NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1091089803|gb|OHQ23032|]
View 

glycosyl transferase [Streptococcus sp. HMSC065H07]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
78-321 2.65e-82

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: 261.35  E-value: 2.65e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  78 PDVDVLIATHNEDPELLYKTINACTFMEYPdKSKVHIYVCDDTNRLEVAKLADELGVGYFGLA----DNKDAKSGNYNNA 153
Cdd:cd06421     1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYP-HDKLRVYVLDDGRRPELRALAAELGVEYGYRYltrpDNRHAKAGNLNNA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 154 LRQTSSPLVATFDADMIPYREFLLETVPYFVeqveayengddyDKSKVGLIQTPQSFYNADIFQFnlfSESTLPNEQDFF 233
Cdd:cd06421    80 LAHTTGDFVAILDADHVPTPDFLRRTLGYFL------------DDPKVALVQTPQFFYNPDPFDW---LADGAPNEQELF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 234 SKEINVFNNSHGAALYTGSNTLIFRKAIEDVGGFPTDTITEDFELGVRINAAGYVNYSTKSPMASGLTPTDLKSVIKQRV 313
Cdd:cd06421   145 YGVIQPGRDRWGAAFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRL 224

                  ....*...
gi 1091089803 314 RWGRGVIR 321
Cdd:cd06421   225 RWARGMLQ 232
PilZ pfam07238
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ...
509-606 6.89e-16

PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, which is involved in regulation of motility, biofilm formation and virulence of many bacterial pathogens. This domain binds c-di-GMP through RXXXR and [D/N]hSXXG motifs, however, some PilZ domains lack these motifs and do not bind c-di-GMP. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias. This is the canonical PilZ domain whose structure consists of six beta-strands that form a beta barrel, followed by a long C-terminal alpha-helix.


:

Pssm-ID: 399904  Cd Length: 102  Bit Score: 73.69  E-value: 6.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 509 RSSERFTVDEAMVIEVDDDSYQVRVCDISETGISFYTDLPLYLPKEK-ELTLNLQSRDYHARVKGHVVRVFAIDNGWRYG 587
Cdd:pfam07238   3 RRFPRVPVSLPVTLRDGGGEYKGRLIDISLGGAAIRLPDEPLALGDRvELSLDLLDDGQELALPGRVVRIRPDEDGARVG 82
                          90
                  ....*....|....*....
gi 1091089803 588 VQFSEVPEADKREFYQYIY 606
Cdd:pfam07238  83 VQFLDLDEEQRRLLVRLLF 101
Cellulose_synt super family cl37525
Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose ...
271-492 2.59e-05

Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues, is the major component of wood and thus paper, and is synthesized by plants, most algae, some bacteria and fungi, and even some animals. The genes that synthesize cellulose in higher plants differ greatly from the well-characterized genes found in Acetobacter and Agrobacterium sp. More correctly designated as 'cellulose synthase catalytic subunits', plant cellulose synthase (CesA) proteins are integral membrane proteins, approximately 1,000 amino acids in length. There are a number of highly conserved residues, including several motifs shown to be necessary for processive glycosyltransferase activity.


The actual alignment was detected with superfamily member pfam03552:

Pssm-ID: 460970 [Multi-domain]  Cd Length: 715  Bit Score: 47.83  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 271 TITEDFELGVRINAAGY--VNYSTKSPMASGLTPTDLKSVIKQRVRWGRGV--IRSSYNMNIFFNPKLTMGQRIVYINGY 346
Cdd:pfam03552 419 SVTEDILTGFRMHCRGWrsIYCMPKRDAFKGSAPINLSDRLHQVLRWALGSveIFFSRHCPIWYGGRLKFLQRFAYINVG 498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 347 LYWWSFFRRLLYILAPILyTVFHVRVVVSNIWLLFLFWLPS-----FALTRLSMR-------EVSKQYQTQVWGEIVETI 414
Cdd:pfam03552 499 IYPFTSIPLLAYCFLPAI-CLFTGKFIVPTLSNFASIYFLSlflsiIATGILELRwsgvsieEWWRNEQFWVIGGTSAHL 577
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 415 FAPYLFIPMMLESFGISnkkFKVTRKGN----------YT-SWTLYLyaLPYLVLWGLAVYGLV-----TFN--YGKFGs 476
Cdd:pfam03552 578 FAVFQGLLKVIAGIDTS---FTVTSKASddeddefadlYIfKWTTLL--IPPTTILIVNLVGIVagvsrAINsgYPSWG- 651
                         250
                  ....*....|....*.
gi 1091089803 477 ELFYGSIISFWLIYHI 492
Cdd:pfam03552 652 PLFGKLFFAFWVIVHL 667
 
Name Accession Description Interval E-value
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
78-321 2.65e-82

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: 261.35  E-value: 2.65e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  78 PDVDVLIATHNEDPELLYKTINACTFMEYPdKSKVHIYVCDDTNRLEVAKLADELGVGYFGLA----DNKDAKSGNYNNA 153
Cdd:cd06421     1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYP-HDKLRVYVLDDGRRPELRALAAELGVEYGYRYltrpDNRHAKAGNLNNA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 154 LRQTSSPLVATFDADMIPYREFLLETVPYFVeqveayengddyDKSKVGLIQTPQSFYNADIFQFnlfSESTLPNEQDFF 233
Cdd:cd06421    80 LAHTTGDFVAILDADHVPTPDFLRRTLGYFL------------DDPKVALVQTPQFFYNPDPFDW---LADGAPNEQELF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 234 SKEINVFNNSHGAALYTGSNTLIFRKAIEDVGGFPTDTITEDFELGVRINAAGYVNYSTKSPMASGLTPTDLKSVIKQRV 313
Cdd:cd06421   145 YGVIQPGRDRWGAAFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRL 224

                  ....*...
gi 1091089803 314 RWGRGVIR 321
Cdd:cd06421   225 RWARGMLQ 232
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
19-629 1.21e-77

