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Conserved domains on  [gi|2535869671|ref|WP_292643002|]
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glycosyltransferase [Nitrososphaera sp.]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
68-298 1.60e-59

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd06427:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 241  Bit Score: 194.78  E-value: 1.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  68 PKISVIIPARNEPILGRTIEACLNHVEYPAGKKEIVVV--ADDEggERIALWYQQKYPETVKLLARRQFFP-TKPSALND 144
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLleEDDE--ETIAAARALRLPSIFRVVVVPPSQPrTKPKACNY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 145 AMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGG--YQAVQVILHIGNTDDSWISKVFGMEYSGWFRVMLNGRFNMGLF 222
Cdd:cd06427    79 ALAFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDdkLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLPGLARLGLP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2535869671 223 APLGGTGNYFKRSALKYVGGYEPTNLAEDAELAIRLRIARWNVAVVDARHWEEAPVTFNAWLKQRTRWFRGWMQSF 298
Cdd:cd06427   159 IPLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLEEANNALGNWIRQRSRWIKGYMQTW 234
nfrB super family cl36493
glycosyl transferase family protein;
196-430 1.27e-07

glycosyl transferase family protein;


The actual alignment was detected with superfamily member PRK15489:

Pssm-ID: 237974 [Multi-domain]  Cd Length: 703  Bit Score: 53.98  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 196 WISKVFGMEYSGWFRVMLNGRFNMGLFAPLGGTGNYFKRSALKYV---GGYEPTN---LAEDAELAIRLR-------IAR 262
Cdd:PRK15489  208 WVAGTYMDEFAEWHQKDLVVRESLTGTVPSAGVGTCFSRRALLALmkeRGNQPFNtssLTEDYDFSFRLAelgmqeiFVR 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 263 WNVA-VVDARHW----------------EEAPVTFNAWLKQRTRW-----FRGWMQSFWKYSgvifkpAVVRRMGF---A 317
Cdd:PRK15489  288 FPVQfRVRRTSWfgprrertremllcvrEYFPDTFRTAYRQKARWvlgiaFQGWEQMGWRGS------LATRYLLFrdrK 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 318 GVFSTFVMLISpLIVVLNWIAysvtvYWALESAGIL----PQVTAGAIpfWSIIPLWFNAL---------YYYIWIKGAK 384
Cdd:PRK15489  362 GIVTSLVSIIA-YVLLLNFLL-----LAVLRRAGWWtmsfPSLFVTGG--WMQYLLAANAValanrlaqrFYFVGRLYGW 433
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2535869671 385 LEGIKVpipkyLPHMFV--YMNVMMPLASLRAFYQELF--KPVFWEKTAH 430
Cdd:PRK15489  434 EQGLLS-----IPRMVVgnFINFMAVCRAWRIFLIYLVtgKPIVWDKTMH 478
 
Name Accession Description Interval E-value
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
68-298 1.60e-59

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: 194.78  E-value: 1.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  68 PKISVIIPARNEPILGRTIEACLNHVEYPAGKKEIVVV--ADDEggERIALWYQQKYPETVKLLARRQFFP-TKPSALND 144
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLleEDDE--ETIAAARALRLPSIFRVVVVPPSQPrTKPKACNY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 145 AMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGG--YQAVQVILHIGNTDDSWISKVFGMEYSGWFRVMLNGRFNMGLF 222
Cdd:cd06427    79 ALAFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDdkLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLPGLARLGLP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2535869671 223 APLGGTGNYFKRSALKYVGGYEPTNLAEDAELAIRLRIARWNVAVVDARHWEEAPVTFNAWLKQRTRWFRGWMQSF 298
Cdd:cd06427   159 IPLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLEEANNALGNWIRQRSRWIKGYMQTW 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
65-386 6.13e-42

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: 150.28  E-value: 6.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  65 DDYPKISVIIPARNEP-ILGRTIEACLNHvEYPAGKKEIVVVAD--DEGGERIALWYQQKYPEtVKLLaRRQFFPTKPSA 141
Cdd:COG1215    26 ADLPRVSVIIPAYNEEaVIEETLRSLLAQ-DYPKEKLEVIVVDDgsTDETAEIARELAAEYPR-VRVI-ERPENGGKAAA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 142 LNDAMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGGYQAVqvilhigntddswiskvfgmeysgwfrvmlngrfnmgl 221
Cdd:COG1215   103 LNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS-------------------------------------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 222 faplgGTGNYFKRSALKYVGGYEPTNLAEDAELAIRLRIARWNVAVV-DARHWEEAPVTFNAWLKQRTRWFRGWMQSFWK 300
Cdd:COG1215   145 -----GANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVpDAVVYEEAPETLRALFRQRRRWARGGLQLLLK 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 301 YsgvifkPAVVRRMGFAGVFstFVMLISPLIVVLNWIAYSVTVYWALESAGILPQVTAGAIPFWSIIPLWFNALYYYIWI 380
Cdd:COG1215   220 H------RPLLRPRRLLLFL--LLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAAL 291

                  ....*.
gi 2535869671 381 KGAKLE 386
Cdd:COG1215   292 RGKKVV 297
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
68-293 1.40e-26

