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Conserved domains on  [gi|295321866|pdb|3L7I|A]
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Chain A, Teichoic acid biosynthesis protein F

Protein Classification

bifunctional glycosyltransferase family 2 protein/CDP-glycerol:glycerophosphate glycerophosphotransferase( domain architecture ID 11536759)

bifunctional glycosyltransferase family 2 protein/CDP-glycerol:glycerophosphate glycerophosphotransferase is a glycosyltransferase (GT) containing both family A (GTA) and family B (GTB) folds, and may be involved in the poly(glycerol phosphate) teichoic acid biosynthesis pathway, which is part of cell wall biogenesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyphos_transf pfam04464
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
350-716 1.12e-166

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: 483.39  E-value: 1.12e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        350 VKPKTIVFESFGGKNYSDSPKYIYEYMQKYYPNYRYIWSFKNPDKNVVPGSAEKVKRNSAEYYQAYSEASHWVSNARTPL 429
Cdd:pfam04464   2 LDPNLVLFESFWGRGYSDNPKAIYEYLRELAPGYRIVWVVKKDHSARLPKGVPVVVRNSFRYLYLLLRAKYLVSNSNFPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        430 YLNKKENQTYIQTWHGTPLKRLANDMKVVRMPGTttpkyKRNFNRETSRWDYLISPNRYSTEIFRSAFWMDEERILEIGY 509
Cdd:pfam04464  82 YVVKRKNQVYLQTWHGTPLKHMGLDILEVPMANT-----GQNFLRNVDRWDYLISANPHSTNIFARAFNIDKERILETGY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        510 PRNDVLVNRANDQeyLDEIRTHLNLPSDKKVIMYAPTWRDDEFVSKGKYLFELKIDLDNLYKELGDDYVILLRMHYLISN 589
Cdd:pfam04464 157 PRNDVLFNANNED--VQRIRERLGIPLGKKVILYAPTWRDDERGSIGSYRFELLIDLERLAFALGNDYVILLKMHPLIQN 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        590 ALDLSGYENFAIDVSNYNDVSELFLISDCLITDYSSVMFDYGILKRPQFFFAYDIDKYDKGlRGFYMNYMEDLPGPIYTE 669
Cdd:pfam04464 235 NIDIFESSGYVVDVSDYEDVEDLLLASDILITDYSSVMFDYAVLDRPIIFYAYDLETYSAT-RGFYLDYESEAPGPVVET 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
3L7I_A        670 PYGLAKELKNLDKVQQQYQEKIDAFYDRFCSVDNGKASQYIGDLIHK 716
Cdd:pfam04464 314 FDELIDALKSGDWDDDYYARKRRAFRDRFCKYDDGRSSERVVRLIFL 360
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-205 1.87e-28

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 113.26  E-value: 1.87e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        1 MNKLTIIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDyDKNIRFIDLDENSGHAHARNIALE 80
Cdd:COG0463   1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAK-DPRIRVIRLERNRGKGAARNAGLA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A       81 EVETPYFMFLDADDELASYAITFYLEKFNNTDGLIApIHSFTTQRPQFvdLDRVRVEYFNAKENINSFLRKQSACNIIFR 160
Cdd:COG0463  80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV-YGSRLIREGES--DLRRLGSRLFNLVRLLTNLPDSTSGFRLFR 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
3L7I_A      161 TAIVRAhhIRFNEnlntyvDWSFVLEYMKYVNKFVRIFNFPFYFR 205
Cdd:COG0463 157 REVLEE--LGFDE------GFLEDTELLRALRHGFRIAEVPVRYR 193
 
Name Accession Description Interval E-value
Glyphos_transf pfam04464
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
350-716 1.12e-166

