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Conserved domains on  [gi|2019423446|ref|XP_040250322|]
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glucomannan 4-beta-mannosyltransferase 1-like [Aegilops tauschii subsp. strangulata]

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 ...
48-284 6.07e-147

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: 415.17  E-value: 6.07e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  48 PMVLVQIPMYNEREVYQLSIGAACGLSWPSDRIVVQVLDDSTDPVIKELVQVECRRWARkGVNIKYEIRDNRRGYKAGAL 127
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 128 KEGMKHGyvkDCDLVAIFDADFQPEPDFLwRAVPFLVHNPDIALVQACWKFVNADECLMTRMQEMSLDYHFKVEQEVGSS 207
Cdd:cd06437    80 AEGMKVA---KGEYVAIFDADFVPPPDFL-QKTPPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019423446 208 TYAFFGFNGTAGVWRISTLNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRWSCGP 284
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 ...
48-284 6.07e-147

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: 415.17  E-value: 6.07e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  48 PMVLVQIPMYNEREVYQLSIGAACGLSWPSDRIVVQVLDDSTDPVIKELVQVECRRWARkGVNIKYEIRDNRRGYKAGAL 127
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 128 KEGMKHGyvkDCDLVAIFDADFQPEPDFLwRAVPFLVHNPDIALVQACWKFVNADECLMTRMQEMSLDYHFKVEQEVGSS 207
Cdd:cd06437    80 AEGMKVA---KGEYVAIFDADFVPPPDFL-QKTPPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019423446 208 TYAFFGFNGTAGVWRISTLNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRWSCGP 284
Cdd:cd06437   156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
44-361 1.22e-38

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: 140.26  E-value: 1.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  44 SAAYPMVLVQIPMYNEREVYQLSIGAACGLSWPSDRIVVQVLDD-STDPVIKelvqvECRRWARKGVNIKYEIRDNRRGy 122
Cdd:COG1215    25 PADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDgSTDETAE-----IARELAAEYPRVRVIERPENGG- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 123 KAGALKEGMKHgyvKDCDLVAIFDADFQPEPDFLWRAVPFLvHNPDIalvqacwkfvnadeclmtrmqemsldyhfkveq 202
Cdd:COG1215    99 KAAALNAGLKA---ARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGV--------------------------------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 203 evgsstyaffGFNGTAGVWRISTLNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRWSC 282
Cdd:COG1215   142 ----------GASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWAR 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019423446 283 GPANLFRKMVMEIIRNKKVTLWkkIHVVYSFFLVRKVVAHIVTFVFYCLVIPATVLVPEVEVPKWGCVYIPTIITLLNA 361
Cdd:COG1215   212 GGLQLLLKHRPLLRPRRLLLFL--LLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLL 288
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
141-333 2.00e-15

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: 73.91  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 141 LVAIFDADFQPEPDFLWRAVPFLVHnPDIALVQaCWKFVNADECLMTRMQEMSLDYHFKVEQEVGSSTYAFFGFNGTAGV 220
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMAS-PEVAIIQ-GPILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 221 WRISTLNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRWSCGPANLFRKMVMEIIRNkk 300
Cdd:pfam13632  79 LRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRLLGYLGT-- 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2019423446 301 vTLWKKIHVVYSFFLVRKVVAHIVTFVFYCLVI 333
Cdd:pfam13632 157 -LLWSGLPLALLLLLLFSISSLALVLLLLALLA 188
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
4-289 4.13e-14

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 73.90  E-value: 4.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446   4 MLFAEKVYMAVVVLA----VRLLGRRPErqyqwePMGDDdpelgSAAYPMVLVQIPMYNER-EVYQLSIGAACGLSWPSD 78
Cdd:PRK11498  223 LLFAETYAWIVLVLGyfqvVWPLNRQPV------PLPKD-----MSLWPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKD 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  79 RIVVQVLDDSTDPvikelvqvECRRWArKGVNIKYEIRDNRRGYKAGALKEGMKHGyvkDCDLVAIFDADFQPEPDFLWR 158
Cdd:PRK11498  292 KLNIWILDDGGRE--------EFRQFA-QEVGVKYIARPTHEHAKAGNINNALKYA---KGEFVAIFDCDHVPTRSFLQM 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 159 AVPFLVHNPDIALVQACWKFVNADEClmtrmqEMSLDYHFKVEQEvGSSTY-----------AFFgFNGTAGVWRISTLN 227
Cdd:PRK11498  360 TMGWFLKDKKLAMMQTPHHFFSPDPF------ERNLGRFRKTPNE-GTLFYglvqdgndmwdATF-FCGSCAVIRRKPLD 431
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019423446 228 EAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRWSCGPANLFR 289
Cdd:PRK11498  432 EIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFR 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 ...
48-284 6.07e-147

