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Conserved domains on  [gi|727182765|ref|WP_033645053|]
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MULTISPECIES: UDP-forming cellulose synthase catalytic subunit [Serratia]

Protein Classification

UDP-forming cellulose synthase catalytic subunit( domain architecture ID 11485364)

UDP-forming cellulose synthase catalytic subunit is part of the cellulose synthase complex in the bacterial membrane, which polymerizes UDP-glucose to cellulose

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
14-863 0e+00

cellulose synthase catalytic subunit; Provisional


:

Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 1701.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  14 RQAVQARYRAYRRSGASALTAFFTTLLVALGWMLLRLESPAWRRVRAGRAYWFPHLSAERPRPADALRYLLQGAWLLLFR 93
Cdd:PRK11498   1 NARLIGRYRDYRRHGASAFSATLGCLWMILAWIFLPLEHPRWQRIRAEHKNLYPHINASRPRPLDPLRYLIQTLWLLIGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  94 SGRA--PVQRDYFAGWRRLQQRYADWLQGLPQRLKNAGVEQRSVERLGRMNRGLRRALFILVGVLAAILAMLCISQPFDL 171
Cdd:PRK11498  81 SRKEtpKPRRRAFSGLQNIRGRYHQWLEELPERVSHKTQHLDEKKELGHLSAGARRLILGIIVTFSLILALICITQPFNP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 172 SAQFVFVLLLWGIAMVVRRVPGRLPALMLIVLSLTVSCRYLWWRYTATLNWDDPLSLVCGLLLLVAETYAWVVLVLGYFQ 251
Cdd:PRK11498 161 LAQFIFLMLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 252 TIWPLNRQPVPLPEDSATWPTIDLMVPTYNEDLGVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAFAAEVGVKYIAR 331
Cdd:PRK11498 241 VVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKYIAR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 332 PTHEHAKAGNINNALKQATGEFVAIFDCDHVPTRSFLQLTMGWFFKDKKLAMLQTPHHFFSPDPFERNLGRFRQTPNEGT 411
Cdd:PRK11498 321 PTHEHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDPFERNLGRFRKTPNEGT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 412 LFYGLVQDGNDMWDATFFCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQ 491
Cdd:PRK11498 401 LFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQ 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 492 RIRWARGMVQIFRLDNPLLGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIFAPALAIALYVLPHMIHA 571
Cdd:PRK11498 481 RIRWARGMVQIFRLDNPLTGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 572 SLTNSRIQGKYRHSFWSEIYETVLAWYIARPTTVALFNPHKGKFNVTAKGGLVEEEHVDWVITRPYMFLVVLNLAGLAFG 651
Cdd:PRK11498 561 SLTNSRIQGKYRHSFWSEIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGGLVEEEYVDWVISRPYIFLVLLNLVGVAVG 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 652 AWRLAYGPTDEVMTVIISLVWVLYNMTILGGAVAVAVEAKQVRQAHRVEIAMPAAIARADGHLYPCTLRDYSDGGVGIEM 731
Cdd:PRK11498 641 IWRYFYGPPNEILTVIVSLVWVFYNLIILGGAVAVSVESKQVRRSHRVEMTMPAAIAREDGHLFSCTVQDFSDGGLGIKI 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 732 RVADTLKEGDKASLLLKRGQQEYSFPCVVTRAFGNKVGVRLVSLSTREHIDFIQCTFARADTWALWQDGFPEDRPIESLR 811
Cdd:PRK11498 721 NGQAQLLEGQKVNLLLKRGQQEYVFPTQVTRVMGNEVGLQLMPLTTQQHIDFVQCTFARADTWALWQDSFPEDKPLESLL 800
                        810       820       830       840       850
                 ....*....|....*....|....*....|....*....|....*....|..
gi 727182765 812 DVLALGFRGYVRMADYAPPLVRGLLVGVTSLTAWVVSFIPRGVGRDPTLGQQ 863
Cdd:PRK11498 801 DILKLGFRGYRHLAEFAPPSVKGIFRVLTSLVSWVVSFIPRRPERQEAAQPS 852
 
Name Accession Description Interval E-value
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
14-863 0e+00

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 1701.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  14 RQAVQARYRAYRRSGASALTAFFTTLLVALGWMLLRLESPAWRRVRAGRAYWFPHLSAERPRPADALRYLLQGAWLLLFR 93
Cdd:PRK11498   1 NARLIGRYRDYRRHGASAFSATLGCLWMILAWIFLPLEHPRWQRIRAEHKNLYPHINASRPRPLDPLRYLIQTLWLLIGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  94 SGRA--PVQRDYFAGWRRLQQRYADWLQGLPQRLKNAGVEQRSVERLGRMNRGLRRALFILVGVLAAILAMLCISQPFDL 171
Cdd:PRK11498  81 SRKEtpKPRRRAFSGLQNIRGRYHQWLEELPERVSHKTQHLDEKKELGHLSAGARRLILGIIVTFSLILALICITQPFNP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 172 SAQFVFVLLLWGIAMVVRRVPGRLPALMLIVLSLTVSCRYLWWRYTATLNWDDPLSLVCGLLLLVAETYAWVVLVLGYFQ 251
Cdd:PRK11498 161 LAQFIFLMLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 252 TIWPLNRQPVPLPEDSATWPTIDLMVPTYNEDLGVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAFAAEVGVKYIAR 331
Cdd:PRK11498 241 VVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKYIAR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 332 PTHEHAKAGNINNALKQATGEFVAIFDCDHVPTRSFLQLTMGWFFKDKKLAMLQTPHHFFSPDPFERNLGRFRQTPNEGT 411
Cdd:PRK11498 321 PTHEHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDPFERNLGRFRKTPNEGT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 412 LFYGLVQDGNDMWDATFFCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQ 491
Cdd:PRK11498 401 LFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQ 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 492 RIRWARGMVQIFRLDNPLLGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIFAPALAIALYVLPHMIHA 571
Cdd:PRK11498 481 RIRWARGMVQIFRLDNPLTGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 572 SLTNSRIQGKYRHSFWSEIYETVLAWYIARPTTVALFNPHKGKFNVTAKGGLVEEEHVDWVITRPYMFLVVLNLAGLAFG 651
Cdd:PRK11498 561 SLTNSRIQGKYRHSFWSEIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGGLVEEEYVDWVISRPYIFLVLLNLVGVAVG 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 652 AWRLAYGPTDEVMTVIISLVWVLYNMTILGGAVAVAVEAKQVRQAHRVEIAMPAAIARADGHLYPCTLRDYSDGGVGIEM 731
Cdd:PRK11498 641 IWRYFYGPPNEILTVIVSLVWVFYNLIILGGAVAVSVESKQVRRSHRVEMTMPAAIAREDGHLFSCTVQDFSDGGLGIKI 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 732 RVADTLKEGDKASLLLKRGQQEYSFPCVVTRAFGNKVGVRLVSLSTREHIDFIQCTFARADTWALWQDGFPEDRPIESLR 811
Cdd:PRK11498 721 NGQAQLLEGQKVNLLLKRGQQEYVFPTQVTRVMGNEVGLQLMPLTTQQHIDFVQCTFARADTWALWQDSFPEDKPLESLL 800
                        810       820       830       840       850
                 ....*....|....*....|....*....|....*....|....*....|..
gi 727182765 812 DVLALGFRGYVRMADYAPPLVRGLLVGVTSLTAWVVSFIPRGVGRDPTLGQQ 863
Cdd:PRK11498 801 DILKLGFRGYRHLAEFAPPSVKGIFRVLTSLVSWVVSFIPRRPERQEAAQPS 852
CelA TIGR03030
cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 ...
144-832 0e+00

cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 polymerization of glucose residues in the formation of cellulose. In bacteria, the substrate is UDP-glucose. The synthase consists of two subunits (or domains in the frequent cases where it is encoded as a single polypeptide), the catalytic domain modelled here and the regulatory domain (pfam03170). The regulatory domain binds the allosteric activator cyclic di-GMP. The protein is membrane-associated and probably assembles into multimers such that the individual cellulose strands can self-assemble into multi-strand fibrils.


Pssm-ID: 274400 [Multi-domain]  Cd Length: 713  Bit Score: 981.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  144 GLRRALFILVGVLAAILAMLCISQPFDLSAQFVFVLLLWGIAMVVRRVPGRLPALMLIVLSLTVSCRYLWWRYTATLNWD 223
Cdd:TIGR03030   4 ALFKGLLFIIAVAGLLALLALITAPVTLETQLIIAGSAFLLLLILKRFNGKRPRLLLLVLSVFISLRYLWWRLTETLPFD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  224 DPLSLVCGLLLLVAETYAWVVLVLGYFQTIWPLNRQPVPLPEDSATWPTIDLMVPTYNEDLGVVKPTIYAALGIDWPKEK 303
Cdd:TIGR03030  84 NTLNFIFGTLLLLAELYSITILLLGYFQTVRPLDRTPVPLPLDPEEWPTVDVFIPTYNEDLEIVATTVLAAKNMDYPADK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  304 VNIYILDDGN------------------RPEFRAFAAEVGVKYIARPTHEHAKAGNINNALKQATGEFVAIFDCDHVPTR 365
Cdd:TIGR03030 164 FRVWILDDGGtdqkrndpdpeqaeaaqrREELKEFCRKLGVNYITRPRNVHAKAGNINNALKHTDGELILIFDADHVPTR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  366 SFLQLTMGWFFKDKKLAMLQTPHHFFSPDPFERNLGRFRQTPNEGTLFYGLVQDGNDMWDATFFCGSCAILRRSALDEIG 445
Cdd:TIGR03030 244 DFLQRTVGWFVEDPKLFLVQTPHFFVSPDPIERNLGTFRRMPNENELFYGLIQDGNDFWNAAFFCGSAAVLRREALDEIG 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  446 GIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLLGKGLKLAQRLCYANA 525
Cdd:TIGR03030 324 GIAGETVTEDAETALKLHRRGWNSAYLDRPLIAGLAPETLSGHIGQRIRWAQGMMQIFRLDNPLLKRGLSFPQRLCYLNA 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  526 MLHFLSGIPRLIFLTAPLAFLLLHAYIIFAPALAIALYVLPHMIHASLTNSRIQGKYRHSFWSEIYETVLAWYIARPTTV 605
Cdd:TIGR03030 404 MLFWFFPLPRVIFLTAPLAYLFFGLNIFVASALEILAYALPHMLHSLLTNSYLFGRVRWPFWSEVYETVLAVYLLPPVLV 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  606 ALFNPHKGKFNVTAKGGLVEEEHVDwVITRPYMFLVVLNLAGLAFGAWRLaYGPTDEVMTVIISLVWVLYNMTILGGAVA 685
Cdd:TIGR03030 484 TLLNPKKPKFNVTPKGELLDEDYFS-PLSRPYLILFALILAGLAFGLYRI-YGYPIERGVLLVVLGWNLLNLILLGAALA 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  686 VAVEAKQVRQAHRVEIAMPAAIARADGHLYPCTLRDYSDGGVGIEMRVADT----LKEGDKASLLLKRGQQEYSFPCVVT 761
Cdd:TIGR03030 562 VVAERRQRRSSPRIPCKIPAEVQRDGGRWVEATVEDASVGGLGIKINAQGApgpqLGAGVLVQIRPKRNGLPALKPARVR 641
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727182765  762 RAFGNKVGVRLVSLSTREHIDFIQCTFARADTWA-LWQDGFPEDRPIESLRDVLALGFRGYVRMADYAPPLV 832
Cdd:TIGR03030 642 GAGGVMIGLEFSPLNVQQVREIVDLVFARSDRWVaLWEERRRPDGPLRGLADFLKIALRGLFRSARDLVRAP 713
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
271-503 2.24e-120

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 363.82  E-value: 2.24e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEDLGVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAFAAEVGVK----YIARPTHEHAKAGNINNAL 346
Cdd:cd06421    1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEygyrYLTRPDNRHAKAGNLNNAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 347 KQATGEFVAIFDCDHVPTRSFLQLTMGWFFKDKKLAMLQTPHHFFSPDPFERnlgRFRQTPNEGTLFYGLVQDGNDMWDA 426
Cdd:cd06421   81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDW---LADGAPNEQELFYGVIQPGRDRWGA 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727182765 427 TFFCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWARGMVQIF 503
Cdd:cd06421  158 AFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
241-620 1.08e-45