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: 483.39  E-value: 1.12e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        350 VKPKTIVFESFGGKNYSDSPKYIYEYMQKYYPNYRYIWSFKNPDKNVVPGSAEKVKRNSAEYYQAYSEASHWVSNARTPL 429
Cdd:pfam04464   2 LDPNLVLFESFWGRGYSDNPKAIYEYLRELAPGYRIVWVVKKDHSARLPKGVPVVVRNSFRYLYLLLRAKYLVSNSNFPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        430 YLNKKENQTYIQTWHGTPLKRLANDMKVVRMPGTttpkyKRNFNRETSRWDYLISPNRYSTEIFRSAFWMDEERILEIGY 509
Cdd:pfam04464  82 YVVKRKNQVYLQTWHGTPLKHMGLDILEVPMANT-----GQNFLRNVDRWDYLISANPHSTNIFARAFNIDKERILETGY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        510 PRNDVLVNRANDQeyLDEIRTHLNLPSDKKVIMYAPTWRDDEFVSKGKYLFELKIDLDNLYKELGDDYVILLRMHYLISN 589
Cdd:pfam04464 157 PRNDVLFNANNED--VQRIRERLGIPLGKKVILYAPTWRDDERGSIGSYRFELLIDLERLAFALGNDYVILLKMHPLIQN 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        590 ALDLSGYENFAIDVSNYNDVSELFLISDCLITDYSSVMFDYGILKRPQFFFAYDIDKYDKGlRGFYMNYMEDLPGPIYTE 669
Cdd:pfam04464 235 NIDIFESSGYVVDVSDYEDVEDLLLASDILITDYSSVMFDYAVLDRPIIFYAYDLETYSAT-RGFYLDYESEAPGPVVET 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
3L7I_A        670 PYGLAKELKNLDKVQQQYQEKIDAFYDRFCSVDNGKASQYIGDLIHK 716
Cdd:pfam04464 314 FDELIDALKSGDWDDDYYARKRRAFRDRFCKYDDGRSSERVVRLIFL 360
TagB COG1887
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ...
332-714 8.93e-133

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


Pssm-ID: 441491  Cd Length: 369  Bit Score: 397.05  E-value: 8.93e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A      332 RRKNKERSLYDLTDKEDNVKPKTIVFESFGGKNYSDSPKYIYEYMQKYYPNYRYIWSFKNPDKNVVPGSAEKVKRNSAEY 411
Cdd:COG1887   1 KLLLLLRRLYYRLSRLLPVKKNIILFESRNGRSYSDNPKALFEYLRKNHPDYEVVWVVDDDSKRLPKEGVKVVKRGSLKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A      412 YQAYSEASHWVSNART--PLYLNKKENQTYIQTWHGTPLKRLANDMKvvrmpgtttPKYKRNFNRETSRWDYLISPNRYS 489
Cdd:COG1887  81 LYALARAKYLVSNHYFpfPSYFRKRKGQKYVQLWHGTPLKKIGLDDP---------PRYLKRVLREYRNWDYLLSSSEES 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A      490 TEIFRSAFWMDEERILEIGYPRNDVLVNrANDQEYLDEIRTHLNLPSDKKVIMYAPTWRDDEfvskGKYLFELKIDLDNL 569
Cdd:COG1887 152 TEIFRRAFGYPEGEVLETGYPRNDVLFD-ADREELREELRERLGIPEDKKVILYAPTWRDDE----DNFDDYLDLDLERL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A      570 YKELGDDYVILLRMHYLISNALDLSgYENFAIDVSNYNDVSELFLISDCLITDYSSVMFDYGILKRPQFFFAYDIDKYDK 649
Cdd:COG1887 227 AELLGDDYVLLVRLHPFVKDSLDEK-YSDRIIDVSDYPDINDLLLASDVLITDYSSVMFDFALLDRPIIFYAYDLEEYRD 305
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
3L7I_A      650 GlRGFYMNYMEDLPGPIYTEPYGLAKELKNLDKVQQQYQEKIDAFYDRFCSVDNGKASQYIGDLI 714
Cdd:COG1887 306 E-RGFYFDYEEDAPGPVVTTFEELIDAIEDILENGDEYAEKYKAFRERFFPYDDGNASERVVDAI 369
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-205 1.87e-28