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 266.89  E-value: 1.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  19 YLTWRLVATIPWhDSWFALIFGILLWGSEV---VSAITGYI-LIW--NKQ-----KDFELekpeiakerYPDVDVLIATH 87
Cdd:PRK11498  200 YIWWRYTSTLNW-DDPVSLVCGLILLFAETyawIVLVLGYFqVVWplNRQpvplpKDMSL---------WPTVDIFVPTY 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  88 NEDPELLYKTINACTFMEYPdKSKVHIYVCDDTNRLEVAKLADELGVGYFGLADNKDAKSGNYNNALRQTSSPLVATFDA 167
Cdd:PRK11498  270 NEDLNVVKNTIYASLGIDWP-KDKLNIWILDDGGREEFRQFAQEVGVKYIARPTHEHAKAGNINNALKYAKGEFVAIFDC 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 168 DMIPYREFLLETVPYFVEqveayengddyDKsKVGLIQTPQSFYNADIFQFNLFSESTLPNEQDFFSKEINVFNNSHGAA 247
Cdd:PRK11498  349 DHVPTRSFLQMTMGWFLK-----------DK-KLAMMQTPHHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDAT 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 248 LYTGSNTLIFRKAIEDVGGFPTDTITEDFELGVRINAAGYVNYSTKSPMASGLTPTDLKSVIKQRVRWGRGVIRSSYNMN 327
Cdd:PRK11498  417 FFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDN 496
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 328 IFFNPKLTMGQRIVYINGYLYWWSFFRRLLYILAPILYTVFHVRVVVSNIWLLFLFWLPSFALTRLSMREVSKQYQTQVW 407
Cdd:PRK11498  497 PLTGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHASLTNSRIQGKYRHSFW 576
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 408 GEIVETIFAPYLFIPMMLESFGISNKKFKVTRKG-----NYTSWTLylyALPYLVLWGLAVYGLVtfnygkFGS-ELFYG 481
Cdd:PRK11498  577 SEIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGglveeEYVDWVI---SRPYIFLVLLNLVGVA------VGIwRYFYG 647
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 482 S-------IISF-WLIYHIINLTFAIFCALGRPIYRSSERFTVDEAMVIEVDD-DSYQVRVCDISETGISFYTDLPLYLP 552
Cdd:PRK11498  648 PpneiltvIVSLvWVFYNLIILGGAVAVSVESKQVRRSHRVEMTMPAAIAREDgHLFSCTVQDFSDGGLGIKINGQAQLL 727
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091089803 553 KEKELTLNLQSRDYHARVKGHVVRVFaidnGWRYGVQFSEVPEADKREFYQYIYDRinynlpkeKDPWmTTWDDLFE 629
Cdd:PRK11498  728 EGQKVNLLLKRGQQEYVFPTQVTRVM----GNEVGLQLMPLTTQQHIDFVQCTFAR--------ADTW-ALWQDSFP 791
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
42-440 3.65e-35

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 135.64  E-value: 3.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  42 LLWGSEVVSAITGYILIWNKQKDfelekpeiAKERYPDVDVLIATHNEdPELLYKTINACTFMEYPdKSKVHIYVCDDTN 121
Cdd:COG1215     1 LLLLLALLALLYLLLLALARRRR--------APADLPRVSVIIPAYNE-EAVIEETLRSLLAQDYP-KEKLEVIVVDDGS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 122 RLEVAKLADELGVGYFGL----ADNKDAKSGNYNNALRQTSSPLVATFDADMIPYREFLLETVPYFveqveayengddyD 197
Cdd:COG1215    71 TDETAEIARELAAEYPRVrvieRPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-------------A 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 198 KSKVGLiqtpqsfynadifqfnlfsestlpneqdffskeinvfnnshgaalyTGSNTLIFRKAIEDVGGFPTDTITEDFE 277
Cdd:COG1215   138 DPGVGA----------------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLD 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 278 LGVRINAAGYVNYSTKSPMASGLTPTDLKSVIKQRVRWGRGVIRSSYNMNIFFNPKLtmgqrivyingylywwsFFRRLL 357
Cdd:COG1215   172 LSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRR-----------------LLLFLL 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 358 YILAPILYTVFhvrvvVSNIWLLFLFWLPSFALTRLSMREVSKqyqtqvwgeIVETIFAPYLFIPMMLESFGISNKKFKV 437
Cdd:COG1215   235 LLLLPLLLLLL-----LLALLALLLLLLPALLLALLLALRRRR---------LLLPLLHLLYGLLLLLAALRGKKVVWKK 300

                  ...
gi 1091089803 438 TRK 440
Cdd:COG1215   301 TPR 303
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
78-318 2.73e-19

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: 87.43  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  78 PDVDVLIATHNEDPELLyKTINACTFMEYPDkskVHIYVCDDTNRLEVAKLADELGVGY---------FGLADNKDAKSG 148
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLG-RVLEAILAQPYPP---VEVVVVVNPSDAETLDVAEEIAARFpdvrlrvirNARLLGPTGKSR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 149 NYNNALRQTSSPLVATFDADMIPYREFLLETVPYFveqveayengddyDKSKVGLIQTPQSfynadifqFNLFSESTLPN 228
Cdd:pfam13641  78 GLNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-------------DSPKVGAVGTPVF--------SLNRSTMLSAL 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 229 EQDFFS---KEINVFNNSHGAALYTGSNTLIFRKAIEDVGGF-PTDTITEDFELGVRINAAGYVNYSTKSPMASGLTPTD 304
Cdd:pfam13641 137 GALEFAlrhLRMMSLRLALGVLPLSGAGSAIRREVLKELGLFdPFFLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTY 216
                         250
                  ....*....|....
gi 1091089803 305 LKSVIKQRVRWGRG 318
Cdd:pfam13641 217 LAASIKQRARWVYG 230
PilZ pfam07238
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ...
509-606 6.89e-16

PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, which is involved in regulation of motility, biofilm formation and virulence of many bacterial pathogens. This domain binds c-di-GMP through RXXXR and [D/N]hSXXG motifs, however, some PilZ domains lack these motifs and do not bind c-di-GMP. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias. This is the canonical PilZ domain whose structure consists of six beta-strands that form a beta barrel, followed by a long C-terminal alpha-helix.


