|
Name |
Accession |
Description |
Interval |
E-value |
| CelA |
TIGR03030 |
cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 ... |
41-701 |
0e+00 |
|
cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 polymerization of glucose residues in the formation of cellulose. In bacteria, the substrate is UDP-glucose. The synthase consists of two subunits (or domains in the frequent cases where it is encoded as a single polypeptide), the catalytic domain modelled here and the regulatory domain (pfam03170). The regulatory domain binds the allosteric activator cyclic di-GMP. The protein is membrane-associated and probably assembles into multimers such that the individual cellulose strands can self-assemble into multi-strand fibrils.
Pssm-ID: 274400 [Multi-domain] Cd Length: 713 Bit Score: 792.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 41 SVRIDPALQGWVSIGTVTLLLVLNRRRGRGITVFLMMLSLLVSLRYIVWRLTATVQFSNWLQTALAVLLLLAEAYALMTL 120
Cdd:TIGR03030 26 TAPVTLETQLIIAGSAFLLLLILKRFNGKRPRLLLLVLSVFISLRYLWWRLTETLPFDNTLNFIFGTLLLLAELYSITIL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 121 CLSYFQMAWPLRRREHPLPEDMAQWPSVDVFVPSYNEELSLVRSTVLGALDLDWPADRLNVYILDDG------------- 187
Cdd:TIGR03030 106 LLGYFQTVRPLDRTPVPLPLDPEEWPTVDVFIPTYNEDLEIVATTVLAAKNMDYPADKFRVWILDDGgtdqkrndpdpeq 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 188 -----RRKAFHDFAVEAGAGYIIRAENNHAKAGNLNHALAVTDSPFAVIFDCDHVPTRGFLRRTIGWMMADPNLALLQTP 262
Cdd:TIGR03030 186 aeaaqRREELKEFCRKLGVNYITRPRNVHAKAGNINNALKHTDGELILIFDADHVPTRDFLQRTVGWFVEDPKLFLVQTP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 263 HHFYAPDPFQRNLAGGMHVPPEGNMFYGLVQDGNDFWDATFFCGSCAIIRREAVMGIGGFATETVTEDAHTALKMQRRGW 342
Cdd:TIGR03030 266 HFFVSPDPIERNLGTFRRMPNENELFYGLIQDGNDFWNAAFFCGSAAVLRREALDEIGGIAGETVTEDAETALKLHRRGW 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 343 GTAYLREPLAAGLATERLILHIGQRVRWARGMIQIMRLDNPMLGAGLRWEQRLCYLSAMSHFLFAIPRLTFLVSPLAFLF 422
Cdd:TIGR03030 346 NSAYLDRPLIAGLAPETLSGHIGQRIRWAQGMMQIFRLDNPLLKRGLSFPQRLCYLNAMLFWFFPLPRVIFLTAPLAYLF 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 423 LGQNIIAASPLAISVYALPHIFHSVITLSRIEGRWRYSFWSEIYETSLALFLVRITIVTLLQPHKGKFNVTDKGGLLARG 502
Cdd:TIGR03030 426 FGLNIFVASALEILAYALPHMLHSLLTNSYLFGRVRWPFWSEVYETVLAVYLLPPVLVTLLNPKKPKFNVTPKGELLDED 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 503 YFDwDAVYPNVILAGVLCAALLRGVFGIVWQFHDRLALqsfILNTLWVVISLIIVLASIAVGRETRQTRNAPRVSVRLPV 582
Cdd:TIGR03030 506 YFS-PLSRPYLILFALILAGLAFGLYRIYGYPIERGVL---LVVLGWNLLNLILLGAALAVVAERRQRRSSPRIPCKIPA 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 583 VVTDAHGRQMEGHTHDISLGGLAVG--TRLATPDMVGGEVTVRYDSARDGIHVGVPARVLDARDGTLRLRWAVRDLEDER 660
Cdd:TIGR03030 582 EVQRDGGRWVEATVEDASVGGLGIKinAQGAPGPQLGAGVLVQIRPKRNGLPALKPARVRGAGGVMIGLEFSPLNVQQVR 661
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 4827175 661 QVVSMVFGRNDAWAGWADFA--PDRPLRSLAMVFRSIGGLLRR 701
Cdd:TIGR03030 662 EIVDLVFARSDRWVALWEERrrPDGPLRGLADFLKIALRGLFR 704
|
|
| bcsA |
PRK11498 |
cellulose synthase catalytic subunit; Provisional |
85-710 |
0e+00 |
|
cellulose synthase catalytic subunit; Provisional
Pssm-ID: 236918 [Multi-domain] Cd Length: 852 Bit Score: 731.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 85 RYIVWRLTATVQFSNWLQTALAVLLLLAEAYALMTLCLSYFQMAWPLRRREHPLPEDMAQWPSVDVFVPSYNEELSLVRS 164
Cdd:PRK11498 199 RYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 165 TVLGALDLDWPADRLNVYILDDGRRKAFHDFAVEAGAGYIIRAENNHAKAGNLNHALAVTDSPFAVIFDCDHVPTRGFLR 244
Cdd:PRK11498 279 TIYASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKYIARPTHEHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFLQ 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 245 RTIGWMMADPNLALLQTPHHFYAPDPFQRNLAGGMHVPPEGNMFYGLVQDGNDFWDATFFCGSCAIIRREAVMGIGGFAT 324
Cdd:PRK11498 359 MTMGWFLKDKKLAMMQTPHHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAV 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 325 ETVTEDAHTALKMQRRGWGTAYLREPLAAGLATERLILHIGQRVRWARGMIQIMRLDNPMLGAGLRWEQRLCYLSAMSHF 404
Cdd:PRK11498 439 ETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLTGKGLKLAQRLCYANAMLHF 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 405 LFAIPRLTFLVSPLAFLFLGQNIIAASPLAISVYALPHIFHSVITLSRIEGRWRYSFWSEIYETSLALFLVRITIVTLLQ 484
Cdd:PRK11498 519 LSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHASLTNSRIQGKYRHSFWSEIYETVLAWYIAPPTTVALFN 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 485 PHKGKFNVTDKGGLLARGYFDWDAVYPNVILAGVLCAALLRGVFGIVWQFHDRLAlqSFILNTLWVVISLIIVLASIAVG 564
Cdd:PRK11498 599 PHKGKFNVTAKGGLVEEEYVDWVISRPYIFLVLLNLVGVAVGIWRYFYGPPNEIL--TVIVSLVWVFYNLIILGGAVAVS 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 565 RETRQTRNAPRVSVRLPVVVTDAHGRQMEGHTHDISLGGLAVGTRLATPDMVGGEVTVRYDsaRDGIHVGVPARVLDARD 644
Cdd:PRK11498 677 VESKQVRRSHRVEMTMPAAIAREDGHLFSCTVQDFSDGGLGIKINGQAQLLEGQKVNLLLK--RGQQEYVFPTQVTRVMG 754
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4827175 645 GTLRLRWAVRDLEDERQVVSMVFGRNDAWAGWAD-FAPDRPLRSLAMVFRsIGGLLRRRPAE-APRAL 710
Cdd:PRK11498 755 NEVGLQLMPLTTQQHIDFVQCTFARADTWALWQDsFPEDKPLESLLDILK-LGFRGYRHLAEfAPPSV 821
|
|
| BcsB |
pfam03170 |
Bacterial cellulose synthase subunit; This family includes bacterial proteins involved in ... |
808-1414 |
0e+00 |
|
Bacterial cellulose synthase subunit; This family includes bacterial proteins involved in cellulose synthesis. Cellulose synthesis has been identified in several bacteria. In Agrobacterium tumefaciens, for instance, cellulose has a pathogenic role: it allows the bacteria to bind tightly to their host plant cells. While several enzymatic steps are involved in cellulose synthesis, potentially the only step unique to this pathway is that catalyzed by cellulose synthase. This enzyme is a multi subunit complex. This family encodes a subunit that is thought to bind the positive effector cyclic di-GMP. This subunit is found in several different bacterial cellulose synthase enzymes. The first recognized sequence for this subunit is BcsB. In the AcsII cellulose synthase, this subunit and the subunit corresponding to BcsA are found in the same protein. Indeed, this alignment only includes the C-terminal half of the AcsAII synthase, which corresponds to BcsB.