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: 106.69  E-value: 1.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  68 PKISVIIPARNEP-ILGRTIEACLNhVEYPAgkKEIVVVAD--DEGGERIALWYQQKYPETVKLLARRQFFPT---KPSA 141
Cdd:pfam13641   2 PDVSVVVPAFNEDsVLGRVLEAILA-QPYPP--VEVVVVVNpsDAETLDVAEEIAARFPDVRLRVIRNARLLGptgKSRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 142 LNDAMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGGYQAVQVILHIGNtDDSWISKVFGMEYSGWFRVMLNGRfNMGL 221
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLN-RSTMLSALGALEFALRHLRMMSLR-LALG 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2535869671 222 FAPLGGTGNYFKRSALKYVGGYEPT-NLAEDAELAIRLRIARWNVAVV-DARHWEEAPVTFNAWLKQRTRWFRG 293
Cdd:pfam13641 157 VLPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYApDAAVRTVFPTYLAASIKQRARWVYG 230
PRK14716 PRK14716
glycosyl transferase family protein;
60-431 9.51e-10

glycosyl transferase family protein;


Pssm-ID: 237800 [Multi-domain]  Cd Length: 504  Bit Score: 60.46  E-value: 9.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  60 PGIKLDDYPKISVIIPA-RNEPILGRTIEACLNHVEYPAGKKEIVVVADDEGGERIALWYQQKYPETVKLLARRQFFPTK 138
Cdd:PRK14716   58 ATLRSVPEKRIAIFVPAwREADVIGRMLEHNLATLDYENYRIFVGTYPNDPATLREVDRLAARYPRVHLVIVPHDGPTSK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 139 PSALN---DAMRL---CTG---DIVVVMDVEDIPDRDVFMKAATAIEKggYQAVQV-ILHIGNTDDSWISKVFGMEYSGW 208
Cdd:PRK14716  138 ADCLNwiyQAIFAferERGirfAIIVLHDAEDVIHPLELRLYNYLLPR--HDFVQLpVFSLPRDWGEWVAGTYMDEFAES 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 209 FRVMLNGRFNMGLFAPLGGTGNYFKRSALKYV------GGYEPTNLAEDAELAIRLRIARWNVAVVDARHW--------- 273
Cdd:PRK14716  216 HLKDLPVREALGGLIPSAGVGTAFSRRALERLaaerggQPFDSDSLTEDYDIGLRLKRAGFRQIFVRVRADdttdrpdrr 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 274 -------EEAPVTFNAWLKQRTRW-----FRGWmqsfwkysgvifkpavvRRMGFAGVFSTFVMLI----SPLIVVLNWI 337
Cdd:PRK14716  296 gepiatrEFFPDTFKAAVRQKARWiygiaFQGW-----------------ERLGWKGPAATKYMLWrdrkGLLTNLLLFL 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 338 AYSVTVYWALESAGILpqVTAGAIPFWSIIP--------LWFNALyYYIW-----------IKGAKlEGIKVPipkylPH 398
Cdd:PRK14716  359 AYLLLLLVALVLFGSW--LGGWAWSYGSPLPpgpwlqalLWVNLA-ILLLrvlvrayfvgrLYGWR-EALLSI-----PR 429
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2535869671 399 MFV--YMNVMMPLASLRAFYQELF--KPVFWEKTAHA 431
Cdd:PRK14716  430 MVVgnIINFAATARAWRLYIRSLLtgKPLVWDKTEHD 466
nfrB PRK15489
glycosyl transferase family protein;
196-430 1.27e-07

glycosyl transferase family protein;


Pssm-ID: 237974 [Multi-domain]  Cd Length: 703  Bit Score: 53.98  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 196 WISKVFGMEYSGWFRVMLNGRFNMGLFAPLGGTGNYFKRSALKYV---GGYEPTN---LAEDAELAIRLR-------IAR 262
Cdd:PRK15489  208 WVAGTYMDEFAEWHQKDLVVRESLTGTVPSAGVGTCFSRRALLALmkeRGNQPFNtssLTEDYDFSFRLAelgmqeiFVR 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 263 WNVA-VVDARHW----------------EEAPVTFNAWLKQRTRW-----FRGWMQSFWKYSgvifkpAVVRRMGF---A 317
Cdd:PRK15489  288 FPVQfRVRRTSWfgprrertremllcvrEYFPDTFRTAYRQKARWvlgiaFQGWEQMGWRGS------LATRYLLFrdrK 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 318 GVFSTFVMLISpLIVVLNWIAysvtvYWALESAGIL----PQVTAGAIpfWSIIPLWFNAL---------YYYIWIKGAK 384
Cdd:PRK15489  362 GIVTSLVSIIA-YVLLLNFLL-----LAVLRRAGWWtmsfPSLFVTGG--WMQYLLAANAValanrlaqrFYFVGRLYGW 433
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2535869671 385 LEGIKVpipkyLPHMFV--YMNVMMPLASLRAFYQELF--KPVFWEKTAH 430
Cdd:PRK15489  434 EQGLLS-----IPRMVVgnFINFMAVCRAWRIFLIYLVtgKPIVWDKTMH 478
 