Pssm-ID: 399904  Cd Length: 102  Bit Score: 73.69  E-value: 6.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 509 RSSERFTVDEAMVIEVDDDSYQVRVCDISETGISFYTDLPLYLPKEK-ELTLNLQSRDYHARVKGHVVRVFAIDNGWRYG 587
Cdd:pfam07238   3 RRFPRVPVSLPVTLRDGGGEYKGRLIDISLGGAAIRLPDEPLALGDRvELSLDLLDDGQELALPGRVVRIRPDEDGARVG 82
                          90
                  ....*....|....*....
gi 1091089803 588 VQFSEVPEADKREFYQYIY 606
Cdd:pfam07238  83 VQFLDLDEEQRRLLVRLLF 101
YcgR COG5581
Cyclic di-GMP-binding flagellar brake protein FlgZ/YcgR, contains PilZNR(YcgR) and PilZ ...
523-608 5.25e-11

Cyclic di-GMP-binding flagellar brake protein FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell motility];


Pssm-ID: 444320 [Multi-domain]  Cd Length: 205  Bit Score: 62.70  E-value: 5.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 523 EVDDDSYQVRVCDISETGISFYTDLPLYLPKEKELTLNLQSRDY-HARVKGHVVRVFAIDNG---WRYGVQFSEVPEADK 598
Cdd:COG5581   108 DGEGEPLEGRLLDISGGGLALVLPEPPPLEVGDILELRLDLPDEgEIVVDAEVRRVVEVELGkgkYRLGCEFVDLSEADR 187
                          90
                  ....*....|
gi 1091089803 599 REFYQYIYDR 608
Cdd:COG5581   188 RKIQRYIFEL 197
Cellulose_synt pfam03552
Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose ...
271-492 2.59e-05

Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues, is the major component of wood and thus paper, and is synthesized by plants, most algae, some bacteria and fungi, and even some animals. The genes that synthesize cellulose in higher plants differ greatly from the well-characterized genes found in Acetobacter and Agrobacterium sp. More correctly designated as 'cellulose synthase catalytic subunits', plant cellulose synthase (CesA) proteins are integral membrane proteins, approximately 1,000 amino acids in length. There are a number of highly conserved residues, including several motifs shown to be necessary for processive glycosyltransferase activity.


Pssm-ID: 460970 [Multi-domain]  Cd Length: 715  Bit Score: 47.83  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 271 TITEDFELGVRINAAGY--VNYSTKSPMASGLTPTDLKSVIKQRVRWGRGV--IRSSYNMNIFFNPKLTMGQRIVYINGY 346
Cdd:pfam03552 419 SVTEDILTGFRMHCRGWrsIYCMPKRDAFKGSAPINLSDRLHQVLRWALGSveIFFSRHCPIWYGGRLKFLQRFAYINVG 498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 347 LYWWSFFRRLLYILAPILyTVFHVRVVVSNIWLLFLFWLPS-----FALTRLSMR-------EVSKQYQTQVWGEIVETI 414
Cdd:pfam03552 499 IYPFTSIPLLAYCFLPAI-CLFTGKFIVPTLSNFASIYFLSlflsiIATGILELRwsgvsieEWWRNEQFWVIGGTSAHL 577
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 415 FAPYLFIPMMLESFGISnkkFKVTRKGN----------YT-SWTLYLyaLPYLVLWGLAVYGLV-----TFN--YGKFGs 476
Cdd:pfam03552 578 FAVFQGLLKVIAGIDTS---FTVTSKASddeddefadlYIfKWTTLL--IPPTTILIVNLVGIVagvsrAINsgYPSWG- 651
                         250
                  ....*....|....*.
gi 1091089803 477 ELFYGSIISFWLIYHI 492
Cdd:pfam03552 652 PLFGKLFFAFWVIVHL 667
PLN02638 PLN02638
cellulose synthase A (UDP-forming), catalytic subunit
271-492 5.21e-05

cellulose synthase A (UDP-forming), catalytic subunit


Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 46.84  E-value: 5.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  271 TITEDFELGVRINAAGY--VNYSTKSPMASGLTPTDLKSVIKQRVRWGRGV--IRSSYNMNIF--FNPKLTMGQRIVYIN 344
Cdd:PLN02638   775 SVTEDILTGFKMHARGWrsIYCMPKRPAFKGSAPINLSDRLNQVLRWALGSveILFSRHCPIWygYGGRLKWLERFAYVN 854
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  345 GYLYWWSFFRRLLYILAP--ILYTVFHVRVVVSN---IWLLFLFwLPSFALTRLSMR-------EVSKQYQTQVWGEIVE 412
Cdd:PLN02638   855 TTIYPITSIPLLLYCTLPavCLLTGKFIIPQISNiasIWFISLF-LSIFATGILEMRwsgvgidEWWRNEQFWVIGGVSA 933
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  413 TIFAPYLFIPMMLEsfGIsNKKFKVTRK-----GNYTS-----WTLYLYALPYLVLWGL--AVYGL---VTFNYGKFGSe 477
Cdd:PLN02638   934 HLFAVFQGLLKVLA--GI-DTNFTVTSKasdedGDFAElymfkWTTLLIPPTTLLIINLvgVVAGIsyaINSGYQSWGP- 1009
                          250
                   ....*....|....*
gi 1091089803  478 LFYGSIISFWLIYHI 492
Cdd:PLN02638  1010 LFGKLFFAFWVIVHL 1024
 
Name Accession Description Interval E-value
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
78-321 2.65e-82

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: 261.35  E-value: 2.65e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  78 PDVDVLIATHNEDPELLYKTINACTFMEYPdKSKVHIYVCDDTNRLEVAKLADELGVGYFGLA----DNKDAKSGNYNNA 153
Cdd:cd06421     1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYP-HDKLRVYVLDDGRRPELRALAAELGVEYGYRYltrpDNRHAKAGNLNNA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 154 LRQTSSPLVATFDADMIPYREFLLETVPYFVeqveayengddyDKSKVGLIQTPQSFYNADIFQFnlfSESTLPNEQDFF 233
Cdd:cd06421    80 LAHTTGDFVAILDADHVPTPDFLRRTLGYFL------------DDPKVALVQTPQFFYNPDPFDW---LADGAPNEQELF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 234 SKEINVFNNSHGAALYTGSNTLIFRKAIEDVGGFPTDTITEDFELGVRINAAGYVNYSTKSPMASGLTPTDLKSVIKQRV 313
Cdd:cd06421   145 YGVIQPGRDRWGAAFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRL 224

                  ....*...
gi 1091089803 314 RWGRGVIR 321
Cdd:cd06421   225 RWARGMLQ 232
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
19-629 1.21e-77

