|
Name |
Accession |
Description |
Interval |
E-value |
| bcsA |
PRK11498 |
cellulose synthase catalytic subunit; Provisional |
14-865 |
0e+00 |
|
cellulose synthase catalytic subunit; Provisional
Pssm-ID: 236918 [Multi-domain] Cd Length: 852 Bit Score: 1786.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 14 GKRLNERYRDYRQHGASWLSAALGCLWASLAWAFMPLETPRWQAIRERHGEFFPHINPHRPRPLDPIRYLLQCVWLLATR 93
Cdd:PRK11498 1 NARLIGRYRDYRRHGASAFSATLGCLWMILAWIFLPLEHPRWQRIRAEHKNLYPHINASRPRPLDPLRYLIQTLWLLIGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 94 VPEPDKKINWRSLAALEGVQGRYAQWLEKLPEKVNARTGHLDKHKELAHLSPKLRRFILGTITFFSLILALLCITQPFNP 173
Cdd:PRK11498 81 SRKETPKPRRRAFSGLQNIRGRYHQWLEELPERVSHKTQHLDEKKELGHLSAGARRLILGIIVTFSLILALICITQPFNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 174 LSQFIFLLLLWGVALLVRRIPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGIILLFAETYAWVVLVLGYFQ 253
Cdd:PRK11498 161 LAQFIFLMLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 254 VVWPLNRQPVPLPEDMAQWPTVDIFVPTYNEDLNVVKNTIYASQGIDWPKDKLNIWILDDGGREEFRQFAKDVGVHYIAR 333
Cdd:PRK11498 241 VVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKYIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 334 TTHEHAKAGNINNALKYAKGEFVSIFDCDHVPTRSFLQMTMGWFLKEKELAMMQTPHHFFSPDPFERNLGRFRKTPNEGT 413
Cdd:PRK11498 321 PTHEHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDPFERNLGRFRKTPNEGT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 414 LFYGLVQDGNDMWDATFFCGSCAVIRRGPLDEIGGIAVETVTEDAHTSLRLHRRGHTSAYMRIPQAAGLATESLSAHIGQ 493
Cdd:PRK11498 401 LFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 494 RIRWARGMVQIFRLDNPLFGKGLKLAQRICYVNAMLHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHA 573
Cdd:PRK11498 481 RIRWARGMVQIFRLDNPLTGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 574 SLTNSKIQGKYRHSFWSEIYETVLAWYIAPPTFVALINPHKGKFNVTAKGGLVEDEYVDWVISRPYIYLVLLNLVGVGVG 653
Cdd:PRK11498 561 SLTNSRIQGKYRHSFWSEIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGGLVEEEYVDWVISRPYIFLVLLNLVGVAVG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 654 IWRFMYGPENEILTVWVSIIWVFYNLIILGGAVAVSVESKQVRRSHRVEMSMPAAIARDDGHLFSCTVHDYSDGGLGVKI 733
Cdd:PRK11498 641 IWRYFYGPPNEILTVIVSLVWVFYNLIILGGAVAVSVESKQVRRSHRVEMTMPAAIAREDGHLFSCTVQDFSDGGLGIKI 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 734 HGEAQVLESQHVKLLLKRGQQEYAFPVRVARVNGSEVGLQLLPLSNQQHIDFVQCTFARADTWALWQDSFPEDKPMESLL 813
Cdd:PRK11498 721 NGQAQLLEGQKVNLLLKRGQQEYVFPTQVTRVMGNEVGLQLMPLTTQQHIDFVQCTFARADTWALWQDSFPEDKPLESLL 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 504652645 814 DILKLGFRGYRHLAEFSPPSVKVIFRSLTMLVAWFVSFIPRRPERAAATLSA 865
Cdd:PRK11498 801 DILKLGFRGYRHLAEFAPPSVKGIFRVLTSLVSWVVSFIPRRPERQEAAQPS 852
|
|
| CelA |
TIGR03030 |
cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 ... |
143-834 |
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: 1057.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 143 LSPKLRRFILGTITFFSLILALLCITQPFNPLSQFIFLLLLWGVALLVRRIPGRFSALMLIVLSLTVSCRYIWWRYTSTL 222
Cdd:TIGR03030 1 GPPALFKGLLFIIAVAGLLALLALITAPVTLETQLIIAGSAFLLLLILKRFNGKRPRLLLLVLSVFISLRYLWWRLTETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 223 NWDDPVSLVCGIILLFAETYAWVVLVLGYFQVVWPLNRQPVPLPEDMAQWPTVDIFVPTYNEDLNVVKNTIYASQGIDWP 302
Cdd:TIGR03030 81 PFDNTLNFIFGTLLLLAELYSITILLLGYFQTVRPLDRTPVPLPLDPEEWPTVDVFIPTYNEDLEIVATTVLAAKNMDYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 303 KDKLNIWILDDGG------------------REEFRQFAKDVGVHYIARTTHEHAKAGNINNALKYAKGEFVSIFDCDHV 364
Cdd:TIGR03030 161 ADKFRVWILDDGGtdqkrndpdpeqaeaaqrREELKEFCRKLGVNYITRPRNVHAKAGNINNALKHTDGELILIFDADHV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 365 PTRSFLQMTMGWFLKEKELAMMQTPHHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCGSCAVIRRGPLD 444
Cdd:TIGR03030 241 PTRDFLQRTVGWFVEDPKLFLVQTPHFFVSPDPIERNLGTFRRMPNENELFYGLIQDGNDFWNAAFFCGSAAVLRREALD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 445 EIGGIAVETVTEDAHTSLRLHRRGHTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLFGKGLKLAQRICY 524
Cdd:TIGR03030 321 EIGGIAGETVTEDAETALKLHRRGWNSAYLDRPLIAGLAPETLSGHIGQRIRWAQGMMQIFRLDNPLLKRGLSFPQRLCY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 525 VNAMLHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHASLTNSKIQGKYRHSFWSEIYETVLAWYIAPP 604
Cdd:TIGR03030 401 LNAMLFWFFPLPRVIFLTAPLAYLFFGLNIFVASALEILAYALPHMLHSLLTNSYLFGRVRWPFWSEVYETVLAVYLLPP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 605 TFVALINPHKGKFNVTAKGGLVEDEYVDwVISRPYIYLVLLNLVGVGVGIWRFmYGPENEILTVWVSIIWVFYNLIILGG 684
Cdd:TIGR03030 481 VLVTLLNPKKPKFNVTPKGELLDEDYFS-PLSRPYLILFALILAGLAFGLYRI-YGYPIERGVLLVVLGWNLLNLILLGA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 685 AVAVSVESKQVRRSHRVEMSMPAAIARDDGHLFSCTVHDYSDGGLGVKIHG----EAQVLESQHVKLLLKRGQQEYAFPV 760
Cdd:TIGR03030 559 ALAVVAERRQRRSSPRIPCKIPAEVQRDGGRWVEATVEDASVGGLGIKINAqgapGPQLGAGVLVQIRPKRNGLPALKPA 638
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504652645 761 RVARVNGSEVGLQLLPLSNQQHIDFVQCTFARADTWA-LWQDSFPEDKPMESLLDILKLGFRGYRHLAEFSPPSV 834
Cdd:TIGR03030 639 RVRGAGGVMIGLEFSPLNVQQVREIVDLVFARSDRWVaLWEERRRPDGPLRGLADFLKIALRGLFRSARDLVRAP 713
|
|
| CESA_CelA_like |
cd06421 |
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ... |
273-505 |
1.28e-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: 364.59 E-value: 1.28e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 273 PTVDIFVPTYNEDLNVVKNTIYASQGIDWPKDKLNIWILDDGGREEFRQFAKDVGV----HYIARTTHEHAKAGNINNAL 348
Cdd:cd06421 1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVeygyRYLTRPDNRHAKAGNLNNAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 349 KYAKGEFVSIFDCDHVPTRSFLQMTMGWFLKEKELAMMQTPHHFFSPDPFERnlgRFRKTPNEGTLFYGLVQDGNDMWDA 428
Cdd:cd06421 81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDW---LADGAPNEQELFYGVIQPGRDRWGA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504652645 429 TFFCGSCAVIRRGPLDEIGGIAVETVTEDAHTSLRLHRRGHTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIF 505
Cdd:cd06421 158 AFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
|
|
| BcsA |
COG1215 |
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ... |
235-622 |
2.37e-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: 165.30 E-value: 2.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 235 ILLFAETYAWVVLVLGYFqvvwplnrqpVPLPEDMAQWPTVDIFVPTYNEDlNVVKNTIYASQGIDWPKDKLNIWILDDG 314
Cdd:COG1215 1 LLLLLALLALLYLLLLAL----------ARRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 315 GREEFRQFAKDVG-----VHYIARTTHEHaKAGNINNALKYAKGEFVSIFDCDHVPTRSFLQMTMGWFLKEKelammqtp 389
Cdd:COG1215 70 STDETAEIARELAaeyprVRVIERPENGG-KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 390 hhffspdpfernlgrfrktpnegtlfyglvqdgndmwdaTFFCGSCAVIRRGPLDEIGGIAVETVTEDAHTSLRLHRRGH 469
Cdd:COG1215 141 ---------------------------------------VGASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGY 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 470 TSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLFGKGLKLAqricyvnamlhflsgipRLIFLTAPLAFLL 549
Cdd:COG1215 182 RIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLL-----------------FLLLLLLPLLLLL 244
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504652645 550 LhayiiYAPALMIALFVLPHMIHASLtnskiqgkyRHSFWSEIYETVLAWYIAPPTFVALINPHKGKFNVTAK 622
Cdd:COG1215 245 L-----LLALLALLLLLLPALLLALL---------LALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
|
|
| CESA_CaSu_A2 |
cd06437 |
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ... |
273-500 |
1.93e-26 |
|
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.