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 166.46  E-value: 1.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 241 AWVVLVLGYFQTIWPLNRQPvplpEDSATWPTIDLMVPTYNEDLgVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAF 320
Cdd:COG1215    3 LLLALLALLYLLLLALARRR----RAPADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 321 AAEVG-----VKYIARPTHEHaKAGNINNALKQATGEFVAIFDCDHVPTRSFLQLTMGwFFKDKKLAMlqtphhffspdp 395
Cdd:COG1215   78 ARELAaeyprVRVIERPENGG-KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVA-AFADPGVGA------------ 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 396 fernlgrfrqtpnegtlfyglvqdgndmwdatffCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIP 475
Cdd:COG1215  144 ----------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 476 QAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLLGKGLKLAqrlcyanamlhflsgipRLIFLTAPLAFLLLhayiiFA 555
Cdd:COG1215  190 VVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLL-----------------FLLLLLLPLLLLLL-----LL 247
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727182765 556 PALAIALYVLPHMIHASLtnsriqgkyRHSFWSEIYETVLAWYIARPTTVALFNPHKGKFNVTAK 620
Cdd:COG1215  248 ALLALLLLLLPALLLALL---------LALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
277-443 8.27e-22

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 93.23  E-value: 8.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  277 VPTYNEdLGVVKPTIYAALgiDWPKEKVNIYILDDGNRPEFRAFAAEV-----GVKYIARPtHEHAKAGNINNALKQATG 351
Cdd:pfam00535   4 IPTYNE-EKYLLETLESLL--NQTYPNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLP-ENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  352 EFVAIFDCDHVPTRSFLQLTMGWFFKDKK-LAMLQTPHHFFSPDPFERNLGRFRQtpnegtLFYGLVQDGNDMWDATFFC 430
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGAdVVVGSRYVIFGETGEYRRASRITLS------RLPFFLGLRLLGLNLPFLI 153
                         170
                  ....*....|...
gi 727182765  431 GSCAILRRSALDE 443
Cdd:pfam00535 154 GGFALYRREALEE 166
 
Name Accession Description Interval E-value
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
14-863 0e+00

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 1701.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  14 RQAVQARYRAYRRSGASALTAFFTTLLVALGWMLLRLESPAWRRVRAGRAYWFPHLSAERPRPADALRYLLQGAWLLLFR 93
Cdd:PRK11498   1 NARLIGRYRDYRRHGASAFSATLGCLWMILAWIFLPLEHPRWQRIRAEHKNLYPHINASRPRPLDPLRYLIQTLWLLIGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  94 SGRA--PVQRDYFAGWRRLQQRYADWLQGLPQRLKNAGVEQRSVERLGRMNRGLRRALFILVGVLAAILAMLCISQPFDL 171
Cdd:PRK11498  81 SRKEtpKPRRRAFSGLQNIRGRYHQWLEELPERVSHKTQHLDEKKELGHLSAGARRLILGIIVTFSLILALICITQPFNP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 172 SAQFVFVLLLWGIAMVVRRVPGRLPALMLIVLSLTVSCRYLWWRYTATLNWDDPLSLVCGLLLLVAETYAWVVLVLGYFQ 251
Cdd:PRK11498 161 LAQFIFLMLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 252 TIWPLNRQPVPLPEDSATWPTIDLMVPTYNEDLGVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAFAAEVGVKYIAR 331
Cdd:PRK11498 241 VVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKYIAR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 332 PTHEHAKAGNINNALKQATGEFVAIFDCDHVPTRSFLQLTMGWFFKDKKLAMLQTPHHFFSPDPFERNLGRFRQTPNEGT 411
Cdd:PRK11498 321 PTHEHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDPFERNLGRFRKTPNEGT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 412 LFYGLVQDGNDMWDATFFCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQ 491
Cdd:PRK11498 401 LFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQ 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 492 RIRWARGMVQIFRLDNPLLGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIFAPALAIALYVLPHMIHA 571
Cdd:PRK11498 481 RIRWARGMVQIFRLDNPLTGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 572 SLTNSRIQGKYRHSFWSEIYETVLAWYIARPTTVALFNPHKGKFNVTAKGGLVEEEHVDWVITRPYMFLVVLNLAGLAFG 651
Cdd:PRK11498 561 SLTNSRIQGKYRHSFWSEIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGGLVEEEYVDWVISRPYIFLVLLNLVGVAVG 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 652 AWRLAYGPTDEVMTVIISLVWVLYNMTILGGAVAVAVEAKQVRQAHRVEIAMPAAIARADGHLYPCTLRDYSDGGVGIEM 731
Cdd:PRK11498 641 IWRYFYGPPNEILTVIVSLVWVFYNLIILGGAVAVSVESKQVRRSHRVEMTMPAAIAREDGHLFSCTVQDFSDGGLGIKI 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 732 RVADTLKEGDKASLLLKRGQQEYSFPCVVTRAFGNKVGVRLVSLSTREHIDFIQCTFARADTWALWQDGFPEDRPIESLR 811
Cdd:PRK11498 721 NGQAQLLEGQKVNLLLKRGQQEYVFPTQVTRVMGNEVGLQLMPLTTQQHIDFVQCTFARADTWALWQDSFPEDKPLESLL 800
                        810       820       830       840       850
                 ....*....|....*....|....*....|....*....|....*....|..
gi 727182765 812 DVLALGFRGYVRMADYAPPLVRGLLVGVTSLTAWVVSFIPRGVGRDPTLGQQ 863
Cdd:PRK11498 801 DILKLGFRGYRHLAEFAPPSVKGIFRVLTSLVSWVVSFIPRRPERQEAAQPS 852
CelA TIGR03030
cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 ...
144-832 0e+00

cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 polymerization of glucose residues in the formation of cellulose. In bacteria, the substrate is UDP-glucose. The synthase consists of two subunits (or domains in the frequent cases where it is encoded as a single polypeptide), the catalytic domain modelled here and the regulatory domain (pfam03170). The regulatory domain binds the allosteric activator cyclic di-GMP. The protein is membrane-associated and probably assembles into multimers such that the individual cellulose strands can self-assemble into multi-strand fibrils.