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 266.89  E-value: 1.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  19 YLTWRLVATIPWhDSWFALIFGILLWGSEV---VSAITGYI-LIW--NKQ-----KDFELekpeiakerYPDVDVLIATH 87
Cdd:PRK11498  200 YIWWRYTSTLNW-DDPVSLVCGLILLFAETyawIVLVLGYFqVVWplNRQpvplpKDMSL---------WPTVDIFVPTY 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  88 NEDPELLYKTINACTFMEYPdKSKVHIYVCDDTNRLEVAKLADELGVGYFGLADNKDAKSGNYNNALRQTSSPLVATFDA 167
Cdd:PRK11498  270 NEDLNVVKNTIYASLGIDWP-KDKLNIWILDDGGREEFRQFAQEVGVKYIARPTHEHAKAGNINNALKYAKGEFVAIFDC 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 168 DMIPYREFLLETVPYFVEqveayengddyDKsKVGLIQTPQSFYNADIFQFNLFSESTLPNEQDFFSKEINVFNNSHGAA 247
Cdd:PRK11498  349 DHVPTRSFLQMTMGWFLK-----------DK-KLAMMQTPHHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDAT 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 248 LYTGSNTLIFRKAIEDVGGFPTDTITEDFELGVRINAAGYVNYSTKSPMASGLTPTDLKSVIKQRVRWGRGVIRSSYNMN 327
Cdd:PRK11498  417 FFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDN 496
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 328 IFFNPKLTMGQRIVYINGYLYWWSFFRRLLYILAPILYTVFHVRVVVSNIWLLFLFWLPSFALTRLSMREVSKQYQTQVW 407
Cdd:PRK11498  497 PLTGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHASLTNSRIQGKYRHSFW 576
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 408 GEIVETIFAPYLFIPMMLESFGISNKKFKVTRKG-----NYTSWTLylyALPYLVLWGLAVYGLVtfnygkFGS-ELFYG 481
Cdd:PRK11498  577 SEIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGglveeEYVDWVI---SRPYIFLVLLNLVGVA------VGIwRYFYG 647
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 482 S-------IISF-WLIYHIINLTFAIFCALGRPIYRSSERFTVDEAMVIEVDD-DSYQVRVCDISETGISFYTDLPLYLP 552
Cdd:PRK11498  648 PpneiltvIVSLvWVFYNLIILGGAVAVSVESKQVRRSHRVEMTMPAAIAREDgHLFSCTVQDFSDGGLGIKINGQAQLL 727
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091089803 553 KEKELTLNLQSRDYHARVKGHVVRVFaidnGWRYGVQFSEVPEADKREFYQYIYDRinynlpkeKDPWmTTWDDLFE 629
Cdd:PRK11498  728 EGQKVNLLLKRGQQEYVFPTQVTRVM----GNEVGLQLMPLTTQQHIDFVQCTFAR--------ADTW-ALWQDSFP 791
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
42-440 3.65e-35

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 135.64  E-value: 3.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  42 LLWGSEVVSAITGYILIWNKQKDfelekpeiAKERYPDVDVLIATHNEdPELLYKTINACTFMEYPdKSKVHIYVCDDTN 121
Cdd:COG1215     1 LLLLLALLALLYLLLLALARRRR--------APADLPRVSVIIPAYNE-EAVIEETLRSLLAQDYP-KEKLEVIVVDDGS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 122 RLEVAKLADELGVGYFGL----ADNKDAKSGNYNNALRQTSSPLVATFDADMIPYREFLLETVPYFveqveayengddyD 197
Cdd:COG1215    71 TDETAEIARELAAEYPRVrvieRPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-------------A 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 198 KSKVGLiqtpqsfynadifqfnlfsestlpneqdffskeinvfnnshgaalyTGSNTLIFRKAIEDVGGFPTDTITEDFE 277
Cdd:COG1215   138 DPGVGA----------------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLD 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 278 LGVRINAAGYVNYSTKSPMASGLTPTDLKSVIKQRVRWGRGVIRSSYNMNIFFNPKLtmgqrivyingylywwsFFRRLL 357
Cdd:COG1215   172 LSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRR-----------------LLLFLL 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 358 YILAPILYTVFhvrvvVSNIWLLFLFWLPSFALTRLSMREVSKqyqtqvwgeIVETIFAPYLFIPMMLESFGISNKKFKV 437
Cdd:COG1215   235 LLLLPLLLLLL-----LLALLALLLLLLPALLLALLLALRRRR---------LLLPLLHLLYGLLLLLAALRGKKVVWKK 300

                  ...
gi 1091089803 438 TRK 440
Cdd:COG1215   301 TPR 303
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
87-321 2.22e-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: 128.29  E-value: 2.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  87 HNEDPELLYKTINACTFMEYPDkskVHIYVCDDTNRLE-----VAKLADELG--VGYFGLADNKDAKSGNYNNALRQTSS 159
Cdd:cd06435     7 YEEPPEMVKETLDSLAALDYPN---FEVIVIDNNTKDEalwkpVEAHCAQLGerFRFFHVEPLPGAKAGALNYALERTAP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 160 --PLVATFDADMIPYREFLLETVPYFveqveayengddyDKSKVGLIQTPQSFYNAD--IFQFNLFSESTLpneqdFFSK 235
Cdd:cd06435    84 daEIIAVIDADYQVEPDWLKRLVPIF-------------DDPRVGFVQAPQDYRDGEesLFKRMCYAEYKG-----FFDI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 236 EInVFNNSHGAALYTGSNTLIFRKAIEDVGGFPTDTITEDFELGVRINAAGYVNYSTKSPMASGLTPTDLKSVIKQRVRW 315
Cdd:cd06435   146 GM-VSRNERNAIIQHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRW 224

                  ....*.
gi 1091089803 316 GRGVIR 321
Cdd:cd06435   225 AYGAVQ 230
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
78-318 8.37e-24

