|
Name |
Accession |
Description |
Interval |
E-value |
| bcsA |
PRK11498 |
cellulose synthase catalytic subunit; Provisional |
14-863 |
0e+00 |
|
cellulose synthase catalytic subunit; Provisional
Pssm-ID: 236918 [Multi-domain] Cd Length: 852 Bit Score: 1701.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 14 RQAVQARYRAYRRSGASALTAFFTTLLVALGWMLLRLESPAWRRVRAGRAYWFPHLSAERPRPADALRYLLQGAWLLLFR 93
Cdd:PRK11498 1 NARLIGRYRDYRRHGASAFSATLGCLWMILAWIFLPLEHPRWQRIRAEHKNLYPHINASRPRPLDPLRYLIQTLWLLIGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 94 SGRA--PVQRDYFAGWRRLQQRYADWLQGLPQRLKNAGVEQRSVERLGRMNRGLRRALFILVGVLAAILAMLCISQPFDL 171
Cdd:PRK11498 81 SRKEtpKPRRRAFSGLQNIRGRYHQWLEELPERVSHKTQHLDEKKELGHLSAGARRLILGIIVTFSLILALICITQPFNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 172 SAQFVFVLLLWGIAMVVRRVPGRLPALMLIVLSLTVSCRYLWWRYTATLNWDDPLSLVCGLLLLVAETYAWVVLVLGYFQ 251
Cdd:PRK11498 161 LAQFIFLMLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 252 TIWPLNRQPVPLPEDSATWPTIDLMVPTYNEDLGVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAFAAEVGVKYIAR 331
Cdd:PRK11498 241 VVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKYIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 332 PTHEHAKAGNINNALKQATGEFVAIFDCDHVPTRSFLQLTMGWFFKDKKLAMLQTPHHFFSPDPFERNLGRFRQTPNEGT 411
Cdd:PRK11498 321 PTHEHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDPFERNLGRFRKTPNEGT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 412 LFYGLVQDGNDMWDATFFCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQ 491
Cdd:PRK11498 401 LFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 492 RIRWARGMVQIFRLDNPLLGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIFAPALAIALYVLPHMIHA 571
Cdd:PRK11498 481 RIRWARGMVQIFRLDNPLTGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 572 SLTNSRIQGKYRHSFWSEIYETVLAWYIARPTTVALFNPHKGKFNVTAKGGLVEEEHVDWVITRPYMFLVVLNLAGLAFG 651
Cdd:PRK11498 561 SLTNSRIQGKYRHSFWSEIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGGLVEEEYVDWVISRPYIFLVLLNLVGVAVG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 652 AWRLAYGPTDEVMTVIISLVWVLYNMTILGGAVAVAVEAKQVRQAHRVEIAMPAAIARADGHLYPCTLRDYSDGGVGIEM 731
Cdd:PRK11498 641 IWRYFYGPPNEILTVIVSLVWVFYNLIILGGAVAVSVESKQVRRSHRVEMTMPAAIAREDGHLFSCTVQDFSDGGLGIKI 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 732 RVADTLKEGDKASLLLKRGQQEYSFPCVVTRAFGNKVGVRLVSLSTREHIDFIQCTFARADTWALWQDGFPEDRPIESLR 811
Cdd:PRK11498 721 NGQAQLLEGQKVNLLLKRGQQEYVFPTQVTRVMGNEVGLQLMPLTTQQHIDFVQCTFARADTWALWQDSFPEDKPLESLL 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 727182765 812 DVLALGFRGYVRMADYAPPLVRGLLVGVTSLTAWVVSFIPRGVGRDPTLGQQ 863
Cdd:PRK11498 801 DILKLGFRGYRHLAEFAPPSVKGIFRVLTSLVSWVVSFIPRRPERQEAAQPS 852
|
|
| CelA |
TIGR03030 |
cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 ... |
144-832 |
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: 981.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 144 GLRRALFILVGVLAAILAMLCISQPFDLSAQFVFVLLLWGIAMVVRRVPGRLPALMLIVLSLTVSCRYLWWRYTATLNWD 223
Cdd:TIGR03030 4 ALFKGLLFIIAVAGLLALLALITAPVTLETQLIIAGSAFLLLLILKRFNGKRPRLLLLVLSVFISLRYLWWRLTETLPFD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 224 DPLSLVCGLLLLVAETYAWVVLVLGYFQTIWPLNRQPVPLPEDSATWPTIDLMVPTYNEDLGVVKPTIYAALGIDWPKEK 303
Cdd:TIGR03030 84 NTLNFIFGTLLLLAELYSITILLLGYFQTVRPLDRTPVPLPLDPEEWPTVDVFIPTYNEDLEIVATTVLAAKNMDYPADK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 304 VNIYILDDGN------------------RPEFRAFAAEVGVKYIARPTHEHAKAGNINNALKQATGEFVAIFDCDHVPTR 365
Cdd:TIGR03030 164 FRVWILDDGGtdqkrndpdpeqaeaaqrREELKEFCRKLGVNYITRPRNVHAKAGNINNALKHTDGELILIFDADHVPTR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 366 SFLQLTMGWFFKDKKLAMLQTPHHFFSPDPFERNLGRFRQTPNEGTLFYGLVQDGNDMWDATFFCGSCAILRRSALDEIG 445
Cdd:TIGR03030 244 DFLQRTVGWFVEDPKLFLVQTPHFFVSPDPIERNLGTFRRMPNENELFYGLIQDGNDFWNAAFFCGSAAVLRREALDEIG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 446 GIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLLGKGLKLAQRLCYANA 525
Cdd:TIGR03030 324 GIAGETVTEDAETALKLHRRGWNSAYLDRPLIAGLAPETLSGHIGQRIRWAQGMMQIFRLDNPLLKRGLSFPQRLCYLNA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 526 MLHFLSGIPRLIFLTAPLAFLLLHAYIIFAPALAIALYVLPHMIHASLTNSRIQGKYRHSFWSEIYETVLAWYIARPTTV 605