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: 415.17  E-value: 6.07e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  48 PMVLVQIPMYNEREVYQLSIGAACGLSWPSDRIVVQVLDDSTDPVIKELVQVECRRWARkGVNIKYEIRDNRRGYKAGAL 127
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 128 KEGMKHGyvkDCDLVAIFDADFQPEPDFLwRAVPFLVHNPDIALVQACWKFVNADECLMTRMQEMSLDYHFKVEQEVGSS 207
Cdd:cd06437    80 AEGMKVA---KGEYVAIFDADFVPPPDFL-QKTPPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019423446 208 TYAFFGFNGTAGVWRISTLNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRWSCGP 284
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 ...
48-288 1.97e-41

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: 145.41  E-value: 1.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  48 PMVLVQIPMYNE-REVYQLSIGAACGLSWPSDRIVVQVLDDSTDPVIKELVQVECRRWarkgvNIKYEIRDNRRGYKAGA 126
Cdd:cd06421     1 PTVDVFIPTYNEpLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEY-----GYRYLTRPDNRHAKAGN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 127 LKEGMKHgyvKDCDLVAIFDADFQPEPDFLWRAVPFLVHNPDIALVQACWKFVNADEC-LMTRMQEMSLDYHFKVEQEVG 205
Cdd:cd06421    76 LNNALAH---TTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFdWLADGAPNEQELFYGVIQPGR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 206 SSTYAFFgFNGTAGVWRISTLNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRWSCGPA 285
Cdd:cd06421   153 DRWGAAF-CCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGML 231

                  ...
gi 2019423446 286 NLF 288
Cdd:cd06421   232 QIL 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
44-361 1.22e-38

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: 140.26  E-value: 1.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  44 SAAYPMVLVQIPMYNEREVYQLSIGAACGLSWPSDRIVVQVLDD-STDPVIKelvqvECRRWARKGVNIKYEIRDNRRGy 122
Cdd:COG1215    25 PADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDgSTDETAE-----IARELAAEYPRVRVIERPENGG- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 123 KAGALKEGMKHgyvKDCDLVAIFDADFQPEPDFLWRAVPFLvHNPDIalvqacwkfvnadeclmtrmqemsldyhfkveq 202
Cdd:COG1215    99 KAAALNAGLKA---ARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGV--------------------------------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 203 evgsstyaffGFNGTAGVWRISTLNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRWSC 282
Cdd:COG1215   142 ----------GASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWAR 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019423446 283 GPANLFRKMVMEIIRNKKVTLWkkIHVVYSFFLVRKVVAHIVTFVFYCLVIPATVLVPEVEVPKWGCVYIPTIITLLNA 361
Cdd:COG1215   212 GGLQLLLKHRPLLRPRRLLLFL--LLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLL 288
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
52-290 2.06e-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: 124.44  E-value: 2.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  52 VQIPMYNER-EVYQLSIGAACGLSWPSDRIVVqVLDDSTDPVIKELVQVECRRWarkGVNIKYEIRDNRRGYKAGALKEG 130
Cdd:cd06435     2 IHVPCYEEPpEMVKETLDSLAALDYPNFEVIV-IDNNTKDEALWKPVEAHCAQL---GERFRFFHVEPLPGAKAGALNYA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 131 MKHGYVkDCDLVAIFDADFQPEPDFLWRAVPfLVHNPDIALVQACWKFVNADECLMTRMQEMSLDYHFKVEQEVGSSTYA 210
Cdd:cd06435    78 LERTAP-DAEIIAVIDADYQVEPDWLKRLVP-IFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRNERNA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 211 FFgFNGTAGVWRISTLNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRWSCGPANLFRK 290
Cdd:cd06435   156 II-QHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILKK 234
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
52-240 5.43e-33