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 113.26  E-value: 1.87e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        1 MNKLTIIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDyDKNIRFIDLDENSGHAHARNIALE 80
Cdd:COG0463   1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAK-DPRIRVIRLERNRGKGAARNAGLA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A       81 EVETPYFMFLDADDELASYAITFYLEKFNNTDGLIApIHSFTTQRPQFvdLDRVRVEYFNAKENINSFLRKQSACNIIFR 160
Cdd:COG0463  80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV-YGSRLIREGES--DLRRLGSRLFNLVRLLTNLPDSTSGFRLFR 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
3L7I_A      161 TAIVRAhhIRFNEnlntyvDWSFVLEYMKYVNKFVRIFNFPFYFR 205
Cdd:COG0463 157 REVLEE--LGFDE------GFLEDTELLRALRHGFRIAEVPVRYR 193
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-160 2.18e-25

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: 102.58  E-value: 2.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYDKNIRFIDlDENSGHAHARNIALEEVETP 85
Cdd:cd00761   1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVIN-EENQGLAAARNAGLKAARGE 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3L7I_A       86 YFMFLDADDELASYAITFYLEKF--NNTDGLIAPIHSFTTQRPQFVDLDRVRVEYFNAKENINSFLRKQSACNIIFR 160
Cdd:cd00761  80 YILFLDADDLLLPDWLERLVAELlaDPEADAVGGPGNLLFRRELLEEIGGFDEALLSGEEDDDFLLRLLRGGKVAFR 156
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-165 3.02e-23

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: 97.08  E-value: 3.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A          5 TIIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDyDKNIRFIDLDENSGHAHARNIALEEVET 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKK-DPRVRVIRLPENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A         85 PYFMFLDADDELASYAITFYLEKF--NNTDGLIAPIHSFTTQRPQFVDLDRVRVEYFNAKENINSFLRK---QSACNIIF 159
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALeeDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNlpfLIGGFALY 159

                  ....*.
3L7I_A        160 RTAIVR 165
Cdd:pfam00535 160 RREALE 165
PRK10073 PRK10073
putative glycosyl transferase; Provisional
2-97 6.00e-16

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 79.70  E-value: 6.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A         2 NKLTIIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYdKNIRFIDlDENSGHAHARNIALEE 81
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENY-PHVRLLH-QANAGVSVARNTGLAV 83
                         90
                 ....*....|....*.
3L7I_A        82 VETPYFMFLDADDELA 97
Cdd:PRK10073  84 ATGKYVAFPDADDVVY 99
 
Name Accession Description Interval E-value
Glyphos_transf pfam04464
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
350-716 1.12e-166

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: 483.39  E-value: 1.12e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        350 VKPKTIVFESFGGKNYSDSPKYIYEYMQKYYPNYRYIWSFKNPDKNVVPGSAEKVKRNSAEYYQAYSEASHWVSNARTPL 429
Cdd:pfam04464   2 LDPNLVLFESFWGRGYSDNPKAIYEYLRELAPGYRIVWVVKKDHSARLPKGVPVVVRNSFRYLYLLLRAKYLVSNSNFPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        430 YLNKKENQTYIQTWHGTPLKRLANDMKVVRMPGTttpkyKRNFNRETSRWDYLISPNRYSTEIFRSAFWMDEERILEIGY 509
Cdd:pfam04464  82 YVVKRKNQVYLQTWHGTPLKHMGLDILEVPMANT-----GQNFLRNVDRWDYLISANPHSTNIFARAFNIDKERILETGY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        510 PRNDVLVNRANDQeyLDEIRTHLNLPSDKKVIMYAPTWRDDEFVSKGKYLFELKIDLDNLYKELGDDYVILLRMHYLISN 589
Cdd:pfam04464 157 PRNDVLFNANNED--VQRIRERLGIPLGKKVILYAPTWRDDERGSIGSYRFELLIDLERLAFALGNDYVILLKMHPLIQN 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        590 ALDLSGYENFAIDVSNYNDVSELFLISDCLITDYSSVMFDYGILKRPQFFFAYDIDKYDKGlRGFYMNYMEDLPGPIYTE 669
Cdd:pfam04464 235 NIDIFESSGYVVDVSDYEDVEDLLLASDILITDYSSVMFDYAVLDRPIIFYAYDLETYSAT-RGFYLDYESEAPGPVVET 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
3L7I_A        670 PYGLAKELKNLDKVQQQYQEKIDAFYDRFCSVDNGKASQYIGDLIHK 716
Cdd:pfam04464 314 FDELIDALKSGDWDDDYYARKRRAFRDRFCKYDDGRSSERVVRLIFL 360
TagB COG1887
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ...
332-714 8.93e-133

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


Pssm-ID: 441491  Cd Length: 369  Bit Score: 397.05  E-value: 8.93e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A      332 RRKNKERSLYDLTDKEDNVKPKTIVFESFGGKNYSDSPKYIYEYMQKYYPNYRYIWSFKNPDKNVVPGSAEKVKRNSAEY 411
Cdd:COG1887   1 KLLLLLRRLYYRLSRLLPVKKNIILFESRNGRSYSDNPKALFEYLRKNHPDYEVVWVVDDDSKRLPKEGVKVVKRGSLKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A      412 YQAYSEASHWVSNART--PLYLNKKENQTYIQTWHGTPLKRLANDMKvvrmpgtttPKYKRNFNRETSRWDYLISPNRYS 489
Cdd:COG1887  81 LYALARAKYLVSNHYFpfPSYFRKRKGQKYVQLWHGTPLKKIGLDDP---------PRYLKRVLREYRNWDYLLSSSEES 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A      490 TEIFRSAFWMDEERILEIGYPRNDVLVNrANDQEYLDEIRTHLNLPSDKKVIMYAPTWRDDEfvskGKYLFELKIDLDNL 569
Cdd:COG1887 152 TEIFRRAFGYPEGEVLETGYPRNDVLFD-ADREELREELRERLGIPEDKKVILYAPTWRDDE----DNFDDYLDLDLERL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A      570 YKELGDDYVILLRMHYLISNALDLSgYENFAIDVSNYNDVSELFLISDCLITDYSSVMFDYGILKRPQFFFAYDIDKYDK 649
Cdd:COG1887 227 AELLGDDYVLLVRLHPFVKDSLDEK-YSDRIIDVSDYPDINDLLLASDVLITDYSSVMFDFALLDRPIIFYAYDLEEYRD 305
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
3L7I_A      650 GlRGFYMNYMEDLPGPIYTEPYGLAKELKNLDKVQQQYQEKIDAFYDRFCSVDNGKASQYIGDLI 714
Cdd:COG1887 306 E-RGFYFDYEEDAPGPVVTTFEELIDAIEDILENGDEYAEKYKAFRERFFPYDDGNASERVVDAI 369
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-205 1.87e-28

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 113.26  E-value: 1.87e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        1 MNKLTIIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDyDKNIRFIDLDENSGHAHARNIALE 80
Cdd:COG0463   1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAK-DPRIRVIRLERNRGKGAARNAGLA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A       81 EVETPYFMFLDADDELASYAITFYLEKFNNTDGLIApIHSFTTQRPQFvdLDRVRVEYFNAKENINSFLRKQSACNIIFR 160
Cdd:COG0463  80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV-YGSRLIREGES--DLRRLGSRLFNLVRLLTNLPDSTSGFRLFR 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
3L7I_A      161 TAIVRAhhIRFNEnlntyvDWSFVLEYMKYVNKFVRIFNFPFYFR 205
Cdd:COG0463 157 REVLEE--LGFDE------GFLEDTELLRALRHGFRIAEVPVRYR 193
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-160 2.18e-25

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: 102.58  E-value: 2.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYDKNIRFIDlDENSGHAHARNIALEEVETP 85
Cdd:cd00761   1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVIN-EENQGLAAARNAGLKAARGE 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3L7I_A       86 YFMFLDADDELASYAITFYLEKF--NNTDGLIAPIHSFTTQRPQFVDLDRVRVEYFNAKENINSFLRKQSACNIIFR 160
Cdd:cd00761  80 YILFLDADDLLLPDWLERLVAELlaDPEADAVGGPGNLLFRRELLEEIGGFDEALLSGEEDDDFLLRLLRGGKVAFR 156
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-165 3.02e-23

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: 97.08  E-value: 3.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A          5 TIIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDyDKNIRFIDLDENSGHAHARNIALEEVET 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKK-DPRVRVIRLPENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A         85 PYFMFLDADDELASYAITFYLEKF--NNTDGLIAPIHSFTTQRPQFVDLDRVRVEYFNAKENINSFLRK---QSACNIIF 159
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALeeDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNlpfLIGGFALY 159

                  ....*.
3L7I_A        160 RTAIVR 165
Cdd:pfam00535 160 RREALE 165
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-102 1.24e-21

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 93.52  E-value: 1.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        1 MNKLTIIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAikdYDKNIRFIDLDENSGHAHARNIALE 80
Cdd:COG1216   2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL---AFPRVRVIRNPENLGFAAARNLGLR 78
                        90       100
                ....*....|....*....|..
3L7I_A       81 EVETPYFMFLDADDELASYAIT 102
Cdd:COG1216  79 AAGGDYLLFLDDDTVVEPDWLE 100
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-112 3.50e-21

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: 94.81  E-value: 3.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        1 MNKLTIIVTYYNAEEYITGCLESIKQQR--TQDFNLIIVNDGSTDQSKKLMDEAIKDYDkNIRFIDLDENSGHAHARNIA 78
Cdd:COG1215  28 LPRVSVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYP-RVRVIERPENGGKAAALNAG 106
                        90       100       110
                ....*....|....*....|....*....|....
3L7I_A       79 LEEVETPYFMFLDADDELASYAITFYLEKFNNTD 112
Cdd:COG1215 107 LKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
6-116 1.83e-19

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: 86.51  E-value: 1.83e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYDKNIRFIDLDENSGHAHARNIALEEVETP 85
Cdd:cd06423   1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRHAKGD 80
                        90       100       110
                ....*....|....*....|....*....|.
3L7I_A       86 YFMFLDADDELASYAITFYLEKFNNTDGLIA 116
Cdd:cd06423  81 IVVVLDADTILEPDALKRLVVPFFADPKVGA 111
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-108 2.93e-18

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: 82.61  E-value: 2.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKklmdEAIKDYDKNIRFIDLDENSGHAHARNIALEEVETP 85
Cdd:cd04186   1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSV----ELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGD 76
                        90       100
                ....*....|....*....|...
3L7I_A       86 YFMFLDADDELASYAITFYLEKF 108
Cdd:cd04186  77 YVLLLNPDTVVEPGALLELLDAA 99
PRK10073 PRK10073
putative glycosyl transferase; Provisional
2-97 6.00e-16

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 79.70  E-value: 6.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A         2 NKLTIIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYdKNIRFIDlDENSGHAHARNIALEE 81
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENY-PHVRLLH-QANAGVSVARNTGLAV 83
                         90
                 ....*....|....*.
3L7I_A        82 VETPYFMFLDADDELA 97
Cdd:PRK10073  84 ATGKYVAFPDADDVVY 99
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
3-197 6.61e-12