Cdd:TIGR03030 404 MLFWFFPLPRVIFLTAPLAYLFFGLNIFVASALEILAYALPHMLHSLLTNSYLFGRVRWPFWSEVYETVLAVYLLPPVLV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 606 ALFNPHKGKFNVTAKGGLVEEEHVDwVITRPYMFLVVLNLAGLAFGAWRLaYGPTDEVMTVIISLVWVLYNMTILGGAVA 685
Cdd:TIGR03030 484 TLLNPKKPKFNVTPKGELLDEDYFS-PLSRPYLILFALILAGLAFGLYRI-YGYPIERGVLLVVLGWNLLNLILLGAALA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 686 VAVEAKQVRQAHRVEIAMPAAIARADGHLYPCTLRDYSDGGVGIEMRVADT----LKEGDKASLLLKRGQQEYSFPCVVT 761
Cdd:TIGR03030 562 VVAERRQRRSSPRIPCKIPAEVQRDGGRWVEATVEDASVGGLGIKINAQGApgpqLGAGVLVQIRPKRNGLPALKPARVR 641
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727182765 762 RAFGNKVGVRLVSLSTREHIDFIQCTFARADTWA-LWQDGFPEDRPIESLRDVLALGFRGYVRMADYAPPLV 832
Cdd:TIGR03030 642 GAGGVMIGLEFSPLNVQQVREIVDLVFARSDRWVaLWEERRRPDGPLRGLADFLKIALRGLFRSARDLVRAP 713
|
|
| CESA_CelA_like |
cd06421 |
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ... |
271-503 |
2.24e-120 |
|
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: 363.82 E-value: 2.24e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEDLGVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAFAAEVGVK----YIARPTHEHAKAGNINNAL 346
Cdd:cd06421 1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEygyrYLTRPDNRHAKAGNLNNAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 347 KQATGEFVAIFDCDHVPTRSFLQLTMGWFFKDKKLAMLQTPHHFFSPDPFERnlgRFRQTPNEGTLFYGLVQDGNDMWDA 426
Cdd:cd06421 81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDW---LADGAPNEQELFYGVIQPGRDRWGA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727182765 427 TFFCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWARGMVQIF 503
Cdd:cd06421 158 AFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
|
|
| BcsA |
COG1215 |
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ... |
241-620 |
1.08e-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: 166.46 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 241 AWVVLVLGYFQTIWPLNRQPvplpEDSATWPTIDLMVPTYNEDLgVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAF 320
Cdd:COG1215 3 LLLALLALLYLLLLALARRR----RAPADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 321 AAEVG-----VKYIARPTHEHaKAGNINNALKQATGEFVAIFDCDHVPTRSFLQLTMGwFFKDKKLAMlqtphhffspdp 395
Cdd:COG1215 78 ARELAaeyprVRVIERPENGG-KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVA-AFADPGVGA------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 396 fernlgrfrqtpnegtlfyglvqdgndmwdatffCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIP 475
Cdd:COG1215 144 ----------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 476 QAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLLGKGLKLAqrlcyanamlhflsgipRLIFLTAPLAFLLLhayiiFA 555
Cdd:COG1215 190 VVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLL-----------------FLLLLLLPLLLLLL-----LL 247
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727182765 556 PALAIALYVLPHMIHASLtnsriqgkyRHSFWSEIYETVLAWYIARPTTVALFNPHKGKFNVTAK 620
Cdd:COG1215 248 ALLALLLLLLPALLLALL---------LALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
|
|
| CESA_CaSu_A2 |
cd06437 |
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ... |
271-498 |
4.10e-30 |
|
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: 118.95 E-value: 4.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEdLGVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAFAAEV--------GVKYIARPTHEHAKAGNI 342
Cdd:cd06437 1 PMVTVQLPVFNE-KYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVeeyaaqgvNIKHVRRADRTGYKAGAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 343 NNALKQATGEFVAIFDCDHVPTRSFLQLTMgWFFKDKKLAMLQTPHHFFSPDpfERNLGRFR------------QTPNEG 410
Cdd:cd06437 80 AEGMKVAKGEYVAIFDADFVPPPDFLQKTP-PYFADPKLGFVQTRWGHINAN--YSLLTRVQamsldyhftieqVARSST 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 411 TLFYGlvqdgndmwdatfFCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIG 490
Cdd:cd06437 157 GLFFN-------------FNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRS 223
|
....*...
gi 727182765 491 QRIRWARG 498
Cdd:cd06437 224 QQHRWSKG 231
|
|
| CESA_NdvC_like |
cd06435 |
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ... |
275-504 |
2.37e-29 |
|
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: 117.12 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 275 LMVPTYNEDLGVVKPTIYAALGIDWPKEKVniYILDDGNRPEF-----RAFAAEVGVK--YIARPTHEHAKAGNINNALK 347
Cdd:cd06435 2 IHVPCYEEPPEMVKETLDSLAALDYPNFEV--IVIDNNTKDEAlwkpvEAHCAQLGERfrFFHVEPLPGAKAGALNYALE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 348 QATG--EFVAIFDCDHVPTRSFLQlTMGWFFKDKKLAMLQTPHHF--FSPDPFERNLGRfrqtpnEGTLFYGLVQDGNDM 423
Cdd:cd06435 80 RTAPdaEIIAVIDADYQVEPDWLK-RLVPIFDDPRVGFVQAPQDYrdGEESLFKRMCYA------EYKGFFDIGMVSRNE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 424 WDATFFCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWARGMVQIF 503
Cdd:cd06435 153 RNAIIQHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQIL 232
|
.
gi 727182765 504 R 504
Cdd:cd06435 233 K 233
|
|
| CESA_like |
cd06423 |
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ... |
275-455 |
3.99e-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: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 275 LMVPTYNEDLgVVKPTIYAALGIDWPKekVNIYILDDGNRPEFRAFAAEVGVKYIA-----RPTHEHAKAGNINNALKQA 349
Cdd:cd06423 1 IIVPAYNEEA-VIERTIESLLALDYPK--LEVIVVDDGSTDDTLEILEELAALYIRrvlvvRDKENGGKAGALNAGLRHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 350 TGEFVAIFDCDHVPTRSFLQ-LTMGWFFKDKKLAMLQTPHHFfspDPFERNLGRFrQTpNEGTLFYGLVQDGNDMWDATF 428
Cdd:cd06423 78 KGDIVVVLDADTILEPDALKrLVVPFFADPKVGAVQGRVRVR---NGSENLLTRL-QA-IEYLSIFRLGRRAQSALGGVL 152
|
170 180
....*....|....*....|....*...
gi 727182765 429 -FCGSCAILRRSALDEIGGIAVETVTED 455
Cdd:cd06423 153 vLSGAFGAFRREALREVGGWDEDTLTED 180
|
|
| Glycos_transf_2 |
pfam00535 |
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ... |
277-443 |
8.27e-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: 93.23 E-value: 8.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 277 VPTYNEdLGVVKPTIYAALgiDWPKEKVNIYILDDGNRPEFRAFAAEV-----GVKYIARPtHEHAKAGNINNALKQATG 351
Cdd:pfam00535 4 IPTYNE-EKYLLETLESLL--NQTYPNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLP-ENRGKAGARNAGLRAATG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 352 EFVAIFDCDHVPTRSFLQLTMGWFFKDKK-LAMLQTPHHFFSPDPFERNLGRFRQtpnegtLFYGLVQDGNDMWDATFFC 430
Cdd:pfam00535 80 DYIAFLDADDEVPPDWLEKLVEALEEDGAdVVVGSRYVIFGETGEYRRASRITLS------RLPFFLGLRLLGLNLPFLI 153
|
170
....*....|...
gi 727182765 431 GSCAILRRSALDE 443
Cdd:pfam00535 154 GGFALYRREALEE 166
|
|
| Glyco_trans_2_3 |
pfam13632 |
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ... |
353-564 |
4.85e-16 |
|
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: 77.38 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 353 FVAIFDCD-HVPTRSFLQLTmgWFFKDKKLAMLQTPHHFF-SPDPFERNLGRFRqtpNEGTLFYGLVQDGNDmwDATFFC 430
Cdd:pfam13632 1 WILLLDADtVLPPDCLLGIA--NEMASPEVAIIQGPILPMnVGNYLEELAALFF---ADDHGKSIPVRMALG--RVLPFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 431 GSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNpll 510
Cdd:pfam13632 74 GSGAFLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRL--- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 727182765 511 gkgLKLAQRLCYANAMLHflsgiprliFLTAPLAFLLLHAYIIFAPALAIALYV 564
Cdd:pfam13632 151 ---LGYLGTLLWSGLPLA---------LLLLLLFSISSLALVLLLLALLAGLLL 192
|
|
| CESA_like_2 |
cd06427 |
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ... |
271-501 |
8.78e-15 |
|
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, Glucan Biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of glucan.
Pssm-ID: 133049 [Multi-domain] Cd Length: 241 Bit Score: 74.98 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEdLGVVkPTIYAALG-IDWPKEKVNIYILDDGNRPEFRAFAAEVGVKYIAR-----PTHEHAKAGNINN 344
Cdd:cd06427 1 PVYTILVPLYKE-AEVL-PQLIASLSaLDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRvvvvpPSQPRTKPKACNY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 345 ALKQATGEFVAIFDCDHVPTRsfLQLTMGW--FFK-DKKLAMLQTPHHFFSPDpfeRNLgRFRQTPNEGTLFYGLVQDGN 421
Cdd:cd06427 79 ALAFARGEYVVIYDAEDAPDP--DQLKKAVaaFARlDDKLACVQAPLNYYNAR---ENW-LTRMFALEYAAWFDYLLPGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 422 DMWDATF-FCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGlATESLSAHIGQRIRWARGMV 500
Cdd:cd06427 153 ARLGLPIpLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLEE-ANNALGNWIRQRSRWIKGYM 231
|
.
gi 727182765 501 Q 501
Cdd:cd06427 232 Q 232
|
|
| Glyco_tranf_2_3 |
pfam13641 |
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ... |
271-498 |
4.48e-14 |
|
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: 72.40 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEDlGVVKPTIYAALGIDWPKekVNIYILDDGNRPEFRAFAAEVGVKY------IARPTHE---HAKAGN 341
Cdd:pfam13641 2 PDVSVVVPAFNED-SVLGRVLEAILAQPYPP--VEVVVVVNPSDAETLDVAEEIAARFpdvrlrVIRNARLlgpTGKSRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 342 INNALKQATGEFVAIFDCDHVPTRSFLQLTMGWFfKDKKLAMLQTPhhffspdPFERNLGRFRQTPneGTLFYGLVQ-DG 420
Cdd:pfam13641 79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-DSPKVGAVGTP-------VFSLNRSTMLSAL--GALEFALRHlRM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 421 NDMWDA---TFFCGSCAILRRSALDEIGGIAVE-TVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWA 496
Cdd:pfam13641 149 MSLRLAlgvLPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWV 228
|
..
gi 727182765 497 RG 498
Cdd:pfam13641 229 YG 230
|
|
| PLN02915 |
PLN02915 |
cellulose synthase A [UDP-forming], catalytic subunit |
443-651 |
1.64e-11 |
|
cellulose synthase A [UDP-forming], catalytic subunit
Pssm-ID: 215494 [Multi-domain] Cd Length: 1044 Bit Score: 68.42 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 443 EIGGIaVETVTEDAHTSLRLHRRGHTSAYI--RIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDN-PL---LGKGLKL 516
Cdd:PLN02915 732 EIGWI-YGSVTEDILTGFKMHCRGWKSVYCmpKRPAFKGSAPINLSDRLHQVLRWALGSVEIFMSRHcPLwyaYGGKLKW 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 517 AQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----FAPALAIALYVlpHMIHASLTNSRIQGKYRHSFW-SEI 590
Cdd:PLN02915 811 LERLAYINTIVYPFTSIPLLAYCTIPAVCLLTGKFIIptlnnLASIWFLALFL--SIIATSVLELRWSGVSIEDLWrNEQ 888
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727182765 591 YetvlaWYIArPTTVALFNPHKG----------KFNVTAKGGLVEEEH------VDW-VITRPYMFLVVLNLAGLAFG 651
Cdd:PLN02915 889 F-----WVIG-GVSAHLFAVFQGllkvlggvdtNFTVTSKAADDEADEfgelylFKWtTLLIPPTTLIILNMVGVVAG 960
|
|
| Cellulose_synt |
pfam03552 |
Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose ... |
442-553 |
5.98e-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: 66.32 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 442 DEIGGIaVETVTEDAHTSLRLHRRGHTSAYIRIPQAA--GLATESLSAHIGQRIRWARGMVQIF-RLDNPLL-GKGLKLA 517
Cdd:pfam03552 411 KEIGWI-YGSVTEDILTGFRMHCRGWRSIYCMPKRDAfkGSAPINLSDRLHQVLRWALGSVEIFfSRHCPIWyGGRLKFL 489
|
90 100 110
....*....|....*....|....*....|....*.
gi 727182765 518 QRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII 553
Cdd:pfam03552 490 QRFAYINVGIYPFTSIPLLAYCFLPAICLFTGKFIV 525
|
|
| CESA_like_1 |
cd06439 |
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ... |
247-501 |
3.30e-10 |
|
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: 61.44 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 247 LGY--FQTIWPLNRQPVPLPEDSATWPTIDLMVPTYNEDlGVVKPTIYAALGIDWPKEKVNIYILDDG---NRPEFRAFA 321
Cdd:cd06439 3 FGYplLLKLLARLRPKPPSLPDPAYLPTVTIIIPAYNEE-AVIEAKLENLLALDYPRDRLEIIVVSDGstdGTAEIAREY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 322 AEVGVKYIARPTHeHAKAGNINNALKQATGEFVAIFDCDHVPTRSFLQLTMGWfFKDKKLAMLQTPHHFFSPDPFERNLG 401
Cdd:cd06439 82 ADKGVKLLRFPER-RGKAAALNRALALATGEIVVFTDANALLDPDALRLLVRH-FADPSVGAVSGELVIVDGGGSGSGEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 402 RFRQtpnegtlFYGLVQDGNDMWDATF-FCGSCAILRRSAldeIGGIAVETVTEDAHTSLRLHRRGHTSAYirIPQAAGL 480
Cdd:cd06439 160 LYWK-------YENWLKRAESRLGSTVgANGAIYAIRREL---FRPLPADTINDDFVLPLRIARQGYRVVY--EPDAVAY 227
|
250 260
....*....|....*....|...
gi 727182765 481 --ATESLSAHIGQRIRWARGMVQ 501
Cdd:cd06439 228 eeVAEDGSEEFRRRVRIAAGNLQ 250
|
|
| PLN02189 |
PLN02189 |
cellulose synthase |
451-564 |
6.41e-10 |
|
cellulose synthase
Pssm-ID: 215121 [Multi-domain] Cd Length: 1040 Bit Score: 63.11 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 451 TVTEDAHTSLRLHRRGHTSAYIRIPQAA--GLATESLSAHIGQRIRWARGMVQI-FRLDNPLL----GKGLKLAQRLCYA 523
Cdd:PLN02189 736 SITEDILTGFKMHCRGWRSIYCMPKRAAfkGSAPINLSDRLNQVLRWALGSVEIfFSRHSPLLygykGGNLKWLERFAYV 815
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 727182765 524 NAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----FAPALAIALYV 564
Cdd:PLN02189 816 NTTIYPFTSLPLLAYCTLPAICLLTGKFIMppistFASLFFIALFM 861
|
|
| PLN02638 |
PLN02638 |
cellulose synthase A (UDP-forming), catalytic subunit |
443-564 |
6.72e-10 |
|
cellulose synthase A (UDP-forming), catalytic subunit
Pssm-ID: 215343 [Multi-domain] Cd Length: 1079 Bit Score: 63.02 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 443 EIGGIaVETVTEDAHTSLRLHRRGHTSAYI--RIPQAAGLATESLSAHIGQRIRWARGMVQI-FRLDNPL---LGKGLKL 516
Cdd:PLN02638 768 EIGWI-YGSVTEDILTGFKMHARGWRSIYCmpKRPAFKGSAPINLSDRLNQVLRWALGSVEIlFSRHCPIwygYGGRLKW 846
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 727182765 517 AQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----FAPALAIALYV 564
Cdd:PLN02638 847 LERFAYVNTTIYPITSIPLLLYCTLPAVCLLTGKFIIpqisnIASIWFISLFL 899
|
|
| PLN02195 |
PLN02195 |
cellulose synthase A |
443-670 |
1.01e-09 |
|
cellulose synthase A
Pssm-ID: 215124 [Multi-domain] Cd Length: 977 Bit Score: 62.30 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 443 EIGGIaVETVTEDAHTSLRLHRRGHTSAY---IRiPQAAGLATESLSAHIGQRIRWARGMVQIFRLDN-PLL----GKGL 514
Cdd:PLN02195 664 EIGWI-YGSVTEDILTGFKMHCRGWRSIYcmpVR-PAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHcPLWygygGGRL 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 515 KLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----FAPALAIALYVlpHMIHASLTNSRIQGKYRHSFW-S 588
Cdd:PLN02195 742 KWLQRLAYINTIVYPFTSLPLIAYCTLPAICLLTGKFIIptlsnLASMLFLGLFI--SIILTSVLELRWSGVSIEDLWrN 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 589 EIYetvlaWYIArPTTVALFNPHKG----------KFNVTAK----GGLVEEEHVDW-VITRPYMFLVVLNLAGLAFG-- 651
Cdd:PLN02195 820 EQF-----WVIG-GVSAHLFAVFQGflkmlagldtNFTVTAKaaddTEFGELYMVKWtTLLIPPTSLLIINLVGVVAGfs 893
|
250 260
....*....|....*....|....*..
gi 727182765 652 --------AWRLAYGPTDEVMTVIISL 670
Cdd:PLN02195 894 dalnkgyeAWGPLFGKVFFAFWVILHL 920
|
|
| Glyco_tranf_GTA_type |
cd00761 |
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ... |
277-403 |
1.05e-09 |
|
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
Pssm-ID: 132997 [Multi-domain] Cd Length: 156 Bit Score: 57.90 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 277 VPTYNEDlGVVKPTIYAALGIDWPKekVNIYILDDGNRPEFRAFAAEVGVKYIARPTHEHA----KAGNINNALKQATGE 352
Cdd:cd00761 3 IPAYNEE-PYLERCLESLLAQTYPN--FEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEenqgLAAARNAGLKAARGE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 727182765 353 FVAIFDCDHVPTRSFLQLTMGWFFKDKKLAMLQTPH-HFFSPDPFERNLGRF 403
Cdd:cd00761 80 YILFLDADDLLLPDWLERLVAELLADPEADAVGGPGnLLFRRELLEEIGGFD 131
|
|
| PLN02400 |
PLN02400 |
cellulose synthase |
443-553 |
1.83e-09 |
|
cellulose synthase
Pssm-ID: 215224 [Multi-domain] Cd Length: 1085 Bit Score: 61.53 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 443 EIGGIaVETVTEDAHTSLRLHRRGHTSAYIRIPQAA--GLATESLSAHIGQRIRWARGMVQIFRLDNPLLGKG----LKL 516
Cdd:PLN02400 773 EIGWI-YGSVTEDILTGFKMHARGWISIYCMPPRPAfkGSAPINLSDRLNQVLRWALGSIEILLSRHCPIWYGyngrLKL 851
|
90 100 110
....*....|....*....|....*....|....*..
gi 727182765 517 AQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII 553
Cdd:PLN02400 852 LERLAYINTIVYPITSIPLLAYCVLPAFCLITNKFII 888
|
|
| PLN02436 |
PLN02436 |
cellulose synthase A |
443-564 |
1.85e-09 |
|
cellulose synthase A
Pssm-ID: 215239 [Multi-domain] Cd Length: 1094 Bit Score: 61.81 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 443 EIGGIaVETVTEDAHTSLRLHRRGHTSAYI--RIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDN-PL---LGKGLKL 516
Cdd:PLN02436 784 EIGWI-YGSVTEDILTGFKMHCHGWRSVYCipKRPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHcPIwygYGGGLKW 862
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 727182765 517 AQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----FAPALAIALYV 564
Cdd:PLN02436 863 LERFSYINSVVYPWTSIPLIVYCTLPAICLLTGKFIVpeisnYASILFMALFI 915
|
|
| PLN02190 |
PLN02190 |
cellulose synthase-like protein |
450-570 |
4.31e-09 |
|
cellulose synthase-like protein
Pssm-ID: 215122 [Multi-domain] Cd Length: 756 Bit Score: 60.26 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 450 ETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLA---TESLSAHIGQRiRWARGMVQI-FRLDNPLLG---KGLKLAQRLCY 522
Cdd:PLN02190 456 DSVAEDLNTSIGIHSRGWTSSYISPDPPAFLGsmpPGGPEAMVQQR-RWATGLIEVlFNKQSPLIGmfcRKIRFRQRLAY 534
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 727182765 523 AnAMLHFLSGIPRLIFLTAPlAFLLLHAYIIFAPALAIALYVLPHMIH 570
Cdd:PLN02190 535 L-YVFTCLRSIPELIYCLLP-AYCLLHNSALFPKGVYLGIIVTLVGMH 580
|
|
| PilZ |
pfam07238 |
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ... |
692-789 |
4.60e-08 |
|
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: 51.73 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 692 QVRQAHRVEIAMPAAIaRADGHLYPCTLRDYSDGGVGIEMRVADtLKEGD--KASLLLKRGQQEYSFPCVVTRAFGN--- 766
Cdd:pfam07238 1 QRRRFPRVPVSLPVTL-RDGGGEYKGRLIDISLGGAAIRLPDEP-LALGDrvELSLDLLDDGQELALPGRVVRIRPDedg 78
|
90 100
....*....|....*....|....
gi 727182765 767 -KVGVRLVSLSTREHIDFIQCTFA 789
Cdd:pfam07238 79 aRVGVQFLDLDEEQRRLLVRLLFG 102
|
|
| Glyco_transf_21 |
pfam13506 |
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ... |
332-497 |
1.33e-07 |
|
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: 52.29 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 332 PTHEHAKAGNINNALKQATGEFVAIFDCDHVPTRSFLQLTMGwFFKDKKLAMLQTPHHFFSPDPFERNLGRFRQTPNEGT 411
Cdd:pfam13506 12 PVGVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLA-PLADPKVGLVTSPPVGSDPKGLAAALEAAFFNTLAGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 412 LFYGLVQdgndmwdATFFCGSCAILRRSALDEIGGIA--VETVTEDAHTSLRLHRRGHTSAYIRIP--QAAGLATESLSA 487
Cdd:pfam13506 91 LQAALSG-------IGFAVGMSMAFRRADLERIGGFEalADYLAEDYALGKLLRAAGLKVVLSPRPilQTSGPRRTSFRA 163
|
170
....*....|
gi 727182765 488 HIGQRIRWAR 497
Cdd:pfam13506 164 FMARQLRWAR 173
|
|
| GT_2_like_e |
cd04192 |
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ... |
297-498 |
1.43e-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: 50.36 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 297 IDWPKEKVNIYILDDGNRPEFR---AFAAEVGVK--YIARPTHEHA--KAGNINNALKQATGEFVAIFDCDHVPTRSFLQ 369
Cdd:cd04192 22 LDYPKEKFEVILVDDHSTDGTVqilEFAAAKPNFqlKILNNSRVSIsgKKNALTTAIKAAKGDWIVTTDADCVVPSNWLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 370 LTMGwFFKDKKLAMLQTPHHFFSPDPFernLGRFRQTPNEGTLFYGLVQDGndmWDATFFCGSCAI-LRRSALDEIGGIA 448
Cdd:cd04192 102 TFVA-FIQKEQIGLVAGPVIYFKGKSL---LAKFQRLDWLSLLGLIAGSFG---LGKPFMCNGANMaYRKEAFFEVGGFE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 727182765 449 --VETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLAT---ESLSAHIGQRIRWARG 498
Cdd:cd04192 175 gnDHIASGDDELLLAKVASKYPKVAYLKNPEALVTTqpvTSWKELLNQRKRWASK 229
|
|
| WcaA |
COG0463 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
271-479 |
3.79e-06 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440231 [Multi-domain] Cd Length: 208 Bit Score: 48.54 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEDlGVVKPTIYAALGIDWPKekVNIYILDDGNRPEFRAFAAEVG-----VKYIARPTHEHaKAGNINNA 345
Cdd:COG0463 2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPD--FEIIVVDDGSTDGTAEILRELAakdprIRVIRLERNRG-KGAARNAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 346 LKQATGEFVAIFDCDHVPTRSFLQLTMGwffkdkklAMLQTPHHFFSPDPFERNLGR-FRQTPNEGTLFYGLVQDGNDMw 424
Cdd:COG0463 78 LAAARGDYIAFLDADDQLDPEKLEELVA--------ALEEGPADLVYGSRLIREGESdLRRLGSRLFNLVRLLTNLPDS- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 727182765 425 datffCGSCAILRRSALDEIGgiAVETVTEDAHTsLRLHRRGHTSAYIRIPQAAG 479
Cdd:COG0463 149 -----TSGFRLFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVPVRYRAG 195
|
|
| PLN02248 |
PLN02248 |
cellulose synthase-like protein |
452-539 |
1.99e-05 |
|
cellulose synthase-like protein
Pssm-ID: 215138 [Multi-domain] Cd Length: 1135 Bit Score: 48.49 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 452 VTEDAHTSLRLHRRGHTSAYIRIPQAA--GLATESLSAHIGQRIRWARGMVQIF--RlDNPLLG-KGLKLAQRLCYAN-A 525
Cdd:PLN02248 835 VTEDVVTGYRMHNRGWRSVYCVTKRDAfrGTAPINLTDRLHQVLRWATGSVEIFfsR-NNALLAsRRLKFLQRIAYLNvG 913
|
90
....*....|....
gi 727182765 526 MLHFLSgiprlIFL 539
Cdd:PLN02248 914 IYPFTS-----IFL 922
|
|
| Glucosylceramide_synthase |
cd02520 |
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ... |
431-497 |
5.36e-05 |
|
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: 44.90 E-value: 5.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727182765 431 GSCAILRRSALDEIGGIAV--ETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWAR 497
Cdd:cd02520 126 GKSMALRREVLDAIGGFEAfaDYLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSR 194
|
|
| YcgR |
COG5581 |
Cyclic di-GMP-binding flagellar brake protein FlgZ/YcgR, contains PilZNR(YcgR) and PilZ ... |
688-779 |
8.83e-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: 41.52 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 688 VEAKQVRQAHRVEIAMPAAI----ARADGHLYPCTLRDYSDGGVGIEMRVADTLKEGDKASLLLK-RGQQEYSFPCVVTR 762
Cdd:COG5581 83 IERIQRREYFRVPVPLDVPVrclrPDGEGEPLEGRLLDISGGGLALVLPEPPPLEVGDILELRLDlPDEGEIVVDAEVRR 162
|
90 100
....*....|....*....|....
gi 727182765 763 AF-------GNKVGVRLVSLSTRE 779
Cdd:COG5581 163 VVevelgkgKYRLGCEFVDLSEAD 186
|
|
| GT2_RfbC_Mx_like |
cd04184 |
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ... |
271-360 |
9.44e-04 |
|
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133027 [Multi-domain] Cd Length: 202 Bit Score: 41.42 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEDLGVVKPTI-------YAalgiDWpkekvNIYILDDG-NRPEFRAFAAEVG-----VKYIARPTHEHA 337
Cdd:cd04184 1 PLISIVMPVYNTPEKYLREAIesvraqtYP----NW-----ELCIADDAsTDPEVKRVLKKYAaqdprIKVVFREENGGI 71
|
90 100
....*....|....*....|...
gi 727182765 338 kAGNINNALKQATGEFVAIFDCD 360
Cdd:cd04184 72 -SAATNSALELATGEFVALLDHD 93
|
|
| PLN02893 |
PLN02893 |
Cellulose synthase-like protein |
451-554 |
1.79e-03 |
|
Cellulose synthase-like protein
Pssm-ID: 215483 [Multi-domain] Cd Length: 734 Bit Score: 42.00 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 451 TVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAH--IGQRIRWARGMVQI-FRLDNPLL--GKGLKLAQRLCYANA 525
Cdd:PLN02893 444 SLVEDYYTGYRLQCEGWKSIFCNPKRPAFLGDSPINLHdvLNQQKRWSVGLLEVaFSKYSPITfgVKSIGLLMGLGYAHY 523
|
90 100 110
....*....|....*....|....*....|...
gi 727182765 526 MLHFLSGIPRLIFltaplAFL----LLHAYIIF 554
Cdd:PLN02893 524 AFWPIWSIPITIY-----AFLpqlaLLNGVSIF 551
|
|
| PLN02638 |
PLN02638 |
cellulose synthase A (UDP-forming), catalytic subunit |
189-312 |
2.24e-03 |
|
cellulose synthase A (UDP-forming), catalytic subunit
Pssm-ID: 215343 [Multi-domain] Cd Length: 1079 Bit Score: 41.83 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 189 RRVP---GRL-PALMLIVLSLTVSCRYLWWRYTATLnwddPLSLVCGLLLLVAETYAWVVLVLGYFQTIWPLNRQP---- 260
Cdd:PLN02638 259 RKVSipsSRInPYRMVIVLRLVILCIFLHYRITNPV----RNAYALWLISVICEIWFALSWILDQFPKWLPVNRETyldr 334
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 727182765 261 VPLPEDSATWPT----IDLMVPTYN---EDLGVVKPTIYAALGIDWPKEKVNIYILDDG 312
Cdd:PLN02638 335 LALRYDREGEPSqlaaVDIFVSTVDplkEPPLVTANTVLSILAVDYPVDKVSCYVSDDG 393
|
|
| DPM_DPG-synthase_like |
cd04179 |
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ... |
277-360 |
4.30e-03 |
|
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.
Pssm-ID: 133022 [Multi-domain] Cd Length: 185 Bit Score: 39.09 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 277 VPTYNEDlGVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAFAAEVGVKYIARPTHEHA----KAGNINNALKQATGE 352
Cdd:cd04179 3 IPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSrnfgKGAAVRAGFKAARGD 81
|
....*...
gi 727182765 353 FVAIFDCD 360
Cdd:cd04179 82 IVVTMDAD 89
|
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