 284
Cdd:cd06423  75 RHaKG----DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGG 150
                       170       180       190
                ....*....|....*....|....*....|
gi 15221657 285 FFSFNGTAGVWRMAAMEEAGGWHDRTTVED 314
Cdd:cd06423 151 VLVLSGAFGAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
119-481 9.97e-36

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: 135.64  E-value: 9.97e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 119 ETYPMVLVQIPMYNEKEVLQLSIGAACRLIWPLDRLIVQVLDD-STDQTIKElvnteCAKWESKGVNIKCERRDNRNGyK 197
Cdd:COG1215  26 ADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDgSTDETAEI-----ARELAAEYPRVRVIERPENGG-K 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 198 AGALKEGMKHnyVKlCNYVVIFDADFQPEPDYLQHSVPFLvHNPEVAlvqarwrfmnankclmtrmqemslnyhfmaeqe 277
Cdd:COG1215 100 AAALNAGLKA--AR-GDIVVFLDADTVLDPDWLRRLVAAF-ADPGVG--------------------------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 278 sgstrhaffsFNGTAGVWRMAAMEEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRWSCG 357
Cdd:COG1215 143 ----------ASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARG 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 358 panlfrkmIMEIIRNKRVTIWKKLYLVYSFFFLRKIIVHCFTFIFYCVILptsvffpevnipawstFYIPSMITLCIVIA 437
Cdd:COG1215 213 --------GLQLLLKHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLL----------------LLLPALLLALLLAL 268
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15221657 438 TPRSFYLVIFWILFENVMSMHRTKGtfigilerqRVNEWVVTEK 481
Cdd:COG1215 269 RRRRLLLPLLHLLYGLLLLLAALRG---------KKVVWKKTPR 303
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
126-364 1.17e-30

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: 119.43  E-value: 1.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 126 VQIPMYNEK-EVLQLSIGAACRLIWPLDRLIVqVLDDSTDQTIKELVNTECAKWeskGVNIKCERRDNRNGYKAGALKEG 204
Cdd:cd06435   2 IHVPCYEEPpEMVKETLDSLAALDYPNFEVIV-IDNNTKDEALWKPVEAHCAQL---GERFRFFHVEPLPGAKAGALNYA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 205 MKHNYVKlCNYVVIFDADFQPEPDYLQHSVPfLVHNPEVALVQARWRFMNANKCLMTRMQEMSLNYHFMAEQESGSTRHA 284
Cdd:cd06435  78 LERTAPD-AEIIAVIDADYQVEPDWLKRLVP-IFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRNERNA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 285 FFsFNGTAGVWRMAAMEEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRWSCGPANLFRK 364
Cdd:cd06435 156 II-QHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILKK 234
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
215-413 3.18e-18

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: 82.77  E-value: 3.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657   215 YVVIFDADFQPEPDYLQHSVPFLVHnPEVALVQARWRFMNANKcLMTRMQEMSLNYHFMAEQESGSTRHAFFSFNGTAGV 294
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMAS-PEVAIIQGPILPMNVGN-YLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657   295 WRMAAMEEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRWSCGpanlfrkmIMEIIRNKR 374
Cdd:pfam13632  79 LRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYG--------CLLILLIRL 150
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 15221657   375 VTIWKKLYLVYSFFFLRKIIVHCFTFIFYCVILPTSVFF 413
Cdd:pfam13632 151 LGYLGTLLWSGLPLALLLLLLFSISSLALVLLLLALLAG 189
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
122-354 5.31e-18