Name Accession Description Interval E-value
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
68-298 1.60e-59

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: 194.78  E-value: 1.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  68 PKISVIIPARNEPILGRTIEACLNHVEYPAGKKEIVVV--ADDEggERIALWYQQKYPETVKLLARRQFFP-TKPSALND 144
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLleEDDE--ETIAAARALRLPSIFRVVVVPPSQPrTKPKACNY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 145 AMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGG--YQAVQVILHIGNTDDSWISKVFGMEYSGWFRVMLNGRFNMGLF 222
Cdd:cd06427    79 ALAFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDdkLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLPGLARLGLP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2535869671 223 APLGGTGNYFKRSALKYVGGYEPTNLAEDAELAIRLRIARWNVAVVDARHWEEAPVTFNAWLKQRTRWFRGWMQSF 298
Cdd:cd06427   159 IPLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLEEANNALGNWIRQRSRWIKGYMQTW 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
65-386 6.13e-42

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: 150.28  E-value: 6.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  65 DDYPKISVIIPARNEP-ILGRTIEACLNHvEYPAGKKEIVVVAD--DEGGERIALWYQQKYPEtVKLLaRRQFFPTKPSA 141
Cdd:COG1215    26 ADLPRVSVIIPAYNEEaVIEETLRSLLAQ-DYPKEKLEVIVVDDgsTDETAEIARELAAEYPR-VRVI-ERPENGGKAAA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 142 LNDAMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGGYQAVqvilhigntddswiskvfgmeysgwfrvmlngrfnmgl 221
Cdd:COG1215   103 LNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS-------------------------------------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 222 faplgGTGNYFKRSALKYVGGYEPTNLAEDAELAIRLRIARWNVAVV-DARHWEEAPVTFNAWLKQRTRWFRGWMQSFWK 300
Cdd:COG1215   145 -----GANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVpDAVVYEEAPETLRALFRQRRRWARGGLQLLLK 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 301 YsgvifkPAVVRRMGFAGVFstFVMLISPLIVVLNWIAYSVTVYWALESAGILPQVTAGAIPFWSIIPLWFNALYYYIWI 380
Cdd:COG1215   220 H------RPLLRPRRLLLFL--LLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAAL 291

                  ....*.
gi 2535869671 381 KGAKLE 386
Cdd:COG1215   292 RGKKVV 297
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
72-251 4.76e-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: 133.51  E-value: 4.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  72 VIIPARNEP-ILGRTIEACLNhVEYPagKKEIVVVAD---DEGGER-IALWYQQKYPETVKLLARRQffpTKPSALNDAM 146
Cdd:cd06423     1 IIVPAYNEEaVIERTIESLLA-LDYP--KLEVIVVDDgstDDTLEIlEELAALYIRRVLVVRDKENG---GKAGALNAGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 147 RLCTGDIVVVMDVEDIPDRDvFMKAATA--IEKGGYQAVQVILHIGNTDDSWISKVFGMEYSGWFRVMLNGRFNMGLFAP 224
Cdd:cd06423    75 RHAKGDIVVVLDADTILEPD-ALKRLVVpfFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLV 153
                         170       180
                  ....*....|....*....|....*..
gi 2535869671 225 LGGTGNYFKRSALKYVGGYEPTNLAED 251
Cdd:cd06423   154 LSGAFGAFRREALREVGGWDEDTLTED 180
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
68-298 2.32e-29

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: 114.59  E-value: 2.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  68 PKISVIIPARNEP--ILGRTIEACLNhVEYPAGKKEiVVVADDEGGERIALWYQQ-KYPETVKLLARRQFFPTKPSALND 144
Cdd:cd06421     1 PTVDVFIPTYNEPleIVRKTLRAALA-IDYPHDKLR-VYVLDDGRRPELRALAAElGVEYGYRYLTRPDNRHAKAGNLNN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 145 AMRLCTGDIVVVMDVEDIPDRD-------VFMKAataiEKGGYqaVQVILHIGNTDD-SWISKVFGMEYSGWFRVMLNGR 216
Cdd:cd06421    79 ALAHTTGDFVAILDADHVPTPDflrrtlgYFLDD----PKVAL--VQTPQFFYNPDPfDWLADGAPNEQELFYGVIQPGR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 217 fNMGLFAPLGGTGNYFKRSALKYVGGYEPTNLAEDAELAIRLRIARWNVAVVDARH-WEEAPVTFNAWLKQRTRWFRGWM 295
Cdd:cd06421   153 -DRWGAAFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLaAGLAPETLAAYIKQRLRWARGML 231

                  ...
gi 2535869671 296 QSF 298
Cdd:cd06421   232 QIL 234
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
68-293 1.40e-26