Pssm-ID: 427177 Cd Length: 607 Bit Score: 624.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 808 TRTLTFRNLGATtGPLTLRGYSPLQGLDVVVPANRVVTHAQLTLSGALSPSLLPEANAVTVTLNEQYVGTLKVDPQHPQF 887
Cdd:pfam03170 3 TQTLSFADLGAP-GPLTLRGVDGSGGLPFGLRADQVVTNASLNLAYTYSPALLPELSHLKVLLNGELLGTLPLPKEQAGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 888 GPVSFDIDPLYFTGDNKLNFHFAGEYRRDCNDLFNEILWARISDMSRITLTTVRITPERKLSRLPAPFFDPNQRSTLRVP 967
Cdd:pfam03170 82 LTVQIDIPPRLLVDFNRLRFELIGHYTLDCEDPAHSSLWATISPDSYLELTYQPLPLPNDLSLLPAPFFDPRDMRPLTLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 968 VVLPATGDRGALRAAGLVASWFGRIADFRKLSFPVST-TIPASGNAVEVGVNL-PVDAEGGRPA--GPMLAEVANPNDRW 1043
Cdd:pfam03170 162 FVFPATPDPGTLQAAGIVASWFGALAGYRGADFPVSTdTLPASGNAVVFATNDeRPGGLADLPAvnGPTLAVIDNPQDPY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1044 GTVLVVTGRTAQEVEVAARALVFSPDTLGGVASKVVSDVSLETRHPYDAPAFVPTDRPVRFGELV-GAADLQGGGFAPAG 1122
Cdd:pfam03170 242 GKLLLVTGRDDAELRQAARALALGSALLSGDTVVVDNVVLLPPRKPYDAPRWVPTDRPVRLGELGtAPQDLQVSGLRPDP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1123 MTLPFHLPPDLYTWRGRPFLMNMWVRAPGGPVVDleTSRVDVSLNNNYLQSYTLSPPGLWRKWSeRLVNQHAGAVGHVTa 1202
Cdd:pfam03170 322 IRVNFRLPPDLFLWRGRGIPLDLRYRYTAPPRID--DSRLDVSLNGQFLGSLPLSSEGGLSFLL-RLGGDSRQESYTVR- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1203 LPPWLLFGQNQLQFNFDARPIDRGACR-RTPGDIHMSVDSDSTLDFRRGYHFAEMPNLSYFAEAAFPFSRMADLSETTVV 1281
Cdd:pfam03170 398 LPPYLLGPRNQLQFDFNLVPLKDGECQtTLPDNLRAAIDPDSTIDLSGYPHYAALPNLAAFANAGFPFTRLADLSETAVV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1282 LPDHPDTGTTGAFLDLMGFFGASTWYPAAGVTVMGADEVAQTpPKGDIVVLGTAAQLgGAASGLLARSPYVIHDRHITVG 1361
Cdd:pfam03170 478 LPDRPTAAEISALLNLMGRMGAATGYPALRVTVTDAADVESL-ADKDLLVIGSLPQQ-PLLQRLLKSLPLLLDGGRLRVP 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 4827175 1362 QRMGLQGIWYLFQDH-DHAGLKDGVTANLNAPIAeagVLLAAQSPYDSQRSVVA 1414
Cdd:pfam03170 556 DRLSLQRSWPGGRLQrDDAPADADLSLSSSGPLA---ALVGFESPYNPGRSVVA 606
|
|
| PRK11114 |
PRK11114 |
cellulose biosynthesis cyclic di-GMP-binding regulatory protein BcsB; |
744-1508 |
0e+00 |
|
cellulose biosynthesis cyclic di-GMP-binding regulatory protein BcsB;
Pssm-ID: 236851 [Multi-domain] Cd Length: 756 Bit Score: 563.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 744 TASAALFVAFTALVPAAMAQEAPSPDQSGVTAetpfgdsnTGVVPDALPAIDPAVADRisdaevTRTLTFRNLGATTGPL 823
Cdd:PRK11114 9 CALALGMSAFPAFATAAAPATQPLANAAGQVM--------PAAPAAAAPVVAQAAPSR------DVTLTFAQLGPAPGPI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 824 TLRGYSPLQGLDVVVPANRVVTHAQLTLSGALSPSLLPEANAVTVTLNEQYVGTLKVDpqHPQFG-PVSF--DIDPLYFT 900
Cdd:PRK11114 75 VLRGVDPQGGIEFGVRSDEVVTKARLNLEYTYSPALLPDLSHLKVYLNGELMGTLPLD--KEQLGkKVLAqlPIDPRFIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 901 GDNKLNFHFAGEYRRDCNDLFNEILWARISDMSRITLTTVRITPERKLSRLPAPFFDPNQRSTLRVPVVLPATGDRGALR 980
Cdd:PRK11114 153 DFNRLRLEFIGHYTDVCEDPASSSLWADISPSSSLDLTYQKLPLPNDLALLPAPFFDPRDNRPLTLPFVFAAKPDLATLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 981 AAGLVASWFGRIADFRKLSFPVSTTIPASGNAVEVGVNlpvdaeGGRPA--------GPMLAEVANPNDRWGTVLVVTGR 1052
Cdd:PRK11114 233 AAGIVASWFGSLADYRGARFPVLYNQLPERNAIVFATN------DQRPDflrlpavdGPTLAVIDNPADPYVKLLLVTGR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1053 TAQEVEVAARALVFSPDTLGGVASKVVSDVSLETRHPYDAPAFVPTDRPVRFGELV-GAADLQGGGFAPAGMTLPFHLPP 1131
Cdd:PRK11114 307 DDKDLLQAAKALALGNALLRGQSVVVNDVKPLAPRKPYDAPNWVPTDRPVTLGELVtYPQQLQVSGLEPDPIRVNLRLPP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1132 DLYTWRGRPFLMNMWVRAPGGPVVDleTSRVDVSLNNNYLQSYTLSPPG-LWRKWSERL-VNQHAGAVGHVTALPPWLLF 1209
Cdd:PRK11114 387 DLFLWRGDGIPLDLNYRYTAPPVRD--DSRLNISLNDQFVQSLPLNPKGeLNRLLRLRLpLLQGLLDGETDVSIPALKLG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1210 GQNQLQFNFDARPIDRGACR-RTPGDIHMSVDSDSTLDFRRGYHFAEMPNLSYFAEAAFPFSRMADLSETTVVLPDHPDT 1288
Cdd:PRK11114 465 SRNQLRFDFDYDSPKTGGCItTQPNNNRAVIDPDSTIDFSGYRHYIAMPNLRAFANSGFPFTRLADLSQTAVVLPENPSE 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1289 GTTGAFLDLMGFFGASTWYPAAGVTVMGADEVAQTPPKgDIVVLGTAAQLgGAASGLLARSPYVIHDRHITVGQRMGLQG 1368
Cdd:PRK11114 545 AEISTLLNLLGRIGAQTGYPALRVTVTDDGDVIQLADK-DLLVIGGLPPQ-ALLDDWRIDLPVQATGESWVKTPLRQIAP 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1369 IWYLFQDhdhaglKDGVTANLNAPIAeagVLLAAQSPYDSQRSVVAFTGDTPERIHDLVLSLRNKGDLPSLQGDLVLKNG 1448
Cdd:PRK11114 623 DESDRAA------DADAYLSSSGAMA---ALIGFESPFNSQRSVVALLADSPRGLALLNDALNDPGKRAQIFGDVAVIRE 693
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1449 DRFTSYRTAPVYTVGSLPLWLRLDWFLGHHPSALYLAGLAGAGLAALGVWAWLRGWSRRR 1508
Cdd:PRK11114 694 NGVRSLRVGEVYYVGHLPWYERLWWALSNHPVLLALLAALSVLLLALVLWRLLRRIARRR 753
|
|
| CESA_CelA_like |
cd06421 |
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ... |
146-378 |
1.25e-106 |
|
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: 338.39 E-value: 1.25e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 146 PSVDVFVPSYNEELSLVRSTVLGALDLDWPADRLNVYILDDGRRKAFHDFA----VEAGAGYIIRAENNHAKAGNLNHAL 221
Cdd:cd06421 1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAaelgVEYGYRYLTRPDNRHAKAGNLNNAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 222 AVTDSPFAVIFDCDHVPTRGFLRRTIGWMMADPNLALLQTPHHFYAPDPFQRNLAGgmhVPPEGNMFYGLVQDGNDFWDA 301
Cdd:cd06421 81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWLADG---APNEQELFYGVIQPGRDRWGA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4827175 302 TFFCGSCAIIRREAVMGIGGFATETVTEDAHTALKMQRRGWGTAYLREPLAAGLATERLILHIGQRVRWARGMIQIM 378
Cdd:cd06421 158 AFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
|
|
| BcsA |
COG1215 |
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ... |
118-495 |
1.12e-45 |
|
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: 167.23 E-value: 1.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 118 MTLCLSYFQMAWPLRRREHPlpedMAQWPSVDVFVPSYNEELSLVRsTVLGALDLDWPADRLNVYILDDGRRKAFHDFAV 197
Cdd:COG1215 5 LALLALLYLLLLALARRRRA----PADLPRVSVIIPAYNEEAVIEE-TLRSLLAQDYPKEKLEVIVVDDGSTDETAEIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 198 EAGAGY----IIRAENNHAKAGNLNHALAVTDSPFAVIFDCDHVPTRGFLRRTIGWMmADPNLAllqtphhfyapdpfqr 273
Cdd:COG1215 80 ELAAEYprvrVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVG---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 274 nlaggmhvppegnmfyglvqdgndfwdatfFCGSCAIIRREAVMGIGGFATETVTEDAHTALKMQRRGWGTAYLREPLAA 353
Cdd:COG1215 143 ------------------------------ASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 354 GLATERLILHIGQRVRWARGMIQIMRLDNPMLgaglrWEQRLCYLsamshflfaiprLTFLVSPLAFLFLGqniiaASPL 433
Cdd:COG1215 193 EEAPETLRALFRQRRRWARGGLQLLLKHRPLL-----RPRRLLLF------------LLLLLLPLLLLLLL-----LALL 250
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4827175 434 AISVYALPHIFHSVitlsriegrWRYSFWSEIYETSLALFLVRITIVTLLQPHKGKFNVTDK 495
Cdd:COG1215 251 ALLLLLLPALLLAL---------LLALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
|
|
| Glycos_transf_2 |
pfam00535 |
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ... |
149-316 |
2.50e-22 |
|
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: 95.15 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 149 DVFVPSYNEELSLVRsTVLGALDLDWPadRLNVYILDDGRRKAFHDFAVEAGAGY----IIRAENNHAKAGNLNHALAVT 224
Cdd:pfam00535 1 SVIIPTYNEEKYLLE-TLESLLNQTYP--NFEIIVVDDGSTDGTVEIAEEYAKKDprvrVIRLPENRGKAGARNAGLRAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 225 DSPFAVIFDCDHVPTRGFLRRTIGWMMADPN-LALLQTPHHFYAPDPFQRNLAggmhvpPEGNMFYGLVQDGNDFWDATF 303
Cdd:pfam00535 78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGAdVVVGSRYVIFGETGEYRRASR------ITLSRLPFFLGLRLLGLNLPF 151
|
170
....*....|...