Pssm-ID: 274400 [Multi-domain]  Cd Length: 713  Bit Score: 981.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  144 GLRRALFILVGVLAAILAMLCISQPFDLSAQFVFVLLLWGIAMVVRRVPGRLPALMLIVLSLTVSCRYLWWRYTATLNWD 223
Cdd:TIGR03030   4 ALFKGLLFIIAVAGLLALLALITAPVTLETQLIIAGSAFLLLLILKRFNGKRPRLLLLVLSVFISLRYLWWRLTETLPFD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  224 DPLSLVCGLLLLVAETYAWVVLVLGYFQTIWPLNRQPVPLPEDSATWPTIDLMVPTYNEDLGVVKPTIYAALGIDWPKEK 303
Cdd:TIGR03030  84 NTLNFIFGTLLLLAELYSITILLLGYFQTVRPLDRTPVPLPLDPEEWPTVDVFIPTYNEDLEIVATTVLAAKNMDYPADK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  304 VNIYILDDGN------------------RPEFRAFAAEVGVKYIARPTHEHAKAGNINNALKQATGEFVAIFDCDHVPTR 365
Cdd:TIGR03030 164 FRVWILDDGGtdqkrndpdpeqaeaaqrREELKEFCRKLGVNYITRPRNVHAKAGNINNALKHTDGELILIFDADHVPTR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  366 SFLQLTMGWFFKDKKLAMLQTPHHFFSPDPFERNLGRFRQTPNEGTLFYGLVQDGNDMWDATFFCGSCAILRRSALDEIG 445
Cdd:TIGR03030 244 DFLQRTVGWFVEDPKLFLVQTPHFFVSPDPIERNLGTFRRMPNENELFYGLIQDGNDFWNAAFFCGSAAVLRREALDEIG 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  446 GIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLLGKGLKLAQRLCYANA 525
Cdd:TIGR03030 324 GIAGETVTEDAETALKLHRRGWNSAYLDRPLIAGLAPETLSGHIGQRIRWAQGMMQIFRLDNPLLKRGLSFPQRLCYLNA 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  526 MLHFLSGIPRLIFLTAPLAFLLLHAYIIFAPALAIALYVLPHMIHASLTNSRIQGKYRHSFWSEIYETVLAWYIARPTTV 605
Cdd:TIGR03030 404 MLFWFFPLPRVIFLTAPLAYLFFGLNIFVASALEILAYALPHMLHSLLTNSYLFGRVRWPFWSEVYETVLAVYLLPPVLV 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  606 ALFNPHKGKFNVTAKGGLVEEEHVDwVITRPYMFLVVLNLAGLAFGAWRLaYGPTDEVMTVIISLVWVLYNMTILGGAVA 685
Cdd:TIGR03030 484 TLLNPKKPKFNVTPKGELLDEDYFS-PLSRPYLILFALILAGLAFGLYRI-YGYPIERGVLLVVLGWNLLNLILLGAALA 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  686 VAVEAKQVRQAHRVEIAMPAAIARADGHLYPCTLRDYSDGGVGIEMRVADT----LKEGDKASLLLKRGQQEYSFPCVVT 761
Cdd:TIGR03030 562 VVAERRQRRSSPRIPCKIPAEVQRDGGRWVEATVEDASVGGLGIKINAQGApgpqLGAGVLVQIRPKRNGLPALKPARVR 641
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727182765  762 RAFGNKVGVRLVSLSTREHIDFIQCTFARADTWA-LWQDGFPEDRPIESLRDVLALGFRGYVRMADYAPPLV 832
Cdd:TIGR03030 642 GAGGVMIGLEFSPLNVQQVREIVDLVFARSDRWVaLWEERRRPDGPLRGLADFLKIALRGLFRSARDLVRAP 713
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
271-503 2.24e-120

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 363.82  E-value: 2.24e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEDLGVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAFAAEVGVK----YIARPTHEHAKAGNINNAL 346
Cdd:cd06421    1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEygyrYLTRPDNRHAKAGNLNNAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 347 KQATGEFVAIFDCDHVPTRSFLQLTMGWFFKDKKLAMLQTPHHFFSPDPFERnlgRFRQTPNEGTLFYGLVQDGNDMWDA 426
Cdd:cd06421   81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDW---LADGAPNEQELFYGVIQPGRDRWGA 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727182765 427 TFFCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWARGMVQIF 503
Cdd:cd06421  158 AFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
241-620 1.08e-45

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 166.46  E-value: 1.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 241 AWVVLVLGYFQTIWPLNRQPvplpEDSATWPTIDLMVPTYNEDLgVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAF 320
Cdd:COG1215    3 LLLALLALLYLLLLALARRR----RAPADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 321 AAEVG-----VKYIARPTHEHaKAGNINNALKQATGEFVAIFDCDHVPTRSFLQLTMGwFFKDKKLAMlqtphhffspdp 395
Cdd:COG1215   78 ARELAaeyprVRVIERPENGG-KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVA-AFADPGVGA------------ 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 396 fernlgrfrqtpnegtlfyglvqdgndmwdatffCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIP 475
Cdd:COG1215  144 ----------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 476 QAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLLGKGLKLAqrlcyanamlhflsgipRLIFLTAPLAFLLLhayiiFA 555
Cdd:COG1215  190 VVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLL-----------------FLLLLLLPLLLLLL-----LL 247
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727182765 556 PALAIALYVLPHMIHASLtnsriqgkyRHSFWSEIYETVLAWYIARPTTVALFNPHKGKFNVTAK 620
Cdd:COG1215  248 ALLALLLLLLPALLLALL---------LALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
271-498 4.10e-30

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 118.95  E-value: 4.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEdLGVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAFAAEV--------GVKYIARPTHEHAKAGNI 342
Cdd:cd06437    1 PMVTVQLPVFNE-KYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVeeyaaqgvNIKHVRRADRTGYKAGAL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 343 NNALKQATGEFVAIFDCDHVPTRSFLQLTMgWFFKDKKLAMLQTPHHFFSPDpfERNLGRFR------------QTPNEG 410
Cdd:cd06437   80 AEGMKVAKGEYVAIFDADFVPPPDFLQKTP-PYFADPKLGFVQTRWGHINAN--YSLLTRVQamsldyhftieqVARSST 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 411 TLFYGlvqdgndmwdatfFCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIG 490
Cdd:cd06437  157 GLFFN-------------FNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRS 223

                 ....*...
gi 727182765 491 QRIRWARG 498
Cdd:cd06437  224 QQHRWSKG 231
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
275-504 2.37e-29

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 117.12  E-value: 2.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 275 LMVPTYNEDLGVVKPTIYAALGIDWPKEKVniYILDDGNRPEF-----RAFAAEVGVK--YIARPTHEHAKAGNINNALK 347
Cdd:cd06435    2 IHVPCYEEPPEMVKETLDSLAALDYPNFEV--IVIDNNTKDEAlwkpvEAHCAQLGERfrFFHVEPLPGAKAGALNYALE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 348 QATG--EFVAIFDCDHVPTRSFLQlTMGWFFKDKKLAMLQTPHHF--FSPDPFERNLGRfrqtpnEGTLFYGLVQDGNDM 423
Cdd:cd06435   80 RTAPdaEIIAVIDADYQVEPDWLK-RLVPIFDDPRVGFVQAPQDYrdGEESLFKRMCYA------EYKGFFDIGMVSRNE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 424 WDATFFCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWARGMVQIF 503
Cdd:cd06435  153 RNAIIQHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQIL 232

                 .
gi 727182765 504 R 504
Cdd:cd06435  233 K 233
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
275-455 3.99e-26

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 105.77  E-value: 3.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 275 LMVPTYNEDLgVVKPTIYAALGIDWPKekVNIYILDDGNRPEFRAFAAEVGVKYIA-----RPTHEHAKAGNINNALKQA 349
Cdd:cd06423    1 IIVPAYNEEA-VIERTIESLLALDYPK--LEVIVVDDGSTDDTLEILEELAALYIRrvlvvRDKENGGKAGALNAGLRHA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 350 TGEFVAIFDCDHVPTRSFLQ-LTMGWFFKDKKLAMLQTPHHFfspDPFERNLGRFrQTpNEGTLFYGLVQDGNDMWDATF 428
Cdd:cd06423   78 KGDIVVVLDADTILEPDALKrLVVPFFADPKVGAVQGRVRVR---NGSENLLTRL-QA-IEYLSIFRLGRRAQSALGGVL 152
                        170       180
                 ....*....|....*....|....*...
gi 727182765 429 -FCGSCAILRRSALDEIGGIAVETVTED 455
Cdd:cd06423  153 vLSGAFGAFRREALREVGGWDEDTLTED 180
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
277-443 8.27e-22

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 93.23  E-value: 8.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  277 VPTYNEdLGVVKPTIYAALgiDWPKEKVNIYILDDGNRPEFRAFAAEV-----GVKYIARPtHEHAKAGNINNALKQATG 351
Cdd:pfam00535   4 IPTYNE-EKYLLETLESLL--NQTYPNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLP-ENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  352 EFVAIFDCDHVPTRSFLQLTMGWFFKDKK-LAMLQTPHHFFSPDPFERNLGRFRQtpnegtLFYGLVQDGNDMWDATFFC 430
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGAdVVVGSRYVIFGETGEYRRASRITLS------RLPFFLGLRLLGLNLPFLI 153
                         170
                  ....*....|...
gi 727182765  431 GSCAILRRSALDE 443
Cdd:pfam00535 154 GGFALYRREALEE 166
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
353-564 4.85e-16

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 77.38  E-value: 4.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  353 FVAIFDCD-HVPTRSFLQLTmgWFFKDKKLAMLQTPHHFF-SPDPFERNLGRFRqtpNEGTLFYGLVQDGNDmwDATFFC 430
Cdd:pfam13632   1 WILLLDADtVLPPDCLLGIA--NEMASPEVAIIQGPILPMnVGNYLEELAALFF---ADDHGKSIPVRMALG--RVLPFV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  431 GSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNpll 510
Cdd:pfam13632  74 GSGAFLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRL--- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 727182765  511 gkgLKLAQRLCYANAMLHflsgiprliFLTAPLAFLLLHAYIIFAPALAIALYV 564
Cdd:pfam13632 151 ---LGYLGTLLWSGLPLA---------LLLLLLFSISSLALVLLLLALLAGLLL 192
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
271-501 8.78e-15

CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, Glucan Biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of glucan.


Pssm-ID: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 74.98  E-value: 8.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEdLGVVkPTIYAALG-IDWPKEKVNIYILDDGNRPEFRAFAAEVGVKYIAR-----PTHEHAKAGNINN 344
Cdd:cd06427    1 PVYTILVPLYKE-AEVL-PQLIASLSaLDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRvvvvpPSQPRTKPKACNY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 345 ALKQATGEFVAIFDCDHVPTRsfLQLTMGW--FFK-DKKLAMLQTPHHFFSPDpfeRNLgRFRQTPNEGTLFYGLVQDGN 421
Cdd:cd06427   79 ALAFARGEYVVIYDAEDAPDP--DQLKKAVaaFARlDDKLACVQAPLNYYNAR---ENW-LTRMFALEYAAWFDYLLPGL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 422 DMWDATF-FCGSCAILRRSALDEIGGIAVETVTEDAHTSLRLHRRGHTSAYIRIPQAAGlATESLSAHIGQRIRWARGMV 500
Cdd:cd06427  153 ARLGLPIpLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLEE-ANNALGNWIRQRSRWIKGYM 231

                 .
gi 727182765 501 Q 501
Cdd:cd06427  232 Q 232
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
271-498 4.48e-14

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 72.40  E-value: 4.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  271 PTIDLMVPTYNEDlGVVKPTIYAALGIDWPKekVNIYILDDGNRPEFRAFAAEVGVKY------IARPTHE---HAKAGN 341
Cdd:pfam13641   2 PDVSVVVPAFNED-SVLGRVLEAILAQPYPP--VEVVVVVNPSDAETLDVAEEIAARFpdvrlrVIRNARLlgpTGKSRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  342 INNALKQATGEFVAIFDCDHVPTRSFLQLTMGWFfKDKKLAMLQTPhhffspdPFERNLGRFRQTPneGTLFYGLVQ-DG 420
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-DSPKVGAVGTP-------VFSLNRSTMLSAL--GALEFALRHlRM 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  421 NDMWDA---TFFCGSCAILRRSALDEIGGIAVE-TVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWA 496
Cdd:pfam13641 149 MSLRLAlgvLPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWV 228