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: 121.57  E-value: 5.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  52 VQIPMYNEREVYQLSIGAACGLSWPSDRIVVqVLDDSTDPVIKELvqvecRRWARKGVNIKYEIRDNRRGYKAGALKEGM 131
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIV-VDDGSTDDTLEIL-----EELAALYIRRVLVVRDKENGGKAGALNAGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 132 KH--GyvkdcDLVAIFDADFQPEPDFLWRAVPFLVHNPDIALVQACWKFVNADECLMTRMQEMSLDYHFKVEQEVGSSTY 209
Cdd:cd06423    75 RHakG-----DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALG 149
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2019423446 210 AFFGFNGTAGVWRISTLNEAGGWKDRTTVED 240
Cdd:cd06423   150 GVLVLSGAFGAFRREALREVGGWDEDTLTED 180
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
141-333 2.00e-15

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: 73.91  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 141 LVAIFDADFQPEPDFLWRAVPFLVHnPDIALVQaCWKFVNADECLMTRMQEMSLDYHFKVEQEVGSSTYAFFGFNGTAGV 220
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMAS-PEVAIIQ-GPILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 221 WRISTLNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRWSCGPANLFRKMVMEIIRNkk 300
Cdd:pfam13632  79 LRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRLLGYLGT-- 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2019423446 301 vTLWKKIHVVYSFFLVRKVVAHIVTFVFYCLVI 333
Cdd:pfam13632 157 -LLWSGLPLALLLLLLFSISSLALVLLLLALLA 188
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
48-283 2.33e-15

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: 74.71  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  48 PMVLVQIPMYNEREVYQLSIGAACGLSWPSDRIVVQVL--DDSTDPVIKELVQVECRRWARKGVNIkyeiRDNRRGYKAG 125
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNpsDAETLDVAEEIAARFPDVRLRVIRNA----RLLGPTGKSR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 126 ALKEGMKHgyVKDcDLVAIFDADFQPEPDFLWRAVPFLVHnPDIALVQACwKFVNADECLMTRMQEMSLDYHFK----VE 201
Cdd:pfam13641  78 GLNHGFRA--VKS-DLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTP-VFSLNRSTMLSALGALEFALRHLrmmsLR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 202 QEVGSSTYaffgfNGTAGVWRISTLNEAGGW-KDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRW 280
Cdd:pfam13641 153 LALGVLPL-----SGAGSAIRREVLKELGLFdPFFLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARW 227

                  ...
gi 2019423446 281 SCG 283
Cdd:pfam13641 228 VYG 230
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
48-280 4.75e-15

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: 73.83  E-value: 4.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  48 PMVLVQIPMYNEREVYQLSIGAACGLSWPSDRIVVQVLDDSTDPVIKELVQVECRRWARKGVNIKY-EIRDnrrgyKAGA 126
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRVVVVPPsQPRT-----KPKA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 127 LKEGMK--HGyvkdcDLVAIFDADFQPEPDFLWRAV-PFLVHNPDIALVQACWKFVNADECLMTRMQEMSLDYHFKVEQE 203
Cdd:cd06427    76 CNYALAfaRG-----EYVVIYDAEDAPDPDQLKKAVaAFARLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLP 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019423446 204 VGSSTYAFFGFNGTAGVWRISTLNEAGGWKDRTTVEDMDLAVRASLKGWKfVYLGDLKVKNELPSTFKAFRYQQHRW 280
Cdd:cd06427   151 GLARLGLPIPLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYR-TGVLNSTTLEEANNALGNWIRQRSRW 226
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
4-289 4.13e-14

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 73.90  E-value: 4.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446   4 MLFAEKVYMAVVVLA----VRLLGRRPErqyqwePMGDDdpelgSAAYPMVLVQIPMYNER-EVYQLSIGAACGLSWPSD 78
Cdd:PRK11498  223 LLFAETYAWIVLVLGyfqvVWPLNRQPV------PLPKD-----MSLWPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKD 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  79 RIVVQVLDDSTDPvikelvqvECRRWArKGVNIKYEIRDNRRGYKAGALKEGMKHGyvkDCDLVAIFDADFQPEPDFLWR 158
Cdd:PRK11498  292 KLNIWILDDGGRE--------EFRQFA-QEVGVKYIARPTHEHAKAGNINNALKYA---KGEFVAIFDCDHVPTRSFLQM 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 159 AVPFLVHNPDIALVQACWKFVNADEClmtrmqEMSLDYHFKVEQEvGSSTY-----------AFFgFNGTAGVWRISTLN 227
Cdd:PRK11498  360 TMGWFLKDKKLAMMQTPHHFFSPDPF------ERNLGRFRKTPNE-GTLFYglvqdgndmwdATF-FCGSCAVIRRKPLD 431
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019423446 228 EAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAFRYQQHRWSCGPANLFR 289
Cdd:PRK11498  432 EIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFR 493
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
54-215 5.77e-13