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: 100.46  E-value: 8.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  78 PDVDVLIATHNEDpELLYKTINACTFMEYPdKSKVHIYVCDDTNRLEVAKLADE--------LGVGYFGLADNKDAKSGN 149
Cdd:cd06437     1 PMVTVQLPVFNEK-YVVERLIEAACALDYP-KDRLEIQVLDDSTDETVRLAREIveeyaaqgVNIKHVRRADRTGYKAGA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 150 YNNALRQTSSPLVATFDADMIPYREFLLETVPYFveqveayengddyDKSKVGLIQTPQSFYNADifqfnlfsESTLPNE 229
Cdd:cd06437    79 LAEGMKVAKGEYVAIFDADFVPPPDFLQKTPPYF-------------ADPKLGFVQTRWGHINAN--------YSLLTRV 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 230 QDF-----FSKEINVFNNSHGAALYTGSNTLIFRKAIEDVGGFPTDTITEDFELGVRINAAGYVNYSTKSPMASGLTPTD 304
Cdd:cd06437   138 QAMsldyhFTIEQVARSSTGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPAS 217
                         250
                  ....*....|....
gi 1091089803 305 LKSVIKQRVRWGRG 318
Cdd:cd06437   218 MSAYRSQQHRWSKG 231
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
78-318 2.73e-19

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: 87.43  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  78 PDVDVLIATHNEDPELLyKTINACTFMEYPDkskVHIYVCDDTNRLEVAKLADELGVGY---------FGLADNKDAKSG 148
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLG-RVLEAILAQPYPP---VEVVVVVNPSDAETLDVAEEIAARFpdvrlrvirNARLLGPTGKSR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 149 NYNNALRQTSSPLVATFDADMIPYREFLLETVPYFveqveayengddyDKSKVGLIQTPQSfynadifqFNLFSESTLPN 228
Cdd:pfam13641  78 GLNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-------------DSPKVGAVGTPVF--------SLNRSTMLSAL 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 229 EQDFFS---KEINVFNNSHGAALYTGSNTLIFRKAIEDVGGF-PTDTITEDFELGVRINAAGYVNYSTKSPMASGLTPTD 304
Cdd:pfam13641 137 GALEFAlrhLRMMSLRLALGVLPLSGAGSAIRREVLKELGLFdPFFLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTY 216
                         250
                  ....*....|....
gi 1091089803 305 LKSVIKQRVRWGRG 318
Cdd:pfam13641 217 LAASIKQRARWVYG 230
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
82-275 2.17e-16

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: 77.65  E-value: 2.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  82 VLIATHNEDpELLYKTINACTFMEYPdksKVHIYV-----CDDTNRLEVAKLADELGVGYFGLADNKDAKSGNYNNALRQ 156
Cdd:cd06423     1 IIVPAYNEE-AVIERTIESLLALDYP---KLEVIVvddgsTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 157 TSSPLVATFDADMIPYREFLLE-TVPYFveqveayengddyDKSKVGLIQTPQSFYNAdifqfnlfSESTLPNEQDFFSK 235
Cdd:cd06423    77 AKGDIVVVLDADTILEPDALKRlVVPFF-------------ADPKVGAVQGRVRVRNG--------SENLLTRLQAIEYL 135
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1091089803 236 EINVF-----NNSHGAALYTGSNTLIFRKAIEDVGGFPTDTITED 275
Cdd:cd06423   136 SIFRLgrraqSALGGVLVLSGAFGAFRREALREVGGWDEDTLTED 180
PilZ pfam07238
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ...
509-606 6.89e-16

PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, which is involved in regulation of motility, biofilm formation and virulence of many bacterial pathogens. This domain binds c-di-GMP through RXXXR and [D/N]hSXXG motifs, however, some PilZ domains lack these motifs and do not bind c-di-GMP. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias. This is the canonical PilZ domain whose structure consists of six beta-strands that form a beta barrel, followed by a long C-terminal alpha-helix.


Pssm-ID: 399904  Cd Length: 102  Bit Score: 73.69  E-value: 6.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 509 RSSERFTVDEAMVIEVDDDSYQVRVCDISETGISFYTDLPLYLPKEK-ELTLNLQSRDYHARVKGHVVRVFAIDNGWRYG 587
Cdd:pfam07238   3 RRFPRVPVSLPVTLRDGGGEYKGRLIDISLGGAAIRLPDEPLALGDRvELSLDLLDDGQELALPGRVVRIRPDEDGARVG 82
                          90
                  ....*....|....*....
gi 1091089803 588 VQFSEVPEADKREFYQYIY 606
Cdd:pfam07238  83 VQFLDLDEEQRRLLVRLLF 101
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
166-385 1.51e-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: 75.45  E-value: 1.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 166 DADMIPYREFLLETVPYFveqveayengddyDKSKVGLIQTPQSFYNADIFQFNLFSESTlpNEQDFFSkeINVFNNSHG 245
Cdd:pfam13632   6 DADTVLPPDCLLGIANEM-------------ASPEVAIIQGPILPMNVGNYLEELAALFF--ADDHGKS--IPVRMALGR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 246 AALYTGSNTLIFRKAIEDVGGFPTDTITEDFELGVRINAAGY-VNYSTkSPMASGLTPTDLKSVIKQRVRWGRGvirssY 324
Cdd:pfam13632  69 VLPFVGSGAFLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYrVRFAP-YSAVYEKSPLTFRDFLRQRRRWAYG-----C 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091089803 325 NMNIFFNpkltmgqRIVYINGYLYWWSFFRRLLYILAPILYTVFHVrvvvsnIWLLFLFWL 385
Cdd:pfam13632 143 LLILLIR-------LLGYLGTLLWSGLPLALLLLLLFSISSLALVL------LLLALLAGL 190
YcgR COG5581
Cyclic di-GMP-binding flagellar brake protein FlgZ/YcgR, contains PilZNR(YcgR) and PilZ ...
523-608 5.25e-11

Cyclic di-GMP-binding flagellar brake protein FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell motility];


Pssm-ID: 444320 [Multi-domain]  Cd Length: 205  Bit Score: 62.70  E-value: 5.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 523 EVDDDSYQVRVCDISETGISFYTDLPLYLPKEKELTLNLQSRDY-HARVKGHVVRVFAIDNG---WRYGVQFSEVPEADK 598
Cdd:COG5581   108 DGEGEPLEGRLLDISGGGLALVLPEPPPLEVGDILELRLDLPDEgEIVVDAEVRRVVEVELGkgkYRLGCEFVDLSEADR 187
                          90
                  ....*....|
gi 1091089803 599 REFYQYIYDR 608
Cdd:COG5581   188 RKIQRYIFEL 197
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
78-318 3.78e-10