Pssm-ID: 133059 [Multi-domain] Cd Length: 232 Bit Score: 108.55 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 273 PTVDIFVPTYNEdLNVVKNTIYASQGIDWPKDKLNIWILDDG--------GREEFRQFAKDVGVHYIARTTHEHAKAGNI 344
Cdd:cd06437 1 PMVTVQLPVFNE-KYVVERLIEAACALDYPKDRLEIQVLDDStdetvrlaREIVEEYAAQGVNIKHVRRADRTGYKAGAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 345 NNALKYAKGEFVSIFDCDHVPTRSFLQMTMgWFLKEKELAMMQTPHHFFSPDpfERNLGRFRKTPNEGtlFYGLVQDGND 424
Cdd:cd06437 80 AEGMKVAKGEYVAIFDADFVPPPDFLQKTP-PYFADPKLGFVQTRWGHINAN--YSLLTRVQAMSLDY--HFTIEQVARS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504652645 425 MWDATF-FCGSCAVIRRGPLDEIGGIAVETVTEDAHTSLRLHRRGHTSAYMRIPQAAGLATESLSAHIGQRIRWARG 500
Cdd:cd06437 155 STGLFFnFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKG 231
|
|
| CESA_NdvC_like |
cd06435 |
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ... |
277-506 |
4.00e-24 |
|
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: 102.09 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 277 IFVPTYNEDLNVVKNTIYASQGIDWPKdkLNIWILDDGGREEFrqFAKDVGVHYIA---RTTHEH------AKAGNINNA 347
Cdd:cd06435 2 IHVPCYEEPPEMVKETLDSLAALDYPN--FEVIVIDNNTKDEA--LWKPVEAHCAQlgeRFRFFHveplpgAKAGALNYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 348 LKYAKG--EFVSIFDCDHVPTRSFLQMTMGWFlKEKELAMMQTPHHFFS--PDPFERNLGRFRKTpnegtlFYGLVQDGN 423
Cdd:cd06435 78 LERTAPdaEIIAVIDADYQVEPDWLKRLVPIF-DDPRVGFVQAPQDYRDgeESLFKRMCYAEYKG------FFDIGMVSR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 424 DMWDATFFCGSCAVIRRGPLDEIGGIAVETVTEDAHTSLRLHRRGHTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQ 503
Cdd:cd06435 151 NERNAIIQHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQ 230
|
...
gi 504652645 504 IFR 506
Cdd:cd06435 231 ILK 233
|
|
| CESA_like |
cd06423 |
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ... |
277-457 |
1.39e-23 |
|
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: 98.45 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 277 IFVPTYNEDLnVVKNTIYASQGIDWPKdkLNIWILDDGG----REEFRQFAKDVGVHYIARTTHEHA-KAGNINNALKYA 351
Cdd:cd06423 1 IIVPAYNEEA-VIERTIESLLALDYPK--LEVIVVDDGStddtLEILEELAALYIRRVLVVRDKENGgKAGALNAGLRHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 352 KGEFVSIFDCDHVPTRSFLQ-MTMGWFLKEKELAMMQTPHHFfspDPFERNLGRFRKtpNEGTLFYGLVQDGNDMWDATF 430
Cdd:cd06423 78 KGDIVVVLDADTILEPDALKrLVVPFFADPKVGAVQGRVRVR---NGSENLLTRLQA--IEYLSIFRLGRRAQSALGGVL 152
|
170 180
....*....|....*....|....*...
gi 504652645 431 -FCGSCAVIRRGPLDEIGGIAVETVTED 457
Cdd:cd06423 153 vLSGAFGAFRREALREVGGWDEDTLTED 180
|
|
| Glycos_transf_2 |
pfam00535 |
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ... |
276-445 |
2.83e-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: 94.38 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 276 DIFVPTYNEdLNVVKNTIYASqgIDWPKDKLNIWILDDGGREEFRQFAK-----DVGVHYIaRTTHEHAKAGNINNALKY 350
Cdd:pfam00535 1 SVIIPTYNE-EKYLLETLESL--LNQTYPNFEIIVVDDGSTDGTVEIAEeyakkDPRVRVI-RLPENRGKAGARNAGLRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 351 AKGEFVSIFDCDHVPTRSFLQMTMGWFLK-EKELAMMQTPHHFFSPDPFERNLGRFRktpnegTLFYGLVQDGNDMWDAT 429
Cdd:pfam00535 77 ATGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRASRITL------SRLPFFLGLRLLGLNLP 150
|
170
....*....|....*.