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: 83.46  E-value: 5.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 122 PMVLVQIPMYNEKEVLQLSIGAACRLIWPLDRLIVQVLDDSTDQ-TIKELVNTECAKWEskgVNIKCERRDNRNGYKAga 200
Cdd:cd06427   1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEeTIAAARALRLPSIF---RVVVVPPSQPRTKPKA-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 201 lkegmkhnyvklCNY---------VVIFDADFQPEPDYLQHSV-PFLVHNPEVALVQARWRFMNANKCLMTRMQEMSLNY 270
Cdd:cd06427  76 ------------CNYalafargeyVVIYDAEDAPDPDQLKKAVaAFARLDDKLACVQAPLNYYNARENWLTRMFALEYAA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 271 HFMAEQESGSTRHAFFSFNGTAGVWRMAAMEEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVKsELPSKFKAFRFQ 350
Cdd:cd06427 144 WFDYLLPGLARLGLPIPLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLE-EANNALGNWIRQ 222

                ....
gi 15221657 351 QHRW 354
Cdd:cd06427 223 RSRW 226
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
122-357 9.89e-17

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: 79.34  E-value: 9.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657   122 PMVLVQIPMYNEKEVLQLSIGAACRLIWPLDRLIVQVL--DDSTDQTIKELVNTEcakwesKGVNIKCERRDNRNGY--K 197
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNpsDAETLDVAEEIAARF------PDVRLRVIRNARLLGPtgK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657   198 AGALKEGMKHnyVKLcNYVVIFDADFQPEPDYLQHSVPFLVHnPEVALVQARwRFMNANKCLMTRMQEMSLNYHFMaeqE 277
Cdd:pfam13641  76 SRGLNHGFRA--VKS-DLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTP-VFSLNRSTMLSALGALEFALRHL---R 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657   278 SGSTRHA--FFSFNGTAGVWRMAAMEEAGGWHDRTTV-EDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRW 354
Cdd:pfam13641 148 MMSLRLAlgVLPLSGAGSAIRREVLKELGLFDPFFLLgDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARW 227

                  ...
gi 15221657   355 SCG 357
Cdd:pfam13641 228 VYG 230
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
128-301 7.42e-15

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: 72.43  E-value: 7.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657   128 IPMYNEKEVLQLSIGAACRLIWPLDRLIVqVLDDSTDQTIKELvntecAKWESKGVNIKCERRDNRNGyKAGALKEGMKH 207
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLNQTYPNFEIIV-VDDGSTDGTVEIA-----EEYAKKDPRVRVIRLPENRG-KAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657   208 nyVKlCNYVVIFDADFQPEPDYLQHSVPFLVHNPEVALVQARWRFMNANKcLMTRMQEMSLNYHFMAEQESGSTRHAFFS 287
Cdd:pfam00535  77 --AT-GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETG-EYRRASRITLSRLPFFLGLRLLGLNLPFL 152
                         170
                  ....*....|....
gi 15221657   288 FNGTAGVWRMAAME 301
Cdd:pfam00535 153 IGGFALYRREALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
128-253 2.43e-13

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: 67.92  E-value: 2.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 128 IPMYNEKEVLQLSIGAACRLIWPLDRLIVqVLDDSTDQTIKELvntecAKWESKGVNIKCeRRDNRNGYKAGALKEGMKH 207
Cdd:cd00761   3 IPAYNEEPYLERCLESLLAQTYPNFEVIV-VDDGSTDGTLEIL-----EEYAKKDPRVIR-VINEENQGLAAARNAGLKA 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15221657 208 NYVKlcnYVVIFDADFQPEPDYLQHSVPFLVHNPEVALVQARWRFM 253
Cdd:cd00761  76 ARGE---YILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLL 118
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
122-332 4.92e-11

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 62.41  E-value: 4.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 122 PMVLVQIPMYNEKEVLQLSIGAACRLIWPLDRLIVqVLDDSTDQTIKELvntecAKWESKGVNIKCERRDnRNGYKAGAL 201
Cdd:COG0463   2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIV-VDDGSTDGTAEIL-----RELAAKDPRIRVIRLE-RNRGKGAAR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 202 KEGMKHnyvklCN--YVVIFDADFQPEPDYLQHSVPFLVHNPeVALVQArWRFMNANKCLMTRMQEMSLNYHfmaeqesg 279
Cdd:COG0463  75 NAGLAA-----ARgdYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYG-SRLIREGESDLRRLGSRLFNLV-------- 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15221657 280 STRHAFFSFNGTAGVWRMAAMEEAGgwHDRTTVEDMDLaVRAGLLGWKFVFLN 332
Cdd:COG0463 140 RLLTNLPDSTSGFRLFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVP 189
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
122-336 3.57e-09

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 56.92  E-value: 3.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 122 PMVLVQIPMYNEKEVLQLSIGAACRLIWPLDRLIVqVLDDSTDQTIKELvntecAKWESKGVNIkcERRDNRNGYkAGAL 201
Cdd:COG1216   3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIV-VDNGSTDGTAELL-----AALAFPRVRV--IRNPENLGF-AAAR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 202 KEGMKHnyVKlCNYVVIFDADFQPEPDYLQhsvpflvhnpevALVQARwrfmnankCLMTRmqemslnyhfmaeqesgst 281
Cdd:COG1216  74 NLGLRA--AG-GDYLLFLDDDTVVEPDWLE------------RLLAAA--------CLLIR------------------- 111
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15221657 282 RHAFfsfngtagvwrmaamEEAGGWHDRTTV--EDMDLAVRAGLLGWKFVFLNDLTV 336
Cdd:COG1216 112 REVF---------------EEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVV 153
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
89-363 5.97e-09

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 58.88  E-value: 5.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657   89 LVVLYVKV---FERKPEkvyrweAMQEDIElgheTYPMVLVQIPMYNEK-EVLQLSIGAACRLIWPLDRLIVQVLDDSTD 164
Cdd:PRK11498 234 LVLGYFQVvwpLNRQPV------PLPKDMS----LWPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDGGR 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657  165 QTIKELvntecakweSKGVNIKCERRDNRNGYKAGALKEGMKHNYVKlcnYVVIFDADFQPEPDYLQHSVPFLVHNPEVA 244
Cdd:PRK11498 304 EEFRQF---------AQEVGVKYIARPTHEHAKAGNINNALKYAKGE---FVAIFDCDHVPTRSFLQMTMGWFLKDKKLA 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657  245 LVQARWRFM-------NANKCLMTRmQEMSLNYHFMaeQESGSTRHAFFsFNGTAGVWRMAAMEEAGGWHDRTTVEDMDL 317
Cdd:PRK11498 372 MMQTPHHFFspdpferNLGRFRKTP-NEGTLFYGLV--QDGNDMWDATF-FCGSCAVIRRKPLDEIGGIAVETVTEDAHT 447
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15221657  318 AVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRWSCGPANLFR 363
Cdd:PRK11498 448 SLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFR 493
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
126-314 1.24e-08

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: 55.08  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 126 VQIPMYNEKEVLQLSIGAACRLiwpLDRLIVQVLDDSTDQTIKELVntECAKWESKgVNIKCERRDN-RNG------YKA 198
Cdd:cd06436   1 VLVPCLNEEAVIQRTLASLLRN---KPNFLVLVIDDASDDDTAGIV--RLAITDSR-VHLLRRHLPNaRTGkgdalnAAY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 199 GALKEGMKHNYVKLCNYVV-IFDADFQPEPDYLQHSVPFLvHNPEVALVQARWRFMNANKCLMTRMQEM---SLNYHFma 274
Cdd:cd06436  75 DQIRQILIEEGADPERVIIaVIDADGRLDPNALEAVAPYF-SDPRVAGTQSRVRMYNRHKNLLTILQDLeffIIIAAT-- 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15221657 275 eqESGSTRHAFFSFNGTAGVWRMAAMEEAGG---WHDRTTvED 314
Cdd:cd06436 152 --QSLRALTGTVGLGGNGQFMRLSALDGLIGeepWSDSLL-ED 191
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
121-354 4.02e-08

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: 54.51  E-value: 4.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 121 YPMVLVQIPMYNEKEVlqlsIGAACR----LIWPLDRL-IVQVLDDSTDQTikelvNTECAKWESKGVniKCERRDNRNG 195
Cdd:cd06439  28 LPTVTIIIPAYNEEAV----IEAKLEnllaLDYPRDRLeIIVVSDGSTDGT-----AEIAREYADKGV--KLLRFPERRG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 196 yKAGALKEGMKHnyVKLcNYVVIFDADFQPEPDYLQHsvpfLVHN---PEVALVQARWRFMNANKclMTRMQEMSLNY-H 271
Cdd:cd06439  97 -KAAALNRALAL--ATG-EIVVFTDANALLDPDALRL----LVRHfadPSVGAVSGELVIVDGGG--SGSGEGLYWKYeN 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 272 FMAEQES--GSTrhafFSFNGTagvwrMAAM--EEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAf 347
Cdd:cd06439 167 WLKRAESrlGST----VGANGA-----IYAIrrELFRPLPADTINDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDGSE- 236

                ....*..
gi 15221657 348 rfqQHRW 354
Cdd:cd06439 237 ---EFRR 240
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
128-230 2.97e-07

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


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 51.38  E-value: 2.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 128 IPMYNEKEVLQLSIGAACRLIWPLDRLIVQVLDDSTDQTIKElvnteCAKWESKGVNIKCERRDNRNGYkAGALKEGMKH 207
Cdd:cd06442   3 IPTYNERENIPELIERLDAALKGIDYEIIVVDDNSPDGTAEI-----VRELAKEYPRVRLIVRPGKRGL-GSAYIEGFKA 76
                        90       100
                ....*....|....*....|...
gi 15221657 208 nyvKLCNYVVIFDADFQPEPDYL 230
Cdd:cd06442  77 ---ARGDVIVVMDADLSHPPEYI 96
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
126-230 8.90e-07

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: 49.49  E-value: 8.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 126 VQIPMYNEKEVLQLSIGAACRLI--WPLDRLIVqVLDDSTDQTIKELvntecAKWESKGVNIKCERRDNRNGyKAGALKE 203
Cdd:cd04179   1 VVIPAYNEEENIPELVERLLAVLeeGYDYEIIV-VDDGSTDGTAEIA-----RELAARVPRVRVIRLSRNFG-KGAAVRA 73
                        90       100
                ....*....|....*....|....*....
gi 15221657 204 GMKHnyvklC--NYVVIFDADFQPEPDYL 230
Cdd:cd04179  74 GFKA-----ArgDIVVTMDADLQHPPEDI 97
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
128-230 1.71e-05

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: 45.67  E-value: 1.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 128 IPMYNEKEVLQLSIGAACRLIWP--LDRLIVqVLDDSTDQTiKELVntecakwESKGVNIkCERRDNRNGYKAGALKEGM 205
Cdd:cd06438   3 IPAHNEEAVIGNTVRSLKAQDYPreLYRIFV-VADNCTDDT-AQVA-------RAAGATV-LERHDPERRGKGYALDFGF 72
                        90       100
                ....*....|....*....|....*..
gi 15221657 206 KHNYVKLCNY--VVIFDADFQPEPDYL 230
Cdd:cd06438  73 RHLLNLADDPdaVVVFDADNLVDPNAL 99
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
124-364 5.62e-05

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: 44.92  E-value: 5.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 124 VLVQIPMYNEKEVLQLSIGAACRLIWPLDRLIVQVLDD-STDQTIkELVNtecaKWESKGVNIKCErrDNRNGYKAGALK 202
Cdd:cd02525   2 VSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGgSTDGTR-EIVQ----EYAAKDPRIRLI--DNPKRIQSAGLN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 203 EGMKH-NYvklcNYVVIFDADFQPEPDYLQHSVPFLVhNPEVALVQARWRFM--NANKCLMTRMQEMSL---NYHFMAEQ 276
Cdd:cd02525  75 IGIRNsRG----DIIIRVDAHAVYPKDYILELVEALK-RTGADNVGGPMETIgeSKFQKAIAVAQSSPLgsgGSAYRGGA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 277 ES-GSTRHAFFsfngtaGVWRMAAMEEAGGWHDR-TTVEDMDLAVRAGLLGWKFVFLNDLTVKSELPSKFKAFRFQQHRW 354
Cdd:cd02525 150 VKiGYVDTVHH------GAYRREVFEKVGGFDESlVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRY 223
                       250
                ....*....|
gi 15221657 355 SCGPANLFRK 364
Cdd:cd02525 224 GKWRARTLRK 233
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
128-222 3.77e-04

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: 41.78  E-value: 3.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 128 IPMYNEKEVLQLSIGAACRL----IWPLDRLIVqVLDDSTDQTIkELVNTECAKwesKGVNIKCERRDNRNGyKAGALKE 203
Cdd:cd04188   3 IPAYNEEKRLPPTLEEAVEYleerPSFSYEIIV-VDDGSKDGTA-EVARKLARK---NPALIRVLTLPKNRG-KGGAVRA 76
                        90
                ....*....|....*....
gi 15221657 204 GMKHNYVKlcnYVVIFDAD 222
Cdd:cd04188  77 GMLAARGD---YILFADAD 92
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
200-337 8.18e-04

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 40.76  E-value: 8.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 200 ALKEGMKHnyvklCNY--VVIFDADFQPEPDYLQHSVPFLVHNPEVALVQARWRFM--NANKCLMTRMQEMSLNYHFMAE 275
Cdd:cd04195  71 ALNEGLKH-----CTYdwVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFdsDGNDIGKRRLPTSHDDILKFAR 145
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221657 276 QESgstrhaffSFNGTAGVWRMAAMEEAGGWHDRTTVEDMDLAVRAGLLGWKFVFLNDLTVK 337
Cdd:cd04195 146 RRS--------PFNHPTVMFRKSKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVK 199
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
131-232 1.18e-03

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 40.31  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 131 YNEKEVLQLSIGAACRLIWPLDRLIVqVLDDSTDQTiKELVNTEcaKWESKGVNIKCERrdnrNGYKAGALKEGMKHNYV 210
Cdd:cd04185   6 YNRLDLLKECLDALLAQTRPPDHIIV-IDNASTDGT-AEWLTSL--GDLDNIVYLRLPE----NLGGAGGFYEGVRRAYE 77
                        90       100
                ....*....|....*....|..
gi 15221657 211 KLCNYVVIFDADFQPEPDYLQH 232
Cdd:cd04185  78 LGYDWIWLMDDDAIPDPDALEK 99
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
128-330 1.27e-03

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: 39.85  E-value: 1.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 128 IPMYNEKEVLQLSIGAACRLIWPLDRLIVqVLDDSTDQTIKELvntecakwESKGVNIKCERRDNRNGYkAGALKEGMKH 207
Cdd:cd04186   3 IVNYNSLEYLKACLDSLLAQTYPDFEVIV-VDNASTDGSVELL--------RELFPEVRLIRNGENLGF-GAGNNQGIRE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221657 208 nyVKlCNYVVIFDADFQPEPDYLQHSVPFLVHNPEVALVQArwRFMNAnkCLMTRmqemslnyhfmaeqesgstRHAFfs 287
Cdd:cd04186  73 --AK-GDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVGP--KVSGA--FLLVR-------------------REVF-- 124
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15221657 288 fngtagvwrmaamEEAGGWHDRTTV--EDMDLAVRAGLLGWKFVF 330
Cdd:cd04186 125 -------------EEVGGFDEDFFLyyEDVDLCLRARLAGYRVLY 156
 
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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