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: 60.73  E-value: 3.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  78 PDVDVLIATHNEdPELLYKTINACTFMEYPdKSKVHI-YVC--DDTNRLEVAKLAD-----ELGVGYFGLADNKdAKSGN 149
Cdd:cd06427     1 PVYTILVPLYKE-AEVLPQLIASLSALDYP-RSKLDVkLLLeeDDEETIAAARALRlpsifRVVVVPPSQPRTK-PKACN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 150 YnnALRQTSSPLVATFDADMIPYREFLLETVpyfveqvEAYENGDDydksKVGLIQTPQSFYNAD--------IFQFNLF 221
Cdd:cd06427    78 Y--ALAFARGEYVVIYDAEDAPDPDQLKKAV-------AAFARLDD----KLACVQAPLNYYNARenwltrmfALEYAAW 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 222 SESTLPneqdFFSKEinvfnnshGAALYTGSNTLIFR-KAIEDVGGFPTDTITEDFELGVRINAAGYvnystKSPMASGL 300
Cdd:cd06427   145 FDYLLP----GLARL--------GLPIPLGGTSNHFRtDVLRELGGWDPFNVTEDADLGLRLARAGY-----RTGVLNST 207
                         250       260
                  ....*....|....*....|..
gi 1091089803 301 T----PTDLKSVIKQRVRWGRG 318
Cdd:cd06427   208 TleeaNNALGNWIRQRSRWIKG 229
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
81-263 7.48e-08

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: 52.78  E-value: 7.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  81 DVLIATHNEdPELLYKTINACTFMEYPDKskvHIYVCDDTNRLEVAKLADELGVGYFGLA----DNKDAKSGNYNNALRQ 156
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF---EIIVVDDGSTDGTVEIAEEYAKKDPRVRvirlPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 157 TSSPLVATFDADMIPYREFLLETVPYFVEqveayengDDYDKSKVGLIQTPQSFYNadIFQFNLFSESTLPNEQDFFSKE 236
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEE--------DGADVVVGSRYVIFGETGE--YRRASRITLSRLPFFLGLRLLG 146
                         170       180
                  ....*....|....*....|....*..
gi 1091089803 237 INVFNNSHGAALYtgsntliFRKAIED 263
Cdd:pfam00535 147 LNLPFLIGGFALY-------RREALEE 166
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
82-315 2.05e-06

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: 49.59  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  82 VLIATHNEDpELLYKTINACTFMEYPdKSKVHIYVCDDTNRLEVAK-LADELGVGYFGLA--DNKDAKSGNYNNAL---- 154
Cdd:cd04192     1 VVIAARNEA-ENLPRLLQSLSALDYP-KEKFEVILVDDHSTDGTVQiLEFAAAKPNFQLKilNNSRVSISGKKNALttai 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 155 RQTSSPLVATFDADMIPYREFLLETVPYfveqveayengddYDKSKVGLIQTPQSFYNADIF--QFNLFSE-STLPNEQD 231
Cdd:cd04192    79 KAAKGDWIVTTDADCVVPSNWLLTFVAF-------------IQKEQIGLVAGPVIYFKGKSLlaKFQRLDWlSLLGLIAG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 232 FFSKEINVFNNshgaalytGSNTLIFRKAIEDVGGFPT--DTITEDFELGVRINAAGYVN-YSTKSPMASGLTP--TDLK 306
Cdd:cd04192   146 SFGLGKPFMCN--------GANMAYRKEAFFEVGGFEGndHIASGDDELLLAKVASKYPKvAYLKNPEALVTTQpvTSWK 217

                  ....*....
gi 1091089803 307 SVIKQRVRW 315
Cdd:cd04192   218 ELLNQRKRW 226
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
146-317 4.65e-06

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


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 47.66  E-value: 4.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 146 KSGNYNNALRQTSSPLVATFDADMIPYREFLLETVPYFVEqveayengddydkSKVGLIQTPqSFYNadifqfnlfsest 225
Cdd:pfam13506  18 KVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLAD-------------PKVGLVTSP-PVGS------------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 226 lpNEQDFFSKEINVFNNSHGAALY---------TGSNTLIFRKAIEDVGGFPT--DTITEDFELGVRINAAGYVNYSTKS 294
Cdd:pfam13506  71 --DPKGLAAALEAAFFNTLAGVLQaalsgigfaVGMSMAFRRADLERIGGFEAlaDYLAEDYALGKLLRAAGLKVVLSPR 148
                         170       180
                  ....*....|....*....|....*
gi 1091089803 295 PMASGLTP--TDLKSVIKQRVRWGR 317
Cdd:pfam13506 149 PILQTSGPrrTSFRAFMARQLRWAR 173
Cellulose_synt pfam03552
Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose ...
271-492 2.59e-05

Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues, is the major component of wood and thus paper, and is synthesized by plants, most algae, some bacteria and fungi, and even some animals. The genes that synthesize cellulose in higher plants differ greatly from the well-characterized genes found in Acetobacter and Agrobacterium sp. More correctly designated as 'cellulose synthase catalytic subunits', plant cellulose synthase (CesA) proteins are integral membrane proteins, approximately 1,000 amino acids in length. There are a number of highly conserved residues, including several motifs shown to be necessary for processive glycosyltransferase activity.


Pssm-ID: 460970 [Multi-domain]  Cd Length: 715  Bit Score: 47.83  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 271 TITEDFELGVRINAAGY--VNYSTKSPMASGLTPTDLKSVIKQRVRWGRGV--IRSSYNMNIFFNPKLTMGQRIVYINGY 346
Cdd:pfam03552 419 SVTEDILTGFRMHCRGWrsIYCMPKRDAFKGSAPINLSDRLHQVLRWALGSveIFFSRHCPIWYGGRLKFLQRFAYINVG 498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 347 LYWWSFFRRLLYILAPILyTVFHVRVVVSNIWLLFLFWLPS-----FALTRLSMR-------EVSKQYQTQVWGEIVETI 414
Cdd:pfam03552 499 IYPFTSIPLLAYCFLPAI-CLFTGKFIVPTLSNFASIYFLSlflsiIATGILELRwsgvsieEWWRNEQFWVIGGTSAHL 577
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 415 FAPYLFIPMMLESFGISnkkFKVTRKGN----------YT-SWTLYLyaLPYLVLWGLAVYGLV-----TFN--YGKFGs 476
Cdd:pfam03552 578 FAVFQGLLKVIAGIDTS---FTVTSKASddeddefadlYIfKWTTLL--IPPTTILIVNLVGIVagvsrAINsgYPSWG- 651
                         250
                  ....*....|....*.
gi 1091089803 477 ELFYGSIISFWLIYHI 492
Cdd:pfam03552 652 PLFGKLFFAFWVIVHL 667
PLN02638 PLN02638
cellulose synthase A (UDP-forming), catalytic subunit
271-492 5.21e-05