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: 106.69  E-value: 1.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  68 PKISVIIPARNEP-ILGRTIEACLNhVEYPAgkKEIVVVAD--DEGGERIALWYQQKYPETVKLLARRQFFPT---KPSA 141
Cdd:pfam13641   2 PDVSVVVPAFNEDsVLGRVLEAILA-QPYPP--VEVVVVVNpsDAETLDVAEEIAARFPDVRLRVIRNARLLGptgKSRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 142 LNDAMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGGYQAVQVILHIGNtDDSWISKVFGMEYSGWFRVMLNGRfNMGL 221
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLN-RSTMLSALGALEFALRHLRMMSLR-LALG 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2535869671 222 FAPLGGTGNYFKRSALKYVGGYEPT-NLAEDAELAIRLRIARWNVAVV-DARHWEEAPVTFNAWLKQRTRWFRG 293
Cdd:pfam13641 157 VLPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYApDAAVRTVFPTYLAASIKQRARWVYG 230
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
153-347 7.27e-21

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: 89.70  E-value: 7.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 153 IVVVMDVEDIPDRDVFMKAATAIEKGGYQAVQVILHIGNTDdSWISKVFGMEYSGWFRVMLNGRFNMGLFAPLGGTGNYF 232
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASPEVAIIQGPILPMNVG-NYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 233 KRSALKYVGGYEPTNLAEDAELAIRLRIARWNVAVVDARH-WEEAPVTFNAWLKQRTRWFRGwmqsfwkysgvIFKPAVV 311
Cdd:pfam13632  80 RRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAvYEKSPLTFRDFLRQRRRWAYG-----------CLLILLI 148
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2535869671 312 RRMGFAGVFSTFVMLISPLIVVLNWIAYSVTVYWAL 347
Cdd:pfam13632 149 RLLGYLGTLLWSGLPLALLLLLLFSISSLALVLLLL 184
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
68-293 1.05e-20

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: 90.45  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  68 PKISVIIPARNEP-ILGRTIEA-CLnhVEYPAGKKEIVVVAD--DEGGERIALWYQQKYPETVKLL----ARRQFFptKP 139
Cdd:cd06437     1 PMVTVQLPVFNEKyVVERLIEAaCA--LDYPKDRLEIQVLDDstDETVRLAREIVEEYAAQGVNIKhvrrADRTGY--KA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 140 SALNDAMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGGYQAVQV-ILHIgNTDDSWISKVFGMEYSGWFRVMLNGRFN 218
Cdd:cd06437    77 GALAEGMKVAKGEYVAIFDADFVPPPDFLQKTPPYFADPKLGFVQTrWGHI-NANYSLLTRVQAMSLDYHFTIEQVARSS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 219 MGLFAPLGGTGNYFKRSALKYVGGYEPTNLAEDAELAIRLRIARWNVA-----VVDArhweEAPVTFNAWLKQRTRWFRG 293
Cdd:cd06437   156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVylddvVVPA----ELPASMSAYRSQQHRWSKG 231
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
68-272 4.39e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 76.66  E-value: 4.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  68 PKISVIIPARNEPilgRTIEACLNHVEYPAGKK-EIVVVAD--DEGGERIALWYQQKYPEtVKLLaRRQFFPTKPSALND 144
Cdd:COG0463     2 PLVSVVIPTYNEE---EYLEEALESLLAQTYPDfEIIVVDDgsTDGTAEILRELAAKDPR-IRVI-RLERNRGKGAARNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 145 AMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGGYQAVQVILHIGntDDSWISKVFGMEYSGWFRVMLNGRFNMGLFap 224
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIR--EGESDLRRLGSRLFNLVRLLTNLPDSTSGF-- 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2535869671 225 lggtgNYFKRSALKYVGgyEPTNLAEDAELaIRLRIARWNVAVVDARH 272
Cdd:COG0463   153 -----RLFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVPVRY 192
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
71-238 6.24e-16

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: 75.12  E-value: 6.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  71 SVIIPARNE-PILGRTIEACLNhveYPAGKKEIVVVaDD---EGGERIALWYQQKYPE-TVKLLARRQFfptKPSALNDA 145
Cdd:pfam00535   1 SVIIPTYNEeKYLLETLESLLN---QTYPNFEIIVV-DDgstDGTVEIAEEYAKKDPRvRVIRLPENRG---KAGARNAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 146 MRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGGYQAV--QVILHIGNTDDSWISKVFGMEYSGWFRVMLNGRFNMGLFA 223
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVvgSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
                         170
                  ....*....|....*
gi 2535869671 224 plgGTGNYFKRSALK 238
Cdd:pfam00535 154 ---GGFALYRREALE 165
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
69-259 6.27e-15

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: 74.19  E-value: 6.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  69 KISVIIPARNEpilGRTIEACLNHV---EYPAGKKEIVVVAD--DEGGERIALWYQQKYPEtVKLL---ARRQffptkPS 140
Cdd:cd02525     1 FVSIIIPVRNE---EKYIEELLESLlnqSYPKDLIEIIVVDGgsTDGTREIVQEYAAKDPR-IRLIdnpKRIQ-----SA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 141 ALNDAMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGGYQAVQVILHIGNTDDSWI------SKVFGMEYSGwFRvmlN 214
Cdd:cd02525    72 GLNIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKaiavaqSSPLGSGGSA-YR---G 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2535869671 215 GRFNMGlFAPlggTGNY--FKRSALKYVGGYEPtNL--AEDAELAIRLR 259
Cdd:cd02525   148 GAVKIG-YVD---TVHHgaYRREVFEKVGGFDE-SLvrNEDAELNYRLR 191
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
72-254 4.63e-14