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: 66.26  E-value: 5.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  54 IPMYNEREVYQLSIGAACGLSWPSDRIVVqVLDDSTDpvikELVQVeCRRWARKGVNIKYEIRDNRRGyKAGALKEGMKH 133
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLNQTYPNFEIIV-VDDGSTD----GTVEI-AEEYAKKDPRVRVIRLPENRG-KAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 134 GyvkDCDLVAIFDADFQPEPDFLWRAVPFLVHNP-DIALVQACWKFVNADECLMTRMQEMSLDYHFKVEQEVGSSTYAFF 212
Cdd:pfam00535  77 A---TGDYIAFLDADDEVPPDWLEKLVEALEEDGaDVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153

                  ...
gi 2019423446 213 GFN 215
Cdd:pfam00535 154 GGF 156
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
48-257 1.28e-12

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 66.26  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  48 PMVLVQIPMYNEREVYQLSIGAACGLSWPSDRIVVqVLDDSTDPVIKELvqvecRRWARKGVNIKYeIRDNRRGYKAGAL 127
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIV-VDDGSTDGTAEIL-----RELAAKDPRIRV-IRLERNRGKGAAR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 128 KEGMKHGyvkDCDLVAIFDADFQPEPDFLWRAVPFLVHNPDIALVqaCWKFVNADEcLMTRMQEMSLDYHFKVEQEVGSS 207
Cdd:COG0463    75 NAGLAAA---RGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY--GSRLIREGE-SDLRRLGSRLFNLVRLLTNLPDS 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2019423446 208 TYAFFGFngtagvwRISTLNEAGgwKDRTTVEDMDLaVRASLKGWKFVYL 257
Cdd:COG0463   149 TSGFRLF-------RREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEV 188
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
48-279 3.12e-10

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 59.24  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  48 PMVLVQIPMYNEREVYQLSIGAACGLSWPSDRIVVqVLDDSTDPVIKELVQVECRRwarkgvnIKYEIRDNRRGYkAGAL 127
Cdd:COG1216     3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIV-VDNGSTDGTAELLAALAFPR-------VRVIRNPENLGF-AAAR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 128 KEGMKHGyvkDCDLVAIFDADFQPEPDFLWRavpflvhnpdiaLVQACwkfvnadeCLMTRMqemsldyhfkveqevgss 207
Cdd:COG1216    74 NLGLRAA---GGDYLLFLDDDTVVEPDWLER------------LLAAA--------CLLIRR------------------ 112
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2019423446 208 tyaffgfngtagvwriSTLNEAGGWKDRTTV--EDMDLAVRASLKGWKFVYLGDLKVKNELPSTFKAF--RYQQHR 279
Cdd:COG1216   113 ----------------EVFEEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLlrAYYLGR 172
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
54-172 8.11e-09

