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Conserved domains on  [gi|1073282073|gb|OEX05879|]
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capsular biosynthesis protein [Campylobacter jejuni]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TagB COG1887
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ...
471-815 1.99e-48

CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


:

Pssm-ID: 441491  Cd Length: 369  Bit Score: 175.95  E-value: 1.99e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 471 ISYEIKKLKKRRAKNKSLWLFADMPFR-ADDNAEHLYRYVMKNYPEKNIAFVLRKNShdyKRLKKEGFKLVDPKSFKFKY 549
Cdd:COG1887     6 LRRLYYRLSRLLPVKKNIILFESRNGRsYSDNPKALFEYLRKNHPDYEVVWVVDDDS---KRLPKEGVKVVKRGSLKYLY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 550 LVFKADKLISSHieRYFFEALGENTLKTKdFVFLQHG-----ITQNDLSSWLNQ-----RKIDLFITGMqDEYDSIAGDf 619
Cdd:COG1887    83 ALARAKYLVSNH--YFPFPSYFRKRKGQK-YVQLWHGtplkkIGLDDPPRYLKRvlreyRNWDYLLSSS-EESTEIFRR- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 620 nRYKFTPKEVKLTGFPRWDALLKNNQI--------------NTKQIIIMPTWREyivgsyskklmkRRFNPKFYESEYFY 685
Cdd:COG1887   158 -AFGYPEGEVLETGYPRNDVLFDADREelreelrerlgipeDKKVILYAPTWRD------------DEDNFDDYLDLDLE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 686 RWDSFLHSkklqelhekyDYKIVFSPHPQIRPYLEGFNLPNYIIIPSvEMSMQKLFCESSLMITDYSSVAFEMAVLKKPV 765
Cdd:COG1887   225 RLAELLGD----------DYVLLVRLHPFVKDSLDEKYSDRIIDVSD-YPDINDLLLASDVLITDYSSVMFDFALLDRPI 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1073282073 766 IYYQFDKDELFAKHtytQGYFDYNKDGFGIVVLDIDNLLYELKMKLQNHS 815
Cdd:COG1887   294 IFYAYDLEEYRDER---GFYFDYEEDAPGPVVTTFEELIDAIEDILENGD 340
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
41-197 3.91e-24

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: 99.50  E-value: 3.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  41 VIVSAvYNVEKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKENGGQASARNLGLKYL 120
Cdd:cd00761     1 VIIPA-YNEEPYLERCLESLLAQTYP---NFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1073282073 121 KENdlnipWVTFTDPDDFLDRDYFYEVDSFLKNQNNIAMVATN-IIFYrekRKILYKDTHALNFKFKKHKSVYDNIKL 197
Cdd:cd00761    77 RGE-----YILFLDADDLLLPDWLERLVAELLADPEADAVGGPgNLLF---RRELLEEIGGFDEALLSGEEDDDFLLR 146
 
Name Accession Description Interval E-value
TagB COG1887
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ...
471-815 1.99e-48

CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 441491  Cd Length: 369  Bit Score: 175.95  E-value: 1.99e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 471 ISYEIKKLKKRRAKNKSLWLFADMPFR-ADDNAEHLYRYVMKNYPEKNIAFVLRKNShdyKRLKKEGFKLVDPKSFKFKY 549
Cdd:COG1887     6 LRRLYYRLSRLLPVKKNIILFESRNGRsYSDNPKALFEYLRKNHPDYEVVWVVDDDS---KRLPKEGVKVVKRGSLKYLY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 550 LVFKADKLISSHieRYFFEALGENTLKTKdFVFLQHG-----ITQNDLSSWLNQ-----RKIDLFITGMqDEYDSIAGDf 619
Cdd:COG1887    83 ALARAKYLVSNH--YFPFPSYFRKRKGQK-YVQLWHGtplkkIGLDDPPRYLKRvlreyRNWDYLLSSS-EESTEIFRR- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 620 nRYKFTPKEVKLTGFPRWDALLKNNQI--------------NTKQIIIMPTWREyivgsyskklmkRRFNPKFYESEYFY 685
Cdd:COG1887   158 -AFGYPEGEVLETGYPRNDVLFDADREelreelrerlgipeDKKVILYAPTWRD------------DEDNFDDYLDLDLE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 686 RWDSFLHSkklqelhekyDYKIVFSPHPQIRPYLEGFNLPNYIIIPSvEMSMQKLFCESSLMITDYSSVAFEMAVLKKPV 765
Cdd:COG1887   225 RLAELLGD----------DYVLLVRLHPFVKDSLDEKYSDRIIDVSD-YPDINDLLLASDVLITDYSSVMFDFALLDRPI 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1073282073 766 IYYQFDKDELFAKHtytQGYFDYNKDGFGIVVLDIDNLLYELKMKLQNHS 815
Cdd:COG1887   294 IFYAYDLEEYRDER---GFYFDYEEDAPGPVVTTFEELIDAIEDILENGD 340
Glyphos_transf pfam04464
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
484-808 1.07e-33

CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid.


Pssm-ID: 398259  Cd Length: 360  Bit Score: 133.24  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 484 KNKSLWLFADMPFRADDNAEHLYRYVMKNYPEKNIAFVLRKnshDYKRLKKEGFKLVDPKSFKFKYLVFKADKLISShie 563
Cdd:pfam04464   3 DPNLVLFESFWGRGYSDNPKAIYEYLRELAPGYRIVWVVKK---DHSARLPKGVPVVVRNSFRYLYLLLRAKYLVSN--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 564 rYFFeALGENTLKTKDFVFLQHG--------------ITQNDLSSWLNQRKIDLFITGmQDEYDSI-AGDFNRYKftpKE 628
Cdd:pfam04464  77 -SNF-PLYVVKRKNQVYLQTWHGtplkhmgldilevpMANTGQNFLRNVDRWDYLISA-NPHSTNIfARAFNIDK---ER 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 629 VKLTGFPRWDALLKNN-------------QINTKQIIIMPTWREYIVGSyskklmkrrfnpkfyesEYFYRWDSFLHSKK 695
Cdd:pfam04464 151 ILETGYPRNDVLFNANnedvqrirerlgiPLGKKVILYAPTWRDDERGS-----------------IGSYRFELLIDLER 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 696 LQELhEKYDYKIVFSPHPQIRPYLEGFNLPNYIIIPSVEMSMQKLFCESSLMITDYSSVAFEMAVLKKPVIYYQFDKDEl 775
Cdd:pfam04464 214 LAFA-LGNDYVILLKMHPLIQNNIDIFESSGYVVDVSDYEDVEDLLLASDILITDYSSVMFDYAVLDRPIIFYAYDLET- 291
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1073282073 776 fakHTYTQG-YFDYNKDGFGIVVLDIDNLLYELK 808
Cdd:pfam04464 292 ---YSATRGfYLDYESEAPGPVVETFDELIDALK 322
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
41-197 3.91e-24

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: 99.50  E-value: 3.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  41 VIVSAvYNVEKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKENGGQASARNLGLKYL 120
Cdd:cd00761     1 VIIPA-YNEEPYLERCLESLLAQTYP---NFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1073282073 121 KENdlnipWVTFTDPDDFLDRDYFYEVDSFLKNQNNIAMVATN-IIFYrekRKILYKDTHALNFKFKKHKSVYDNIKL 197
Cdd:cd00761    77 RGE-----YILFLDADDLLLPDWLERLVAELLADPEADAVGGPgNLLF---RRELLEEIGGFDEALLSGEEDDDFLLR 146
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
39-183 1.75e-20

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 90.53  E-value: 1.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  39 KYVIVSAVYNVEKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKENGGQASARNLGLK 118
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYP---DFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1073282073 119 YLKEndlniPWVTFTDPDDFLDRDYFYEVDSFLKnQNNIAMVATNIIFYREKRKILYKDTHALNF 183
Cdd:COG0463    80 AARG-----DYIAFLDADDQLDPEKLEELVAALE-EGPADLVYGSRLIREGESDLRRLGSRLFNL 138
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
42-187 2.67e-20

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: 88.61  E-value: 2.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  42 IVSAVYNVEKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKENGGQASARNLGLKYLK 121
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1073282073 122 EndlniPWVTFTDPDDFLDRDYFYE-VDSFLKNQNNIAMVATNIIFYREKRKILYKDTHALNFKFKK 187
Cdd:pfam00535  79 G-----DYIAFLDADDEVPPDWLEKlVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFL 140
PRK10073 PRK10073
putative glycosyl transferase; Provisional
38-177 2.30e-19