                  ..
gi 727182765  497 RG 498
Cdd:pfam13641 229 YG 230
PLN02915 PLN02915
cellulose synthase A [UDP-forming], catalytic subunit
443-651 1.64e-11

cellulose synthase A [UDP-forming], catalytic subunit


Pssm-ID: 215494 [Multi-domain]  Cd Length: 1044  Bit Score: 68.42  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  443 EIGGIaVETVTEDAHTSLRLHRRGHTSAYI--RIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDN-PL---LGKGLKL 516
Cdd:PLN02915  732 EIGWI-YGSVTEDILTGFKMHCRGWKSVYCmpKRPAFKGSAPINLSDRLHQVLRWALGSVEIFMSRHcPLwyaYGGKLKW 810
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  517 AQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----FAPALAIALYVlpHMIHASLTNSRIQGKYRHSFW-SEI 590
Cdd:PLN02915  811 LERLAYINTIVYPFTSIPLLAYCTIPAVCLLTGKFIIptlnnLASIWFLALFL--SIIATSVLELRWSGVSIEDLWrNEQ 888
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727182765  591 YetvlaWYIArPTTVALFNPHKG----------KFNVTAKGGLVEEEH------VDW-VITRPYMFLVVLNLAGLAFG 651
Cdd:PLN02915  889 F-----WVIG-GVSAHLFAVFQGllkvlggvdtNFTVTSKAADDEADEfgelylFKWtTLLIPPTTLIILNMVGVVAG 960
Cellulose_synt pfam03552
Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose ...
442-553 5.98e-11

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


Pssm-ID: 460970 [Multi-domain]  Cd Length: 715  Bit Score: 66.32  E-value: 5.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  442 DEIGGIaVETVTEDAHTSLRLHRRGHTSAYIRIPQAA--GLATESLSAHIGQRIRWARGMVQIF-RLDNPLL-GKGLKLA 517
Cdd:pfam03552 411 KEIGWI-YGSVTEDILTGFRMHCRGWRSIYCMPKRDAfkGSAPINLSDRLHQVLRWALGSVEIFfSRHCPIWyGGRLKFL 489
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 727182765  518 QRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII 553
Cdd:pfam03552 490 QRFAYINVGIYPFTSIPLLAYCFLPAICLFTGKFIV 525
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
247-501 3.30e-10

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 61.44  E-value: 3.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 247 LGY--FQTIWPLNRQPVPLPEDSATWPTIDLMVPTYNEDlGVVKPTIYAALGIDWPKEKVNIYILDDG---NRPEFRAFA 321
Cdd:cd06439    3 FGYplLLKLLARLRPKPPSLPDPAYLPTVTIIIPAYNEE-AVIEAKLENLLALDYPRDRLEIIVVSDGstdGTAEIAREY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 322 AEVGVKYIARPTHeHAKAGNINNALKQATGEFVAIFDCDHVPTRSFLQLTMGWfFKDKKLAMLQTPHHFFSPDPFERNLG 401
Cdd:cd06439   82 ADKGVKLLRFPER-RGKAAALNRALALATGEIVVFTDANALLDPDALRLLVRH-FADPSVGAVSGELVIVDGGGSGSGEG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 402 RFRQtpnegtlFYGLVQDGNDMWDATF-FCGSCAILRRSAldeIGGIAVETVTEDAHTSLRLHRRGHTSAYirIPQAAGL 480
Cdd:cd06439  160 LYWK-------YENWLKRAESRLGSTVgANGAIYAIRREL---FRPLPADTINDDFVLPLRIARQGYRVVY--EPDAVAY 227
                        250       260
                 ....*....|....*....|...
gi 727182765 481 --ATESLSAHIGQRIRWARGMVQ 501
Cdd:cd06439  228 eeVAEDGSEEFRRRVRIAAGNLQ 250
PLN02189 PLN02189
cellulose synthase
451-564 6.41e-10

cellulose synthase


Pssm-ID: 215121 [Multi-domain]  Cd Length: 1040  Bit Score: 63.11  E-value: 6.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  451 TVTEDAHTSLRLHRRGHTSAYIRIPQAA--GLATESLSAHIGQRIRWARGMVQI-FRLDNPLL----GKGLKLAQRLCYA 523
Cdd:PLN02189  736 SITEDILTGFKMHCRGWRSIYCMPKRAAfkGSAPINLSDRLNQVLRWALGSVEIfFSRHSPLLygykGGNLKWLERFAYV 815
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 727182765  524 NAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----FAPALAIALYV 564
Cdd:PLN02189  816 NTTIYPFTSLPLLAYCTLPAICLLTGKFIMppistFASLFFIALFM 861
PLN02638 PLN02638
cellulose synthase A (UDP-forming), catalytic subunit
443-564 6.72e-10

cellulose synthase A (UDP-forming), catalytic subunit


Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 63.02  E-value: 6.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  443 EIGGIaVETVTEDAHTSLRLHRRGHTSAYI--RIPQAAGLATESLSAHIGQRIRWARGMVQI-FRLDNPL---LGKGLKL 516
Cdd:PLN02638  768 EIGWI-YGSVTEDILTGFKMHARGWRSIYCmpKRPAFKGSAPINLSDRLNQVLRWALGSVEIlFSRHCPIwygYGGRLKW 846
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 727182765  517 AQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----FAPALAIALYV 564
Cdd:PLN02638  847 LERFAYVNTTIYPITSIPLLLYCTLPAVCLLTGKFIIpqisnIASIWFISLFL 899
PLN02195 PLN02195
cellulose synthase A
443-670 1.01e-09

cellulose synthase A


Pssm-ID: 215124 [Multi-domain]  Cd Length: 977  Bit Score: 62.30  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 443 EIGGIaVETVTEDAHTSLRLHRRGHTSAY---IRiPQAAGLATESLSAHIGQRIRWARGMVQIFRLDN-PLL----GKGL 514
Cdd:PLN02195 664 EIGWI-YGSVTEDILTGFKMHCRGWRSIYcmpVR-PAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHcPLWygygGGRL 741
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 515 KLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----FAPALAIALYVlpHMIHASLTNSRIQGKYRHSFW-S 588
Cdd:PLN02195 742 KWLQRLAYINTIVYPFTSLPLIAYCTLPAICLLTGKFIIptlsnLASMLFLGLFI--SIILTSVLELRWSGVSIEDLWrN 819
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 589 EIYetvlaWYIArPTTVALFNPHKG----------KFNVTAK----GGLVEEEHVDW-VITRPYMFLVVLNLAGLAFG-- 651
Cdd:PLN02195 820 EQF-----WVIG-GVSAHLFAVFQGflkmlagldtNFTVTAKaaddTEFGELYMVKWtTLLIPPTSLLIINLVGVVAGfs 893
                        250       260
                 ....*....|....*....|....*..
gi 727182765 652 --------AWRLAYGPTDEVMTVIISL 670
Cdd:PLN02195 894 dalnkgyeAWGPLFGKVFFAFWVILHL 920
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
277-403 1.05e-09

