|
Name |
Accession |
Description |
Interval |
E-value |
| CelA |
TIGR03030 |
cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 ... |
1-715 |
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: 1086.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 1 MNKAITVIVWLLVSLCVLAIITMPVSLQTHLVATAISLILLATIKSFNGQGAwRLVALGFGTAIVLRYVYWRTTSTLPPv 80
Cdd:TIGR03030 5 LFKGLLFIIAVAGLLALLALITAPVTLETQLIIAGSAFLLLLILKRFNGKRP-RLLLLVLSVFISLRYLWWRLTETLPF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 81 NQLENFIPGFLLYLAEMYSVVMLGLSLVIVSMPLPS-RKTRPGSPDYRPTVDVFVPSYNEDAELLANTLAAAKNMDYPAD 159
Cdd:TIGR03030 83 DNTLNFIFGTLLLLAELYSITILLLGYFQTVRPLDRtPVPLPLDPEEWPTVDVFIPTYNEDLEIVATTVLAAKNMDYPAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 160 RFTVWLLDDGGSVQKRNAANIVEAQAAQRRhEELKKLCEDLDVRYLTRERNVHAKAGNLNNGLAHSTGELVTVFDADHAP 239
Cdd:TIGR03030 163 KFRVWILDDGGTDQKRNDPDPEQAEAAQRR-EELKEFCRKLGVNYITRPRNVHAKAGNINNALKHTDGELILIFDADHVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 240 ARDFLLETVGYFDEDPRLFLVQTPHFFVNPDPIERNLRTFETMPSENEMFYGIIQRGLDKWNGAFFCGSAAVLRREALQD 319
Cdd:TIGR03030 242 TRDFLQRTVGWFVEDPKLFLVQTPHFFVSPDPIERNLGTFRRMPNENELFYGLIQDGNDFWNAAFFCGSAAVLRREALDE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 320 SDGFSGVSITEDCETALALHSRGWNSVYVDKPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQPLFKRGLSFTQRLCYM 399
Cdd:TIGR03030 322 IGGIAGETVTEDAETALKLHRRGWNSAYLDRPLIAGLAPETLSGHIGQRIRWAQGMMQIFRLDNPLLKRGLSFPQRLCYL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 400 SSTLFWLFPFPRTIFLFAPLFYLFFDLQIFVASGGEFLAYTAAYMLVNLMMQNYLYGSFRWPWISELYEYVQTVHLLPAV 479
Cdd:TIGR03030 402 NAMLFWFFPLPRVIFLTAPLAYLFFGLNIFVASALEILAYALPHMLHSLLTNSYLFGRVRWPFWSEVYETVLAVYLLPPV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 480 VSVIFNPGKPTFKVTAKDESIAEARLSEISRPFFVIFALLLVAMAFAVWRIYSEPYKADVTLVVGGWNLLNLIFAGCALG 559
Cdd:TIGR03030 482 LVTLLNPKKPKFNVTPKGELLDEDYFSPLSRPYLILFALILAGLAFGLYRIYGYPIERGVLLVVLGWNLLNLILLGAALA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 560 VVSERGDKSASRRITVKRRCEVQLGGSDtWVPASIDNVSVHGLLINIFDS-ATNIEKGATAIVKVKPHSEGVPETMPLNv 638
Cdd:TIGR03030 562 VVAERRQRRSSPRIPCKIPAEVQRDGGR-WVEATVEDASVGGLGIKINAQgAPGPQLGAGVLVQIRPKRNGLPALKPAR- 639
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15160069 639 vrtVRGEGFVSIGCTFSPQRAVDHRLIADLIFANSEQWSEFQRVRRKNPGLIRGTAIFLAIALFQTQRGLYYLVRAR 715
Cdd:TIGR03030 640 ---VRGAGGVMIGLEFSPLNVQQVREIVDLVFARSDRWVALWEERRRPDGPLRGLADFLKIALRGLFRSARDLVRAP 713
|
|
| bcsA |
PRK11498 |
cellulose synthase catalytic subunit; Provisional |
2-594 |
1.94e-135 |
|
cellulose synthase catalytic subunit; Provisional
Pssm-ID: 236918 [Multi-domain] Cd Length: 852 Bit Score: 420.20 E-value: 1.94e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 2 NKAITVIVWLLVslCVLAI--ITMPVSLQthlvATAISLILLATIKSFNGQGAWRLVALgfgTAIVL------RYVYWRT 73
Cdd:PRK11498 135 RRLILGIIVTFS--LILALicITQPFNPL----AQFIFLMLLWGVALLVRRMPGRFSAL---MLIVLsltvscRYIWWRY 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 74 TSTL---PPVNqlenFIPGFLLYLAEMYSVVMLGLSLVIVSMPLpSRK--TRPGSPDYRPTVDVFVPSYNEDAELLANTL 148
Cdd:PRK11498 206 TSTLnwdDPVS----LVCGLILLFAETYAWIVLVLGYFQVVWPL-NRQpvPLPKDMSLWPTVDIFVPTYNEDLNVVKNTI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 149 AAAKNMDYPADRFTVWLLDDGGsvqkrnaaniveaqaaqrrHEELKKLCEDLDVRYLTRERNVHAKAGNLNNGLAHSTGE 228
Cdd:PRK11498 281 YASLGIDWPKDKLNIWILDDGG-------------------REEFRQFAQEVGVKYIARPTHEHAKAGNINNALKYAKGE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 229 LVTVFDADHAPARDFLLETVGYFDEDPRLFLVQTPHFFVNPDPIERNLRTFETMPSENEMFYGIIQRGLDKWNGAFFCGS 308
Cdd:PRK11498 342 FVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCGS 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 309 AAVLRREALQDSDGFSGVSITEDCETALALHSRGWNSVYVDKPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQPLFKR 388
Cdd:PRK11498 422 CAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLTGK 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 389 GLSFTQRLCYMSSTLFWLFPFPRTIFLFAPLFYLFFDLQIFVASGGEFLAYTAAYM----LVNLMMQnylyGSFRWPWIS 464
Cdd:PRK11498 502 GLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMihasLTNSRIQ----GKYRHSFWS 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 465 ELYEYVQTVHLLPAVVSVIFNPGKPTFKVTAKDESIAEARLS-EISRPFFVIFALLLVAMAFAVWRIYSEPYKADVTLVV 543
Cdd:PRK11498 578 EIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGGLVEEEYVDwVISRPYIFLVLLNLVGVAVGIWRYFYGPPNEILTVIV 657
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 15160069 544 G-GWNLLNLIFAGCALGVVSErgdksaSRRITVKRRCEVQLggsdtwvPASI 594
Cdd:PRK11498 658 SlVWVFYNLIILGGAVAVSVE------SKQVRRSHRVEMTM-------PAAI 696
|
|
| CESA_CelA_like |
cd06421 |
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ... |
128-379 |
6.08e-121 |
|
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: 361.50 E-value: 6.08e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 128 PTVDVFVPSYNEDAELLANTLAAAKNMDYPADRFTVWLLDDGGSVQKRNAAniveaqaaqrrheelKKLCEDLDVRYLTR 207
Cdd:cd06421 1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALA---------------AELGVEYGYRYLTR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 208 ERNVHAKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFDEDPRLFLVQTPHFFVNPDPIERnlrTFETMPSENE 287
Cdd:cd06421 66 PDNRHAKAGNLNNALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDW---LADGAPNEQE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 288 MFYGIIQRGLDKWNGAFFCGSAAVLRREALQDSDGFSGVSITEDCETALALHSRGWNSVYVDKPLIAGLQPATFASFIGQ 367
Cdd:cd06421 143 LFYGVIQPGRDRWGAAFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQ 222
|
250
....*....|..