gi 504652645 430 FFCGSCAVIRRGPLDE 445
Cdd:pfam00535 151 FLIGGFALYRREALEE 166
|
|
| PLN02915 |
PLN02915 |
cellulose synthase A [UDP-forming], catalytic subunit |
445-654 |
7.98e-14 |
|
cellulose synthase A [UDP-forming], catalytic subunit
Pssm-ID: 215494 [Multi-domain] Cd Length: 1044 Bit Score: 75.74 E-value: 7.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 445 EIGGIaVETVTEDAHTSLRLHRRGHTSAYM--RIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDN-PL---FGKGLKL 518
Cdd:PLN02915 732 EIGWI-YGSVTEDILTGFKMHCRGWKSVYCmpKRPAFKGSAPINLSDRLHQVLRWALGSVEIFMSRHcPLwyaYGGKLKW 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 519 AQRICYVNAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----YAPALMIALF---VLPHMIHASLTNSKIQGKYRH-SFW 589
Cdd:PLN02915 811 LERLAYINTIVYPFTSIPLLAYCTIPAVCLLTGKFIIptlnnLASIWFLALFlsiIATSVLELRWSGVSIEDLWRNeQFW 890
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504652645 590 seIYETVLAWYIAppTFVALINPHKG---KFNVTAKGGLVE-DEYVDWVISR------PYIYLVLLNLVGVGVGI 654
Cdd:PLN02915 891 --VIGGVSAHLFA--VFQGLLKVLGGvdtNFTVTSKAADDEaDEFGELYLFKwttlliPPTTLIILNMVGVVAGV 961
|
|
| Cellulose_synt |
pfam03552 |
Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose ... |
444-659 |
1.04e-13 |
|
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: 75.18 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 444 DEIGGIaVETVTEDAHTSLRLHRRGHTSAYMRIPQAA--GLATESLSAHIGQRIRWARGMVQIF-RLDNPLF-GKGLKLA 519
Cdd:pfam03552 411 KEIGWI-YGSVTEDILTGFRMHCRGWRSIYCMPKRDAfkGSAPINLSDRLHQVLRWALGSVEIFfSRHCPIWyGGRLKFL 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 520 QRICYVNAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----YAPALMIALFVlpHMIHASLTNSKIQGKYRHSFW-SEIY 593
Cdd:pfam03552 490 QRFAYINVGIYPFTSIPLLAYCFLPAICLFTGKFIVptlsnFASIYFLSLFL--SIIATGILELRWSGVSIEEWWrNEQF 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 594 etvlaWYIAPPT------FVALINPHKG---KFNVTAK-GGLVEDEYVDWVISR------PYIYLVLLNLVGVGVGIWRF 657
Cdd:pfam03552 568 -----WVIGGTSahlfavFQGLLKVIAGidtSFTVTSKaSDDEDDEFADLYIFKwttlliPPTTILIVNLVGIVAGVSRA 642
|
..
gi 504652645 658 MY 659
Cdd:pfam03552 643 IN 644
|
|
| CESA_like_2 |
cd06427 |
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ... |
273-503 |
1.70e-12 |
|
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: 68.05 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 273 PTVDIFVPTYNEdLNVVKNTIYASQGIDWPKDKLNIWILDDGGREEFRQFAKDVGVHYIAR---------TThehaKAGN 343
Cdd:cd06427 1 PVYTILVPLYKE-AEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRvvvvppsqpRT----KPKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 344 INNALKYAKGEFVSIFDCDHVPTRSFLQMTMGWFLKEKE-LAMMQTPHHFFSPDpfERNLGRFrkTPNEGTLFYGLVQDG 422
Cdd:cd06427 76 CNYALAFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDDkLACVQAPLNYYNAR--ENWLTRM--FALEYAAWFDYLLPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 423 NDMWDATFFCGSCAVI-RRGPLDEIGGIAVETVTEDAHTSLRLHRRGHTSaymRIPQAAGL--ATESLSAHIGQRIRWAR 499
Cdd:cd06427 152 LARLGLPIPLGGTSNHfRTDVLRELGGWDPFNVTEDADLGLRLARAGYRT---GVLNSTTLeeANNALGNWIRQRSRWIK 228
|
....
gi 504652645 500 GMVQ 503
Cdd:cd06427 229 GYMQ 232
|
|
| Glyco_trans_2_3 |
pfam13632 |
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ... |
360-560 |
9.75e-12 |
|
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: 64.66 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 360 DCD-HVPTRSFLQMTmgWFLKEKELAMMQTPHHFF-SPDPFERNLGRFRktpNEGTLFYGLVQDGNDmwDATFFCGSCAV 437
Cdd:pfam13632 6 DADtVLPPDCLLGIA--NEMASPEVAIIQGPILPMnVGNYLEELAALFF---ADDHGKSIPVRMALG--RVLPFVGSGAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 438 IRRGPLDEIGGIAVETVTEDAHTSLRLHRRGHTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNplfgkgLK 517
Cdd:pfam13632 79 LRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRL------LG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504652645 518 LAQRICYVNAMLHFLSGIprlIFLTAPLAFLLLHAYIIYAPAL 560
Cdd:pfam13632 153 YLGTLLWSGLPLALLLLL---LFSISSLALVLLLLALLAGLLL 192
|
|
| PLN02436 |
PLN02436 |
cellulose synthase A |
445-654 |
1.18e-11 |
|
cellulose synthase A
Pssm-ID: 215239 [Multi-domain] Cd Length: 1094 Bit Score: 68.74 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 445 EIGGIaVETVTEDAHTSLRLHRRGHTSAYM--RIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDN-PL---FGKGLKL 518
Cdd:PLN02436 784 EIGWI-YGSVTEDILTGFKMHCHGWRSVYCipKRPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHcPIwygYGGGLKW 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 519 AQRICYVNAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----YAPALMIALFV---LPHMIHASLTNSKIQGKYRH-SFW 589
Cdd:PLN02436 863 LERFSYINSVVYPWTSIPLIVYCTLPAICLLTGKFIVpeisnYASILFMALFIsiaATGILEMQWGGVGIDDWWRNeQFW 942
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504652645 590 seIYETVLAWYIAppTFVALINPHKG---KFNVTAKGGlVEDEYVDWVISR------PYIYLVLLNLVGVGVGI 654
Cdd:PLN02436 943 --VIGGVSSHLFA--LFQGLLKVLAGvntNFTVTSKAA-DDGEFSELYLFKwtslliPPTTLLIINIIGVIVGV 1011
|
|
| PLN02195 |
PLN02195 |
cellulose synthase A |
445-653 |
2.02e-11 |
|
cellulose synthase A
Pssm-ID: 215124 [Multi-domain] Cd Length: 977 Bit Score: 68.07 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 445 EIGGIaVETVTEDAHTSLRLHRRGHTSAY-MRI-PQAAGLATESLSAHIGQRIRWARGMVQIFRLDN-PL---FGKG-LK 517
Cdd:PLN02195 664 EIGWI-YGSVTEDILTGFKMHCRGWRSIYcMPVrPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHcPLwygYGGGrLK 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 518 LAQRICYVNAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----YAPALMIALF---VLPHMIHASLTNSKIQGKYRH-SF 588
Cdd:PLN02195 743 WLQRLAYINTIVYPFTSLPLIAYCTLPAICLLTGKFIIptlsnLASMLFLGLFisiILTSVLELRWSGVSIEDLWRNeQF 822
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504652645 589 WseIYETVLAWYIAP-PTFVALINPHKGKFNVTAK----GGLVEDEYVDW-VISRPYIYLVLLNLVGVGVG 653
Cdd:PLN02195 823 W--VIGGVSAHLFAVfQGFLKMLAGLDTNFTVTAKaaddTEFGELYMVKWtTLLIPPTSLLIINLVGVVAG 891
|
|
| PLN02638 |
PLN02638 |
cellulose synthase A (UDP-forming), catalytic subunit |
445-654 |
2.09e-11 |
|
cellulose synthase A (UDP-forming), catalytic subunit
Pssm-ID: 215343 [Multi-domain] Cd Length: 1079 Bit Score: 68.03 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 445 EIGGIaVETVTEDAHTSLRLHRRGHTSAYM--RIPQAAGLATESLSAHIGQRIRWARGMVQI-FRLDNPL---FGKGLKL 518
Cdd:PLN02638 768 EIGWI-YGSVTEDILTGFKMHARGWRSIYCmpKRPAFKGSAPINLSDRLNQVLRWALGSVEIlFSRHCPIwygYGGRLKW 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 519 AQRICYVNAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----YAPALMIALFV---LPHMIHASLTNSKIQGKYRH-SFW 589
Cdd:PLN02638 847 LERFAYVNTTIYPITSIPLLLYCTLPAVCLLTGKFIIpqisnIASIWFISLFLsifATGILEMRWSGVGIDEWWRNeQFW 926
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504652645 590 seIYETVLAWYIAppTFVALINPHKG---KFNVTAK-----GGLVEDEYVDW-VISRPYIYLVLLNLVGVGVGI 654
Cdd:PLN02638 927 --VIGGVSAHLFA--VFQGLLKVLAGidtNFTVTSKasdedGDFAELYMFKWtTLLIPPTTLLIINLVGVVAGI 996
|
|
| PLN02400 |
PLN02400 |
cellulose synthase |
445-654 |
2.12e-11 |
|
cellulose synthase
Pssm-ID: 215224 [Multi-domain] Cd Length: 1085 Bit Score: 68.08 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 445 EIGGIaVETVTEDAHTSLRLHRRGHTSAYMRIPQAA--GLATESLSAHIGQRIRWARGMVQIFRLDN-PL---FGKGLKL 518
Cdd:PLN02400 773 EIGWI-YGSVTEDILTGFKMHARGWISIYCMPPRPAfkGSAPINLSDRLNQVLRWALGSIEILLSRHcPIwygYNGRLKL 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 519 AQRICYVNAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----YAPALMIALFV---LPHMIHASLTNSKIQGKYRH-SFW 589
Cdd:PLN02400 852 LERLAYINTIVYPITSIPLLAYCVLPAFCLITNKFIIpeisnYASMWFILLFIsifATGILELRWSGVGIEDWWRNeQFW 931
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504652645 590 seIYETVLAWYIAppTFVALINPHKG---KFNVTAKGGLVEDEYVDWVISR------PYIYLVLLNLVGVGVGI 654
Cdd:PLN02400 932 --VIGGTSAHLFA--VFQGLLKVLAGidtNFTVTSKASDEDGDFAELYVFKwtslliPPTTVLLVNLVGIVAGV 1001
|
|
| PilZ |
pfam07238 |
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ... |
694-791 |
5.29e-11 |
|
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: 60.21 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 694 QVRRSHRVEMSMPAAIaRDDGHLFSCTVHDYSDGGLGVKIHGEAQVLESQ-HVKLLLKRGQQEYAFPVRVARVNGSE--- 769
Cdd:pfam07238 1 QRRRFPRVPVSLPVTL-RDGGGEYKGRLIDISLGGAAIRLPDEPLALGDRvELSLDLLDDGQELALPGRVVRIRPDEdga 79
|
90 100
....*....|....*....|...