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 57.90  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 277 VPTYNEDlGVVKPTIYAALGIDWPKekVNIYILDDGNRPEFRAFAAEVGVKYIARPTHEHA----KAGNINNALKQATGE 352
Cdd:cd00761    3 IPAYNEE-PYLERCLESLLAQTYPN--FEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEenqgLAAARNAGLKAARGE 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 727182765 353 FVAIFDCDHVPTRSFLQLTMGWFFKDKKLAMLQTPH-HFFSPDPFERNLGRF 403
Cdd:cd00761   80 YILFLDADDLLLPDWLERLVAELLADPEADAVGGPGnLLFRRELLEEIGGFD 131
PLN02400 PLN02400
cellulose synthase
443-553 1.83e-09

cellulose synthase


Pssm-ID: 215224 [Multi-domain]  Cd Length: 1085  Bit Score: 61.53  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  443 EIGGIaVETVTEDAHTSLRLHRRGHTSAYIRIPQAA--GLATESLSAHIGQRIRWARGMVQIFRLDNPLLGKG----LKL 516
Cdd:PLN02400  773 EIGWI-YGSVTEDILTGFKMHARGWISIYCMPPRPAfkGSAPINLSDRLNQVLRWALGSIEILLSRHCPIWYGyngrLKL 851
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 727182765  517 AQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII 553
Cdd:PLN02400  852 LERLAYINTIVYPITSIPLLAYCVLPAFCLITNKFII 888
PLN02436 PLN02436
cellulose synthase A
443-564 1.85e-09

cellulose synthase A


Pssm-ID: 215239 [Multi-domain]  Cd Length: 1094  Bit Score: 61.81  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  443 EIGGIaVETVTEDAHTSLRLHRRGHTSAYI--RIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDN-PL---LGKGLKL 516
Cdd:PLN02436  784 EIGWI-YGSVTEDILTGFKMHCHGWRSVYCipKRPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHcPIwygYGGGLKW 862
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 727182765  517 AQRLCYANAMLHFLSGIPRLIFLTAPLAFLLLHAYII-----FAPALAIALYV 564
Cdd:PLN02436  863 LERFSYINSVVYPWTSIPLIVYCTLPAICLLTGKFIVpeisnYASILFMALFI 915
PLN02190 PLN02190
cellulose synthase-like protein
450-570 4.31e-09

cellulose synthase-like protein


Pssm-ID: 215122 [Multi-domain]  Cd Length: 756  Bit Score: 60.26  E-value: 4.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 450 ETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLA---TESLSAHIGQRiRWARGMVQI-FRLDNPLLG---KGLKLAQRLCY 522
Cdd:PLN02190 456 DSVAEDLNTSIGIHSRGWTSSYISPDPPAFLGsmpPGGPEAMVQQR-RWATGLIEVlFNKQSPLIGmfcRKIRFRQRLAY 534
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 727182765 523 AnAMLHFLSGIPRLIFLTAPlAFLLLHAYIIFAPALAIALYVLPHMIH 570
Cdd:PLN02190 535 L-YVFTCLRSIPELIYCLLP-AYCLLHNSALFPKGVYLGIIVTLVGMH 580
PilZ pfam07238
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ...
692-789 4.60e-08

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


Pssm-ID: 399904  Cd Length: 102  Bit Score: 51.73  E-value: 4.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  692 QVRQAHRVEIAMPAAIaRADGHLYPCTLRDYSDGGVGIEMRVADtLKEGD--KASLLLKRGQQEYSFPCVVTRAFGN--- 766
Cdd:pfam07238   1 QRRRFPRVPVSLPVTL-RDGGGEYKGRLIDISLGGAAIRLPDEP-LALGDrvELSLDLLDDGQELALPGRVVRIRPDedg 78
                          90       100
                  ....*....|....*....|....
gi 727182765  767 -KVGVRLVSLSTREHIDFIQCTFA 789
Cdd:pfam07238  79 aRVGVQFLDLDEEQRRLLVRLLFG 102
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
332-497 1.33e-07

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


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 52.29  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  332 PTHEHAKAGNINNALKQATGEFVAIFDCDHVPTRSFLQLTMGwFFKDKKLAMLQTPHHFFSPDPFERNLGRFRQTPNEGT 411
Cdd:pfam13506  12 PVGVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLA-PLADPKVGLVTSPPVGSDPKGLAAALEAAFFNTLAGV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  412 LFYGLVQdgndmwdATFFCGSCAILRRSALDEIGGIA--VETVTEDAHTSLRLHRRGHTSAYIRIP--QAAGLATESLSA 487
Cdd:pfam13506  91 LQAALSG-------IGFAVGMSMAFRRADLERIGGFEalADYLAEDYALGKLLRAAGLKVVLSPRPilQTSGPRRTSFRA 163
                         170
                  ....*....|
gi 727182765  488 HIGQRIRWAR 497
Cdd:pfam13506 164 FMARQLRWAR 173
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
297-498 1.43e-06

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 50.36  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 297 IDWPKEKVNIYILDDGNRPEFR---AFAAEVGVK--YIARPTHEHA--KAGNINNALKQATGEFVAIFDCDHVPTRSFLQ 369
Cdd:cd04192   22 LDYPKEKFEVILVDDHSTDGTVqilEFAAAKPNFqlKILNNSRVSIsgKKNALTTAIKAAKGDWIVTTDADCVVPSNWLL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 370 LTMGwFFKDKKLAMLQTPHHFFSPDPFernLGRFRQTPNEGTLFYGLVQDGndmWDATFFCGSCAI-LRRSALDEIGGIA 448
Cdd:cd04192  102 TFVA-FIQKEQIGLVAGPVIYFKGKSL---LAKFQRLDWLSLLGLIAGSFG---LGKPFMCNGANMaYRKEAFFEVGGFE 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 727182765 449 --VETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLAT---ESLSAHIGQRIRWARG 498
Cdd:cd04192  175 gnDHIASGDDELLLAKVASKYPKVAYLKNPEALVTTqpvTSWKELLNQRKRWASK 229
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
271-479 3.79e-06