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: 70.32  E-value: 4.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  72 VIIPARNEP-ILGRTIEaCLNHVEYPAGKKEIVVVAD---DEGGERI----ALWYQQKYPEtvkllaRRqffpTKPSALN 143
Cdd:cd06438     1 ILIPAHNEEaVIGNTVR-SLKAQDYPRELYRIFVVADnctDDTAQVAraagATVLERHDPE------RR----GKGYALD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 144 DAMR-----LCTGDIVVVMDVEDIPDRDVFMKAATAIEKGgYQAVQVILHIGNTDDSWISKVFGMEYSGWFRVMLNGRFN 218
Cdd:cd06438    70 FGFRhllnlADDPDAVVVFDADNLVDPNALEELNARFAAG-ARVVQAYYNSKNPDDSWITRLYAFAFLVFNRLRPLGRSN 148
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2535869671 219 MGLFAPLGGTGNYFKRSALKYVgGYEPTNLAEDAEL 254
Cdd:cd06438   149 LGLSCQLGGTGMCFPWAVLRQA-PWAAHSLTEDLEF 183
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
71-301 2.15e-13

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: 69.35  E-value: 2.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  71 SVIIPARNEP--ILGRTIEAcLNHVEYPagKKEIVVVADDEGGEriALW-----YQQKYPETVKLLARRQFFPTKPSALN 143
Cdd:cd06435     1 SIHVPCYEEPpeMVKETLDS-LAALDYP--NFEVIVIDNNTKDE--ALWkpveaHCAQLGERFRFFHVEPLPGAKAGALN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 144 DAMRLCTGD--IVVVMDVEDIPDRDVFMKAATAIEKGGYQAVQVILHIGNTDDSWISKVFGMEYSGWFRVMLNGR--FNM 219
Cdd:cd06435    76 YALERTAPDaeIIAVIDADYQVEPDWLKRLVPIFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRneRNA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 220 GLFAplgGTGNYFKRSALKYVGGYEPTNLAEDAELAIRLRIARWNVAVVDARHWEE-APVTFNAWLKQRTRWFRGWMQSF 298
Cdd:cd06435   156 IIQH---GTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGlIPDTFEAFKKQRFRWAYGAVQIL 232

                  ...
gi 2535869671 299 WKY 301
Cdd:cd06435   233 KKH 235
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
44-297 2.62e-13

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: 69.53  E-value: 2.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  44 VYHLIVTLSGLGQPMDPGIKLDDY-PKISVIIPARNE-PILGRTIEACLNhVEYPAGKKEIVVVAD---DEGGERIALWY 118
Cdd:cd06439     4 GYPLLLKLLARLRPKPPSLPDPAYlPTVTIIIPAYNEeAVIEAKLENLLA-LDYPRDRLEIIVVSDgstDGTAEIAREYA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 119 QQKypetVKLLarrqFFPT---KPSALNDAMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGGYQAVQVILHIGNTDDS 195
Cdd:cd06439    83 DKG----VKLL----RFPErrgKAAALNRALALATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGELVIVDGGGS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 196 WISKVFGMEYSGWFRVMlNGRFNmglfAPLGGTGN-Y-FKRSAlkyVGGYEPTNLAEDAELAIRLRIARWNVAVV-DARH 272
Cdd:cd06439   155 GSGEGLYWKYENWLKRA-ESRLG----STVGANGAiYaIRREL---FRPLPADTINDDFVLPLRIARQGYRVVYEpDAVA 226
                         250       260
                  ....*....|....*....|....*
gi 2535869671 273 WEEAPVTFNAWLKQRTRWFRGWMQS 297
Cdd:cd06439   227 YEEVAEDGSEEFRRRVRIAAGNLQA 251
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
72-293 1.73e-11

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 63.85  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  72 VIIPARNEpilGRTIEACLNHVE---YPAGKKEIVVVAD---DEGGERIALWYQQKYPETVKLLARRQFFPTKPSALNDA 145
Cdd:cd04192     1 VVIAARNE---AENLPRLLQSLSaldYPKEKFEVILVDDhstDGTVQILEFAAAKPNFQLKILNNSRVSISGKKNALTTA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 146 MRLCTGDIVVVMDVEDIPDRD--VFMKAATAIEKGGYQAVQVIlhiGNTDDSWISKVFGMEysgWFRVMLNGRFNMGLFA 223
Cdd:cd04192    78 IKAAKGDWIVTTDADCVVPSNwlLTFVAFIQKEQIGLVAGPVI---YFKGKSLLAKFQRLD---WLSLLGLIAGSFGLGK 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2535869671 224 PLGGTGNYF--KRSALKYVGGYE--PTNLAEDAELAIRLRIARW-NVAVV---DARHWEEAPVTFNAWLKQRTRWFRG 293
Cdd:cd04192   152 PFMCNGANMayRKEAFFEVGGFEgnDHIASGDDELLLAKVASKYpKVAYLknpEALVTTQPVTSWKELLNQRKRWASK 229
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
68-303 5.14e-10