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: 65.30  E-value: 6.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        3 KLTIIVTYYNA-EEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYDKNIRFIDLDENSGHAHARNIALEE 81
Cdd:cd04184   2 LISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A       82 VETPYFMFLDADDELASYAITFYLEKFNNTDgliapihsfttqRPQFV--DLDRV-----RVE-YFNAKENINSFLrkqs 153
Cdd:cd04184  82 ATGEFVALLDHDDELAPHALYEVVKALNEHP------------DADLIysDEDKIdeggkRSEpFFKPDWSPDLLL---- 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
3L7I_A      154 ACNIIFRTAIVRAHHIR----FNENLNTYVDWSFVLEYMKYVNKFVRI 197
Cdd:cd04184 146 SQNYIGHLLVYRRSLVRqvggFREGFEGAQDYDLVLRVSEHTDRIAHI 193
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
6-93 4.04e-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: 62.59  E-value: 4.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYNAEEYITGCLESIKQ--QRTQDFNLIIVNDGSTDQSKKLMDEAIKDYdKNIRFIDLDENSGHAHARNIALEEVE 83
Cdd:cd04179   1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELAARV-PRVRVIRLSRNFGKGAAVRAGFKAAR 79
                        90
                ....*....|
3L7I_A       84 TPYFMFLDAD 93
Cdd:cd04179  80 GDIVVTMDAD 89
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
6-197 4.71e-11

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: 62.56  E-value: 4.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYyNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKklmdEAIKDY-DKNIRFI---DldenSGHAHARNIALEE 81
Cdd:cd06433   3 ITPTY-NQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTV----DIIKKYeDKITYWIsepD----KGIYDAMNKGIAL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A       82 VETPYFMFLDADDELASYAI---TFYLEKFNNTDGLIAPIHSFTTQrpqfvdlDRVRVEYFNAKENINSFLRKQSACN-- 156
Cdd:cd06433  74 ATGDIIGFLNSDDTLLPGALlavVAAFAEHPEVDVVYGDVLLVDEN-------GRVIGRRRPPPFLDKFLLYGMPICHqa 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
3L7I_A      157 IIFRTAIVRAHHiRFNENLNTYVDWSFVLEYMKYVNKFVRI 197
Cdd:cd06433 147 TFFRRSLFEKYG-GFDESYRIAADYDLLLRLLLAGKIFKYL 186
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-94 1.03e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 61.88  E-value: 1.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        5 TIIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYDKNIRFIDLDENSGhaHARNI--ALEEV 82
Cdd:cd04196   1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLG--VARNFesLLQAA 78
                        90
                ....*....|..
3L7I_A       83 ETPYFMFLDADD 94
Cdd:cd04196  79 DGDYVFFCDQDD 90
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
3-93 8.61e-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: 59.90  E-value: 8.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        3 KLTIIVTYYNAEEYITGCLESIKQQ--RTQDFNLIIVNDGSTDQSkklmDEAIKDY-DKNIRFIDLDENSGHAHARNIAL 79
Cdd:cd06439  30 TVTIIIPAYNEEAVIEAKLENLLALdyPRDRLEIIVVSDGSTDGT----AEIAREYaDKGVKLLRFPERRGKAAALNRAL 105
                        90
                ....*....|....
3L7I_A       80 EEVETPYFMFLDAD 93
Cdd:cd06439 106 ALATGEIVVFTDAN 119
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
6-94 6.17e-09

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: 56.70  E-value: 6.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYNAEEYITGCLESIKQQR-TQDFNLIIVNDGSTDQS-KKLMDEAIKDYDKNIRFIDLDENS----GHAHARNIAL 79
Cdd:cd06913   1 IILPVHNGEQWLDECLESVLQQDfEGTLELSVFNDASTDKSaEIIEKWRKKLEDSGVIVLVGSHNSpspkGVGYAKNQAI 80
                        90
                ....*....|....*
3L7I_A       80 EEVETPYFMFLDADD 94
Cdd:cd06913  81 AQSSGRYLCFLDSDD 95
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
6-93 7.52e-09

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: 56.42  E-value: 7.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYNAEEYITGCLESI----KQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYDKNIRFIDLDENSGHAHARNIALEE 81
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAveylEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLPKNRGKGGAVRAGMLA 80
                        90
                ....*....|..
3L7I_A       82 VETPYFMFLDAD 93
Cdd:cd04188  81 ARGDYILFADAD 92
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
5-93 7.56e-09

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: 57.24  E-value: 7.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        5 TIIVTYYNAEEYITGCLESIKQQRTQ--DFNLIIVNDGSTDQSKKLMDEaIKDYDKNIRFID-LDENSghAHARNIALEE 81
Cdd:cd02525   3 SIIIPVRNEEKYIEELLESLLNQSYPkdLIEIIVVDGGSTDGTREIVQE-YAAKDPRIRLIDnPKRIQ--SAGLNIGIRN 79
                        90
                ....*....|..
3L7I_A       82 VETPYFMFLDAD 93
Cdd:cd02525  80 SRGDIIIRVDAH 91
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
3-96 1.89e-08

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: 55.76  E-value: 1.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        3 KLTIIVTYYNAEEYITGCLESIKqqrtqDFN--LIIVNDGSTDQSKKLmdeaIKDYdkNIRFIDLDENsGHAHARNIALE 80
Cdd:cd02511   1 TLSVVIITKNEERNIERCLESVK-----WAVdeIIVVDSGSTDRTVEI----AKEY--GAKVYQRWWD-GFGAQRNFALE 68
                        90
                ....*....|....*.
3L7I_A       81 EVETPYFMFLDADDEL 96
Cdd:cd02511  69 LATNDWVLSLDADERL 84
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
6-93 2.06e-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: 54.41  E-value: 2.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYNAEEYITGCLESIKQ---QRTQDFNLIIVNDGSTDQSKKLMDEAIKDyDKNIRFIDLDENSGHAHARNIALEEV 82
Cdd:cd04187   1 IVVPVYNEEENLPELYERLKAvleSLGYDYEIIFVDDGSTDRTLEILRELAAR-DPRVKVIRLSRNFGQQAALLAGLDHA 79
                        90
                ....*....|.
3L7I_A       83 ETPYFMFLDAD 93
Cdd:cd04187  80 RGDAVITMDAD 90
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-116 8.11e-08

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: 53.83  E-value: 8.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYNAEEYITGCLESI-KQQRTQD-FNLIIVNDGSTDQSKKLMDEAIKDYDKNIRFIDLDE--NSGHAHARNIALEE 81
Cdd:cd04192   1 VVIAARNEAENLPRLLQSLsALDYPKEkFEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRvsISGKKNALTTAIKA 80
                        90       100       110
                ....*....|....*....|....*....|....*.
3L7I_A       82 VETPYFMFLDADDELASYAITFYLEKFN-NTDGLIA 116
Cdd:cd04192  81 AKGDWIVTTDADCVVPSNWLLTFVAFIQkEQIGLVA 116
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
6-93 7.24e-06

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: 47.19  E-value: 7.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYDKNIRFIdLDENSGH--AHARNIALEEVE 83
Cdd:cd06420   1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIKHV-WQEDEGFrkAKIRNKAIAAAK 79
                        90
                ....*....|
3L7I_A       84 TPYFMFLDAD 93
Cdd:cd06420  80 GDYLIFIDGD 89
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
1-93 4.83e-05

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 46.27  E-value: 4.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A         1 MNKLTIIVTYYNAEEYITGCLE---SIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYDKNIRFIDLDENSGHAHARNI 77
Cdd:PRK10714   5 IKKVSVVIPVYNEQESLPELIRrttAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNYGQHSAIMA 84
                         90
                 ....*....|....*.
3L7I_A        78 ALEEVETPYFMFLDAD 93
Cdd:PRK10714  85 GFSHVTGDLIITLDAD 100
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-72 5.99e-05

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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 44.55  E-value: 5.99e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3L7I_A        6 IIVTYyNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEaiKDYDKNIRFIDLDENSGHA 72
Cdd:cd04185   2 VVVTY-NRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTS--LGDLDNIVYLRLPENLGGA 65
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
6-93 9.21e-05

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 44.55  E-value: 9.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYNAEEYITGCLESIKQQrtQDFNLIIVNDGStDQSKKLMDEAIKDYDKniRFIDLDENSGHAHARNIALEEVETP 85
Cdd:cd06434   5 IIPVYDEDPDVFRECLRSILRQ--KPLEIIVVTDGD-DEPYLSILSQTVKYGG--IFVITVPHPGKRRALAEGIRHVTTD 79

                ....*...
3L7I_A       86 YFMFLDAD 93
Cdd:cd06434  80 IVVLLDSD 87
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
4-93 2.89e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 43.60  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A         4 LTIIVTYYNAEEYITGCLES--------IKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYDK---NIRFIDLDENSGHA 72
Cdd:PTZ00260  72 LSIVIPAYNEEDRLPKMLKEtikylesrSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINpniDIRLLSLLRNKGKG 151
                         90       100
                 ....*....|....*....|.
3L7I_A        73 HARNIALEEVETPYFMFLDAD 93
Cdd:PTZ00260 152 GAVRIGMLASRGKYILMVDAD 172
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
5-94 5.03e-04

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 42.65  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A          5 TIIVTYYNAEE--YITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMdEAIKDYDKNIRFIDLDENS-GHAHARNIALEE 81
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTLEEV-SSIKDHNLQVYYPNAPDTTySLAASRNRGTSH 79
                          90
                  ....*....|...
3L7I_A         82 VETPYFMFLDADD 94
Cdd:pfam10111  80 AIGEYISFIDGDC 92
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
4-45 1.04e-03

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily 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: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 41.02  E-value: 1.04e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
3L7I_A        4 LTIIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQS 45
Cdd:cd02522   1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGT 42
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
6-119 1.62e-03

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 40.73  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        6 IIVTYYnaeEYITGCLESIKQQRTQDFNLIIVnDGSTDQSKKLMDEAIKDydkNIRFIDLDENSGHAHARNIALE---EV 82
Cdd:cd02526   2 VVVTYN---PDLSKLKELLAALAEQVDKVVVV-DNSSGNDIELRLRLNSE---KIELIHLGENLGIAKALNIGIKaalEN 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
3L7I_A       83 ETPYFMFLDADDELA-SYAITFYLEKFNNTD----GLIAPIH 119
Cdd:cd02526  75 GADYVLLFDQDSVPPpDMVEKLLAYKILSDKnsniGAVGPRI 116
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
5-94 2.41e-03

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: 39.99  E-value: 2.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A        5 TIIVTYYNAE--EYITGCLESIKQQRTQDFNLIIVNDGSTDQSkklMDEAIKDYDK--NIRFIDLDENSGHAHARNIALE 80
Cdd:cd04195   1 SVLMSVYIKEkpEFLREALESILKQTLPPDEVVLVKDGPVTQS---LNEVLEEFKRklPLKVVPLEKNRGLGKALNEGLK 77
                        90
                ....*....|....
3L7I_A       81 EVETPYFMFLDADD 94
Cdd:cd04195  78 HCTYDWVARMDTDD 91
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
34-92 2.91e-03

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 40.27  E-value: 2.91e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A       34 LIIVNDGSTDQ-SKKLMDEAIKDYDKNIRFIDLDENSGHAHARNIALEEVETPYFMFLDA 92
Cdd:cd02510  33 IILVDDFSDKPeLKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGARAATGDVLVFLDS 92
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
2-133 6.14e-03

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: 38.89  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L7I_A          2 NKLTIIVTYYNAEEYITGCLESIKQQRTQDFNLIIVNDGSTDQSKKLMDEAIKDYDKN----IRFIDLDENSGHAHARNI 77
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVrlrvIRNARLLGPTGKSRGLNH 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
3L7I_A         78 ALEEVETPYFMFLDADDELASYAITFYLEKFnntdgLIAPIHSFTTqrPQFVDLDR 133
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-----DSPKVGAVGT--PVFSLNRS 130
 
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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