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 48.54  E-value: 3.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEDlGVVKPTIYAALGIDWPKekVNIYILDDGNRPEFRAFAAEVG-----VKYIARPTHEHaKAGNINNA 345
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPD--FEIIVVDDGSTDGTAEILRELAakdprIRVIRLERNRG-KGAARNAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 346 LKQATGEFVAIFDCDHVPTRSFLQLTMGwffkdkklAMLQTPHHFFSPDPFERNLGR-FRQTPNEGTLFYGLVQDGNDMw 424
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVA--------ALEEGPADLVYGSRLIREGESdLRRLGSRLFNLVRLLTNLPDS- 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 727182765 425 datffCGSCAILRRSALDEIGgiAVETVTEDAHTsLRLHRRGHTSAYIRIPQAAG 479
Cdd:COG0463  149 -----TSGFRLFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVPVRYRAG 195
PLN02248 PLN02248
cellulose synthase-like protein
452-539 1.99e-05

cellulose synthase-like protein


Pssm-ID: 215138 [Multi-domain]  Cd Length: 1135  Bit Score: 48.49  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  452 VTEDAHTSLRLHRRGHTSAYIRIPQAA--GLATESLSAHIGQRIRWARGMVQIF--RlDNPLLG-KGLKLAQRLCYAN-A 525
Cdd:PLN02248  835 VTEDVVTGYRMHNRGWRSVYCVTKRDAfrGTAPINLTDRLHQVLRWATGSVEIFfsR-NNALLAsRRLKFLQRIAYLNvG 913
                          90
                  ....*....|....
gi 727182765  526 MLHFLSgiprlIFL 539
Cdd:PLN02248  914 IYPFTS-----IFL 922
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
431-497 5.36e-05

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


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 44.90  E-value: 5.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727182765 431 GSCAILRRSALDEIGGIAV--ETVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAHIGQRIRWAR 497
Cdd:cd02520  126 GKSMALRREVLDAIGGFEAfaDYLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSR 194
YcgR COG5581
Cyclic di-GMP-binding flagellar brake protein FlgZ/YcgR, contains PilZNR(YcgR) and PilZ ...
688-779 8.83e-04

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


Pssm-ID: 444320 [Multi-domain]  Cd Length: 205  Bit Score: 41.52  E-value: 8.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 688 VEAKQVRQAHRVEIAMPAAI----ARADGHLYPCTLRDYSDGGVGIEMRVADTLKEGDKASLLLK-RGQQEYSFPCVVTR 762
Cdd:COG5581   83 IERIQRREYFRVPVPLDVPVrclrPDGEGEPLEGRLLDISGGGLALVLPEPPPLEVGDILELRLDlPDEGEIVVDAEVRR 162
                         90       100
                 ....*....|....*....|....
gi 727182765 763 AF-------GNKVGVRLVSLSTRE 779
Cdd:COG5581  163 VVevelgkgKYRLGCEFVDLSEAD 186
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
271-360 9.44e-04

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 41.42  E-value: 9.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 271 PTIDLMVPTYNEDLGVVKPTI-------YAalgiDWpkekvNIYILDDG-NRPEFRAFAAEVG-----VKYIARPTHEHA 337
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIesvraqtYP----NW-----ELCIADDAsTDPEVKRVLKKYAaqdprIKVVFREENGGI 71
                         90       100
                 ....*....|....*....|...
gi 727182765 338 kAGNINNALKQATGEFVAIFDCD 360
Cdd:cd04184   72 -SAATNSALELATGEFVALLDHD 93
PLN02893 PLN02893
Cellulose synthase-like protein
451-554 1.79e-03

Cellulose synthase-like protein


Pssm-ID: 215483 [Multi-domain]  Cd Length: 734  Bit Score: 42.00  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 451 TVTEDAHTSLRLHRRGHTSAYIRIPQAAGLATESLSAH--IGQRIRWARGMVQI-FRLDNPLL--GKGLKLAQRLCYANA 525
Cdd:PLN02893 444 SLVEDYYTGYRLQCEGWKSIFCNPKRPAFLGDSPINLHdvLNQQKRWSVGLLEVaFSKYSPITfgVKSIGLLMGLGYAHY 523
                         90       100       110
                 ....*....|....*....|....*....|...
gi 727182765 526 MLHFLSGIPRLIFltaplAFL----LLHAYIIF 554
Cdd:PLN02893 524 AFWPIWSIPITIY-----AFLpqlaLLNGVSIF 551
PLN02638 PLN02638
cellulose synthase A (UDP-forming), catalytic subunit
189-312 2.24e-03

cellulose synthase A (UDP-forming), catalytic subunit


Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 41.83  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765  189 RRVP---GRL-PALMLIVLSLTVSCRYLWWRYTATLnwddPLSLVCGLLLLVAETYAWVVLVLGYFQTIWPLNRQP---- 260
Cdd:PLN02638  259 RKVSipsSRInPYRMVIVLRLVILCIFLHYRITNPV----RNAYALWLISVICEIWFALSWILDQFPKWLPVNRETyldr 334
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 727182765  261 VPLPEDSATWPT----IDLMVPTYN---EDLGVVKPTIYAALGIDWPKEKVNIYILDDG 312
Cdd:PLN02638  335 LALRYDREGEPSqlaaVDIFVSTVDplkEPPLVTANTVLSILAVDYPVDKVSCYVSDDG 393
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
277-360 4.30e-03

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 39.09  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727182765 277 VPTYNEDlGVVKPTIYAALGIDWPKEKVNIYILDDGNRPEFRAFAAEVGVKYIARPTHEHA----KAGNINNALKQATGE 352
Cdd:cd04179    3 IPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSrnfgKGAAVRAGFKAARGD 81

                 ....*...
gi 727182765 353 FVAIFDCD 360
Cdd:cd04179   82 IVVTMDAD 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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