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 58.85  E-value: 5.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  68 PKISVIIPARNEP-ILGRTIEACLNHVEYPAgkkEIVVVaDDEGGERIALWYQQKYPETVKLLA--RRQFFptkPSALND 144
Cdd:COG1216     3 PKVSVVIPTYNRPeLLRRCLESLLAQTYPPF---EVIVV-DNGSTDGTAELLAALAFPRVRVIRnpENLGF---AAARNL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 145 AMRLCTGDIVVVMDvedipdrdvfmkaataiekggyqavqvilhigntDDSWISkvfgmeySGWFRVMLNgRFNMglfap 224
Cdd:COG1216    76 GLRAAGGDYLLFLD----------------------------------DDTVVE-------PDWLERLLA-AACL----- 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 225 lggtgnYFKRSALKYVGGYEPTNLA--EDAELAIRLRIARWNVAVV-DARHWEEAPVTFNAWLKQRtRWFRGWMQSFWKY 301
Cdd:COG1216   109 ------LIRREVFEEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVpDAVVYHLGGASSGPLLRAY-YLGRNRLLFLRKH 181

                  ..
gi 2535869671 302 SG 303
Cdd:COG1216   182 GP 183
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
72-217 5.70e-10

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: 57.90  E-value: 5.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  72 VIIPARN-EPILGRTIEACLNHVEYPAgkkEIVVVAD--DEGGERIALWYQQKYPETVKLlaRRQFFPTKPSALNDAMRL 148
Cdd:cd00761     1 VIIPAYNeEPYLERCLESLLAQTYPNF---EVIVVDDgsTDGTLEILEEYAKKDPRVIRV--INEENQGLAAARNAGLKA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 149 CTGDIVVVMDVEDIPDRDVF-MKAATAIEKGGYQAV----------QVILHIGNTDDSWISkvFGMEYSGWFRVMLNGRF 217
Cdd:cd00761    76 ARGEYILFLDADDLLLPDWLeRLVAELLADPEADAVggpgnllfrrELLEEIGGFDEALLS--GEEDDDFLLRLLRGGKV 153
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
70-294 8.69e-10

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 58.35  E-value: 8.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  70 ISVIIPARNEpilGRTIEACLNHV-EYPAGKKEIVVVaddEGGErialwyQQKYPETVKLLARRqFFPTKPS---ALNDA 145
Cdd:cd02522     1 LSIIIPTLNE---AENLPRLLASLrRLNPLPLEIIVV---DGGS------TDGTVAIARSAGVV-VISSPKGrarQMNAG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 146 MRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKGGYQAVQVILHIgnTDDSWiskvfgmeysgWFRVMLNG---RFNmGLF 222
Cdd:cd02522    68 AAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAFRLRF--DDPGP-----------RLRLLELGanlRSR-LFG 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2535869671 223 APLGGTGNYFKRSALKYVGGYEPTNLAEDAELAIRL-RIARW----NVAVVDARHWEEAPVTFNAWLKQ--RTRWFRGW 294
Cdd:cd02522   134 LPYGDQGLFIRRELFEELGGFPELPLMEDVELVRRLrRRGRPallpSPVTTSARRWERNGWLRTTLLNWllLLLYLLGV 212
PRK14716 PRK14716
glycosyl transferase family protein;
60-431 9.51e-10

glycosyl transferase family protein;


Pssm-ID: 237800 [Multi-domain]  Cd Length: 504  Bit Score: 60.46  E-value: 9.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  60 PGIKLDDYPKISVIIPA-RNEPILGRTIEACLNHVEYPAGKKEIVVVADDEGGERIALWYQQKYPETVKLLARRQFFPTK 138
Cdd:PRK14716   58 ATLRSVPEKRIAIFVPAwREADVIGRMLEHNLATLDYENYRIFVGTYPNDPATLREVDRLAARYPRVHLVIVPHDGPTSK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 139 PSALN---DAMRL---CTG---DIVVVMDVEDIPDRDVFMKAATAIEKggYQAVQV-ILHIGNTDDSWISKVFGMEYSGW 208
Cdd:PRK14716  138 ADCLNwiyQAIFAferERGirfAIIVLHDAEDVIHPLELRLYNYLLPR--HDFVQLpVFSLPRDWGEWVAGTYMDEFAES 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 209 FRVMLNGRFNMGLFAPLGGTGNYFKRSALKYV------GGYEPTNLAEDAELAIRLRIARWNVAVVDARHW--------- 273
Cdd:PRK14716  216 HLKDLPVREALGGLIPSAGVGTAFSRRALERLaaerggQPFDSDSLTEDYDIGLRLKRAGFRQIFVRVRADdttdrpdrr 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 274 -------EEAPVTFNAWLKQRTRW-----FRGWmqsfwkysgvifkpavvRRMGFAGVFSTFVMLI----SPLIVVLNWI 337
Cdd:PRK14716  296 gepiatrEFFPDTFKAAVRQKARWiygiaFQGW-----------------ERLGWKGPAATKYMLWrdrkGLLTNLLLFL 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 338 AYSVTVYWALESAGILpqVTAGAIPFWSIIP--------LWFNALyYYIW-----------IKGAKlEGIKVPipkylPH 398
Cdd:PRK14716  359 AYLLLLLVALVLFGSW--LGGWAWSYGSPLPpgpwlqalLWVNLA-ILLLrvlvrayfvgrLYGWR-EALLSI-----PR 429
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2535869671 399 MFV--YMNVMMPLASLRAFYQELF--KPVFWEKTAHA 431
Cdd:PRK14716  430 MVVgnIINFAATARAWRLYIRSLLtgKPLVWDKTEHD 466
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
72-238 2.27e-08