cellulose synthase A (UDP-forming), catalytic subunit


Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 46.84  E-value: 5.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  271 TITEDFELGVRINAAGY--VNYSTKSPMASGLTPTDLKSVIKQRVRWGRGV--IRSSYNMNIF--FNPKLTMGQRIVYIN 344
Cdd:PLN02638   775 SVTEDILTGFKMHARGWrsIYCMPKRPAFKGSAPINLSDRLNQVLRWALGSveILFSRHCPIWygYGGRLKWLERFAYVN 854
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  345 GYLYWWSFFRRLLYILAP--ILYTVFHVRVVVSN---IWLLFLFwLPSFALTRLSMR-------EVSKQYQTQVWGEIVE 412
Cdd:PLN02638   855 TTIYPITSIPLLLYCTLPavCLLTGKFIIPQISNiasIWFISLF-LSIFATGILEMRwsgvgidEWWRNEQFWVIGGVSA 933
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  413 TIFAPYLFIPMMLEsfGIsNKKFKVTRK-----GNYTS-----WTLYLYALPYLVLWGL--AVYGL---VTFNYGKFGSe 477
Cdd:PLN02638   934 HLFAVFQGLLKVLA--GI-DTNFTVTSKasdedGDFAElymfkWTTLLIPPTTLLIINLvgVVAGIsyaINSGYQSWGP- 1009
                          250
                   ....*....|....*
gi 1091089803  478 LFYGSIISFWLIYHI 492
Cdd:PLN02638  1010 LFGKLFFAFWVIVHL 1024
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
79-322 1.15e-04

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: 44.17  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  79 DVDVLIATHNEDPELLYKTINACTFMEyPDKSkvhIYVCDDTNRLEVAKLADELG-VGYFGLADNKDAKSGNYNNALRQT 157
Cdd:cd06434     1 DVTVIIPVYDEDPDVFRECLRSILRQK-PLEI---IVVTDGDDEPYLSILSQTVKyGGIFVITVPHPGKRRALAEGIRHV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 158 SSPLVATFDADMIPYREFLLETVPYFVEQveayengddydksKVGLIQTPQSFYNAD----IFQFNLFSEStlpneqDFF 233
Cdd:cd06434    77 TTDIVVLLDSDTVWPPNALPEMLKPFEDP-------------KVGGVGTNQRILRPRdskwSFLAAEYLER------RNE 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 234 skEINVFNNSHGAALYTGSNTLIFRKAI------------EDVGGFPTDtITEDFELGVRINAAGYVNYSTKSPMASGLT 301
Cdd:cd06434   138 --EIRAAMSYDGGVPCLSGRTAAYRTEIlkdflfleeftnETFMGRRLN-AGDDRFLTRYVLSHGYKTVYQYTSEAYTET 214
                         250       260
                  ....*....|....*....|.
gi 1091089803 302 PTDLKSVIKQRVRWGRGVIRS 322
Cdd:cd06434   215 PENYKKFLKQQLRWSRSNWRS 235
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
78-287 1.40e-04

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 43.54  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  78 PDVDVLIATHNEdPELLYKTINACTFMEYPDkskVHIYVCDD--TNR-LEVAK--LADELGVGYFGLADNKDaKSGNYNN 152
Cdd:COG0463     2 PLVSVVIPTYNE-EEYLEEALESLLAQTYPD---FEIIVVDDgsTDGtAEILRelAAKDPRIRVIRLERNRG-KGAARNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 153 ALRQTSSPLVATFDADMIPYREFLletvpyfVEQVEAYENGDdydkskvgliqtpqsfynADIFQFNLFSESTLPNEQDF 232
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKL-------EELVAALEEGP------------------ADLVYGSRLIREGESDLRRL 131
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1091089803 233 FSKEINVFNNSHGAALYTGSNTLIFRKAIEDVgGFPTDTItEDFELgVRINAAGY 287
Cdd:COG0463   132 GSRLFNLVRLLTNLPDSTSGFRLFRREVLEEL-GFDEGFL-EDTEL-LRALRHGF 183
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
78-290 5.53e-04

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 41.90  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  78 PDVDVLIATHNeDPELLYKTINACTFMEYPDkskVHIYVCDDTNRLEVAKLADELGVGYFGLADNKDAK--SGNYNNALR 155
Cdd:COG1216     3 PKVSVVIPTYN-RPELLRRCLESLLAQTYPP---FEVIVVDNGSTDGTAELLAALAFPRVRVIRNPENLgfAAARNLGLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 156 QTSSPLVATFDADMIPYREFLletvpyfveqveayengddydkskvgliqtpqsfynadifqfnlfsestlpneqdffsk 235
Cdd:COG1216    79 AAGGDYLLFLDDDTVVEPDWL----------------------------------------------------------- 99
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1091089803 236 einvfnnshgAALYTGSNTLIFRKAIEDVGGFPTDTIT--EDFELGVRINAAGYVNY 290
Cdd:COG1216   100 ----------ERLLAAACLLIRREVFEEVGGFDERFFLygEDVDLCLRLRKAGYRIV 146
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
82-287 7.98e-04