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 90.11  E-value: 2.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  38 NKYVIVSAVYNVEKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNSANIIKKYQKKYPkNIIYLYKENGGQASARNLGL 117
Cdd:PRK10073    6 PKLSIIIPLYNAGKDFRAFMESLIAQTWT---ALEIIIVNDGSTDNSVEIAKHYAENYP-HVRLLHQANAGVSVARNTGL 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1073282073 118 -----KYlkendlnipwVTFTDPDDFLDRDyFYE--VDSFLKNQNNIAMVATNIIFY--REKRKILYKD 177
Cdd:PRK10073   82 avatgKY----------VAFPDADDVVYPT-MYEtlMTMALEDDLDVAQCNADWCFRdtGETWQSIPSD 139
surf_polysacc TIGR04396
surface carbohydrate biosynthesis protein; This model describes an uncharacterized homology ...
532-779 4.58e-05

surface carbohydrate biosynthesis protein; This model describes an uncharacterized homology region found broadly in proteins of surface carbohydrate biosynthesis regions. This family shows distant homology to regions of family TIGR04326, of spore coat polysaccharide biosynthesis protein SpsB from Bacillus subtilis, etc. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 275189  Cd Length: 321  Bit Score: 46.50  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 532 LKKEGFK--LVDPKSFKFKYLVFKADKLISSHIERY---FFEALGENTLK-----------TKDFVFLQHGITQNDLSSw 595
Cdd:TIGR04396  23 AAKRGYRvvLGPLYLIRSLLPYLPPGIYLLKHLRPGnkeLFERLKKLGHKvgvldeeglvyPNPDLYADFRIGAGVLDL- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 596 lnqrkIDLFITGMQDEYDSIAgdfNRYKFTPKEVKLTGFPRWDALLKNNQ---------INTK--QIIIMPT-------- 656
Cdd:TIGR04396 102 -----VDAFFAWGEEQADAIE---KAYPLKADKIVITGNPRFDLLRPKYRefysnearaLKKKygDFILINTnftqanpf 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 657 -WREYIVgsYSKKLMKRRFNPKFYESEYFYR---WDSFLHSkkLQELHEKY-DYKIVFSPHP--QIRPYLEGF-NLPNYI 728
Cdd:TIGR04396 174 dGGLGFL--ERLKKGGKGEDEKFFEKLIEYIrkiFESFIDL--LKELSKAFpDVNIVLRPHPseNLEPYRKLFsGYSNVH 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1073282073 729 IIPsvEMSMQKLFCESSLMITDYSSVAFEMAVLKKPVIYYQFDKDELFAKH 779
Cdd:TIGR04396 250 VIH--EGNVIPWILASDLLIHNGCTTAIEAYMLGKPVISYRPINSERYESE 298
GTB_UDP-GlcNAc_2-Epimerase cd03786
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ...
626-766 2.68e-04

UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340819 [Multi-domain]  Cd Length: 365  Bit Score: 44.12  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 626 PKEVKLTGFPRWDALLKNNQINTKQIIIMPTW---REYIVGSYskklmKRRFNpkFYESEYFyrwDSFLHSkkLQELHEK 702
Cdd:cd03786   163 PERIFVTGNTVIDALLSAALRIRDELVLSKLGlleKKYILVTL-----HRREN--VDSGERL---EELLEA--LEELAEK 230
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1073282073 703 YDYKIVFSPHPQIRPYLEGFNL------PNYIIIPSV-EMSMQKLFCESSLMITDYSSVAFEMAVLKKPVI 766
Cdd:cd03786   231 YDLIVVYPNHPRTRPRIREVGLkflgglPNIRLIDPLgYLDLVLLKKRAKLVLTDSGGIQEEASFLGKPVL 301
 
Name Accession Description Interval E-value
TagB COG1887
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ...
471-815 1.99e-48

CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 441491  Cd Length: 369  Bit Score: 175.95  E-value: 1.99e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 471 ISYEIKKLKKRRAKNKSLWLFADMPFR-ADDNAEHLYRYVMKNYPEKNIAFVLRKNShdyKRLKKEGFKLVDPKSFKFKY 549
Cdd:COG1887     6 LRRLYYRLSRLLPVKKNIILFESRNGRsYSDNPKALFEYLRKNHPDYEVVWVVDDDS---KRLPKEGVKVVKRGSLKYLY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 550 LVFKADKLISSHieRYFFEALGENTLKTKdFVFLQHG-----ITQNDLSSWLNQ-----RKIDLFITGMqDEYDSIAGDf 619
Cdd:COG1887    83 ALARAKYLVSNH--YFPFPSYFRKRKGQK-YVQLWHGtplkkIGLDDPPRYLKRvlreyRNWDYLLSSS-EESTEIFRR- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 620 nRYKFTPKEVKLTGFPRWDALLKNNQI--------------NTKQIIIMPTWREyivgsyskklmkRRFNPKFYESEYFY 685
Cdd:COG1887   158 -AFGYPEGEVLETGYPRNDVLFDADREelreelrerlgipeDKKVILYAPTWRD------------DEDNFDDYLDLDLE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 686 RWDSFLHSkklqelhekyDYKIVFSPHPQIRPYLEGFNLPNYIIIPSvEMSMQKLFCESSLMITDYSSVAFEMAVLKKPV 765
Cdd:COG1887   225 RLAELLGD----------DYVLLVRLHPFVKDSLDEKYSDRIIDVSD-YPDINDLLLASDVLITDYSSVMFDFALLDRPI 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1073282073 766 IYYQFDKDELFAKHtytQGYFDYNKDGFGIVVLDIDNLLYELKMKLQNHS 815
Cdd:COG1887   294 IFYAYDLEEYRDER---GFYFDYEEDAPGPVVTTFEELIDAIEDILENGD 340
Glyphos_transf pfam04464
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
484-808 1.07e-33

CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid.


Pssm-ID: 398259  Cd Length: 360  Bit Score: 133.24  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 484 KNKSLWLFADMPFRADDNAEHLYRYVMKNYPEKNIAFVLRKnshDYKRLKKEGFKLVDPKSFKFKYLVFKADKLISShie 563
Cdd:pfam04464   3 DPNLVLFESFWGRGYSDNPKAIYEYLRELAPGYRIVWVVKK---DHSARLPKGVPVVVRNSFRYLYLLLRAKYLVSN--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 564 rYFFeALGENTLKTKDFVFLQHG--------------ITQNDLSSWLNQRKIDLFITGmQDEYDSI-AGDFNRYKftpKE 628
Cdd:pfam04464  77 -SNF-PLYVVKRKNQVYLQTWHGtplkhmgldilevpMANTGQNFLRNVDRWDYLISA-NPHSTNIfARAFNIDK---ER 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 629 VKLTGFPRWDALLKNN-------------QINTKQIIIMPTWREYIVGSyskklmkrrfnpkfyesEYFYRWDSFLHSKK 695
Cdd:pfam04464 151 ILETGYPRNDVLFNANnedvqrirerlgiPLGKKVILYAPTWRDDERGS-----------------IGSYRFELLIDLER 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 696 LQELhEKYDYKIVFSPHPQIRPYLEGFNLPNYIIIPSVEMSMQKLFCESSLMITDYSSVAFEMAVLKKPVIYYQFDKDEl 775
Cdd:pfam04464 214 LAFA-LGNDYVILLKMHPLIQNNIDIFESSGYVVDVSDYEDVEDLLLASDILITDYSSVMFDYAVLDRPIIFYAYDLET- 291
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1073282073 776 fakHTYTQG-YFDYNKDGFGIVVLDIDNLLYELK 808
Cdd:pfam04464 292 ---YSATRGfYLDYESEAPGPVVETFDELIDALK 322
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
41-197 3.91e-24

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: 99.50  E-value: 3.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  41 VIVSAvYNVEKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKENGGQASARNLGLKYL 120
Cdd:cd00761     1 VIIPA-YNEEPYLERCLESLLAQTYP---NFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1073282073 121 KENdlnipWVTFTDPDDFLDRDYFYEVDSFLKNQNNIAMVATN-IIFYrekRKILYKDTHALNFKFKKHKSVYDNIKL 197
Cdd:cd00761    77 RGE-----YILFLDADDLLLPDWLERLVAELLADPEADAVGGPgNLLF---RRELLEEIGGFDEALLSGEEDDDFLLR 146
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
39-183 1.75e-20

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 90.53  E-value: 1.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  39 KYVIVSAVYNVEKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKENGGQASARNLGLK 118
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYP---DFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1073282073 119 YLKEndlniPWVTFTDPDDFLDRDYFYEVDSFLKnQNNIAMVATNIIFYREKRKILYKDTHALNF 183
Cdd:COG0463    80 AARG-----DYIAFLDADDQLDPEKLEELVAALE-EGPADLVYGSRLIREGESDLRRLGSRLFNL 138
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
42-187 2.67e-20

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: 88.61  E-value: 2.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  42 IVSAVYNVEKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKENGGQASARNLGLKYLK 121
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1073282073 122 EndlniPWVTFTDPDDFLDRDYFYE-VDSFLKNQNNIAMVATNIIFYREKRKILYKDTHALNFKFKK 187
Cdd:pfam00535  79 G-----DYIAFLDADDEVPPDWLEKlVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFL 140
PRK10073 PRK10073
putative glycosyl transferase; Provisional
38-177 2.30e-19

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 90.11  E-value: 2.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  38 NKYVIVSAVYNVEKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNSANIIKKYQKKYPkNIIYLYKENGGQASARNLGL 117
Cdd:PRK10073    6 PKLSIIIPLYNAGKDFRAFMESLIAQTWT---ALEIIIVNDGSTDNSVEIAKHYAENYP-HVRLLHQANAGVSVARNTGL 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1073282073 118 -----KYlkendlnipwVTFTDPDDFLDRDyFYE--VDSFLKNQNNIAMVATNIIFY--REKRKILYKD 177
Cdd:PRK10073   82 avatgKY----------VAFPDADDVVYPT-MYEtlMTMALEDDLDVAQCNADWCFRdtGETWQSIPSD 139
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
29-169 1.51e-17

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: 84.41  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  29 FKPKKYKAYNKYVIVSAVYNVEKYLDDFFKSIINQRLDfKNNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKENGG 108
Cdd:COG1215    20 RRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYP-KEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGG 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1073282073 109 QASARNLGLKYLKendlnIPWVTFTDPDDFLDRDYFYEVDSFLKNqNNIAMVATNIIFYRE 169
Cdd:COG1215    99 KAAALNAGLKAAR-----GDIVVFLDADTVLDPDWLRRLVAAFAD-PGVGASGANLAFRRE 153
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
42-276 3.33e-14

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 73.03  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  42 IVSAVYNVEKYLDDFFKSIINQRLDfKNNIHLICVDDGSTDNSANIIKKYQKKYPKnIIYLYKENGGQASARNLGLKYLK 121
Cdd:cd02525     4 IIIPVRNEEKYIEELLESLLNQSYP-KDLIEIIVVDGGSTDGTREIVQEYAAKDPR-IRLIDNPKRIQSAGLNIGIRNSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 122 ENdlnipWVTFTDPDDFLDRDYFYE-VDSFLKNQNNIAMVATNIIFYREKRKILykdTHALNFKFKKHKSVYdniKLNEN 200
Cdd:cd02525    82 GD-----IIIRVDAHAVYPKDYILElVEALKRTGADNVGGPMETIGESKFQKAI---AVAQSSPLGSGGSAY---RGGAV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 201 IQLSVASCFLKCdYLKDTF-----FDENLTLNfEDGKFiNIYLFKNlNLKSIFLKNARYFYRKRfdksSTLDKKNKNKFY 275
Cdd:cd02525   151 KIGYVDTVHHGA-YRREVFekvggFDESLVRN-EDAEL-NYRLRKA-GYKIWLSPDIRVYYYPR----STLKKLARQYFR 222

                  .
gi 1073282073 276 Y 276
Cdd:cd02525   223 Y 223
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
42-137 4.78e-13

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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 69.20  E-value: 4.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  42 IVSAVYNVEKYLDDFFKSIINQrldFKNNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKE-NGGqaSARN-LGLKY 119
Cdd:cd04196     2 VLMATYNGEKYLREQLDSILAQ---TYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGkNLG--VARNfESLLQ 76
                          90
                  ....*....|....*...
gi 1073282073 120 LKENDlnipWVTFTDPDD 137
Cdd:cd04196    77 AADGD----YVFFCDQDD 90
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
41-144 2.15e-12