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: 53.73  E-value: 2.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  72 VIIPARNE-PILGRTIEACLNHVEyPAGKKEIVVVaDD---EGGERIALWYQQKYPETVKLLARRQFfpTKPSALNDAMR 147
Cdd:cd04179     1 VVIPAYNEeENIPELVERLLAVLE-EGYDYEIIVV-DDgstDGTAEIARELAARVPRVRVIRLSRNF--GKGAAVRAGFK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 148 LCTGDIVVVMD------VEDIPDrdvFMKaatAIEKGGYQAVqvilhIGN-------TDDSWISKVFGMEYSGWFRVMLN 214
Cdd:cd04179    77 AARGDIVVTMDadlqhpPEDIPK---LLE---KLLEGGADVV-----IGSrfvrgggAGMPLLRRLGSRLFNFLIRLLLG 145
                         170       180
                  ....*....|....*....|....*..
gi 2535869671 215 GRFNM---GLFAplggtgnyFKRSALK 238
Cdd:cd04179   146 VRISDtqsGFRL--------FRREVLE 164
nfrB PRK15489
glycosyl transferase family protein;
196-430 1.27e-07

glycosyl transferase family protein;


Pssm-ID: 237974 [Multi-domain]  Cd Length: 703  Bit Score: 53.98  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 196 WISKVFGMEYSGWFRVMLNGRFNMGLFAPLGGTGNYFKRSALKYV---GGYEPTN---LAEDAELAIRLR-------IAR 262
Cdd:PRK15489  208 WVAGTYMDEFAEWHQKDLVVRESLTGTVPSAGVGTCFSRRALLALmkeRGNQPFNtssLTEDYDFSFRLAelgmqeiFVR 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 263 WNVA-VVDARHW----------------EEAPVTFNAWLKQRTRW-----FRGWMQSFWKYSgvifkpAVVRRMGF---A 317
Cdd:PRK15489  288 FPVQfRVRRTSWfgprrertremllcvrEYFPDTFRTAYRQKARWvlgiaFQGWEQMGWRGS------LATRYLLFrdrK 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 318 GVFSTFVMLISpLIVVLNWIAysvtvYWALESAGIL----PQVTAGAIpfWSIIPLWFNAL---------YYYIWIKGAK 384
Cdd:PRK15489  362 GIVTSLVSIIA-YVLLLNFLL-----LAVLRRAGWWtmsfPSLFVTGG--WMQYLLAANAValanrlaqrFYFVGRLYGW 433
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2535869671 385 LEGIKVpipkyLPHMFV--YMNVMMPLASLRAFYQELF--KPVFWEKTAH 430
Cdd:PRK15489  434 EQGLLS-----IPRMVVgnFINFMAVCRAWRIFLIYLVtgKPIVWDKTMH 478
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
72-164 7.63e-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: 49.84  E-value: 7.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  72 VIIPARNE----PILGRTIEACLNHVEYpagkkEIVVVADD--EGGERIALWYQQKYPEtVKLLARrqffPTKP---SAL 142
Cdd:cd06442     1 IIIPTYNEreniPELIERLDAALKGIDY-----EIIVVDDNspDGTAEIVRELAKEYPR-VRLIVR----PGKRglgSAY 70
                          90       100
                  ....*....|....*....|....*...
gi 2535869671 143 NDAMRLCTGDIVVVMD------VEDIPD 164
Cdd:cd06442    71 IEGFKAARGDVIVVMDadlshpPEYIPE 98
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
70-293 8.10e-06

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 46.86  E-value: 8.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  70 ISVIIPARNEP--ILGRTIEACLNHveypaGKKEIVVVADDEGGERIALWYQQKYPETVKLLARRQffPTKPSALNDAMR 147
Cdd:cd06434     2 VTVIIPVYDEDpdVFRECLRSILRQ-----KPLEIIVVTDGDDEPYLSILSQTVKYGGIFVITVPH--PGKRRALAEGIR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 148 LCTGDIVVVMDvedipdRDVFMKAATAIEK---------GGYQAVQVILhigNTDDSWISKVFGMEYSgwfRVMLNGRFN 218
Cdd:cd06434    75 HVTTDIVVLLD------SDTVWPPNALPEMlkpfedpkvGGVGTNQRIL---RPRDSKWSFLAAEYLE---RRNEEIRAA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 219 MGLFAPL----GGTGNYfKRSALK-----------YVGGYePTNLAEDAELAIRLRIARWNVAVVDARHWE-EAPVTFNA 282
Cdd:cd06434   143 MSYDGGVpclsGRTAAY-RTEILKdflfleeftneTFMGR-RLNAGDDRFLTRYVLSHGYKTVYQYTSEAYtETPENYKK 220
                         250
                  ....*....|.
gi 2535869671 283 WLKQRTRWFRG 293
Cdd:cd06434   221 FLKQQLRWSRS 231
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
72-251 2.27e-05