gi 504652645 770 -VGLQLLPLSNQQHIDFVQCTFA 791
Cdd:pfam07238 80 rVGVQFLDLDEEQRRLLVRLLFG 102
|
|
| Glyco_tranf_2_3 |
pfam13641 |
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ... |
273-500 |
1.09e-10 |
|
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: 62.39 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 273 PTVDIFVPTYNEDlNVVKNTIYASQGIDWPKDKLniwIL-----DDGGREEFRQFA---KDVGVHYIaRTTHE---HAKA 341
Cdd:pfam13641 2 PDVSVVVPAFNED-SVLGRVLEAILAQPYPPVEV---VVvvnpsDAETLDVAEEIAarfPDVRLRVI-RNARLlgpTGKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 342 GNINNALKYAKGEFVSIFDCDHVPTRSFLQMTMGWFLKEKeLAMMQTPHHFFSPDPFERNLGRFRktpnegtlFYGLVQD 421
Cdd:pfam13641 77 RGLNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPK-VGAVGTPVFSLNRSTMLSALGALE--------FALRHLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 422 GNDMWDA---TFFCGSCAVIRRGPLDEIGGIAVE-TVTEDAHTSLRLHRRGHTSAYmrIPQAA--GLATESLSAHIGQRI 495
Cdd:pfam13641 148 MMSLRLAlgvLPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAY--APDAAvrTVFPTYLAASIKQRA 225
|
....*
gi 504652645 496 RWARG 500
Cdd:pfam13641 226 RWVYG 230
|
|
| PLN02189 |
PLN02189 |
cellulose synthase |
453-654 |
4.30e-10 |
|
cellulose synthase
Pssm-ID: 215121 [Multi-domain] Cd Length: 1040 Bit Score: 63.88 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 453 TVTEDAHTSLRLHRRGHTSAYMRIPQAA--GLATESLSAHIGQRIRWARGMVQIF-RLDNPLF----GKGLKLAQRICYV 525
Cdd:PLN02189 736 SITEDILTGFKMHCRGWRSIYCMPKRAAfkGSAPINLSDRLNQVLRWALGSVEIFfSRHSPLLygykGGNLKWLERFAYV 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 526 NAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----YAPALMIALFV---LPHMIHASLTNSKIQGKYRH-SFW--SEIYE 594
Cdd:PLN02189 816 NTTIYPFTSLPLLAYCTLPAICLLTGKFIMppistFASLFFIALFMsifATGILELRWSGVSIEEWWRNeQFWviGGVSA 895
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504652645 595 TVLAWYIAPPTFVALINPHkgkFNVTAKgGLVEDEYVD-----W-VISRPYIYLVLLNLVGVGVGI 654
Cdd:PLN02189 896 HLFAVVQGLLKVLAGIDTN---FTVTSK-ATDDDEFGElyafkWtTLLIPPTTLLIINIVGVVAGI 957
|
|
| Glyco_tranf_GTA_type |
cd00761 |
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ... |
277-412 |
2.32e-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: 57.13 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 277 IFVPTYNEDlNVVKNTIYA--SQGIDwpkdKLNIWILDDGGREEFRQFAKDVGVHYIARTTHEHA----KAGNINNALKY 350
Cdd:cd00761 1 VIIPAYNEE-PYLERCLESllAQTYP----NFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEenqgLAAARNAGLKA 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504652645 351 AKGEFVSIFDCDHVPTRSFLQMTMGWFLKEKELAMMQTPH-HFFSPDPFERNLGRFRKTPNEG 412
Cdd:cd00761 76 ARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGnLLFRRELLEEIGGFDEALLSGE 138
|
|
| CESA_like_1 |
cd06439 |
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ... |
249-503 |
6.91e-09 |
|
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: 57.59 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 249 LGYFQVVWPL--NRQPVPLPEDMAQWPTVDIFVPTYNEDlNVVKNTIYASQGIDWPKDKLNIWILDDGGR----EEFRQF 322
Cdd:cd06439 3 FGYPLLLKLLarLRPKPPSLPDPAYLPTVTIIIPAYNEE-AVIEAKLENLLALDYPRDRLEIIVVSDGSTdgtaEIAREY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 323 A-KDVGVHyiaRTTHEHAKAGNINNALKYAKGEFVSIFDCDHVPTRSFLQMTMGWFLKEK------ELammqtphHFFSP 395
Cdd:cd06439 82 AdKGVKLL---RFPERRGKAAALNRALALATGEIVVFTDANALLDPDALRLLVRHFADPSvgavsgEL-------VIVDG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 396 DPFERNLGRFRKtpnegtlFYGLVQDGNDMWDATF-FCGSCAVIRR---GPLDEiggiavETVTEDAHTSLRLHRRGHTS 471
Cdd:cd06439 152 GGSGSGEGLYWK-------YENWLKRAESRLGSTVgANGAIYAIRRelfRPLPA------DTINDDFVLPLRIARQGYRV 218
|
250 260 270
....*....|....*....|....*....|....
gi 504652645 472 AYMriPQAAGL--ATESLSAHIGQRIRWARGMVQ 503
Cdd:cd06439 219 VYE--PDAVAYeeVAEDGSEEFRRRVRIAAGNLQ 250
|
|
| PLN02190 |
PLN02190 |
cellulose synthase-like protein |
452-572 |
1.85e-07 |
|
cellulose synthase-like protein
Pssm-ID: 215122 [Multi-domain] Cd Length: 756 Bit Score: 54.87 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 452 ETVTEDAHTSLRLHRRGHTSAYMRIPQAAGLA---TESLSAHIGQRiRWARGMVQI-FRLDNPLFG---KGLKLAQRICY 524
Cdd:PLN02190 456 DSVAEDLNTSIGIHSRGWTSSYISPDPPAFLGsmpPGGPEAMVQQR-RWATGLIEVlFNKQSPLIGmfcRKIRFRQRLAY 534
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 504652645 525 VnAMLHFLSGIPRLIFLTAPlAFLLLHAYIIYAPALMIALFVLPHMIH 572
Cdd:PLN02190 535 L-YVFTCLRSIPELIYCLLP-AYCLLHNSALFPKGVYLGIIVTLVGMH 580
|
|
| WcaA |
COG0463 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
273-447 |
1.13e-06 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440231 [Multi-domain] Cd Length: 208 Bit Score: 50.09 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 273 PTVDIFVPTYNEDLNVVK--NTIYASQGIDWPkdklnIWILDDGG----REEFRQFA-KDVGVHYIaRTTHEHAKAGNIN 345
Cdd:COG0463 2 PLVSVVIPTYNEEEYLEEalESLLAQTYPDFE-----IIVVDDGStdgtAEILRELAaKDPRIRVI-RLERNRGKGAARN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 346 NALKYAKGEFVSIFDCDHVPTRSFLQMtmgwFLKekelAMMQTPHHFFSPDPFERNLGR-FRKTPNEGTLFYGLVQDGND 424
Cdd:COG0463 76 AGLAAARGDYIAFLDADDQLDPEKLEE----LVA----ALEEGPADLVYGSRLIREGESdLRRLGSRLFNLVRLLTNLPD 147
|
170 180
....*....|....*....|...
gi 504652645 425 MwdatffCGSCAVIRRGPLDEIG 447
Cdd:COG0463 148 S------TSGFRLFRREVLEELG 164
|
|
| GT_2_like_e |
cd04192 |
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ... |
277-500 |
1.32e-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: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 277 IFVPTYNEDLNVvKNTIYASQGIDWPKDKLNIWILDDGGREEFRQ----FAKDVGVH-YIARTTHEHA--KAGNINNALK 349
Cdd:cd04192 1 VVIAARNEAENL-PRLLQSLSALDYPKEKFEVILVDDHSTDGTVQilefAAAKPNFQlKILNNSRVSIsgKKNALTTAIK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 350 YAKGEFVSIFDCDHVPTRSFLQMTMGWFLKEKeLAMMQTPHHFFSPDPFernLGRFRKTPNEGTLFYGLVQDGndmWDAT 429
Cdd:cd04192 80 AAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQ-IGLVAGPVIYFKGKSL---LAKFQRLDWLSLLGLIAGSFG---LGKP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504652645 430 FFC-GSCAVIRRGPLDEIGGIA--VETVTEDahTSLRLHR---RGHTSAYMRIPQAAGL--ATESLSAHIGQRIRWARG 500
Cdd:cd04192 153 FMCnGANMAYRKEAFFEVGGFEgnDHIASGD--DELLLAKvasKYPKVAYLKNPEALVTtqPVTSWKELLNQRKRWASK 229
|
|
| PLN02248 |
PLN02248 |
cellulose synthase-like protein |
454-541 |
2.08e-06 |
|
cellulose synthase-like protein
Pssm-ID: 215138 [Multi-domain] Cd Length: 1135 Bit Score: 51.57 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 454 VTEDAHTSLRLHRRGHTSAYMRIPQAA--GLATESLSAHIGQRIRWARGMVQIF--RlDNPLFG-KGLKLAQRICYVN-A 527
Cdd:PLN02248 835 VTEDVVTGYRMHNRGWRSVYCVTKRDAfrGTAPINLTDRLHQVLRWATGSVEIFfsR-NNALLAsRRLKFLQRIAYLNvG 913
|
90
....*....|....
gi 504652645 528 MLHFLSgiprlIFL 541
Cdd:PLN02248 914 IYPFTS-----IFL 922
|
|
| PLN02638 |
PLN02638 |
cellulose synthase A (UDP-forming), catalytic subunit |
201-314 |
3.49e-05 |
|
cellulose synthase A (UDP-forming), catalytic subunit
Pssm-ID: 215343 [Multi-domain] Cd Length: 1079 Bit Score: 47.61 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 201 MLIVLSLTVSCRYIWWRYTSTLNWDDP---VSLVCGIilLFAetYAWVvlvLGYFQVVWPLNRQP----VPLPEDM---- 269
Cdd:PLN02638 273 MVIVLRLVILCIFLHYRITNPVRNAYAlwlISVICEI--WFA--LSWI---LDQFPKWLPVNRETyldrLALRYDRegep 345
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 504652645 270 AQWPTVDIFVPTYN---EDLNVVKNTIYASQGIDWPKDKLNIWILDDG 314
Cdd:PLN02638 346 SQLAAVDIFVSTVDplkEPPLVTANTVLSILAVDYPVDKVSCYVSDDG 393
|
|
| DPM_DPG-synthase_like |
cd04179 |
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ... |
277-362 |
4.53e-04 |
|
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: 42.18 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 277 IFVPTYNEDLN---VVKNTI-YASQGIDWpkdklNIWILDDGGREEFRQFAKDVGVHYIARTTHEHA----KAGNINNAL 348
Cdd:cd04179 1 VVIPAYNEEENipeLVERLLaVLEEGYDY-----EIIVVDDGSTDGTAEIARELAARVPRVRVIRLSrnfgKGAAVRAGF 75
|
90
....*....|....
gi 504652645 349 KYAKGEFVSIFDCD 362
Cdd:cd04179 76 KAARGDIVVTMDAD 89
|
|
| DPM1_like |
cd06442 |
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ... |
277-363 |
2.48e-03 |
|
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.
Pssm-ID: 133062 [Multi-domain] Cd Length: 224 Bit Score: 40.21 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 277 IFVPTYNEDLNVVKnTIY----ASQGIDWpkdklNIWILD----DGGREEFRQFAKDVGVHYIARTTHEHAKAGNINNAL 348
Cdd:cd06442 1 IIIPTYNERENIPE-LIErldaALKGIDY-----EIIVVDdnspDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGF 74
|
90
....*....|....*
gi 504652645 349 KYAKGEFVSIFDCDH 363
Cdd:cd06442 75 KAARGDVIVVMDADL 89
|
|
| Glucosylceramide_synthase |
cd02520 |
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ... |
339-499 |
2.50e-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: 39.89 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 339 AKAGNINNALKYAKGEFVSIFDCDHVPTRSFLQ-MTmgwflkekelammqtpHHFFSPDpfernlgrfrktpnegtlfYG 417
Cdd:cd02520 73 PKVNNLIKGYEEARYDILVISDSDISVPPDYLRrMV----------------APLMDPG-------------------VG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 418 LVQdgndmwdATFFCGSCAVIRRGPLDEIGGIAV--ETVTEDAHTSLRLHRRGHTSAYMRIPQAAGLATESLSAHIGQRI 495
Cdd:cd02520 118 LVT-------CLCAFGKSMALRREVLDAIGGFEAfaDYLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQL 190
|
....
gi 504652645 496 RWAR 499
Cdd:cd02520 191 RWSR 194
|
|
| WcaE |
COG1216 |
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism]; |
273-371 |
3.60e-03 |
|
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
Pssm-ID: 440829 [Multi-domain] Cd Length: 202 Bit Score: 39.59 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 273 PTVDIFVPTYN--EDLNVVKNTIYASQGIDWPkdklnIWILDDGGREEFRQFAKDV---GVHYIaRTTHEHAKAGNINNA 347
Cdd:COG1216 3 PKVSVVIPTYNrpELLRRCLESLLAQTYPPFE-----VIVVDNGSTDGTAELLAALafpRVRVI-RNPENLGFAAARNLG 76
|
90 100
....*....|....*....|....
gi 504652645 348 LKYAKGEFVSIFDCDHVPTRSFLQ 371
Cdd:COG1216 77 LRAAGGDYLLFLDDDTVVEPDWLE 100
|
|
| PRK05454 |
PRK05454 |
glucans biosynthesis glucosyltransferase MdoH; |
191-344 |
6.10e-03 |
|
glucans biosynthesis glucosyltransferase MdoH;
Pssm-ID: 235476 [Multi-domain] Cd Length: 605 Bit Score: 40.25 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 191 RRIPGRFSALMLIVLSLTVSCrYIWWRYTSTLNWDDPVSLVCGIILLFAETYAWVVL-----VLGYFQVVWPLNRQPVPL 265
Cdd:PRK05454 34 WRTVGTLRRLILLGLTLAQTA-VATWEMKAVLPYGGWTLLEPALLVLFALLFAWISLgfwtaLMGFLQLLRGRDKYSISA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 266 PEDMAQWPTVD----IFVPTYNED-------LNVVKNTIYASQGIDWpkdkLNIWILDD------GGREE--FRQFAKDV 326
Cdd:PRK05454 113 SAAGDPPPPPEartaILMPIYNEDparvfagLRAMYESLAATGHGAH----FDFFILSDtrdpdiAAAEEaaWLELRAEL 188
|
170 180
....*....|....*....|..
gi 504652645 327 G----VHYIARTTHEHAKAGNI 344
Cdd:PRK05454 189 GgegrIFYRRRRRNVGRKAGNI 210
|
|
| PLN02248 |
PLN02248 |
cellulose synthase-like protein |
201-315 |
8.67e-03 |
|
cellulose synthase-like protein
Pssm-ID: 215138 [Multi-domain] Cd Length: 1135 Bit Score: 40.01 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504652645 201 MLIVLSLTVSCRYIWWRYTSTLN---WDDPVSLVCGIilLFAetYAWVvlvLGYFQVVWPLNR------------QPVPL 265
Cdd:PLN02248 286 LLILIRLVVLGLFLTWRVRNPNEdamWLWGMSVVCEI--WFA--FSWL---LDQLPKLCPINRatdlavlkekfeTPSPS 358
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504652645 266 -PEDMAQWPTVDIFVPT---YNEDLNVVKNTIYASQGIDWPKDKLNIWILDDGG 315
Cdd:PLN02248 359 nPTGRSDLPGIDVFVSTadpEKEPPLVTANTILSILAADYPVEKLACYLSDDGG 412
|
|
| |