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 66.94  E-value: 2.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  41 VIVSavYNVEKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNSANIIKKYQkkYPKNIIYLYKENGGQASARNLGLKYL 120
Cdd:COG1216     8 VIPT--YNRPELLRRCLESLLAQTYP---PFEVIVVDNGSTDGTAELLAALA--FPRVRVIRNPENLGFAAARNLGLRAA 80
                          90       100
                  ....*....|....*....|....
gi 1073282073 121 KendlnIPWVTFTDPDDFLDRDYF 144
Cdd:COG1216    81 G-----GDYLLFLDDDTVVEPDWL 99
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
41-176 1.81e-11

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: 63.79  E-value: 1.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  41 VIVSAvYNVEKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLY-KENGGQASARNLGLKY 119
Cdd:cd06423     1 IIVPA-YNEEAVIERTIESLLALDYP---KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRdKENGGKAGALNAGLRH 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1073282073 120 LKEndlniPWVTFTDPDDFLDRDYFYEVDSFLKNQNNIAMVATNIIFYREKRKILYK 176
Cdd:cd06423    77 AKG-----DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTR 128
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
42-136 9.54e-11

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: 61.82  E-value: 9.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  42 IVSAVYNVEKYLDDFFKSIInQRLDFKNNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKENGGQASARNLGLKYLK 121
Cdd:cd04179     1 VVIPAYNEEENIPELVERLL-AVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79
                          90
                  ....*....|....*
gi 1073282073 122 EndlniPWVTFTDPD 136
Cdd:cd04179    80 G-----DIVVTMDAD 89
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
42-160 5.23e-10

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: 59.91  E-value: 5.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  42 IVSAVYNV-EKYLDDFFKSIINQRLDfknNIHLICVDDGSTDNS-ANIIKKYQKKYPKNIIYLYKENGGQASARNLGLKy 119
Cdd:cd04184     5 IVMPVYNTpEKYLREAIESVRAQTYP---NWELCIADDASTDPEvKRVLKKYAAQDPRIKVVFREENGGISAATNSALE- 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1073282073 120 LKENDlnipWVTFTDPDDFLDRDYFYEVDSFLKNQNNIAMV 160
Cdd:cd04184    81 LATGE----FVALLDHDDELAPHALYEVVKALNEHPDADLI 117
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
42-161 6.86e-10

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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 58.72  E-value: 6.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  42 IVSAVYNVEKYLDDFFKSIINQRldfKNNIHLICVDDGSTDNSANIIKKYqkkYPKNIIYLYKENGGQASARNLGLKYLK 121
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQT---YPDFEVIVVDNASTDGSVELLREL---FPEVRLIRNGENLGFGAGNNQGIREAK 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1073282073 122 endlnIPWVTFTDPDDFLDRDYFYEVDSFLKNQNNIAMVA 161
Cdd:cd04186    75 -----GDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVG 109
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
42-224 7.64e-10

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 59.48  E-value: 7.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  42 IVSAVYNVEKYLDDFFKSIINQRLdfkNNIHLICVDDGSTDNSANIIKKYQKKypknIIYLYKEN-GGQASARNLGLKYL 120
Cdd:cd06433     2 IITPTYNQAETLEETIDSVLSQTY---PNIEYIVIDGGSTDGTVDIIKKYEDK----ITYWISEPdKGIYDAMNKGIALA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 121 K-EndlnipWVTFTDPDDFLDRDYFYEVDSFLKNQNNIAMVATNIIFYREKRKILYKdtHALNFKFKKHKSVYDNIklne 199
Cdd:cd06433    75 TgD------IIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGR--RRPPPFLDKFLLYGMPI---- 142
                         170       180
                  ....*....|....*....|....*.
gi 1073282073 200 NIQlsvaSCFLKCDYLKDT-FFDENL 224
Cdd:cd06433   143 CHQ----ATFFRRSLFEKYgGFDESY 164
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
18-142 3.58e-08

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: 55.28  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  18 LLISLQNFLKQFKPKKYKAYNKYVIVSAVYNVEKYLDDFFKSIINqrLDF-KNNIHLICVDDGSTDNSANIIKKYQKKyp 96
Cdd:cd06439     9 LKLLARLRPKPPSLPDPAYLPTVTIIIPAYNEEAVIEAKLENLLA--LDYpRDRLEIIVVSDGSTDGTAEIAREYADK-- 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1073282073  97 KNIIYLYKENGGQASARNLGLKYLKEnDLnipwVTFTDPDDFLDRD 142
Cdd:cd06439    85 GVKLLRFPERRGKAAALNRALALATG-EI----VVFTDANALLDPD 125
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
42-97 9.84e-08

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 52.86  E-value: 9.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1073282073  42 IVSAVYNVEKYLDDFFKSIINQRLDFKNNIHLICVDDGSTDNSANIIKKYQKKYPK 97
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPR 56
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
41-136 1.68e-07

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 52.57  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  41 VIVSAvYNVEKYLDDFFKSII---NQRLDFknNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYL-YKENGGQASARNLG 116
Cdd:cd04188     1 VVIPA-YNEEKRLPPTLEEAVeylEERPSF--SYEIIVVDDGSKDGTAEVARKLARKNPALIRVLtLPKNRGKGGAVRAG 77
                          90       100
                  ....*....|....*....|
gi 1073282073 117 LKYLKENdlnipWVTFTDPD 136
Cdd:cd04188    78 MLAARGD-----YILFADAD 92
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
42-116 4.66e-07

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 51.30  E-value: 4.66e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1073282073  42 IVSAVYNVEKYLDDFFKSIINQrlDFKNNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKENGGQASARNLG 116
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQ--DFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVG 73
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
41-143 2.55e-05

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 45.65  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  41 VIVSaVYNVEKYLDDFFKSIINQ-RLDFKnnihLICVDDGSTDNSANIIKKYQKKYPKNIIYLYKE-NGGQASA-RNLGL 117
Cdd:cd06420     1 LIIT-TYNRPEALELVLKSVLNQsILPFE----VIIADDGSTEETKELIEEFKSQFPIPIKHVWQEdEGFRKAKiRNKAI 75
                          90       100
                  ....*....|....*....|....*.
gi 1073282073 118 KYLKENdlnipWVTFTDPDDFLDRDY 143
Cdd:cd06420    76 AAAKGD-----YLIFIDGDCIPHPDF 96
surf_polysacc TIGR04396
surface carbohydrate biosynthesis protein; This model describes an uncharacterized homology ...
532-779 4.58e-05

surface carbohydrate biosynthesis protein; This model describes an uncharacterized homology region found broadly in proteins of surface carbohydrate biosynthesis regions. This family shows distant homology to regions of family TIGR04326, of spore coat polysaccharide biosynthesis protein SpsB from Bacillus subtilis, etc. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 275189  Cd Length: 321  Bit Score: 46.50  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 532 LKKEGFK--LVDPKSFKFKYLVFKADKLISSHIERY---FFEALGENTLK-----------TKDFVFLQHGITQNDLSSw 595
Cdd:TIGR04396  23 AAKRGYRvvLGPLYLIRSLLPYLPPGIYLLKHLRPGnkeLFERLKKLGHKvgvldeeglvyPNPDLYADFRIGAGVLDL- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 596 lnqrkIDLFITGMQDEYDSIAgdfNRYKFTPKEVKLTGFPRWDALLKNNQ---------INTK--QIIIMPT-------- 656
Cdd:TIGR04396 102 -----VDAFFAWGEEQADAIE---KAYPLKADKIVITGNPRFDLLRPKYRefysnearaLKKKygDFILINTnftqanpf 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 657 -WREYIVgsYSKKLMKRRFNPKFYESEYFYR---WDSFLHSkkLQELHEKY-DYKIVFSPHP--QIRPYLEGF-NLPNYI 728
Cdd:TIGR04396 174 dGGLGFL--ERLKKGGKGEDEKFFEKLIEYIrkiFESFIDL--LKELSKAFpDVNIVLRPHPseNLEPYRKLFsGYSNVH 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1073282073 729 IIPsvEMSMQKLFCESSLMITDYSSVAFEMAVLKKPVIYYQFDKDELFAKH 779
Cdd:TIGR04396 250 VIH--EGNVIPWILASDLLIHNGCTTAIEAYMLGKPVISYRPINSERYESE 298
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
45-153 2.67e-04

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 43.07  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  45 AVYNVEK--YLDDFFKSIINQRLdfkNNIHLICVDDGSTDNSAN-IIKKYQKKYPKNIIYLyKENGGQASARNLGLKYLK 121
Cdd:cd04195     5 SVYIKEKpeFLREALESILKQTL---PPDEVVLVKDGPVTQSLNeVLEEFKRKLPLKVVPL-EKNRGLGKALNEGLKHCT 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1073282073 122 ENdlnipWVTFTDPDDFLDRDYF-YEVDSFLKN 153
Cdd:cd04195    81 YD-----WVARMDTDDISLPDRFeKQLDFIEKN 108
GTB_UDP-GlcNAc_2-Epimerase cd03786
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ...
626-766 2.68e-04

UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340819 [Multi-domain]  Cd Length: 365  Bit Score: 44.12  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 626 PKEVKLTGFPRWDALLKNNQINTKQIIIMPTW---REYIVGSYskklmKRRFNpkFYESEYFyrwDSFLHSkkLQELHEK 702
Cdd:cd03786   163 PERIFVTGNTVIDALLSAALRIRDELVLSKLGlleKKYILVTL-----HRREN--VDSGERL---EELLEA--LEELAEK 230
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1073282073 703 YDYKIVFSPHPQIRPYLEGFNL------PNYIIIPSV-EMSMQKLFCESSLMITDYSSVAFEMAVLKKPVI 766
Cdd:cd03786   231 YDLIVVYPNHPRTRPRIREVGLkflgglPNIRLIDPLgYLDLVLLKKRAKLVLTDSGGIQEEASFLGKPVL 301
WecB COG0381
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
696-766 6.22e-04

UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440150  Cd Length: 366  Bit Score: 43.13  E-value: 6.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1073282073 696 LQELHEKYDYKIVFSPHPQIRPYLEGF--NLPNYIIIPSVE-MSMQKLFCESSLMITDYSSVAFEMAVLKKPVI 766
Cdd:COG0381   224 LRELAERYDLPVVFPVHPRTRKRLEEFlgGHPNIRLIEPLGyLDFLNLMKRAYLVLTDSGGIQEEAPSLGKPCL 297
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
74-286 9.66e-04

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 41.51  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  74 ICVDDGSTDNSANIIKKYQKKypkniIYLYKeNGGQASARNLGLKYLKendlnIPWVTFTDPDDFLDRDYFYEVDSFLKN 153
Cdd:cd02511    30 IVVDSGSTDRTVEIAKEYGAK-----VYQRW-WDGFGAQRNFALELAT-----NDWVLSLDADERLTPELADEILALLAT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 154 --QNNIAMVATNIIFYREKRKILYKDTHALNFkFKKHKSVYDNIKLNENIQLS-VASCFLKCDYLKDTffdenltlnfed 230
Cdd:cd02511    99 ddYDGYYVPRRNFFLGRWIRHGGWYPDRQLRL-FRRGKARFEDGRVHEQVVVDgGVGIVLKGDILHYG------------ 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1073282073 231 gkFINIYLFKNLNLKSIFLKNARYF--YRKRFDKSSTLDKKNKNKFYYLEILEKGYLE 286
Cdd:cd02511   166 --YKSLEEFLEKHNRYSSLEAKDLAakGKKRSLLKGLLLGRPLLAFLKMYILKRGFLD 221
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
42-173 1.22e-03

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: 41.12  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073  42 IVSAVYNVEKYLDDFFKSIINQRLDfKNNIHLICVDDGSTDNSANIIKKYQKKYPKNIIYL---YKENGGQASARNLGLK 118
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYP-KEKFEVILVDDHSTDGTVQILEFAAAKPNFQLKILnnsRVSISGKKNALTTAIK 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1073282073 119 YLKeNDlnipWVTFTDPDDFLDRDYFYEVDSFLkNQNNIAMVATNIIFYREKRKI 173
Cdd:cd04192    80 AAK-GD----WIVTTDADCVVPSNWLLTFVAFI-QKEQIGLVAGPVIYFKGKSLL 128
Epimerase_2 pfam02350
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ...
696-766 5.06e-03

UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.


Pssm-ID: 426733 [Multi-domain]  Cd Length: 336  Bit Score: 39.83  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073282073 696 LQELHEKYDYKIVFSPHPQ------IRPYLEGFnlPNYIIIPSVE----MSMQKlfcESSLMITDYSSVAFEMAVLKKPV 765
Cdd:pfam02350 202 LRALAERPDVPVVFPVHNNprtrrrLNERLEGY--PRVRLIEPLGyldfLSLLK---RADLVITDSGGIQEEAPSLGVPV 276

                  .
gi 1073282073 766 I 766
Cdd:pfam02350 277 V 277
 
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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