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: 45.07  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  72 VIIPARNEP-ILGRTIeACLNHVEypagKKEIVVVADDEGGERIA-LWYQQKYPETVKLLARRQffPT----KPSALNDA 145
Cdd:cd06436     1 VLVPCLNEEaVIQRTL-ASLLRNK----PNFLVLVIDDASDDDTAgIVRLAITDSRVHLLRRHL--PNartgKGDALNAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 146 ------MRLCTGD-----IVVVMDVEDIPDRDVFMKAATAIEKGGYQAVQVILHIGNTDDSWISKVFGMEYSGWFRVMLN 214
Cdd:cd06436    74 ydqirqILIEEGAdpervIIAVIDADGRLDPNALEAVAPYFSDPRVAGTQSRVRMYNRHKNLLTILQDLEFFIIIAATQS 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2535869671 215 GRFNMGLFApLGGTGNYFKRSALKYVGGYEP--TNLAED 251
Cdd:cd06436   154 LRALTGTVG-LGGNGQFMRLSALDGLIGEEPwsDSLLED 191
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
72-183 2.54e-05

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: 45.25  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  72 VIIPARNEPI-LGRTIEACLNHV-EYPAGKKEIVVVAD--DEGGERIALWYQQKYPETVKLLA--RRQffpTKPSALNDA 145
Cdd:cd04188     1 VVIPAYNEEKrLPPTLEEAVEYLeERPSFSYEIIVVDDgsKDGTAEVARKLARKNPALIRVLTlpKNR---GKGGAVRAG 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2535869671 146 MRLCTGDIVVVMDVE---DIPDrdvFMKAATAIEKGGYQAV 183
Cdd:cd04188    78 MLAARGDYILFADADlatPFEE---LEKLEEALKTSGYDIA 115
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
68-262 2.24e-04

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 42.19  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  68 PKISVIIPARNEPI--LGRTIEACLNHVeYPagKKEIVVVADDEGGERIALwYQQKYPETVKLLarRQFFPTK----PSA 141
Cdd:cd04184     1 PLISIVMPVYNTPEkyLREAIESVRAQT-YP--NWELCIADDASTDPEVKR-VLKKYAAQDPRI--KVVFREEnggiSAA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 142 LNDAMRLCTGDIVVVMDVEDIPDRDVFMKAATAIEKggYQAVQVILhignTDDSWISKvFGMEYSGWFRvmlnGRFNMGL 221
Cdd:cd04184    75 TNSALELATGEFVALLDHDDELAPHALYEVVKALNE--HPDADLIY----SDEDKIDE-GGKRSEPFFK----PDWSPDL 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2535869671 222 FAplggTGNY------FKRSALKYVGGYEPT-NLAEDAELAIRL-----RIAR 262
Cdd:cd04184   144 LL----SQNYighllvYRRSLVRQVGGFREGfEGAQDYDLVLRVsehtdRIAH 192
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
201-292 2.81e-04

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


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 41.50  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 201 FGMEYSGWFRVMLNGRFNMG---LFAPLGGTGN------YFKRSALKYVGGYEP--TNLAEDAELAIRLRIARWNVAVVD 269
Cdd:pfam13506  68 VGSDPKGLAAALEAAFFNTLagvLQAALSGIGFavgmsmAFRRADLERIGGFEAlaDYLAEDYALGKLLRAAGLKVVLSP 147
                          90       100
                  ....*....|....*....|....*.
gi 2535869671 270 A-RHWEEAPV--TFNAWLKQRTRWFR 292
Cdd:pfam13506 148 RpILQTSGPRrtSFRAFMARQLRWAR 173
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
72-220 1.45e-03

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 39.38  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671  72 VIIPARNE----PILGRTIEACLNHVEYPAgkkEIVVVAD---DEGGERIALWyQQKYPETVKLLARRQFfpTKPSALND 144
Cdd:cd04187     1 IVVPVYNEeenlPELYERLKAVLESLGYDY---EIIFVDDgstDRTLEILREL-AARDPRVKVIRLSRNF--GQQAALLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869671 145 AMRLCTGDIVVVMDV------EDIPDrdvFMKAataiEKGGYQAVqvilhIG---NTDDSWISKVFGMEYSGWFRVMLNG 215
Cdd:cd04187    75 GLDHARGDAVITMDAdlqdppELIPE---MLAK----WEEGYDVV-----YGvrkNRKESWLKRLTSKLFYRLINKLSGV 142

                  ....*
gi 2535869671 216 RFNMG 220
Cdd:cd04187   143 DIPDN 147
 
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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