gi 4827175 304 FCGSCAIIRREAV 316
Cdd:pfam00535 152 LIGGFALYRREAL 164
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CelA |
TIGR03030 |
cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 ... |
41-701 |
0e+00 |
|
cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 polymerization of glucose residues in the formation of cellulose. In bacteria, the substrate is UDP-glucose. The synthase consists of two subunits (or domains in the frequent cases where it is encoded as a single polypeptide), the catalytic domain modelled here and the regulatory domain (pfam03170). The regulatory domain binds the allosteric activator cyclic di-GMP. The protein is membrane-associated and probably assembles into multimers such that the individual cellulose strands can self-assemble into multi-strand fibrils.
Pssm-ID: 274400 [Multi-domain] Cd Length: 713 Bit Score: 792.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 41 SVRIDPALQGWVSIGTVTLLLVLNRRRGRGITVFLMMLSLLVSLRYIVWRLTATVQFSNWLQTALAVLLLLAEAYALMTL 120
Cdd:TIGR03030 26 TAPVTLETQLIIAGSAFLLLLILKRFNGKRPRLLLLVLSVFISLRYLWWRLTETLPFDNTLNFIFGTLLLLAELYSITIL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 121 CLSYFQMAWPLRRREHPLPEDMAQWPSVDVFVPSYNEELSLVRSTVLGALDLDWPADRLNVYILDDG------------- 187
Cdd:TIGR03030 106 LLGYFQTVRPLDRTPVPLPLDPEEWPTVDVFIPTYNEDLEIVATTVLAAKNMDYPADKFRVWILDDGgtdqkrndpdpeq 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 188 -----RRKAFHDFAVEAGAGYIIRAENNHAKAGNLNHALAVTDSPFAVIFDCDHVPTRGFLRRTIGWMMADPNLALLQTP 262
Cdd:TIGR03030 186 aeaaqRREELKEFCRKLGVNYITRPRNVHAKAGNINNALKHTDGELILIFDADHVPTRDFLQRTVGWFVEDPKLFLVQTP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 263 HHFYAPDPFQRNLAGGMHVPPEGNMFYGLVQDGNDFWDATFFCGSCAIIRREAVMGIGGFATETVTEDAHTALKMQRRGW 342
Cdd:TIGR03030 266 HFFVSPDPIERNLGTFRRMPNENELFYGLIQDGNDFWNAAFFCGSAAVLRREALDEIGGIAGETVTEDAETALKLHRRGW 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 343 GTAYLREPLAAGLATERLILHIGQRVRWARGMIQIMRLDNPMLGAGLRWEQRLCYLSAMSHFLFAIPRLTFLVSPLAFLF 422
Cdd:TIGR03030 346 NSAYLDRPLIAGLAPETLSGHIGQRIRWAQGMMQIFRLDNPLLKRGLSFPQRLCYLNAMLFWFFPLPRVIFLTAPLAYLF 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 423 LGQNIIAASPLAISVYALPHIFHSVITLSRIEGRWRYSFWSEIYETSLALFLVRITIVTLLQPHKGKFNVTDKGGLLARG 502
Cdd:TIGR03030 426 FGLNIFVASALEILAYALPHMLHSLLTNSYLFGRVRWPFWSEVYETVLAVYLLPPVLVTLLNPKKPKFNVTPKGELLDED 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 503 YFDwDAVYPNVILAGVLCAALLRGVFGIVWQFHDRLALqsfILNTLWVVISLIIVLASIAVGRETRQTRNAPRVSVRLPV 582
Cdd:TIGR03030 506 YFS-PLSRPYLILFALILAGLAFGLYRIYGYPIERGVL---LVVLGWNLLNLILLGAALAVVAERRQRRSSPRIPCKIPA 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 583 VVTDAHGRQMEGHTHDISLGGLAVG--TRLATPDMVGGEVTVRYDSARDGIHVGVPARVLDARDGTLRLRWAVRDLEDER 660
Cdd:TIGR03030 582 EVQRDGGRWVEATVEDASVGGLGIKinAQGAPGPQLGAGVLVQIRPKRNGLPALKPARVRGAGGVMIGLEFSPLNVQQVR 661
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 4827175 661 QVVSMVFGRNDAWAGWADFA--PDRPLRSLAMVFRSIGGLLRR 701
Cdd:TIGR03030 662 EIVDLVFARSDRWVALWEERrrPDGPLRGLADFLKIALRGLFR 704
|
|
| bcsA |
PRK11498 |
cellulose synthase catalytic subunit; Provisional |
85-710 |
0e+00 |
|
cellulose synthase catalytic subunit; Provisional
Pssm-ID: 236918 [Multi-domain] Cd Length: 852 Bit Score: 731.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 85 RYIVWRLTATVQFSNWLQTALAVLLLLAEAYALMTLCLSYFQMAWPLRRREHPLPEDMAQWPSVDVFVPSYNEELSLVRS 164
Cdd:PRK11498 199 RYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 165 TVLGALDLDWPADRLNVYILDDGRRKAFHDFAVEAGAGYIIRAENNHAKAGNLNHALAVTDSPFAVIFDCDHVPTRGFLR 244
Cdd:PRK11498 279 TIYASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKYIARPTHEHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFLQ 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 245 RTIGWMMADPNLALLQTPHHFYAPDPFQRNLAGGMHVPPEGNMFYGLVQDGNDFWDATFFCGSCAIIRREAVMGIGGFAT 324
Cdd:PRK11498 359 MTMGWFLKDKKLAMMQTPHHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAV 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 325 ETVTEDAHTALKMQRRGWGTAYLREPLAAGLATERLILHIGQRVRWARGMIQIMRLDNPMLGAGLRWEQRLCYLSAMSHF 404
Cdd:PRK11498 439 ETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLTGKGLKLAQRLCYANAMLHF 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 405 LFAIPRLTFLVSPLAFLFLGQNIIAASPLAISVYALPHIFHSVITLSRIEGRWRYSFWSEIYETSLALFLVRITIVTLLQ 484
Cdd:PRK11498 519 LSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHASLTNSRIQGKYRHSFWSEIYETVLAWYIAPPTTVALFN 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 485 PHKGKFNVTDKGGLLARGYFDWDAVYPNVILAGVLCAALLRGVFGIVWQFHDRLAlqSFILNTLWVVISLIIVLASIAVG 564
Cdd:PRK11498 599 PHKGKFNVTAKGGLVEEEYVDWVISRPYIFLVLLNLVGVAVGIWRYFYGPPNEIL--TVIVSLVWVFYNLIILGGAVAVS 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 565 RETRQTRNAPRVSVRLPVVVTDAHGRQMEGHTHDISLGGLAVGTRLATPDMVGGEVTVRYDsaRDGIHVGVPARVLDARD 644
Cdd:PRK11498 677 VESKQVRRSHRVEMTMPAAIAREDGHLFSCTVQDFSDGGLGIKINGQAQLLEGQKVNLLLK--RGQQEYVFPTQVTRVMG 754
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4827175 645 GTLRLRWAVRDLEDERQVVSMVFGRNDAWAGWAD-FAPDRPLRSLAMVFRsIGGLLRRRPAE-APRAL 710
Cdd:PRK11498 755 NEVGLQLMPLTTQQHIDFVQCTFARADTWALWQDsFPEDKPLESLLDILK-LGFRGYRHLAEfAPPSV 821
|
|
| BcsB |
pfam03170 |
Bacterial cellulose synthase subunit; This family includes bacterial proteins involved in ... |
808-1414 |
0e+00 |
|
Bacterial cellulose synthase subunit; This family includes bacterial proteins involved in cellulose synthesis. Cellulose synthesis has been identified in several bacteria. In Agrobacterium tumefaciens, for instance, cellulose has a pathogenic role: it allows the bacteria to bind tightly to their host plant cells. While several enzymatic steps are involved in cellulose synthesis, potentially the only step unique to this pathway is that catalyzed by cellulose synthase. This enzyme is a multi subunit complex. This family encodes a subunit that is thought to bind the positive effector cyclic di-GMP. This subunit is found in several different bacterial cellulose synthase enzymes. The first recognized sequence for this subunit is BcsB. In the AcsII cellulose synthase, this subunit and the subunit corresponding to BcsA are found in the same protein. Indeed, this alignment only includes the C-terminal half of the AcsAII synthase, which corresponds to BcsB.
Pssm-ID: 427177 Cd Length: 607 Bit Score: 624.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 808 TRTLTFRNLGATtGPLTLRGYSPLQGLDVVVPANRVVTHAQLTLSGALSPSLLPEANAVTVTLNEQYVGTLKVDPQHPQF 887
Cdd:pfam03170 3 TQTLSFADLGAP-GPLTLRGVDGSGGLPFGLRADQVVTNASLNLAYTYSPALLPELSHLKVLLNGELLGTLPLPKEQAGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 888 GPVSFDIDPLYFTGDNKLNFHFAGEYRRDCNDLFNEILWARISDMSRITLTTVRITPERKLSRLPAPFFDPNQRSTLRVP 967
Cdd:pfam03170 82 LTVQIDIPPRLLVDFNRLRFELIGHYTLDCEDPAHSSLWATISPDSYLELTYQPLPLPNDLSLLPAPFFDPRDMRPLTLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 968 VVLPATGDRGALRAAGLVASWFGRIADFRKLSFPVST-TIPASGNAVEVGVNL-PVDAEGGRPA--GPMLAEVANPNDRW 1043
Cdd:pfam03170 162 FVFPATPDPGTLQAAGIVASWFGALAGYRGADFPVSTdTLPASGNAVVFATNDeRPGGLADLPAvnGPTLAVIDNPQDPY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1044 GTVLVVTGRTAQEVEVAARALVFSPDTLGGVASKVVSDVSLETRHPYDAPAFVPTDRPVRFGELV-GAADLQGGGFAPAG 1122
Cdd:pfam03170 242 GKLLLVTGRDDAELRQAARALALGSALLSGDTVVVDNVVLLPPRKPYDAPRWVPTDRPVRLGELGtAPQDLQVSGLRPDP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1123 MTLPFHLPPDLYTWRGRPFLMNMWVRAPGGPVVDleTSRVDVSLNNNYLQSYTLSPPGLWRKWSeRLVNQHAGAVGHVTa 1202
Cdd:pfam03170 322 IRVNFRLPPDLFLWRGRGIPLDLRYRYTAPPRID--DSRLDVSLNGQFLGSLPLSSEGGLSFLL-RLGGDSRQESYTVR- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1203 LPPWLLFGQNQLQFNFDARPIDRGACR-RTPGDIHMSVDSDSTLDFRRGYHFAEMPNLSYFAEAAFPFSRMADLSETTVV 1281
Cdd:pfam03170 398 LPPYLLGPRNQLQFDFNLVPLKDGECQtTLPDNLRAAIDPDSTIDLSGYPHYAALPNLAAFANAGFPFTRLADLSETAVV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1282 LPDHPDTGTTGAFLDLMGFFGASTWYPAAGVTVMGADEVAQTpPKGDIVVLGTAAQLgGAASGLLARSPYVIHDRHITVG 1361
Cdd:pfam03170 478 LPDRPTAAEISALLNLMGRMGAATGYPALRVTVTDAADVESL-ADKDLLVIGSLPQQ-PLLQRLLKSLPLLLDGGRLRVP 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 4827175 1362 QRMGLQGIWYLFQDH-DHAGLKDGVTANLNAPIAeagVLLAAQSPYDSQRSVVA 1414
Cdd:pfam03170 556 DRLSLQRSWPGGRLQrDDAPADADLSLSSSGPLA---ALVGFESPYNPGRSVVA 606
|
|
| PRK11114 |
PRK11114 |
cellulose biosynthesis cyclic di-GMP-binding regulatory protein BcsB; |
744-1508 |
0e+00 |
|
cellulose biosynthesis cyclic di-GMP-binding regulatory protein BcsB;
Pssm-ID: 236851 [Multi-domain] Cd Length: 756 Bit Score: 563.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 744 TASAALFVAFTALVPAAMAQEAPSPDQSGVTAetpfgdsnTGVVPDALPAIDPAVADRisdaevTRTLTFRNLGATTGPL 823
Cdd:PRK11114 9 CALALGMSAFPAFATAAAPATQPLANAAGQVM--------PAAPAAAAPVVAQAAPSR------DVTLTFAQLGPAPGPI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 824 TLRGYSPLQGLDVVVPANRVVTHAQLTLSGALSPSLLPEANAVTVTLNEQYVGTLKVDpqHPQFG-PVSF--DIDPLYFT 900
Cdd:PRK11114 75 VLRGVDPQGGIEFGVRSDEVVTKARLNLEYTYSPALLPDLSHLKVYLNGELMGTLPLD--KEQLGkKVLAqlPIDPRFIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 901 GDNKLNFHFAGEYRRDCNDLFNEILWARISDMSRITLTTVRITPERKLSRLPAPFFDPNQRSTLRVPVVLPATGDRGALR 980
Cdd:PRK11114 153 DFNRLRLEFIGHYTDVCEDPASSSLWADISPSSSLDLTYQKLPLPNDLALLPAPFFDPRDNRPLTLPFVFAAKPDLATLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 981 AAGLVASWFGRIADFRKLSFPVSTTIPASGNAVEVGVNlpvdaeGGRPA--------GPMLAEVANPNDRWGTVLVVTGR 1052
Cdd:PRK11114 233 AAGIVASWFGSLADYRGARFPVLYNQLPERNAIVFATN------DQRPDflrlpavdGPTLAVIDNPADPYVKLLLVTGR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1053 TAQEVEVAARALVFSPDTLGGVASKVVSDVSLETRHPYDAPAFVPTDRPVRFGELV-GAADLQGGGFAPAGMTLPFHLPP 1131
Cdd:PRK11114 307 DDKDLLQAAKALALGNALLRGQSVVVNDVKPLAPRKPYDAPNWVPTDRPVTLGELVtYPQQLQVSGLEPDPIRVNLRLPP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1132 DLYTWRGRPFLMNMWVRAPGGPVVDleTSRVDVSLNNNYLQSYTLSPPG-LWRKWSERL-VNQHAGAVGHVTALPPWLLF 1209
Cdd:PRK11114 387 DLFLWRGDGIPLDLNYRYTAPPVRD--DSRLNISLNDQFVQSLPLNPKGeLNRLLRLRLpLLQGLLDGETDVSIPALKLG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1210 GQNQLQFNFDARPIDRGACR-RTPGDIHMSVDSDSTLDFRRGYHFAEMPNLSYFAEAAFPFSRMADLSETTVVLPDHPDT 1288
Cdd:PRK11114 465 SRNQLRFDFDYDSPKTGGCItTQPNNNRAVIDPDSTIDFSGYRHYIAMPNLRAFANSGFPFTRLADLSQTAVVLPENPSE 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1289 GTTGAFLDLMGFFGASTWYPAAGVTVMGADEVAQTPPKgDIVVLGTAAQLgGAASGLLARSPYVIHDRHITVGQRMGLQG 1368
Cdd:PRK11114 545 AEISTLLNLLGRIGAQTGYPALRVTVTDDGDVIQLADK-DLLVIGGLPPQ-ALLDDWRIDLPVQATGESWVKTPLRQIAP 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1369 IWYLFQDhdhaglKDGVTANLNAPIAeagVLLAAQSPYDSQRSVVAFTGDTPERIHDLVLSLRNKGDLPSLQGDLVLKNG 1448
Cdd:PRK11114 623 DESDRAA------DADAYLSSSGAMA---ALIGFESPFNSQRSVVALLADSPRGLALLNDALNDPGKRAQIFGDVAVIRE 693
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 1449 DRFTSYRTAPVYTVGSLPLWLRLDWFLGHHPSALYLAGLAGAGLAALGVWAWLRGWSRRR 1508
Cdd:PRK11114 694 NGVRSLRVGEVYYVGHLPWYERLWWALSNHPVLLALLAALSVLLLALVLWRLLRRIARRR 753
|
|
| CESA_CelA_like |
cd06421 |
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ... |
146-378 |
1.25e-106 |
|
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: 338.39 E-value: 1.25e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 146 PSVDVFVPSYNEELSLVRSTVLGALDLDWPADRLNVYILDDGRRKAFHDFA----VEAGAGYIIRAENNHAKAGNLNHAL 221
Cdd:cd06421 1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAaelgVEYGYRYLTRPDNRHAKAGNLNNAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 222 AVTDSPFAVIFDCDHVPTRGFLRRTIGWMMADPNLALLQTPHHFYAPDPFQRNLAGgmhVPPEGNMFYGLVQDGNDFWDA 301
Cdd:cd06421 81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWLADG---APNEQELFYGVIQPGRDRWGA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4827175 302 TFFCGSCAIIRREAVMGIGGFATETVTEDAHTALKMQRRGWGTAYLREPLAAGLATERLILHIGQRVRWARGMIQIM 378
Cdd:cd06421 158 AFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
|
|
| BcsA |
COG1215 |
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ... |
118-495 |
1.12e-45 |
|
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: 167.23 E-value: 1.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 118 MTLCLSYFQMAWPLRRREHPlpedMAQWPSVDVFVPSYNEELSLVRsTVLGALDLDWPADRLNVYILDDGRRKAFHDFAV 197
Cdd:COG1215 5 LALLALLYLLLLALARRRRA----PADLPRVSVIIPAYNEEAVIEE-TLRSLLAQDYPKEKLEVIVVDDGSTDETAEIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 198 EAGAGY----IIRAENNHAKAGNLNHALAVTDSPFAVIFDCDHVPTRGFLRRTIGWMmADPNLAllqtphhfyapdpfqr 273
Cdd:COG1215 80 ELAAEYprvrVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVG---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 274 nlaggmhvppegnmfyglvqdgndfwdatfFCGSCAIIRREAVMGIGGFATETVTEDAHTALKMQRRGWGTAYLREPLAA 353
Cdd:COG1215 143 ------------------------------ASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 354 GLATERLILHIGQRVRWARGMIQIMRLDNPMLgaglrWEQRLCYLsamshflfaiprLTFLVSPLAFLFLGqniiaASPL 433
Cdd:COG1215 193 EEAPETLRALFRQRRRWARGGLQLLLKHRPLL-----RPRRLLLF------------LLLLLLPLLLLLLL-----LALL 250
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4827175 434 AISVYALPHIFHSVitlsriegrWRYSFWSEIYETSLALFLVRITIVTLLQPHKGKFNVTDK 495
Cdd:COG1215 251 ALLLLLLPALLLAL---------LLALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
|
|
| CESA_CaSu_A2 |
cd06437 |
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ... |
146-373 |
2.90e-26 |
|
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: 108.94 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 146 PSVDVFVPSYNEELSLVRStVLGALDLDWPADRLNVYILDDGRRKAFHDFAVE----AGAG----YIIRAENNHAKAGNL 217
Cdd:cd06437 1 PMVTVQLPVFNEKYVVERL-IEAACALDYPKDRLEIQVLDDSTDETVRLAREIveeyAAQGvnikHVRRADRTGYKAGAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 218 NHALAVTDSPFAVIFDCDHVPTRGFLRRTIgWMMADPNLALLQTPHHFYAPDP--FQRNLAGGMhvppegNMFYGLVQDG 295
Cdd:cd06437 80 AEGMKVAKGEYVAIFDADFVPPPDFLQKTP-PYFADPKLGFVQTRWGHINANYslLTRVQAMSL------DYHFTIEQVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 296 ----NDFWDatfFCGSCAIIRREAVMGIGGFATETVTEDAHTALKMQRRGWGTAYLREPLAAGLATERLILHIGQRVRWA 371
Cdd:cd06437 153 rsstGLFFN---FNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWS 229
|
..
gi 4827175 372 RG 373
Cdd:cd06437 230 KG 231
|
|
| CESA_like |
cd06423 |
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ... |
150-330 |
7.52e-26 |
|
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: 105.77 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 150 VFVPSYNEELSlVRSTVLGALDLDWPadRLNVYILDDGRRKAFHDFAVEAGAGY-----IIRAENNHAKAGNLNHALAVT 224
Cdd:cd06423 1 IIVPAYNEEAV-IERTIESLLALDYP--KLEVIVVDDGSTDDTLEILEELAALYirrvlVVRDKENGGKAGALNAGLRHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 225 DSPFAVIFDCDHVPTRGFLRRTIGWMMADPNLALLQTphHFYAPDPFQRNLAGGMHVppEGNMFYGLVQDGNDFWDATF- 303
Cdd:cd06423 78 KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQG--RVRVRNGSENLLTRLQAI--EYLSIFRLGRRAQSALGGVLv 153
|
170 180
....*....|....*....|....*..
gi 4827175 304 FCGSCAIIRREAVMGIGGFATETVTED 330
Cdd:cd06423 154 LSGAFGAFRREALREVGGWDEDTLTED 180
|
|
| Glycos_transf_2 |
pfam00535 |
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ... |
149-316 |
2.50e-22 |
|
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: 95.15 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 149 DVFVPSYNEELSLVRsTVLGALDLDWPadRLNVYILDDGRRKAFHDFAVEAGAGY----IIRAENNHAKAGNLNHALAVT 224
Cdd:pfam00535 1 SVIIPTYNEEKYLLE-TLESLLNQTYP--NFEIIVVDDGSTDGTVEIAEEYAKKDprvrVIRLPENRGKAGARNAGLRAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 225 DSPFAVIFDCDHVPTRGFLRRTIGWMMADPN-LALLQTPHHFYAPDPFQRNLAggmhvpPEGNMFYGLVQDGNDFWDATF 303
Cdd:pfam00535 78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGAdVVVGSRYVIFGETGEYRRASR------ITLSRLPFFLGLRLLGLNLPF 151
|
170
....*....|...
gi 4827175 304 FCGSCAIIRREAV 316
Cdd:pfam00535 152 LIGGFALYRREAL 164
|
|
| CESA_NdvC_like |
cd06435 |
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ... |
152-379 |
6.24e-22 |
|
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: 96.32 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 152 VPSYNEELSLVRSTVLGALDLDWPadRLNVYILDD------------------GRRKAFHDFAVEAGAgyiiraennhaK 213
Cdd:cd06435 4 VPCYEEPPEMVKETLDSLAALDYP--NFEVIVIDNntkdealwkpveahcaqlGERFRFFHVEPLPGA-----------K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 214 AGNLNHALAVTDSPFAVI--FDCDHVPTRGFLRRTIGwMMADPNLALLQTPHHFY--APDPFQRNLAGgmhvppEGNMFY 289
Cdd:cd06435 71 AGALNYALERTAPDAEIIavIDADYQVEPDWLKRLVP-IFDDPRVGFVQAPQDYRdgEESLFKRMCYA------EYKGFF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 290 GLVQDGNDFWDATFFCGSCAIIRREAVMGIGGFATETVTEDAHTALKMQRRGWGTAYLREPLAAGLATERLILHIGQRVR 369
Cdd:cd06435 144 DIGMVSRNERNAIIQHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFR 223
|
250
....*....|
gi 4827175 370 WARGMIQIMR 379
Cdd:cd06435 224 WAYGAVQILK 233
|
|
| Glyco_trans_2_3 |
pfam13632 |
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ... |
230-423 |
1.42e-17 |
|
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.
Pssm-ID: 433365 [Multi-domain] Cd Length: 192 Bit Score: 82.38 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 230 VIFDCDHVPTRGFLRRTIGWMmADPNLALLQTPHHFYAPdpfqRNLAGGMHVPPEGNMFYGLVQDGNDFWDATFFCGSCA 309
Cdd:pfam13632 3 LLLDADTVLPPDCLLGIANEM-ASPEVAIIQGPILPMNV----GNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 310 IIRREAVMGIGGFATETVTEDAHTALKMQRRGWGTAYLREPLAAGLATERLILHIGQRVRWARGMIQIMRLDNPMLGAGL 389
Cdd:pfam13632 78 FLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRLLGYLGTL 157
|
170 180 190
....*....|....*....|....*....|....
gi 4827175 390 RWEQRLCYLSAMSHFLFAIPRLTFLVSPLAFLFL 423
Cdd:pfam13632 158 LWSGLPLALLLLLLFSISSLALVLLLLALLAGLL 191
|
|
| PilZ |
pfam07238 |
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ... |
569-668 |
7.77e-13 |
|
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: 65.99 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 569 QTRNAPRVSVRLPVVVTDAhGRQMEGHTHDISLGGLAVGTRLATPDmVGGEVTVRYDSARDGIHVGVPARVLDARDGTLR 648
Cdd:pfam07238 1 QRRRFPRVPVSLPVTLRDG-GGEYKGRLIDISLGGAAIRLPDEPLA-LGDRVELSLDLLDDGQELALPGRVVRIRPDEDG 78
|
90 100
....*....|....*....|....
gi 4827175 649 LRWAVR----DLEDERQVVSMVFG 668
Cdd:pfam07238 79 ARVGVQfldlDEEQRRLLVRLLFG 102
|
|
| CESA_like_1 |
cd06439 |
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ... |
128-376 |
2.03e-11 |
|
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: 66.07 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 128 AWPLRRREHPLPEDMAQWPSVDVFVPSYNEElSLVRSTVLGALDLDWPADRLNVYILDDGRRKAFHDFAVEAGAGYI--I 205
Cdd:cd06439 11 LLARLRPKPPSLPDPAYLPTVTIIIPAYNEE-AVIEAKLENLLALDYPRDRLEIIVVSDGSTDGTAEIAREYADKGVklL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 206 RAENNHAKAGNLNHALAVTDSPFAVIFDCDHVPTRGFLRRtIGWMMADPNLALLQTPHHFYAPDPFQRNlaggmhvppEG 285
Cdd:cd06439 90 RFPERRGKAAALNRALALATGEIVVFTDANALLDPDALRL-LVRHFADPSVGAVSGELVIVDGGGSGSG---------EG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 286 nmFYGLVQDGNDFWDATF-----FCGSCAIIRREAvmgIGGFATETVTEDAHTALKMQRRGWGTAYlrEPLAagLATERL 360
Cdd:cd06439 160 --LYWKYENWLKRAESRLgstvgANGAIYAIRREL---FRPLPADTINDDFVLPLRIARQGYRVVY--EPDA--VAYEEV 230
|
250 260
....*....|....*....|
gi 4827175 361 ILHIG----QRVRWARGMIQ 376
Cdd:cd06439 231 AEDGSeefrRRVRIAAGNLQ 250
|
|
| Glyco_tranf_2_3 |
pfam13641 |
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ... |
146-373 |
2.24e-11 |
|
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: 65.47 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 146 PSVDVFVPSYNEElSLVRSTVLGALDLDWPADRlnVYILDDGRRKAFHDFAVEAGAGY-------IIRAENN--HAKAGN 216
Cdd:pfam13641 2 PDVSVVVPAFNED-SVLGRVLEAILAQPYPPVE--VVVVVNPSDAETLDVAEEIAARFpdvrlrvIRNARLLgpTGKSRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 217 LNHALAVTDSPFAVIFDCDHVPTRGFLRRTIGWMmADPNLALLQTPHHFYAPDPFQrNLAGGMHVPPEGNMFYGLVQDGN 296
Cdd:pfam13641 79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-DSPKVGAVGTPVFSLNRSTML-SALGALEFALRHLRMMSLRLALG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4827175 297 dfwdATFFCGSCAIIRREAVMGIGGFATE-TVTEDAHTALKMQRRGWGTAYLREPLAAGLATERLILHIGQRVRWARG 373
Cdd:pfam13641 157 ----VLPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
|
|
| Cellulose_synt |
pfam03552 |
Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose ... |
326-497 |
3.03e-11 |
|
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: 68.24 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 326 TVTEDAHTALKMQRRGWGTAYLREPLAA--GLATERLILHIGQRVRWARGMIQI-MRLDNPML-GAGLRWEQRLCYLSAM 401
Cdd:pfam03552 419 SVTEDILTGFRMHCRGWRSIYCMPKRDAfkGSAPINLSDRLHQVLRWALGSVEIfFSRHCPIWyGGRLKFLQRFAYINVG 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 402 SHFLFAIPRLTFLVSPLAFLFLGQNIIAASPLAISVYALPhIFHSVITLSRIEGRW----------RYSFWSeIYETSLA 471
Cdd:pfam03552 499 IYPFTSIPLLAYCFLPAICLFTGKFIVPTLSNFASIYFLS-LFLSIIATGILELRWsgvsieewwrNEQFWV-IGGTSAH 576
|
170 180
....*....|....*....|....*.
gi 4827175 472 LFLVRITIVTLLQPHKGKFNVTDKGG 497
Cdd:pfam03552 577 LFAVFQGLLKVIAGIDTSFTVTSKAS 602
|
|
| Glyco_transf_21 |
pfam13506 |
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ... |
213-372 |
1.13e-10 |
|
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: 61.92 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 213 KAGNLNHALAVTDSPFAVIFDCDHVPTRGFLRRTIGwMMADPNLALLQTPHHFYAPDPFQRNLAGGMHvppegNMFYGLV 292
Cdd:pfam13506 18 KVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLA-PLADPKVGLVTSPPVGSDPKGLAAALEAAFF-----NTLAGVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 293 QDGndFWDATFFCGSCAIIRREAVMGIGGFAT--ETVTEDAHTALKMQRRGWGTAYLREPLAAGLATERLIL-HIGQR-V 368
Cdd:pfam13506 92 QAA--LSGIGFAVGMSMAFRRADLERIGGFEAlaDYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPRRTSFrAFMARqL 169
|
....
gi 4827175 369 RWAR 372
Cdd:pfam13506 170 RWAR 173
|
|
| PLN02915 |
PLN02915 |
cellulose synthase A [UDP-forming], catalytic subunit |
321-496 |
1.13e-10 |
|
cellulose synthase A [UDP-forming], catalytic subunit
Pssm-ID: 215494 [Multi-domain] Cd Length: 1044 Bit Score: 66.49 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 321 GFATETVTEDAHTALKMQRRGWGTAYLREPLAA--GLATERLILHIGQRVRWARGMIQI-MRLDNPM---LGAGLRWEQR 394
Cdd:PLN02915 734 GWIYGSVTEDILTGFKMHCRGWKSVYCMPKRPAfkGSAPINLSDRLHQVLRWALGSVEIfMSRHCPLwyaYGGKLKWLER 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 395 LCYLSAMSHFLFAIPRLTFLVSPLAFLFLGQNIIAASPLAISVYALPhIFHSVITLSRIEGRW----------RYSFWSe 464
Cdd:PLN02915 814 LAYINTIVYPFTSIPLLAYCTIPAVCLLTGKFIIPTLNNLASIWFLA-LFLSIIATSVLELRWsgvsiedlwrNEQFWV- 891
|
170 180 190
....*....|....*....|....*....|..
gi 4827175 465 IYETSLALFLVRITIVTLLQPHKGKFNVTDKG 496
Cdd:PLN02915 892 IGGVSAHLFAVFQGLLKVLGGVDTNFTVTSKA 923
|
|
| PLN02195 |
PLN02195 |
cellulose synthase A |
321-568 |
5.67e-10 |
|
cellulose synthase A
Pssm-ID: 215124 [Multi-domain] Cd Length: 977 Bit Score: 64.22 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 321 GFATETVTEDAHTALKMQRRGWGTAY---LRePLAAGLATERLILHIGQRVRWARGMIQIMRLDNPML-----GAGLRWE 392
Cdd:PLN02195 666 GWIYGSVTEDILTGFKMHCRGWRSIYcmpVR-PAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHCPLwygygGGRLKWL 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 393 QRLCYLSAMSHFLFAIPRLTFLVSPLAFLFLGQNIIAASPLAISVYALpHIFHSVITLSRIEGRW----------RYSFW 462
Cdd:PLN02195 745 QRLAYINTIVYPFTSLPLIAYCTLPAICLLTGKFIIPTLSNLASMLFL-GLFISIILTSVLELRWsgvsiedlwrNEQFW 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 463 SeIYETSLALFLVRITIVTLLQPHKGKFNVTDKG---GLLARGY-FDWDAVY--PNVIlagvlcaaLLRGVFGIVWQFHD 536
Cdd:PLN02195 824 V-IGGVSAHLFAVFQGFLKMLAGLDTNFTVTAKAaddTEFGELYmVKWTTLLipPTSL--------LIINLVGVVAGFSD 894
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 4827175 537 RL--------ALQSFILNTLWVVISLIIVLASIaVGRETR 568
Cdd:PLN02195 895 ALnkgyeawgPLFGKVFFAFWVILHLYPFLKGL-MGRQNR 933
|
|
| PLN02400 |
PLN02400 |
cellulose synthase |
321-568 |
6.06e-10 |
|
cellulose synthase
Pssm-ID: 215224 [Multi-domain] Cd Length: 1085 Bit Score: 64.23 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 321 GFATETVTEDAHTALKMQRRGWGTAYLREPLAA--GLATERLILHIGQRVRWARGMIQIMRLDNPMLGAG----LRWEQR 394
Cdd:PLN02400 775 GWIYGSVTEDILTGFKMHARGWISIYCMPPRPAfkGSAPINLSDRLNQVLRWALGSIEILLSRHCPIWYGyngrLKLLER 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 395 LCYLSAMSHFLFAIPRLTFLVSPLAFLFLGQNIIAasplAISVYA-------LPHIFHSVITLSR-----IEGRWR-YSF 461
Cdd:PLN02400 855 LAYINTIVYPITSIPLLAYCVLPAFCLITNKFIIP----EISNYAsmwfillFISIFATGILELRwsgvgIEDWWRnEQF 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 462 WSeIYETSLALFLVRITIVTLLQPHKGKFNVT----DKGGLLARGY-FDWDAVY--PNVILAgVLCAALLRGV-FGIVWQ 533
Cdd:PLN02400 931 WV-IGGTSAHLFAVFQGLLKVLAGIDTNFTVTskasDEDGDFAELYvFKWTSLLipPTTVLL-VNLVGIVAGVsYAINSG 1008
|
250 260 270
....*....|....*....|....*....|....*
gi 4827175 534 FHDRLALQSFILNTLWVVISLIIVLASIaVGRETR 568
Cdd:PLN02400 1009 YQSWGPLFGKLFFAIWVIAHLYPFLKGL-LGRQNR 1042
|
|
| Glucan_BSP_MdoH |
cd04191 |
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ... |
150-343 |
6.34e-10 |
|
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic Glucan Biosynthesis protein MdoH is a glucosyltransferase that catalyzes the elongation of beta-1,2 polyglucose chains of glucan, requiring a beta-glucoside as a primer and UDP-glucose as a substrate. Glucans are composed of 5 to 10 units of glucose forming a highly branched structure, where beta-1,2-linked glucose constitutes a linear backbone to which branches are attached by beta-1,6 linkages. In Escherichia coli, glucans are located in the periplasmic space, functioning as regulator of osmolarity. It is synthesized at a maximum when cells are grown in a medium with low osmolarity. It has been shown to span the cytoplasmic membrane.
Pssm-ID: 133034 [Multi-domain] Cd Length: 254 Bit Score: 61.52 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 150 VFVPSYNEELSLVRSTVLG-ALDL--DWPADRLNVYILDDGRR--------KAFHDFAVEAGAG----YIIRAENNHAKA 214
Cdd:cd04191 3 IVMPVYNEDPARVFAGLRAmYESLakTGLADHFDFFILSDTRDpdiwlaeeAAWLDLCEELGAQgriyYRRRRENTGRKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 215 GNLNHALAVTDSPFA--VIFDCDHVPTRGFLRRTIGWMMADPNLALLQT-PHHFYAPDPFQRNLAGGMHvppegnmFYG- 290
Cdd:cd04191 83 GNIADFCRRWGSRYDymVVLDADSLMSGDTIVRLVRRMEANPRAGIIQTaPKLIGAETLFARLQQFANR-------LYGp 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4827175 291 LVQDGNDFW--DATFFCGSCAIIRREAVM---------GIGGFATETVTEDAHTALKMQRRGWG 343
Cdd:cd04191 156 VFGRGLAAWqgGEGNYWGHNAIIRVAAFMehcalpvlpGRPPFGGHILSHDFVEAALMRRAGWE 219
|
|
| CESA_like_2 |
cd06427 |
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ... |
146-376 |
9.26e-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: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 146 PSVDVFVPSYNEeLSLVRSTVLGALDLDWPADRLNVYIL---DD----------GRRKAFHDFAVEAGAgyiIRAennha 212
Cdd:cd06427 1 PVYTILVPLYKE-AEVLPQLIASLSALDYPRSKLDVKLLleeDDeetiaaaralRLPSIFRVVVVPPSQ---PRT----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 213 KAGNLNHALAVTDSPFAVIFDCDHVPTRGFLRRT-IGWMMADPNLALLQTPHHFYAPDpfqRNLAGGMHVpPEGNMFYGL 291
Cdd:cd06427 72 KPKACNYALAFARGEYVVIYDAEDAPDPDQLKKAvAAFARLDDKLACVQAPLNYYNAR---ENWLTRMFA-LEYAAWFDY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 292 VQDGNDFWDATF-FCGSCAIIRREAVMGIGGFATETVTEDAHTALKMQRRGWGTAYLREPLAAGlATERLILHIGQRVRW 370
Cdd:cd06427 148 LLPGLARLGLPIpLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLEE-ANNALGNWIRQRSRW 226
|
....*.
gi 4827175 371 ARGMIQ 376
Cdd:cd06427 227 IKGYMQ 232
|
|
| PLN02638 |
PLN02638 |
cellulose synthase A (UDP-forming), catalytic subunit |
321-568 |
1.54e-09 |
|
cellulose synthase A (UDP-forming), catalytic subunit
Pssm-ID: 215343 [Multi-domain] Cd Length: 1079 Bit Score: 63.02 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 321 GFATETVTEDAHTALKMQRRGWGTAYL--REPLAAGLATERLILHIGQRVRWARGMIQIMRLDN-PM---LGAGLRWEQR 394
Cdd:PLN02638 770 GWIYGSVTEDILTGFKMHARGWRSIYCmpKRPAFKGSAPINLSDRLNQVLRWALGSVEILFSRHcPIwygYGGRLKWLER 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 395 LCYLSAMSHFLFAIPRLTFLVSPLAFLFLGQNIIAASPLAISVYALPhIFHSVITLSRIEGRW----------RYSFWSe 464
Cdd:PLN02638 850 FAYVNTTIYPITSIPLLLYCTLPAVCLLTGKFIIPQISNIASIWFIS-LFLSIFATGILEMRWsgvgidewwrNEQFWV- 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 465 IYETSLALFLVRITIVTLLQPHKGKFNVT----DKGGLLARGY-FDWDA--VYPNVILAGVLCAALLRGVFGIVWQFHDR 537
Cdd:PLN02638 928 IGGVSAHLFAVFQGLLKVLAGIDTNFTVTskasDEDGDFAELYmFKWTTllIPPTTLLIINLVGVVAGISYAINSGYQSW 1007
|
250 260 270
....*....|....*....|....*....|.
gi 4827175 538 LALQSFILNTLWVVISLIIVLASIaVGRETR 568
Cdd:PLN02638 1008 GPLFGKLFFAFWVIVHLYPFLKGL-MGRQNR 1037
|
|
| PLN02189 |
PLN02189 |
cellulose synthase |
321-568 |
5.31e-09 |
|
cellulose synthase
Pssm-ID: 215121 [Multi-domain] Cd Length: 1040 Bit Score: 61.18 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 321 GFATETVTEDAHTALKMQRRGWGTAYL--REPLAAGLATERLILHIGQRVRWARGMIQI-MRLDNPML----GAGLRWEQ 393
Cdd:PLN02189 731 GWIYGSITEDILTGFKMHCRGWRSIYCmpKRAAFKGSAPINLSDRLNQVLRWALGSVEIfFSRHSPLLygykGGNLKWLE 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 394 RLCYLSAMSHFLFAIPRLTFLVSPLAFLFLGQNIIAASPLAISVYALPhIFHSVITLSRIEGRW----------RYSFWS 463
Cdd:PLN02189 811 RFAYVNTTIYPFTSLPLLAYCTLPAICLLTGKFIMPPISTFASLFFIA-LFMSIFATGILELRWsgvsieewwrNEQFWV 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 464 eIYETSLALFLVRITIVTLLQPHKGKFNVTDK-------GGLLArgyFDWDAVY--PNVIlagvlcaaLLRGVFGIVWQF 534
Cdd:PLN02189 890 -IGGVSAHLFAVVQGLLKVLAGIDTNFTVTSKatdddefGELYA---FKWTTLLipPTTL--------LIINIVGVVAGI 957
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 4827175 535 HDRL--ALQSF------ILNTLWVVISLIIVLASIaVGRETR 568
Cdd:PLN02189 958 SDAInnGYQSWgplfgkLFFAFWVIVHLYPFLKGL-MGRQNR 998
|
|
| PLN02436 |
PLN02436 |
cellulose synthase A |
321-497 |
1.40e-07 |
|
cellulose synthase A
Pssm-ID: 215239 [Multi-domain] Cd Length: 1094 Bit Score: 56.41 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 321 GFATETVTEDAHTALKMQRRGWGTAYL--REPLAAGLATERLILHIGQRVRWARGMIQIMRLDN-PM---LGAGLRWEQR 394
Cdd:PLN02436 786 GWIYGSVTEDILTGFKMHCHGWRSVYCipKRPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHcPIwygYGGGLKWLER 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 395 LCYLSAMSHFLFAIPRLTFLVSPLAFLFLGQNIIAasplAISVYA---LPHIFHSVITLSRIEGRW----------RYSF 461
Cdd:PLN02436 866 FSYINSVVYPWTSIPLIVYCTLPAICLLTGKFIVP----EISNYAsilFMALFISIAATGILEMQWggvgiddwwrNEQF 941
|
170 180 190
....*....|....*....|....*....|....*.
gi 4827175 462 WSeIYETSLALFLVRITIVTLLQPHKGKFNVTDKGG 497
Cdd:PLN02436 942 WV-IGGVSSHLFALFQGLLKVLAGVNTNFTVTSKAA 976
|
|
| Glyco_tranf_GTA_type |
cd00761 |
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ... |
150-263 |
2.34e-07 |
|
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: 52.12 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 150 VFVPSYNEElSLVRSTVLGALDLDWPADRlnVYILDDGR----RKAFHDFAVEAGAGYIIRAENNHAKAGNLNHALAVTD 225
Cdd:cd00761 1 VIIPAYNEE-PYLERCLESLLAQTYPNFE--VIVVDDGStdgtLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 4827175 226 SPFAVIFDCDHVPTRGFLRRTIGWMMADPNLALLQTPH 263
Cdd:cd00761 78 GEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPG 115
|
|
| PRK05454 |
PRK05454 |
glucans biosynthesis glucosyltransferase MdoH; |
131-485 |
2.10e-06 |
|
glucans biosynthesis glucosyltransferase MdoH;
Pssm-ID: 235476 [Multi-domain] Cd Length: 605 Bit Score: 52.19 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 131 LRRREHPLPEDMAQWPSVD------VFVPSYNEE----LSLVRSTVLgALDLDWPADRLNVYILDDGRR--------KAF 192
Cdd:PRK05454 103 RGRDKYSISASAAGDPPPPpeartaILMPIYNEDparvFAGLRAMYE-SLAATGHGAHFDFFILSDTRDpdiaaaeeAAW 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 193 HDFAVEAGAG----YIIRAENNHAKAGNLnhALAVT----DSPFAVIFDCDHVPTRGFLRRTIGWMMADPNLALLQT-PH 263
Cdd:PRK05454 182 LELRAELGGEgrifYRRRRRNVGRKAGNI--ADFCRrwggAYDYMVVLDADSLMSGDTLVRLVRLMEANPRAGLIQTlPV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 264 HFYAPDPFQRNLAGGMHVppegnmfYG-LVQDGNDFW---DATFFcGSCAIIRREAVM---------GIGGFATETVTED 330
Cdd:PRK05454 260 AVGADTLFARLQQFATRV-------YGpLFAAGLAWWqggEGNYW-GHNAIIRVKAFAehcglpplpGRGPFGGHILSHD 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 331 AHTALKMQRRGWG---TAYLRE-----P--LAAGLATERlilhigqrvRWARGMIQIMRLdnpMLGAGLRWEQRLcylsa 400
Cdd:PRK05454 332 FVEAALMRRAGWGvwlAPDLPGsyeelPpnLLDELKRDR---------RWCQGNLQHLRL---LLAKGLHPVSRL----- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 401 msHFLFAIprLTFLVSPLAFLFLGQNIIAAsplAISVYALPHIFHSvitlsriegRWRYSFWSEIyETSLALFLVRITIV 480
Cdd:PRK05454 395 --HFLTGI--MSYLSAPLWLLFLLLGTALA---LQAALTEPEYFQP---------RQLFPVWPQW-DPELAIALFAATMV 457
|
....*
gi 4827175 481 TLLQP 485
Cdd:PRK05454 458 LLFLP 462
|
|
| PLN02190 |
PLN02190 |
cellulose synthase-like protein |
321-495 |
2.97e-05 |
|
cellulose synthase-like protein
Pssm-ID: 215122 [Multi-domain] Cd Length: 756 Bit Score: 48.71 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 321 GFATETVTEDAHTALKMQRRGWGTAYLR-EPLAAGLATERLILH-IGQRVRWARGMIQIM-RLDNPMLGA---GLRWEQR 394
Cdd:PLN02190 452 GWLYDSVAEDLNTSIGIHSRGWTSSYISpDPPAFLGSMPPGGPEaMVQQRRWATGLIEVLfNKQSPLIGMfcrKIRFRQR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 395 LCYLSAMSHfLFAIPRLTFLVSPlAFLFLGQNIIAASPLAISVYALPHIFHSVITLsriegrWRY--------------S 460
Cdd:PLN02190 532 LAYLYVFTC-LRSIPELIYCLLP-AYCLLHNSALFPKGVYLGIIVTLVGMHCLYTL------WEFmslgfsvqswyvsqS 603
|
170 180 190
....*....|....*....|....*....|....*
gi 4827175 461 FWsEIYETSLALFLVRITIVTLLQPHKGKFNVTDK 495
Cdd:PLN02190 604 FW-RIKATSSWLFSIQDIILKLLGISKTVFIVTKK 637
|
|
| MdoH |
COG2943 |
Membrane glycosyltransferase [Cell wall/membrane/envelope biogenesis, Carbohydrate transport ... |
150-485 |
1.06e-04 |
|
Membrane glycosyltransferase [Cell wall/membrane/envelope biogenesis, Carbohydrate transport and metabolism];
Pssm-ID: 442186 [Multi-domain] Cd Length: 661 Bit Score: 46.79 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 150 VFVPSYNEE----LSLVRSTV--LGALDLdwpADRLNVYILDDGRR--------KAFHDFAVEAGAG----YIIRAENNH 211
Cdd:COG2943 100 ILMPVYNEDparvFAGLRAMYesLAATGQ---LDHFDFFILSDTTDpdiwaaeeAAWAALRARLGGGgrifYRRRRRNTG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 212 AKAGNlnhalaVTD--------SPFAVIFDCDHVPTRGFLRRTIGWMMADPNLALLQTPhhfyaPDP------FQRNLAG 277
Cdd:COG2943 177 RKAGN------IADfcrrwggaYDYMLVLDADSLMSGETIVRLVRRMEANPRAGLIQTL-----PVLvgretlFARLQQF 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 278 GMHVppegnmfYGLV----------QDGNdFWdatffcGSCAIIRREAVM---------GIGGFATETVTEDAHTALKMQ 338
Cdd:COG2943 246 AARV-------YGPLfaaglawwqgGEGN-YW------GHNAIIRVRAFAehcglpvlpGRGPFGGHILSHDFVEAALMR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 339 RRGWGTAylrepLAAGLA--------TerLILHIGQRVRWARGMIQIMRLdnpMLGAGLRWEQRLcylsamsHFLFAIpr 410
Cdd:COG2943 312 RAGWEVW-----LAPDLGgsyeesppT--LIDFAKRDRRWCQGNLQHLRL---LGAPGLHPVSRF-------HFLTGI-- 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4827175 411 LTFLVSPLAFLFLgqnIIAASPLAISVYALPHIFHsvitlsriEGRWRYSFWSEIY-ETSLALFLVriTIVTLLQP 485
Cdd:COG2943 373 MSYLSSPLWLLFL---LLGTALALQAALIRPEYFP--------EPFQLFPVWPVFDpERALALFVL--TMALLFLP 435
|
|
| PLN02190 |
PLN02190 |
cellulose synthase-like protein |
120-187 |
2.31e-04 |
|
cellulose synthase-like protein
Pssm-ID: 215122 [Multi-domain] Cd Length: 756 Bit Score: 46.01 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 120 LCLSYFQMAW---------PLRRREHP--LPEDMAQWPSVDVFVPSYN---EELSLVRSTVLGALDLDWPADRLNVYILD 185
Cdd:PLN02190 56 LCESCFSFVWllitcikwsPAEYKPYPdrLDERVHDLPSVDMFVPTADpvrEPPIIVVNTVLSLLAVNYPANKLACYVSD 135
|
..
gi 4827175 186 DG 187
Cdd:PLN02190 136 DG 137
|
|
| WcaA |
COG0463 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
146-349 |
2.57e-04 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440231 [Multi-domain] Cd Length: 208 Bit Score: 43.92 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 146 PSVDVFVPSYNEELSLVR--STVLGALDLDWPadrlnVYILDDGRRKAFHDFAVEAGAGY----IIRAENNHAKAGNLNH 219
Cdd:COG0463 2 PLVSVVIPTYNEEEYLEEalESLLAQTYPDFE-----IIVVDDGSTDGTAEILRELAAKDprirVIRLERNRGKGAARNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 220 ALAVTDSPFAVIFDCDHVPTRGFLRRtigwMMAdpnlALLQTPHHFYAPDPFQRNlaGGMHVPPEGNMFYGLVQDGNDFW 299
Cdd:COG0463 77 GLAAARGDYIAFLDADDQLDPEKLEE----LVA----ALEEGPADLVYGSRLIRE--GESDLRRLGSRLFNLVRLLTNLP 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 4827175 300 DATffcGSCAIIRREAVMGIG---GFATETVTedahtaLKMQRRGWGTAYLRE 349
Cdd:COG0463 147 DST---SGFRLFRREVLEELGfdeGFLEDTEL------LRALRHGFRIAEVPV 190
|
|
| YcgR |
COG5581 |
Cyclic di-GMP-binding flagellar brake protein FlgZ/YcgR, contains PilZNR(YcgR) and PilZ ... |
569-667 |
2.70e-04 |
|
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: 43.83 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 569 QTRNAPRVSVRLPVVVT----DAHGRQMEGHTHDISLGGLavgtRLATPDMVGGEVTVRYD---SARDGIHVGVPARVld 641
Cdd:COG5581 87 QRREYFRVPVPLDVPVRclrpDGEGEPLEGRLLDISGGGL----ALVLPEPPPLEVGDILElrlDLPDEGEIVVDAEV-- 160
|
90 100
....*....|....*....|....*.
gi 4827175 642 ardgtlrLRWAVRDLEDERQVVSMVF 667
Cdd:COG5581 161 -------RRVVEVELGKGKYRLGCEF 179
|
|
| EpsO_like |
cd06438 |
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ... |
150-245 |
5.38e-04 |
|
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: 42.59 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 150 VFVPSYNEElSLVRSTVLGALDLDWPADRLNVYILDDGRRKAFHDFAVEAGAGYIIRAENNH-----AKAGNLNHALAVT 224
Cdd:cd06438 1 ILIPAHNEE-AVIGNTVRSLKAQDYPRELYRIFVVADNCTDDTAQVARAAGATVLERHDPERrgkgyALDFGFRHLLNLA 79
|
90 100
....*....|....*....|..
gi 4827175 225 DSPFAV-IFDCDHVPTRGFLRR 245
Cdd:cd06438 80 DDPDAVvVFDADNLVDPNALEE 101
|
|
| PLN02248 |
PLN02248 |
cellulose synthase-like protein |
327-451 |
3.13e-03 |
|
cellulose synthase-like protein
Pssm-ID: 215138 [Multi-domain] Cd Length: 1135 Bit Score: 42.33 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4827175 327 VTEDAHTALKMQRRGWGTAYLREPLAA--GLA----TERliLHigQRVRWARGMIQIMRLDNPMLGAG--LRWEQRLCYL 398
Cdd:PLN02248 835 VTEDVVTGYRMHNRGWRSVYCVTKRDAfrGTApinlTDR--LH--QVLRWATGSVEIFFSRNNALLASrrLKFLQRIAYL 910
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 4827175 399 SA-----MSHFLfaiprLTFLVSPLAFLFLGQNIIAASPLAISVYALphifhsVITLS 451
Cdd:PLN02248 911 NVgiypfTSIFL-----IVYCFLPALSLFSGQFIVQTLNVTFLVYLL------IITIT 957
|
|
| |