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


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 41.53  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  82 VLIATH-NEDPELLYKTINACTFMEYPDKSKVHIY----------VCDDTNR---LEVAKLADELGVGYfgladnkdaks 147
Cdd:cd04195     2 VLMSVYiKEKPEFLREALESILKQTLPPDEVVLVKdgpvtqslneVLEEFKRklpLKVVPLEKNRGLGK----------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 148 gNYNNALRQTSSPLVATFDADMIPYREFLLETVPYFVEQVEAYENGD-----DYDKSKVGLIQTPQSfyNADIFQFnlfs 222
Cdd:cd04195    71 -ALNEGLKHCTYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGgvlefDSDGNDIGKRRLPTS--HDDILKF---- 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091089803 223 estlpneqdffSKEINVFNnsHGAALYTgsntlifRKAIEDVGGFPTDTITEDFELGVRINAAGY 287
Cdd:cd04195   144 -----------ARRRSPFN--HPTVMFR-------KSKVLAVGGYQDLPLVEDYALWARMLANGA 188
PLN02400 PLN02400
cellulose synthase
266-492 1.18e-03

cellulose synthase


Pssm-ID: 215224 [Multi-domain]  Cd Length: 1085  Bit Score: 42.27  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  266 GFPTDTITEDFELGVRINAAGYVN-YSTKS-PMASGLTPTDLKSVIKQRVRWGRGVIRS--SYNMNIFF--NPKLTMGQR 339
Cdd:PLN02400   775 GWIYGSVTEDILTGFKMHARGWISiYCMPPrPAFKGSAPINLSDRLNQVLRWALGSIEIllSRHCPIWYgyNGRLKLLER 854
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  340 IVYINGYLYWWSFFRRLLYILAPILYTVFHVRVV--VSN---IWLLFLFwLPSFALTRLSMR-------EVSKQYQTQVW 407
Cdd:PLN02400   855 LAYINTIVYPITSIPLLAYCVLPAFCLITNKFIIpeISNyasMWFILLF-ISIFATGILELRwsgvgieDWWRNEQFWVI 933
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  408 GEIVETIFAPYlfiPMMLESFGISNKKFKVTRK-----GNYTS-----WTLYLYALPYLVLWGLA--VYGL---VTFNYG 472
Cdd:PLN02400   934 GGTSAHLFAVF---QGLLKVLAGIDTNFTVTSKasdedGDFAElyvfkWTSLLIPPTTVLLVNLVgiVAGVsyaINSGYQ 1010
                          250       260
                   ....*....|....*....|
gi 1091089803  473 KFGSeLFYGSIISFWLIYHI 492
Cdd:PLN02400  1011 SWGP-LFGKLFFAIWVIAHL 1029
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
250-317 1.29e-03

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 40.66  E-value: 1.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091089803 250 TGSNTLIFRKAIEDVGGFP--TDTITEDFELGVRINAAGY-VNYSTKsPMASGLTPTDLKSVIKQRVRWGR 317
Cdd:cd02520   125 FGKSMALRREVLDAIGGFEafADYLAEDYFLGKLIWRLGYrVVLSPY-VVMQPLGSTSLASFWRRQLRWSR 194
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
82-233 3.30e-03

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: 39.03  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  82 VLIATHNEDPELLYkTINACTFMEYPDkskVHIYVCD----DTNRLEVAKLADELGVGYFGLADNKDAKSGNYNNALRQT 157
Cdd:cd00761     1 VIIPAYNEEPYLER-CLESLLAQTYPN---FEVIVVDdgstDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091089803 158 SSPLVATFDADMIPYREFLLetvpyfvEQVEAYENGDDYDkskvGLIQTPQSFYNADIF-QFNLFSESTLPNEQDFF 233
Cdd:cd00761    77 RGEYILFLDADDLLLPDWLE-------RLVAELLADPEAD----AVGGPGNLLFRRELLeEIGGFDEALLSGEEDDD 142
PRK05454 PRK05454
glucans biosynthesis glucosyltransferase MdoH;
6-218 3.51e-03

glucans biosynthesis glucosyltransferase MdoH;


Pssm-ID: 235476 [Multi-domain]  Cd Length: 605  Bit Score: 40.63  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803   6 RILYFVAFVTTAFYLTWRLVATIPWHD-SW--------FALIFGILLWGseVVSAITGYILIwNKQKDFELEKPEIAKER 76
Cdd:PRK05454   42 RLILLGLTLAQTAVATWEMKAVLPYGGwTLlepallvlFALLFAWISLG--FWTALMGFLQL-LRGRDKYSISASAAGDP 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803  77 YPDVD----VLIATHNEDPELLYKTINAC--TFMEYPDKSKVHIYVCDDTNRLEVA--------KLADELG----VGYFG 138
Cdd:PRK05454  119 PPPPEartaILMPIYNEDPARVFAGLRAMyeSLAATGHGAHFDFFILSDTRDPDIAaaeeaawlELRAELGgegrIFYRR 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 139 LADNKDAKSGNynnalrqtssplVATF--------------DAD--MIPyrefllETVpyfVEQVEAYENGDDydkskVG 202
Cdd:PRK05454  199 RRRNVGRKAGN------------IADFcrrwggaydymvvlDADslMSG------DTL---VRLVRLMEANPR-----AG 252
                         250       260
                  ....*....|....*....|..
gi 1091089803 203 LIQTP------QSFYnADIFQF 218
Cdd:PRK05454  253 LIQTLpvavgaDTLF-ARLQQF 273
nfrB PRK11234
phage adsorption protein NrfB;
251-396 5.55e-03

phage adsorption protein NrfB;


Pssm-ID: 236884 [Multi-domain]  Cd Length: 727  Bit Score: 40.11  E-value: 5.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 251 GSNTLIFRKAI----EDVGG--FPTDTITEDFELGVRINAAG----YVNYSTKSPMASG-------------------LT 301
Cdd:PRK11234  231 GVGTCFSRRAVtallEDGDGiaFDVQSLTEDYDIGFRLKEKGmreiFVRFPVVDEAKEReqrkflqhartsnmicvreYF 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091089803 302 PTDLKSVIKQRVRWGRG-VIRSSYNMNIFFNPKLTM----GQR--IVYINGYLYWWSFFRRLLYILAPILY-TVFHVRVV 373
Cdd:PRK11234  311 PDTFSAAVRQKSRWIIGiVFQGFKTLGWTSSLTLNYflwrDRKgaITNFVSFLAMLLMLQLLLLLLYESLWpDAWHFLSI 390
                         170       180
                  ....*....|....*....|....*
gi 1091089803 374 VSNIWLLFLFWLPSFALT--RLSMR 396
Cdd:PRK11234  391 FSGSAWLMTLLWLNFGLMvnRIVQR 415
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
257-322 9.94e-03

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: 38.37  E-value: 9.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091089803 257 FRKAI-EDVGGFPTD-TITEDFELGVRINAAGYVNYSTKSPMASGLTPTDLKSVIKQRVRWGRGVIRS 322
Cdd:cd02525   163 YRREVfEKVGGFDESlVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKWRART 230
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH