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Conserved domains on  [gi|1435114256|ref|XP_025810646|]
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alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase [Panicum hallii]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
19-441 0e+00

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.


The actual alignment was detected with superfamily member pfam03071:

Pssm-ID: 472172  Cd Length: 434  Bit Score: 563.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256  19 FIYIQVRLFATQSHYADRLAEAEKSENQCTSQLKSLIDQVSMQQEKIVALEE-MKIRQDEERAQLKILIQDLEKRSVQKL 97
Cdd:pfam03071   7 FIYIQMRLFQTWTQYADRLSSAIESENHDTSQMRGLIDEVAIKQSRIVALEDkMKNRQDEELVQLRDLIQTFEKKGIAKL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256  98 LNKNVVPVAAVVIMACNRPDYLERTVESILKYQTSvASKFPLFISQDGTNGAVKKKALDY-KQITYMQHVNLEPVQTErP 176
Cdd:pfam03071  87 TQGGQMPVIPVLVMACSRADYVRRTVKKLLTYRPS-AEKFPIIVSQDCSDEAVKSKSLSYgNQVTYIQHLDFEPIVTP-P 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 177 GE--LTAYYKIAKHYKWALDELFIKHNFARVIILEDDMEIAPDFFDYFEAAAKLLDNDKTIMAVSSWNDNGQKQFVNDQK 254
Cdd:pfam03071 165 GHrqLTAYYKIARHYKWALDQVFYKHKFSRVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGKKQFVDDTA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 255 --ALYRSDFFPGLGWMLTKSTWLELSPKWPKAYWDDWMRLKEIHGNRQFIRPEICRTYNFGKHGSSLGQFFEQYLEPIKL 332
Cdd:pfam03071 245 pyALYRSDFFPGLGWMLKRSTWDELEPKWPKAFWDDWMRLPENRKGRQCIRPEISRTMNFGEHGSSLGQFFSQHLEPIKL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 333 NDVHIDWNSEDLSYLGEDKFSTKFGKEVASATPLHGSDAVLKAHNMAADVRIQYDDQEDFERIARQFGIFEEWKDGIPRT 412
Cdd:pfam03071 325 NDVTVDFKAKDLGYLTEGNYTKYFSGLVRQARPLQGSDVVLKAQNIKGDVRVRYKGQVEFERIAGELGIMEDWKDGVPRT 404
                         410       420
                  ....*....|....*....|....*....
gi 1435114256 413 AYKGVVVFRYKSspRRIFLVSPDSLRQLG 441
Cdd:pfam03071 405 AYKGIVTFRIQG--RRVFLVPPDTVMQYG 431
 
Name Accession Description Interval E-value
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
19-441 0e+00

GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, GLCNAC-T I) EC:2.4.1.101 transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide. This is an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus, and is probably distributed in all tissues. The catalytic domain is located at the C-terminus.


Pssm-ID: 397273  Cd Length: 434  Bit Score: 563.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256  19 FIYIQVRLFATQSHYADRLAEAEKSENQCTSQLKSLIDQVSMQQEKIVALEE-MKIRQDEERAQLKILIQDLEKRSVQKL 97
Cdd:pfam03071   7 FIYIQMRLFQTWTQYADRLSSAIESENHDTSQMRGLIDEVAIKQSRIVALEDkMKNRQDEELVQLRDLIQTFEKKGIAKL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256  98 LNKNVVPVAAVVIMACNRPDYLERTVESILKYQTSvASKFPLFISQDGTNGAVKKKALDY-KQITYMQHVNLEPVQTErP 176
Cdd:pfam03071  87 TQGGQMPVIPVLVMACSRADYVRRTVKKLLTYRPS-AEKFPIIVSQDCSDEAVKSKSLSYgNQVTYIQHLDFEPIVTP-P 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 177 GE--LTAYYKIAKHYKWALDELFIKHNFARVIILEDDMEIAPDFFDYFEAAAKLLDNDKTIMAVSSWNDNGQKQFVNDQK 254
Cdd:pfam03071 165 GHrqLTAYYKIARHYKWALDQVFYKHKFSRVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGKKQFVDDTA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 255 --ALYRSDFFPGLGWMLTKSTWLELSPKWPKAYWDDWMRLKEIHGNRQFIRPEICRTYNFGKHGSSLGQFFEQYLEPIKL 332
Cdd:pfam03071 245 pyALYRSDFFPGLGWMLKRSTWDELEPKWPKAFWDDWMRLPENRKGRQCIRPEISRTMNFGEHGSSLGQFFSQHLEPIKL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 333 NDVHIDWNSEDLSYLGEDKFSTKFGKEVASATPLHGSDAVLKAHNMAADVRIQYDDQEDFERIARQFGIFEEWKDGIPRT 412
Cdd:pfam03071 325 NDVTVDFKAKDLGYLTEGNYTKYFSGLVRQARPLQGSDVVLKAQNIKGDVRVRYKGQVEFERIAGELGIMEDWKDGVPRT 404
                         410       420
                  ....*....|....*....|....*....
gi 1435114256 413 AYKGVVVFRYKSspRRIFLVSPDSLRQLG 441
Cdd:pfam03071 405 AYKGIVTFRIQG--RRVFLVPPDTVMQYG 431
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
105-436 4.60e-174

GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13.


Pssm-ID: 133007  Cd Length: 334  Bit Score: 490.30  E-value: 4.60e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 105 VAAVVIMACNRPDYLERTVESILKYQTSvASKFPLFISQDGTNGAVKKKALDY-KQITYMQHVNLEPVQTERPGELTAYY 183
Cdd:cd02514     1 VIPVLVIACNRPDYLRRMLDSLLSYRPS-AEKFPIIVSQDGGYEEVADVAKSFgDGVTHIQHPPISIKNVNPPHKFQGYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 184 KIAKHYKWALDELFIKHNFARVIILEDDMEIAPDFFDYFEAAAKLLDNDKTIMAVSSWNDNGQKQFVNDQ-KALYRSDFF 262
Cdd:cd02514    80 RIARHYKWALTQTFNLFGYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDTpSLLYRTDFF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 263 PGLGWMLTKSTWLELSPKWPKAYWDDWMRLKEIHGNRQFIRPEICRTYNFGKHGSSLGQFFEQYLEPIKLNDVHIDWNSE 342
Cdd:cd02514   160 PGLGWMLTRKLWKELEPKWPKAFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGVSNGQFFDKYLKKIKLNTVFVVFTKL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 343 DLSYLGEDKFSTKFGKEVASATPLHGSDA---VLKAHNMAADVRIQYDDQEDFERIARQFGIFEEWKDGIPRTAYKGVVV 419
Cdd:cd02514   240 DLSYLKKDNYDKEFHRLVYGAVVLDHEKNpceLSFVPDTEGKVRVVYTGRDDFKTWAKAFGVMDDLKDGVPRTAYKGIVR 319
                         330
                  ....*....|....*..
gi 1435114256 420 FRYKSspRRIFLVSPDS 436
Cdd:cd02514   320 FFFKG--NRVFLVPPPT 334
COG3306 COG3306
Glycosyltransferase involved in LPS biosynthesis, GR25 family [Cell wall/membrane/envelope ...
175-321 2.10e-03

Glycosyltransferase involved in LPS biosynthesis, GR25 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442535 [Multi-domain]  Cd Length: 238  Bit Score: 39.60  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 175 RPGELTAYykiAKHYK-WaldELFIKHNFARVIILEDDMEIAPDFFDYFEAAAKLLDNDKTI----MAVSSWNDNGQKQF 249
Cdd:COG3306    62 TPGEIGCF---LSHRKaW---QKIVESGLPYALILEDDVILSPDFAEVLEALAWLPADWDIVkletSKRKVFLGRRKIKK 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1435114256 250 VNDQKaLYRSdFFPGLG---WMLTKST---WLELSPKWPKAYwDDWMRLKEIHGNRQF-IRPEICRTyNFGKHGSSLGQ 321
Cdd:COG3306   136 LGGYR-LVRP-YSPPLGtagYLISRKAakkLLALLEPIDRPV-DDFLFRFWLHGLRVYqVRPALVIQ-DSGLLGSTIEA 210
 
Name Accession Description Interval E-value
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
19-441 0e+00

GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, GLCNAC-T I) EC:2.4.1.101 transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide. This is an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus, and is probably distributed in all tissues. The catalytic domain is located at the C-terminus.


Pssm-ID: 397273  Cd Length: 434  Bit Score: 563.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256  19 FIYIQVRLFATQSHYADRLAEAEKSENQCTSQLKSLIDQVSMQQEKIVALEE-MKIRQDEERAQLKILIQDLEKRSVQKL 97
Cdd:pfam03071   7 FIYIQMRLFQTWTQYADRLSSAIESENHDTSQMRGLIDEVAIKQSRIVALEDkMKNRQDEELVQLRDLIQTFEKKGIAKL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256  98 LNKNVVPVAAVVIMACNRPDYLERTVESILKYQTSvASKFPLFISQDGTNGAVKKKALDY-KQITYMQHVNLEPVQTErP 176
Cdd:pfam03071  87 TQGGQMPVIPVLVMACSRADYVRRTVKKLLTYRPS-AEKFPIIVSQDCSDEAVKSKSLSYgNQVTYIQHLDFEPIVTP-P 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 177 GE--LTAYYKIAKHYKWALDELFIKHNFARVIILEDDMEIAPDFFDYFEAAAKLLDNDKTIMAVSSWNDNGQKQFVNDQK 254
Cdd:pfam03071 165 GHrqLTAYYKIARHYKWALDQVFYKHKFSRVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGKKQFVDDTA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 255 --ALYRSDFFPGLGWMLTKSTWLELSPKWPKAYWDDWMRLKEIHGNRQFIRPEICRTYNFGKHGSSLGQFFEQYLEPIKL 332
Cdd:pfam03071 245 pyALYRSDFFPGLGWMLKRSTWDELEPKWPKAFWDDWMRLPENRKGRQCIRPEISRTMNFGEHGSSLGQFFSQHLEPIKL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 333 NDVHIDWNSEDLSYLGEDKFSTKFGKEVASATPLHGSDAVLKAHNMAADVRIQYDDQEDFERIARQFGIFEEWKDGIPRT 412
Cdd:pfam03071 325 NDVTVDFKAKDLGYLTEGNYTKYFSGLVRQARPLQGSDVVLKAQNIKGDVRVRYKGQVEFERIAGELGIMEDWKDGVPRT 404
                         410       420
                  ....*....|....*....|....*....
gi 1435114256 413 AYKGVVVFRYKSspRRIFLVSPDSLRQLG 441
Cdd:pfam03071 405 AYKGIVTFRIQG--RRVFLVPPDTVMQYG 431
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
105-436 4.60e-174

GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13.


Pssm-ID: 133007  Cd Length: 334  Bit Score: 490.30  E-value: 4.60e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 105 VAAVVIMACNRPDYLERTVESILKYQTSvASKFPLFISQDGTNGAVKKKALDY-KQITYMQHVNLEPVQTERPGELTAYY 183
Cdd:cd02514     1 VIPVLVIACNRPDYLRRMLDSLLSYRPS-AEKFPIIVSQDGGYEEVADVAKSFgDGVTHIQHPPISIKNVNPPHKFQGYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 184 KIAKHYKWALDELFIKHNFARVIILEDDMEIAPDFFDYFEAAAKLLDNDKTIMAVSSWNDNGQKQFVNDQ-KALYRSDFF 262
Cdd:cd02514    80 RIARHYKWALTQTFNLFGYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDTpSLLYRTDFF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 263 PGLGWMLTKSTWLELSPKWPKAYWDDWMRLKEIHGNRQFIRPEICRTYNFGKHGSSLGQFFEQYLEPIKLNDVHIDWNSE 342
Cdd:cd02514   160 PGLGWMLTRKLWKELEPKWPKAFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGVSNGQFFDKYLKKIKLNTVFVVFTKL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 343 DLSYLGEDKFSTKFGKEVASATPLHGSDA---VLKAHNMAADVRIQYDDQEDFERIARQFGIFEEWKDGIPRTAYKGVVV 419
Cdd:cd02514   240 DLSYLKKDNYDKEFHRLVYGAVVLDHEKNpceLSFVPDTEGKVRVVYTGRDDFKTWAKAFGVMDDLKDGVPRTAYKGIVR 319
                         330
                  ....*....|....*..
gi 1435114256 420 FRYKSspRRIFLVSPDS 436
Cdd:cd02514   320 FFFKG--NRVFLVPPPT 334
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
108-303 5.38e-04

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: 40.57  E-value: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 108 VVIMACNRPDYLERTVESILKyQTSvaSKFPLFI----SQDGTNGAVKKKALDYKQITYmqhvnlePVQTERPGeltayy 183
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLA-QTY--PNFEVIVvddgSTDGTLEILEEYAKKDPRVIR-------VINEENQG------ 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 184 kIAKHYKWALDelFIKHNFarVIILEDDMEIAPDFfdyFEAAAKLLDNDKTIMAVSSWNdngqkqfvndqkalyrsdffp 263
Cdd:cd00761    65 -LAAARNAGLK--AARGEY--ILFLDADDLLLPDW---LERLVAELLADPEADAVGGPG--------------------- 115
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1435114256 264 glGWMLTKSTWLELSPKWPKAYW---DDWMRLKEIHGNRQFIR 303
Cdd:cd00761   116 --NLLFRRELLEEIGGFDEALLSgeeDDDFLLRLLRGGKVAFR 156
Glyco_transf_25 cd06532
Glycosyltransferase family 25 [lipooligosaccharide (LOS) biosynthesis protein] is a family of ...
175-237 2.04e-03

Glycosyltransferase family 25 [lipooligosaccharide (LOS) biosynthesis protein] is a family of glycosyltransferases involved in LOS biosynthesis. The members include the beta(1,4) galactosyltransferases: Lgt2 of Moraxella catarrhalis, LgtB and LgtE of Neisseria gonorrhoeae and Lic2A of Haemophilus influenzae. M. catarrhalis Lgt2 catalyzes the addition of galactose (Gal) to the growing chain of LOS on the cell surface. N. gonorrhoeae LgtB and LgtE link Gal-beta(1,4) to GlcNAc (N-acetylglucosamine) and Glc (glucose), respectively. The genes encoding LgtB and LgtE are two genes of a five gene locus involved in the synthesis of gonococcal LOS. LgtE is believed to perform the first step in LOS biosynthesis.


Pssm-ID: 133474  Cd Length: 128  Bit Score: 37.97  E-value: 2.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1435114256 175 RPGELTAYykiAKHYK-WaldELFIKHNFARVIILEDDMEIAPDF-FDYF---EAAAKLLDNDKTIMA 237
Cdd:cd06532    61 TPGEIGCF---LSHYKlW---QKIVESNLEYALILEDDAILDPDGtAGYLvsrKGAKKLLAALEPIDL 122
COG3306 COG3306
Glycosyltransferase involved in LPS biosynthesis, GR25 family [Cell wall/membrane/envelope ...
175-321 2.10e-03

Glycosyltransferase involved in LPS biosynthesis, GR25 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442535 [Multi-domain]  Cd Length: 238  Bit Score: 39.60  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 175 RPGELTAYykiAKHYK-WaldELFIKHNFARVIILEDDMEIAPDFFDYFEAAAKLLDNDKTI----MAVSSWNDNGQKQF 249
Cdd:COG3306    62 TPGEIGCF---LSHRKaW---QKIVESGLPYALILEDDVILSPDFAEVLEALAWLPADWDIVkletSKRKVFLGRRKIKK 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1435114256 250 VNDQKaLYRSdFFPGLG---WMLTKST---WLELSPKWPKAYwDDWMRLKEIHGNRQF-IRPEICRTyNFGKHGSSLGQ 321
Cdd:COG3306   136 LGGYR-LVRP-YSPPLGtagYLISRKAakkLLALLEPIDRPV-DDFLFRFWLHGLRVYqVRPALVIQ-DSGLLGSTIEA 210
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
104-240 3.22e-03

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: 39.34  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 104 PVAAVVIMACNRPDYLERTVESILKyQTSVASKFPLFI----SQDGTNGAVKKKALDYKQITYMqhvnlepVQTERPGel 179
Cdd:COG1215    29 PRVSVIIPAYNEEAVIEETLRSLLA-QDYPKEKLEVIVvddgSTDETAEIARELAAEYPRVRVI-------ERPENGG-- 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1435114256 180 tayyKiakhyKWALDELFIKHNFARVIILEDDMEIAPdffDYFEAAAKLLDNDKTIMAVSS 240
Cdd:COG1215    99 ----K-----AAALNAGLKAARGDIVVFLDADTVLDP---DWLRRLVAAFADPGVGASGAN 147
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
108-241 8.38e-03

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 37.37  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435114256 108 VVIMACNRPDYLERTVESILKyQTsvASKFPLFI----SQDGTNGAVKKKALDYKQITYMQHvnlepvqTERPGeltayy 183
Cdd:COG0463     6 VVIPTYNEEEYLEEALESLLA-QT--YPDFEIIVvddgSTDGTAEILRELAAKDPRIRVIRL-------ERNRG------ 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1435114256 184 kIAKHYKWALDElfikhnfAR---VIILEDDMEIAPDFfdyFEAAAKLLDNDKTIMAVSSW 241
Cdd:COG0463    70 -KGAARNAGLAA-------ARgdyIAFLDADDQLDPEK---LEELVAALEEGPADLVYGSR 119
 
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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