gi 15160069 368 RSRWAQGMMQIL 379
Cdd:cd06421 223 RLRWARGMLQIL 234
|
|
| BcsA |
COG1215 |
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ... |
91-460 |
3.44e-50 |
|
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: 177.63 E-value: 3.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 91 LLYLAEMYSVVMLGLSLVIvsmplpsrkTRPGSPDYRPTVDVFVPSYNEdAELLANTLAAAKNMDYPADRFTVWLLDDGG 170
Cdd:COG1215 1 LLLLLALLALLYLLLLALA---------RRRRAPADLPRVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLEVIVVDDGS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 171 SvqkRNAANIVEAQAAqrrheelkklcEDLDVRYLTRERNVHaKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGY 250
Cdd:COG1215 71 T---DETAEIARELAA-----------EYPRVRVIERPENGG-KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 251 FDEDprlflvqtphffvnpdpiernlrtfetmpsenemfygiiqrgldkwnGAFFCGSAAVLRREALQDSDGFSGVSITE 330
Cdd:COG1215 136 FADP-----------------------------------------------GVGASGANLAFRREALEEVGGFDEDTLGE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 331 DCETALALHSRGWNSVYVDKPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQPLFKRGLSFTQRLCYMSSTLFWLFPFP 410
Cdd:COG1215 169 DLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLLLLLLPLLLLLLLLA 248
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15160069 411 RTIFLFAPLFYLFFDLQIFVASGGEFLAYTAAYMLVNLMMQNYLYGSFRW 460
Cdd:COG1215 249 LLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKKVVW 298
|
|
| CESA_CaSu_A2 |
cd06437 |
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ... |
128-374 |
7.95e-39 |
|
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: 143.60 E-value: 7.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 128 PTVDVFVPSYNEdAELLANTLAAAKNMDYPADRFTVWLLDDGGSVQKRNAANIVEAQAAQrrheelkklceDLDVRYLTR 207
Cdd:cd06437 1 PMVTVQLPVFNE-KYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-----------GVNIKHVRR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 208 ERNVHAKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFDeDPRLFLVQTPHFFVNPDpieRNLRT-FETMpsEN 286
Cdd:cd06437 69 ADRTGYKAGALAEGMKVAKGEYVAIFDADFVPPPDFLQKTPPYFA-DPKLGFVQTRWGHINAN---YSLLTrVQAM--SL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 287 EMFYGIIQRGLDKWNGAF-FCGSAAVLRREALQDSDGFSGVSITEDCETALALHSRGWNSVYVDKPLIAGLQPATFASFI 365
Cdd:cd06437 143 DYHFTIEQVARSSTGLFFnFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYR 222
|
....*....
gi 15160069 366 GQRSRWAQG 374
Cdd:cd06437 223 SQQHRWSKG 231
|
|
| CESA_NdvC_like |
cd06435 |
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ... |
134-379 |
5.12e-36 |
|
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: 135.99 E-value: 5.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 134 VPSYNEDAELLANTLAAAKNMDYPadRFTVWLLDDggSVQKRNAANIVEAqaaqrrheelkkLCEDLDVR--YLTRERNV 211
Cdd:cd06435 4 VPCYEEPPEMVKETLDSLAALDYP--NFEVIVIDN--NTKDEALWKPVEA------------HCAQLGERfrFFHVEPLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 212 HAKAGNLNNGLAHSTG--ELVTVFDADHAPARDFLLETVGYFDeDPRLFLVQTPHFFVNPdpiERNLrTFETMPSENEMF 289
Cdd:cd06435 68 GAKAGALNYALERTAPdaEIIAVIDADYQVEPDWLKRLVPIFD-DPRVGFVQAPQDYRDG---EESL-FKRMCYAEYKGF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 290 YGIIQRGLDKWNGAFFCGSAAVLRREALQDSDGFSGVSITEDCETALALHSRGWNSVYVDKPLIAGLQPATFASFIGQRS 369
Cdd:cd06435 143 FDIGMVSRNERNAIIQHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRF 222
|
250
....*....|
gi 15160069 370 RWAQGMMQIL 379
Cdd:cd06435 223 RWAYGAVQIL 232
|
|
| CESA_like |
cd06423 |
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ... |
132-331 |
4.93e-27 |
|
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: 108.08 E-value: 4.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 132 VFVPSYNEDAELlANTLAAAKNMDYPadRFTVWLLDDGGsvqKRNAANIVEAQAAQRRHeelkklcedlDVRYLTRERNv 211
Cdd:cd06423 1 IIVPAYNEEAVI-ERTIESLLALDYP--KLEVIVVDDGS---TDDTLEILEELAALYIR----------RVLVVRDKEN- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 212 HAKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFDEDPRLFLVQTphffvNPDPIERNLRTFETMPS-ENEMFY 290
Cdd:cd06423 64 GGKAGALNAGLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQG-----RVRVRNGSENLLTRLQAiEYLSIF 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15160069 291 GIIQRGLDKWNG-AFFCGSAAVLRREALQDSDGFSGVSITED 331
Cdd:cd06423 139 RLGRRAQSALGGvLVLSGAFGAFRREALREVGGWDEDTLTED 180
|
|
| Glycos_transf_2 |
pfam00535 |
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ... |
131-319 |
1.14e-26 |
|
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: 106.71 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 131 DVFVPSYNEdAELLANTLAAAKNMDYPadRFTVWLLDDGgsvQKRNAANIVEAQAAQrrheelkklceDLDVRYLTRERN 210
Cdd:pfam00535 1 SVIIPTYNE-EKYLLETLESLLNQTYP--NFEIIVVDDG---STDGTVEIAEEYAKK-----------DPRVRVIRLPEN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 211 vHAKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFDEDPR-LFLVQTPHFFVNPDPIERNLRTFetmpseNEMF 289
Cdd:pfam00535 64 -RGKAGARNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGAdVVVGSRYVIFGETGEYRRASRIT------LSRL 136
|
170 180 190
....*....|....*....|....*....|
gi 15160069 290 YGIIQRGLDKWNGAFFCGSAAVLRREALQD 319
Cdd:pfam00535 137 PFFLGLRLLGLNLPFLIGGFALYRREALEE 166
|
|
| Glyco_trans_2_3 |
pfam13632 |
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ... |
229-424 |
4.64e-21 |
|
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.
Pssm-ID: 433365 [Multi-domain] Cd Length: 192 Bit Score: 91.63 E-value: 4.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 229 LVTVFDADHAPARDFLLETVGYFdEDPRLFLVQTPHFFVNPDPIERNLRTFETmpseNEMFYGIIQRGLDKWNGAFFCGS 308
Cdd:pfam13632 1 WILLLDADTVLPPDCLLGIANEM-ASPEVAIIQGPILPMNVGNYLEELAALFF----ADDHGKSIPVRMALGRVLPFVGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 309 AAVLRREALQDSDGFSGVSITEDCETALALHSRGWNSVYVDKPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQplfkR 388
Cdd:pfam13632 76 GAFLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRL----L 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 15160069 389 GLSFTQRLCYMSSTLFWLFPFPRTIFLFAPLFYLFF 424
Cdd:pfam13632 152 GYLGTLLWSGLPLALLLLLLFSISSLALVLLLLALL 187
|
|
| Glyco_tranf_2_3 |
pfam13641 |
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ... |
128-374 |
6.87e-19 |
|
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.
Pssm-ID: 433372 [Multi-domain] Cd Length: 230 Bit Score: 86.27 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 128 PTVDVFVPSYNEDAeLLANTLAAAKNMDYPADRftVWLLDDGGsvqKRNAANIVEAQAAQrrheelkklCEDLDVRYLTR 207
Cdd:pfam13641 2 PDVSVVVPAFNEDS-VLGRVLEAILAQPYPPVE--VVVVVNPS---DAETLDVAEEIAAR---------FPDVRLRVIRN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 208 ERN--VHAKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFDeDPRLFLVQTPHFFVNPD-------PIERNLRT 278
Cdd:pfam13641 67 ARLlgPTGKSRGLNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFD-SPKVGAVGTPVFSLNRStmlsalgALEFALRH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 279 FETMPSENEmfygiiqRGLDKWNGAFFCGSAAVLRReaLQDSDGFSgvSITEDCETALALHSRGWNSVYVDKPLIAGLQP 358
Cdd:pfam13641 146 LRMMSLRLA-------LGVLPLSGAGSAIRREVLKE--LGLFDPFF--LLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFP 214
|
250
....*....|....*.
gi 15160069 359 ATFASFIGQRSRWAQG 374
Cdd:pfam13641 215 TYLAASIKQRARWVYG 230
|
|
| CESA_like_2 |
cd06427 |
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ... |
128-384 |
7.63e-19 |
|
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: 86.54 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 128 PTVDVFVPSYNEdAELLANTLAAAKNMDYPADRFTVWLL---DDggsvqkrnaaniVEAQAAQRRHEeLKKLCEDLDVRY 204
Cdd:cd06427 1 PVYTILVPLYKE-AEVLPQLIASLSALDYPRSKLDVKLLleeDD------------EETIAAARALR-LPSIFRVVVVPP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 205 LTrernVHAKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFD-EDPRLFLVQTPHFFVNPDpieRNLRT-FETM 282
Cdd:cd06427 67 SQ----PRTKPKACNYALAFARGEYVVIYDAEDAPDPDQLKKAVAAFArLDDKLACVQAPLNYYNAR---ENWLTrMFAL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 283 psENEMFYGIIQRGLDKWNGAF-FCGSAAVLRREALQDSDGFSGVSITEDCETALALHSRGW-----NSVYVDKPliagl 356
Cdd:cd06427 140 --EYAAWFDYLLPGLARLGLPIpLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYrtgvlNSTTLEEA----- 212
|
250 260 270
....*....|....*....|....*....|
gi 15160069 357 qPATFASFIGQRSRWAQGMMQILI--FRQP 384
Cdd:cd06427 213 -NNALGNWIRQRSRWIKGYMQTWLvhMRNP 241
|
|
| GT_2_like_e |
cd04192 |
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ... |
132-374 |
1.45e-16 |
|
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: 79.64 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 132 VFVPSYNEdAELLANTLAAAKNMDYPADRFTVWLLDDG---GSVQkrnaanIVEAqAAQRRHEELKKLceDLDVRYLTRE 208
Cdd:cd04192 1 VVIAARNE-AENLPRLLQSLSALDYPKEKFEVILVDDHstdGTVQ------ILEF-AAAKPNFQLKIL--NNSRVSISGK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 209 RNVhakagnLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFDEDPRLFLVQTPHFFVNPDPIERnLRTFETMpseneM 288
Cdd:cd04192 71 KNA------LTTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKSLLAK-FQRLDWL-----S 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 289 FYGIIQRGLDkWNGAFFC-GSAAVLRREALQDSDGFSGV--SITEDCETALALHSRGWNSVY--VDKPLIAGLQPA-TFA 362
Cdd:cd04192 139 LLGLIAGSFG-LGKPFMCnGANMAYRKEAFFEVGGFEGNdhIASGDDELLLAKVASKYPKVAylKNPEALVTTQPVtSWK 217
|
250
....*....|..
gi 15160069 363 SFIGQRSRWAQG 374
Cdd:cd04192 218 ELLNQRKRWASK 229
|
|
| Glyco_tranf_GTA_type |
cd00761 |
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ... |
132-293 |
1.18e-12 |
|
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: 66.38 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 132 VFVPSYNEdAELLANTLAAAKNMDYPADRftVWLLDDGgsvQKRNAANIVEAQAAQrrheelkklceDLDVRYLTRERNV 211
Cdd:cd00761 1 VIIPAYNE-EPYLERCLESLLAQTYPNFE--VIVVDDG---STDGTLEILEEYAKK-----------DPRVIRVINEENQ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 212 HaKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFDEDPRLFLVQTPH-FFVNPDPIERNLRTFETMPSENEMFY 290
Cdd:cd00761 64 G-LAAARNAGLKAARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGnLLFRRELLEEIGGFDEALLSGEEDDD 142
|
...
gi 15160069 291 GII 293
Cdd:cd00761 143 FLL 145
|
|
| CESA_like_1 |
cd06439 |
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ... |
98-377 |
2.06e-12 |
|
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: 67.61 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 98 YSVVMLGLSlvivsmPLPSRKTRPGSPDYRPTVDVFVPSYNEDA---ELLANTLAaaknMDYPADRFTVWLLDDGGSvqk 174
Cdd:cd06439 5 YPLLLKLLA------RLRPKPPSLPDPAYLPTVTIIIPAYNEEAvieAKLENLLA----LDYPRDRLEIIVVSDGST--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 175 RNAANIVEAQAAQRRHeelkklcedldvryLTRERNVHAKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFdED 254
Cdd:cd06439 72 DGTAEIAREYADKGVK--------------LLRFPERRGKAAALNRALALATGEIVVFTDANALLDPDALRLLVRHF-AD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 255 PRLFLVQTPHFFVNPDPIernlrtfetmpSENEMFYGIIQRGLDKWNGAF-----FCGSAAVLRREALQdsdGFSGVSIT 329
Cdd:cd06439 137 PSVGAVSGELVIVDGGGS-----------GSGEGLYWKYENWLKRAESRLgstvgANGAIYAIRRELFR---PLPADTIN 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15160069 330 EDCETALALHSRGWNSVYVDKPLIAGLQPATFASFIGQRSRWAQGMMQ 377
Cdd:cd06439 203 DDFVLPLRIARQGYRVVYEPDAVAYEEVAEDGSEEFRRRVRIAAGNLQ 250
|
|
| Glyco_transf_21 |
pfam13506 |
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ... |
208-372 |
3.05e-12 |
|
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: 65.38 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 208 ERNVHAKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFdEDPRLFLVQTPHFFVNPDPIernLRTFETmpSENE 287
Cdd:pfam13506 12 PVGVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPL-ADPKVGLVTSPPVGSDPKGL---AAALEA--AFFN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 288 MFYGIIQRGLdkwNGAFFC-GSAAVLRREALQDSDGFSGVS--ITEDCETALALHSRGWNSVYVDKPLIAGLQPA--TFA 362
Cdd:pfam13506 86 TLAGVLQAAL---SGIGFAvGMSMAFRRADLERIGGFEALAdyLAEDYALGKLLRAAGLKVVLSPRPILQTSGPRrtSFR 162
|
170
....*....|
gi 15160069 363 SFIGQRSRWA 372
Cdd:pfam13506 163 AFMARQLRWA 172
|
|
| PLN02190 |
PLN02190 |
cellulose synthase-like protein |
327-429 |
1.82e-10 |
|
cellulose synthase-like protein
Pssm-ID: 215122 [Multi-domain] Cd Length: 756 Bit Score: 64.50 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 327 SITEDCETALALHSRGWNSVYV--DKPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQ-PL---FKRGLSFTQRLCYms 400
Cdd:PLN02190 457 SVAEDLNTSIGIHSRGWTSSYIspDPPAFLGSMPPGGPEAMVQQRRWATGLIEVLFNKQsPLigmFCRKIRFRQRLAY-- 534
|
90 100 110
....*....|....*....|....*....|...
gi 15160069 401 stlFWLF----PFPRTIFLFAPLFYLFFDLQIF 429
Cdd:PLN02190 535 ---LYVFtclrSIPELIYCLLPAYCLLHNSALF 564
|
|
| Glucan_BSP_MdoH |
cd04191 |
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ... |
132-377 |
2.63e-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: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 132 VFVPSYNEDAELLANTLAAAKN---MDYPADRFTVWLLDDggsvqKRNAANIVEAQAAqrrheeLKKLCEDLD----VRY 204
Cdd:cd04191 3 IVMPVYNEDPARVFAGLRAMYEslaKTGLADHFDFFILSD-----TRDPDIWLAEEAA------WLDLCEELGaqgrIYY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 205 LTRERNVHAKAGNLNNGLAH--STGELVTVFDADHAPARDFLLETVGYFDEDPRLFLVQTPHFFVNPDPIERNLRTFETM 282
Cdd:cd04191 72 RRRRENTGRKAGNIADFCRRwgSRYDYMVVLDADSLMSGDTIVRLVRRMEANPRAGIIQTAPKLIGAETLFARLQQFANR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 283 psenemFYG-IIQRGLDKWNGAF--FCGSAAVLRREA---------LQDSDGFSGVSITED-CETALaLHSRGWnSVYVD 349
Cdd:cd04191 152 ------LYGpVFGRGLAAWQGGEgnYWGHNAIIRVAAfmehcalpvLPGRPPFGGHILSHDfVEAAL-MRRAGW-EVRLA 223
|
250 260 270
....*....|....*....|....*....|
gi 15160069 350 KPLIAGL--QPATFASFIGQRSRWAQGMMQ 377
Cdd:cd04191 224 PDLEGSYeeCPPTLIDFLKRDRRWCQGNLQ 253
|
|
| WcaA |
COG0463 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
127-255 |
9.45e-10 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440231 [Multi-domain] Cd Length: 208 Bit Score: 58.95 E-value: 9.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 127 RPTVDVFVPSYNEdAELLANTLAAAKNMDYPADRftVWLLDDG---GSVQkrnaanIVEAQAAqrrheelkklcEDLDVR 203
Cdd:COG0463 1 MPLVSVVIPTYNE-EEYLEEALESLLAQTYPDFE--IIVVDDGstdGTAE------ILRELAA-----------KDPRIR 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15160069 204 YLTRERNVHaKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFDEDP 255
Cdd:COG0463 61 VIRLERNRG-KGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP 111
|
|
| PLN02189 |
PLN02189 |
cellulose synthase |
327-430 |
2.67e-08 |
|
cellulose synthase
Pssm-ID: 215121 [Multi-domain] Cd Length: 1040 Bit Score: 57.33 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 327 SITEDCETALALHSRGWNSVYV--DKPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQ-PL---FKRG-LSFTQRLCYM 399
Cdd:PLN02189 736 SITEDILTGFKMHCRGWRSIYCmpKRAAFKGSAPINLSDRLNQVLRWALGSVEIFFSRHsPLlygYKGGnLKWLERFAYV 815
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15160069 400 SSTLFWLFPFP-------------------RTIFLFAPLFYLFFDLQIFV 430
Cdd:PLN02189 816 NTTIYPFTSLPllayctlpaiclltgkfimPPISTFASLFFIALFMSIFA 865
|
|
| Cellulose_synt |
pfam03552 |
Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose ... |
327-423 |
2.67e-08 |
|
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: 57.46 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 327 SITEDCETALALHSRGWNSVYV--DKPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQ-PLF-KRGLSFTQRLCYMSST 402
Cdd:pfam03552 419 SVTEDILTGFRMHCRGWRSIYCmpKRDAFKGSAPINLSDRLHQVLRWALGSVEIFFSRHcPIWyGGRLKFLQRFAYINVG 498
|
90 100
....*....|....*....|.
gi 15160069 403 LFWLFPFPRTIFLFAPLFYLF 423
Cdd:pfam03552 499 IYPFTSIPLLAYCFLPAICLF 519
|
|
| PLN02638 |
PLN02638 |
cellulose synthase A (UDP-forming), catalytic subunit |
327-425 |
3.46e-08 |
|
cellulose synthase A (UDP-forming), catalytic subunit
Pssm-ID: 215343 [Multi-domain] Cd Length: 1079 Bit Score: 57.24 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 327 SITEDCETALALHSRGWNSVYV--DKPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQ-PL---FKRGLSFTQRLCYMS 400
Cdd:PLN02638 775 SVTEDILTGFKMHARGWRSIYCmpKRPAFKGSAPINLSDRLNQVLRWALGSVEILFSRHcPIwygYGGRLKWLERFAYVN 854
|
90 100
....*....|....*....|....*
gi 15160069 401 STLFWLFPFPRTIFLFAPLFYLFFD 425
Cdd:PLN02638 855 TTIYPITSIPLLLYCTLPAVCLLTG 879
|
|
| PilZ |
pfam07238 |
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ... |
570-671 |
5.93e-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: 51.35 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 570 SRRITVKRRCEVQLGGSdtWVPASIDNVSVHGLLINIfdSATNIEKGATAIVKVKPHSEGVPETMPLNVVRTVRGEGFVS 649
Cdd:pfam07238 5 FPRVPVSLPVTLRDGGG--EYKGRLIDISLGGAAIRL--PDEPLALGDRVELSLDLLDDGQELALPGRVVRIRPDEDGAR 80
|
90 100
....*....|....*....|..
gi 15160069 650 IGCTFSPQRAVDHRLIADLIFA 671
Cdd:pfam07238 81 VGVQFLDLDEEQRRLLVRLLFG 102
|
|
| WcaE |
COG1216 |
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism]; |
127-259 |
7.03e-08 |
|
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
Pssm-ID: 440829 [Multi-domain] Cd Length: 202 Bit Score: 53.46 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 127 RPTVDVFVPSYNeDAELLANTLAAAKNMDYPADRftVWLLDDGGSvqkRNAANIVEAQAAQRrheelkklcedldVRYLT 206
Cdd:COG1216 2 RPKVSVVIPTYN-RPELLRRCLESLLAQTYPPFE--VIVVDNGST---DGTAELLAALAFPR-------------VRVIR 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15160069 207 RERNVHAkAGNLNNGLAHSTGELVTVFDADHAPARDFL---------------LETVGYFDEdpRLFL 259
Cdd:COG1216 63 NPENLGF-AAARNLGLRAAGGDYLLFLDDDTVVEPDWLerllaaacllirrevFEEVGGFDE--RFFL 127
|
|
| PLN02400 |
PLN02400 |
cellulose synthase |
327-425 |
8.40e-08 |
|
cellulose synthase
Pssm-ID: 215224 [Multi-domain] Cd Length: 1085 Bit Score: 55.75 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 327 SITEDCETALALHSRGWNSVYV--DKPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQ-PL---FKRGLSFTQRLCYMS 400
Cdd:PLN02400 780 SVTEDILTGFKMHARGWISIYCmpPRPAFKGSAPINLSDRLNQVLRWALGSIEILLSRHcPIwygYNGRLKLLERLAYIN 859
|
90 100
....*....|....*....|....*
gi 15160069 401 STLFWLFPFPRTIFLFAPLFYLFFD 425
Cdd:PLN02400 860 TIVYPITSIPLLAYCVLPAFCLITN 884
|
|
| PLN02893 |
PLN02893 |
Cellulose synthase-like protein |
322-429 |
1.35e-07 |
|
Cellulose synthase-like protein
Pssm-ID: 215483 [Multi-domain] Cd Length: 734 Bit Score: 55.10 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 322 GFSGVSITEDCETALALHSRGWNSVYV--DKPLIAGLQPATFASFIGQRSRWAQGMMQILIFR-QPLF--KRGLSFTQRL 396
Cdd:PLN02893 439 GFRYGSLVEDYYTGYRLQCEGWKSIFCnpKRPAFLGDSPINLHDVLNQQKRWSVGLLEVAFSKySPITfgVKSIGLLMGL 518
|
90 100 110
....*....|....*....|....*....|....
gi 15160069 397 CYMSSTlFWLF-PFPRTIFLFAPLFYLFFDLQIF 429
Cdd:PLN02893 519 GYAHYA-FWPIwSIPITIYAFLPQLALLNGVSIF 551
|
|
| EpsO_like |
cd06438 |
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ... |
132-333 |
1.28e-06 |
|
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: 49.14 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 132 VFVPSYNEdAELLANTLAAAKNMDYPADRFTVWLLDDGGSvqkRNAANIVEAQAAQ--RRHEELKK-----LceDLDVRY 204
Cdd:cd06438 1 ILIPAHNE-EAVIGNTVRSLKAQDYPRELYRIFVVADNCT---DDTAQVARAAGATvlERHDPERRgkgyaL--DFGFRH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 205 LTRERNVHakagnlnnglahstgELVTVFDADHAPARDFLLETVGYFDEDPRlfLVQTPHFFVNPDpieRNLRTfETMPS 284
Cdd:cd06438 75 LLNLADDP---------------DAVVVFDADNLVDPNALEELNARFAAGAR--VVQAYYNSKNPD---DSWIT-RLYAF 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15160069 285 ENEMFYGIIQRGLDKWNG-AFFCGSAAVLRREALQDSdGFSGVSITEDCE 333
Cdd:cd06438 134 AFLVFNRLRPLGRSNLGLsCQLGGTGMCFPWAVLRQA-PWAAHSLTEDLE 182
|
|
| PLN02436 |
PLN02436 |
cellulose synthase A |
327-423 |
1.62e-06 |
|
cellulose synthase A
Pssm-ID: 215239 [Multi-domain] Cd Length: 1094 Bit Score: 51.79 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 327 SITEDCETALALHSRGWNSVYV--DKPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQ-PL---FKRGLSFTQRLCYMS 400
Cdd:PLN02436 791 SVTEDILTGFKMHCHGWRSVYCipKRPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHcPIwygYGGGLKWLERFSYIN 870
|
90 100
....*....|....*....|...
gi 15160069 401 STLFWLFPFPRTIFLFAPLFYLF 423
Cdd:PLN02436 871 SVVYPWTSIPLIVYCTLPAICLL 893
|
|
| PLN02195 |
PLN02195 |
cellulose synthase A |
327-409 |
1.78e-06 |
|
cellulose synthase A
Pssm-ID: 215124 [Multi-domain] Cd Length: 977 Bit Score: 51.51 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 327 SITEDCETALALHSRGWNSVYVD--KPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQ-PL---FKRG-LSFTQRLCYM 399
Cdd:PLN02195 671 SVTEDILTGFKMHCRGWRSIYCMpvRPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHcPLwygYGGGrLKWLQRLAYI 750
|
90
....*....|
gi 15160069 400 SSTlfwLFPF 409
Cdd:PLN02195 751 NTI---VYPF 757
|
|
| PLN02915 |
PLN02915 |
cellulose synthase A [UDP-forming], catalytic subunit |
327-409 |
4.29e-06 |
|
cellulose synthase A [UDP-forming], catalytic subunit
Pssm-ID: 215494 [Multi-domain] Cd Length: 1044 Bit Score: 50.32 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 327 SITEDCETALALHSRGWNSVYV--DKPLIAGLQPATFASFIGQRSRWAQGMMQILIFRQ-PL---FKRGLSFTQRLCYMS 400
Cdd:PLN02915 739 SVTEDILTGFKMHCRGWKSVYCmpKRPAFKGSAPINLSDRLHQVLRWALGSVEIFMSRHcPLwyaYGGKLKWLERLAYIN 818
|
....*....
gi 15160069 401 STlfwLFPF 409
Cdd:PLN02915 819 TI---VYPF 824
|
|
| DPG_synthase |
cd04188 |
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ... |
132-243 |
6.59e-06 |
|
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.
Pssm-ID: 133031 [Multi-domain] Cd Length: 211 Bit Score: 47.56 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 132 VFVPSYNEDAELLAntlAAAKNMDY----PADRFTVWLLDDGGsvqKRNAANIVEAQAAQRrheelkklceDLDVRYLTR 207
Cdd:cd04188 1 VVIPAYNEEKRLPP---TLEEAVEYleerPSFSYEIIVVDDGS---KDGTAEVARKLARKN----------PALIRVLTL 64
|
90 100 110
....*....|....*....|....*....|....*..
gi 15160069 208 ERNvHAKAGNLNNGLAHSTGELVTVFDADHA-PARDF 243
Cdd:cd04188 65 PKN-RGKGGAVRAGMLAARGDYILFADADLAtPFEEL 100
|
|
| PLN02248 |
PLN02248 |
cellulose synthase-like protein |
327-439 |
6.34e-05 |
|
cellulose synthase-like protein
Pssm-ID: 215138 [Multi-domain] Cd Length: 1135 Bit Score: 46.56 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 327 SITEDCETALALHSRGWNSVY-VDKP-LIAGLQPATFASFIGQRSRWAQGMMQILIFRQPLF--KRGLSFTQRLCYMSST 402
Cdd:PLN02248 834 SVTEDVVTGYRMHNRGWRSVYcVTKRdAFRGTAPINLTDRLHQVLRWATGSVEIFFSRNNALlaSRRLKFLQRIAYLNVG 913
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15160069 403 lfwLFPFPrTIFL----FAPLFYLFFDlQIFVAS-GGEFLAY 439
Cdd:PLN02248 914 ---IYPFT-SIFLivycFLPALSLFSG-QFIVQTlNVTFLVY 950
|
|
| GT2_RfbC_Mx_like |
cd04184 |
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ... |
128-262 |
1.68e-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: 43.35 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 128 PTVDVFVPSYNEDAELLANTLAAAKNMDYPAdrftvW---LLDDGGSvqKRNAANIVEAQAAQrrheelkklceDLDVRY 204
Cdd:cd04184 1 PLISIVMPVYNTPEKYLREAIESVRAQTYPN-----WelcIADDAST--DPEVKRVLKKYAAQ-----------DPRIKV 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15160069 205 LTRERNVHAkAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFDEDPRLFLVQT 262
Cdd:cd04184 63 VFREENGGI-SAATNSALELATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYS 119
|
|
| PLN02915 |
PLN02915 |
cellulose synthase A [UDP-forming], catalytic subunit |
50-321 |
2.03e-04 |
|
cellulose synthase A [UDP-forming], catalytic subunit
Pssm-ID: 215494 [Multi-domain] Cd Length: 1044 Bit Score: 44.92 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 50 QGAWRLVALG------FGTAIVLRYV----YWRTTSTLPPVNqlenfipGFLLYLAEMYSVVMLGLSLVIVSMP------ 113
Cdd:PLN02915 193 QPLWRKVPIPsskinpYRIVIVLRLVilcfFFRFRILTPAYD-------AYPLWLISVICEIWFALSWILDQFPkwfpin 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 114 -------LPSRKTRPGSPDYRPTVDVFVPSYNEDAE---LLANTLAAAKNMDYPADRFTVWLLDDGGSV----------- 172
Cdd:PLN02915 266 retyldrLSMRFERDGEPNRLAPVDVFVSTVDPLKEppiITANTVLSILAVDYPVDKVSCYVSDDGASMllfdtlsetae 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 173 -------------------------------QKRNAANIVEAQAAQRRHEELK-----------KLCED----------- 199
Cdd:PLN02915 346 farrwvpfckkhnieprapefyfsqkidylkDKVQPTFVKERRAMKREYEEFKvrinalvakaqKKPEEgwvmqdgtpwp 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 200 --------------------LDVR--------YLTRER----NVHAKAGNLnNGLAHSTGELVTV-----FDADHAPARD 242
Cdd:PLN02915 426 gnntrdhpgmiqvylgsegaLDVEgkelprlvYVSREKrpgyNHHKKAGAM-NALVRVSAVLTNApfmlnLDCDHYINNS 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 243 FLLETVGYFDEDP----RLFLVQTPHFFvnpDPIERNLRtfetMPSENEMFYGIIQRGLDKWNGAFFCGSAAVLRREALQ 318
Cdd:PLN02915 505 KAVREAMCFLMDPqlgkKLCYVQFPQRF---DGIDRHDR----YANRNVVFFDINMKGLDGIQGPVYVGTGCVFNRQALY 577
|
...
gi 15160069 319 DSD 321
Cdd:PLN02915 578 GYD 580
|
|
| PLN02436 |
PLN02436 |
cellulose synthase A |
54-321 |
2.09e-04 |
|
cellulose synthase A
Pssm-ID: 215239 [Multi-domain] Cd Length: 1094 Bit Score: 44.86 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 54 RLVALGFgtaivlrYVYWRTtstLPPVNQlenfipGFLLYLAEMYSVVMLGLSLVIVSMP-------------LPSRKTR 120
Cdd:PLN02436 294 RLVILGL-------FFHYRI---LHPVND------AYGLWLTSVICEIWFAVSWILDQFPkwypieretyldrLSLRYEK 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 121 PGSPDYRPTVDVFVPSYNEDAE---LLANTLAAAKNMDYPADRFTVWLLDDGGSV------------------------- 172
Cdd:PLN02436 358 EGKPSELASVDVFVSTVDPMKEpplITANTVLSILAVDYPVDKVACYVSDDGAAMltfealsetsefarkwvpfckkfsi 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 173 -----------------QKRNAANIVEAQAAQRRHEELK-----------KLCED------------LDVR--------- 203
Cdd:PLN02436 438 eprapewyfsqkmdylkNKVHPAFVRERRAMKREYEEFKvkinalvataqKVPEDgwtmqdgtpwpgNNVRdhpgmiqvf 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 204 ------------------YLTRER----NVHAKAGNLN-----NGLAHSTGELVTVfDADHAPARDFLLETVGYFDEDP- 255
Cdd:PLN02436 518 lghsgvrdvegnelprlvYVSREKrpgfDHHKKAGAMNslirvSAVLSNAPYLLNV-DCDHYINNSKALREAMCFMMDPq 596
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15160069 256 ---RLFLVQTPHFFvnpDPIERNLRtfetMPSENEMFYGIIQRGLDKWNGAFFCGSAAVLRREALQDSD 321
Cdd:PLN02436 597 sgkKICYVQFPQRF---DGIDRHDR----YSNRNVVFFDINMKGLDGIQGPIYVGTGCVFRRQALYGYD 658
|
|
| GT2_HAS |
cd06434 |
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ... |
129-372 |
2.21e-04 |
|
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.
Pssm-ID: 133056 [Multi-domain] Cd Length: 235 Bit Score: 43.40 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 129 TVDVFVPSYNEDAELLANTLAAAKNMDyPADrftVWLLDDGgsvqkrnaaniveaqAAQRRHEELKKLCEDLDVR-YLTR 207
Cdd:cd06434 1 DVTVIIPVYDEDPDVFRECLRSILRQK-PLE---IIVVTDG---------------DDEPYLSILSQTVKYGGIFvITVP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 208 ERNvhaKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFdEDPRLFLVQTphffvnpdpierNLRTFETMPSENE 287
Cdd:cd06434 62 HPG---KRRALAEGIRHVTTDIVVLLDSDTVWPPNALPEMLKPF-EDPKVGGVGT------------NQRILRPRDSKWS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 288 MFYGI-------IQRGLDKWNGAFFC--GSAAVLRREALQD---SDGFSGV-------SITEDCETALALHSRGWNSVYV 348
Cdd:cd06434 126 FLAAEylerrneEIRAAMSYDGGVPClsGRTAAYRTEILKDflfLEEFTNEtfmgrrlNAGDDRFLTRYVLSHGYKTVYQ 205
|
250 260
....*....|....*....|....
gi 15160069 349 DKPLIAGLQPATFASFIGQRSRWA 372
Cdd:cd06434 206 YTSEAYTETPENYKKFLKQQLRWS 229
|
|
| PRK05454 |
PRK05454 |
glucans biosynthesis glucosyltransferase MdoH; |
89-407 |
1.32e-03 |
|
glucans biosynthesis glucosyltransferase MdoH;
Pssm-ID: 235476 [Multi-domain] Cd Length: 605 Bit Score: 42.17 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 89 GFLLYLAEMYSVVMLGLSLVIVSMPLPSRKTRPGSPdyrptVDVFVPSYNEDAE-LLAN------TLAAAKNmdypADRF 161
Cdd:PRK05454 90 GFWTALMGFLQLLRGRDKYSISASAAGDPPPPPEAR-----TAILMPIYNEDPArVFAGlramyeSLAATGH----GAHF 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 162 TVWLLDDggsvqKRNAANIVEAQAAQRRheelkkLCEDLD----VRYLTRERNVHAKAGNLNNGLAHSTG--ELVTVFDA 235
Cdd:PRK05454 161 DFFILSD-----TRDPDIAAAEEAAWLE------LRAELGgegrIFYRRRRRNVGRKAGNIADFCRRWGGayDYMVVLDA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 236 DHAPARDFLLETVGYFDEDPRLFLVQTPhffvnPDPIerNLRTFetmpsenemF----------YG-IIQRGLDKWNG-- 302
Cdd:PRK05454 230 DSLMSGDTLVRLVRLMEANPRAGLIQTL-----PVAV--GADTL---------FarlqqfatrvYGpLFAAGLAWWQGge 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 303 AFFCGSAAVLRREALQDSDG---------FSGVSITED-CETALaLHSRGWnSVYVDkPLIAGL---QPATFASFIGQRS 369
Cdd:PRK05454 294 GNYWGHNAIIRVKAFAEHCGlpplpgrgpFGGHILSHDfVEAAL-MRRAGW-GVWLA-PDLPGSyeeLPPNLLDELKRDR 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15160069 370 RWAQGMMQILIFrqpLFKRGLSFTQRL-------CYMSSTLfWLF 407
Cdd:PRK05454 371 RWCQGNLQHLRL---LLAKGLHPVSRLhfltgimSYLSAPL-WLL 411
|
|
| GlcNAc-1-P_transferase |
cd06436 |
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ... |
132-331 |
1.75e-03 |
|
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.
Pssm-ID: 133058 [Multi-domain] Cd Length: 191 Bit Score: 40.06 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 132 VFVPSYNEDAeLLANTLAAAKNMDypaDRFTVWLLDDGGSvqkRNAANIVEAQAaqrrheelkklcEDLDVRYLTRER-N 210
Cdd:cd06436 1 VLVPCLNEEA-VIQRTLASLLRNK---PNFLVLVIDDASD---DDTAGIVRLAI------------TDSRVHLLRRHLpN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 211 VHAKAGN-LNNGLAH------STGE-----LVTVFDADHAPARDFLLETVGYFDeDPRLFLVQTPhffVNPDPIERNLRT 278
Cdd:cd06436 62 ARTGKGDaLNAAYDQirqiliEEGAdpervIIAVIDADGRLDPNALEAVAPYFS-DPRVAGTQSR---VRMYNRHKNLLT 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15160069 279 FetmpSENEMFYGII---QRGLDKWNGAFFCGSAAVLRREALQDSDGFS--GVSITED 331
Cdd:cd06436 138 I----LQDLEFFIIIaatQSLRALTGTVGLGGNGQFMRLSALDGLIGEEpwSDSLLED 191
|
|
| PLN02400 |
PLN02400 |
cellulose synthase |
54-340 |
2.03e-03 |
|
cellulose synthase
Pssm-ID: 215224 [Multi-domain] Cd Length: 1085 Bit Score: 41.50 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 54 RLVALGFgtaivlrYVYWRTTStlpPVNQlenfipGFLLYLAEMYSVVMLGLSLVIVSMP-------------LPSRKTR 120
Cdd:PLN02400 285 RLIILGF-------FLQYRVTH---PVKD------AYGLWLTSVICEIWFALSWLLDQFPkwypinretyldrLALRYDR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 121 PGSPDYRPTVDVFVPSYN---EDAELLANTLAAAKNMDYPADRFTVWLLDDGGSV------------------------- 172
Cdd:PLN02400 349 DGEPSQLAPVDVFVSTVDplkEPPLVTANTVLSILAVDYPVDKVSCYVSDDGSAMltfealsetaefarkwvpfckkhni 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 173 -----------------QKRNAANIVEAQAAQRRHEELK-----------KLCED------------------------- 199
Cdd:PLN02400 429 eprapefyfaqkidylkDKIQPSFVKERRAMKREYEEFKvrinalvakaqKIPEEgwtmqdgtpwpgnnprdhpgmiqvf 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 200 ------LDVR--------YLTRER----NVHAKAGNLNNGLAHS----TGELVTVFDADHAPARDFLLETVGYFDEDP-- 255
Cdd:PLN02400 509 lghsggLDTDgnelprlvYVSREKrpgfQHHKKAGAMNALIRVSavltNGAYLLNVDCDHYFNNSKALKEAMCFMMDPai 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 256 --RLFLVQTPHFFvnpDPIERNLRtfetMPSENEMFYGIIQRGLDKWNGAFFCGSAAVLRREALQdsdGFSGVSITEDCE 333
Cdd:PLN02400 589 gkKTCYVQFPQRF---DGIDLHDR----YANRNIVFFDINLKGLDGIQGPVYVGTGCCFNRQALY---GYDPVLTEEDLE 658
|
....*..
gi 15160069 334 TALALHS 340
Cdd:PLN02400 659 PNIIVKS 665
|
|
| Succinoglycan_BP_ExoA |
cd02525 |
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ... |
129-248 |
3.71e-03 |
|
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.
Pssm-ID: 133016 [Multi-domain] Cd Length: 249 Bit Score: 39.91 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 129 TVDVFVPSYNEdAELLANTLAAAKNMDYPADRFTVwLLDDGGSVQkrNAANIVEAQAAqrrheelkklcEDLDVRYLTRE 208
Cdd:cd02525 1 FVSIIIPVRNE-EKYIEELLESLLNQSYPKDLIEI-IVVDGGSTD--GTREIVQEYAA-----------KDPRIRLIDNP 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15160069 209 RNVHAKAgnLNNGLAHSTGELVTVFDADHAPARDFLLETV 248
Cdd:cd02525 66 KRIQSAG--LNIGIRNSRGDIIIRVDAHAVYPKDYILELV 103
|
|
| DPM1_like_bac |
cd04187 |
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ... |
132-240 |
6.55e-03 |
|
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.
Pssm-ID: 133030 [Multi-domain] Cd Length: 181 Bit Score: 38.23 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 132 VFVPSYNEDA---ELLANTLAAAKNMDYpadRFTVWLLDDG---GSVqkrnaaniveaqaaqrrhEELKKLCE-DLDVRY 204
Cdd:cd04187 1 IVVPVYNEEEnlpELYERLKAVLESLGY---DYEIIFVDDGstdRTL------------------EILRELAArDPRVKV 59
|
90 100 110
....*....|....*....|....*....|....*....
gi 15160069 205 LTRERNV-HAKAgnLNNGLAHSTGELVTVFDAD--HAPA 240
Cdd:cd04187 60 IRLSRNFgQQAA--LLAGLDHARGDAVITMDADlqDPPE 96
|
|
| Glucosylceramide_synthase |
cd02520 |
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ... |
193-373 |
8.32e-03 |
|
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.
Pssm-ID: 133012 [Multi-domain] Cd Length: 196 Bit Score: 38.35 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 193 LKKLCE---DLDVRYLT--RERNVHAKAGNLNNGLAHSTGELVTVFDADHAPARDFLLETVGYFdEDPRLFLVQTPhfFV 267
Cdd:cd02520 48 VRKLIAkypNVDARLLIggEKVGINPKVNNLIKGYEEARYDILVISDSDISVPPDYLRRMVAPL-MDPGVGLVTCL--CA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15160069 268 NpdpiernlrtfetmpsenemfygiiqrgldkwngaffcGSAAVLRREALQDSDGFSGVS--ITEDCETALALHSRGWNS 345
Cdd:cd02520 125 F--------------------------------------GKSMALRREVLDAIGGFEAFAdyLAEDYFLGKLIWRLGYRV 166
|
170 180
....*....|....*....|....*...
gi 15160069 346 VYVDKPLIAGLQPATFASFIGQRSRWAQ 373
Cdd:cd02520 167 VLSPYVVMQPLGSTSLASFWRRQLRWSR 194
|
|
| |