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: 54.05  E-value: 8.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  54 IPMYNEREVYQLSIGAACGLSWPSDRIVVqVLDDSTDPVIKELvqvecRRWARKGVNIKYEIRDNRRGyKAGALKEGMKH 133
Cdd:cd00761     3 IPAYNEEPYLERCLESLLAQTYPNFEVIV-VDDGSTDGTLEIL-----EEYAKKDPRVIRVINEENQG-LAAARNAGLKA 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2019423446 134 GyvkDCDLVAIFDADFQPEPDFLWRAVPFLVHNPDIALV 172
Cdd:cd00761    76 A---RGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
17-271 4.31e-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: 53.74  E-value: 4.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  17 LAVRLLGRRPERQyqwEPMGDDDPelgsaaYPMVLVQIPMYNEREVyqlsIGA----ACGLSWPSDRI-VVQVLDDSTDp 91
Cdd:cd06439     7 LLLKLLARLRPKP---PSLPDPAY------LPTVTIIIPAYNEEAV----IEAklenLLALDYPRDRLeIIVVSDGSTD- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  92 VIKELVqvecRRWARKGVniKYEIRDNRRGyKAGALKEGMKHgyVKDcDLVAIFDADFQPEPDFLWRAV-PFLvhNPDIA 170
Cdd:cd06439    73 GTAEIA----REYADKGV--KLLRFPERRG-KAAALNRALAL--ATG-EIVVFTDANALLDPDALRLLVrHFA--DPSVG 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 171 LVQACWKFVNADEclMTRMQEMSLDYHFKV-EQEvgSSTYAFFGFNGTAGVWR---ISTLNEaggwkdRTTVEDMDLAVR 246
Cdd:cd06439   141 AVSGELVIVDGGG--SGSGEGLYWKYENWLkRAE--SRLGSTVGANGAIYAIRrelFRPLPA------DTINDDFVLPLR 210
                         250       260
                  ....*....|....*....|....*
gi 2019423446 247 ASLKGWKFVYLGDLKVKNELPSTFK 271
Cdd:cd06439   211 IARQGYRVVYEPDAVAYEEVAEDGS 235
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
52-156 1.09e-06

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: 48.34  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  52 VQIPMYNEREvyqlSIGA------ACGLSWPSDRIVVqVLDDSTDPVIKELvqvecRRWARKGVNIKYEIRDNRRGyKAG 125
Cdd:cd04179     1 VVIPAYNEEE----NIPElverllAVLEEGYDYEIIV-VDDGSTDGTAEIA-----RELAARVPRVRVIRLSRNFG-KGA 69
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2019423446 126 ALKEGMKH--GyvkdcDLVAIFDADFQ--PE--PDFL 156
Cdd:cd04179    70 AVRAGFKAarG-----DIVVTMDADLQhpPEdiPKLL 101
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
52-192 1.19e-04

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: 42.76  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  52 VQIPMYNEREVYQLSIGAACGLSwpsDRIVVQVLDDSTDPviKELVQVECRRWARKgVNIKYEIRDNRRGYKAGALKEGM 131
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRNK---PNFLVLVIDDASDD--DTAGIVRLAITDSR-VHLLRRHLPNARTGKGDALNAAY 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019423446 132 KH--------GYVKDCDLVAIFDADFQPEPDFLWRAVPFLvHNPDIALVQACWKFVNADECLMTRMQEM 192
Cdd:cd06436    75 DQirqilieeGADPERVIIAVIDADGRLDPNALEAVAPYF-SDPRVAGTQSRVRMYNRHKNLLTILQDL 142
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
54-156 2.33e-04

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: 42.14  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  54 IPMYNERE-----VYQLSiGAACGLSWpsdRIVVqVLDDSTDPVIKElvqveCRRWARKGVNIKYEIRDNRRGYkAGALK 128
Cdd:cd06442     3 IPTYNEREnipelIERLD-AALKGIDY---EIIV-VDDNSPDGTAEI-----VRELAKEYPRVRLIVRPGKRGL-GSAYI 71
                          90       100
                  ....*....|....*....|....*...
gi 2019423446 129 EGMKHGYvkdCDLVAIFDADFQPEPDFL 156
Cdd:cd06442    72 EGFKAAR---GDVIVVMDADLSHPPEYI 96
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
54-243 1.83e-03

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: 39.12  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446  54 IPMYNEREVYQLSIGAACGLSWPSD--RIVVqVLDDSTDpvikELVQVecrrwAR-KGVNIkYEIRDN-RRGyKAGALKE 129
Cdd:cd06438     3 IPAHNEEAVIGNTVRSLKAQDYPRElyRIFV-VADNCTD----DTAQV-----ARaAGATV-LERHDPeRRG-KGYALDF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019423446 130 GMKH--GYVKDCDLVAIFDADFQPEPDFLwravpfLVHNPDIAL----VQACWKFVNADECLMTRMQEMsldyHFKVEQE 203
Cdd:cd06438    71 GFRHllNLADDPDAVVVFDADNLVDPNAL------EELNARFAAgarvVQAYYNSKNPDDSWITRLYAF----AFLVFNR 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2019423446 204 V--------GSSTyaffGFNGTAGVWRISTLnEAGGWKDRTTVEDMDL 243
Cdd:cd06438   141 LrplgrsnlGLSC----QLGGTGMCFPWAVL-RQAPWAAHSLTEDLEF 183
 
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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