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Conserved domains on  [gi|1835265595|gb|QJE45169|]
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N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase [Campylobacter sp. CFSAN093256]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133538)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  12691742|10521532|16037492
SCOP:  3001586

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 2-366 3.39e-91

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


:

Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 277.94  E-value: 3.39e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595   2 RIGFLSHAGASIYHFRMPIIKALKDRKDEVFVIVPQDEY-TQKLRDLGLKVIVYEFSRASLNPFVVLKNFFYLAKVLKNL 80
Cdd:cd03808     1 KILFIVNVDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKlSDELKELGVKVIDIPILRRGINPLKDLKALFKLYKLLKKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  81 NLDFIQSAAHKSNTFGILAAKWAKIPYRFALVEGLGSFYIDQGFKanlvRFVINSLYKLSFKFAHQFIFVNESNAEFMRN 160
Cdd:cd03808    81 KPDIVHCHTPKPGILGRLAARLAGVPKVIYTVHGLGFVFTEGKLL----RLLYLLLEKLALLFTDKVIFVNEDDRDLAIK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 161 LGL-KENKICVIKSVGINLKKFFPIYVEsekkelfwknlNIDKKPIVLMIARALWHKGVKEFYESATMLKDKAN---FVL 236
Cdd:cd03808   157 KGIiKKKKTVLIPGSGVDLDRFQYSPES-----------LPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPnvrFLL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 237 VGGRDENPSCASL--EFLNSGAVHYLGARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNA 314
Cdd:cd03808   226 VGDGELENPSEILieKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDG 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1835265595 315 YDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDALQ-YDENIIAQRYL 366
Cdd:cd03808   306 VNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEkFDEEKVVNKLL 358
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 2-366 3.39e-91

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 277.94  E-value: 3.39e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595   2 RIGFLSHAGASIYHFRMPIIKALKDRKDEVFVIVPQDEY-TQKLRDLGLKVIVYEFSRASLNPFVVLKNFFYLAKVLKNL 80
Cdd:cd03808     1 KILFIVNVDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKlSDELKELGVKVIDIPILRRGINPLKDLKALFKLYKLLKKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  81 NLDFIQSAAHKSNTFGILAAKWAKIPYRFALVEGLGSFYIDQGFKanlvRFVINSLYKLSFKFAHQFIFVNESNAEFMRN 160
Cdd:cd03808    81 KPDIVHCHTPKPGILGRLAARLAGVPKVIYTVHGLGFVFTEGKLL----RLLYLLLEKLALLFTDKVIFVNEDDRDLAIK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 161 LGL-KENKICVIKSVGINLKKFFPIYVEsekkelfwknlNIDKKPIVLMIARALWHKGVKEFYESATMLKDKAN---FVL 236
Cdd:cd03808   157 KGIiKKKKTVLIPGSGVDLDRFQYSPES-----------LPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPnvrFLL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 237 VGGRDENPSCASL--EFLNSGAVHYLGARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNA 314
Cdd:cd03808   226 VGDGELENPSEILieKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDG 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1835265595 315 YDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDALQ-YDENIIAQRYL 366
Cdd:cd03808   306 VNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEkFDEEKVVNKLL 358
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 202-352 2.50e-38

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 134.71  E-value: 2.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 202 KKPIVLMIARALWHKGVKEFYESATMLK---DKANFVLVGG--RDENPSCASLEFLNSGAVHYLGARS--DIVELLQNCD 274
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKeknPNLKLVIAGDgeEEKRLKKLAEKLGLGDNVIFLGFVSdeDLPELLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835265595 275 IFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQD 352
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 269-374 1.55e-26

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 102.38  E-value: 1.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 269 LLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKN 348
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                          90       100
                  ....*....|....*....|....*..
gi 1835265595 349 AAQDALQ-YDENIIAQRYLKLYDRVIK 374
Cdd:COG0438    97 ARERAEErFSWEAIAERLLALYEELLA 123
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 232-371 1.64e-08

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 55.87  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 232 ANFVLVGG---------RDENPSCASLEFLNSGAVHYLG--ARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIV 300
Cdd:TIGR04047 225 AQLVIAGGatlfdydayRREFRARAAELGVDPGPVVITGpvPDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVV 304

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835265595 301 VSDCEGCVEAIsNAYDGLWAKTKNAKDLSEKISLLLEDEkLRLNLAKNAAQDALQYDENIIAQRYLKLYDR 371
Cdd:TIGR04047 305 ASDIAPFTEYL-GRFDAAWADPSDPDSIADALALALDPA-RRPALRAAGPELAARYTWDASARAHLEFYRR 373
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 274-357 1.10e-03

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 40.85  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 274 DIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGlwaKTK------NAKDLSEKISLLLEDEKLRLNLAK 347
Cdd:PLN02871  333 DVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPDQEG---KTGflytpgDVDDCVEKLETLLADPELRERMGA 409

                          90
                  ....*....|
gi 1835265595 348 NAAQDALQYD 357
Cdd:PLN02871  410 AAREEVEKWD 419
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 2-366 3.39e-91

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 277.94  E-value: 3.39e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595   2 RIGFLSHAGASIYHFRMPIIKALKDRKDEVFVIVPQDEY-TQKLRDLGLKVIVYEFSRASLNPFVVLKNFFYLAKVLKNL 80
Cdd:cd03808     1 KILFIVNVDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKlSDELKELGVKVIDIPILRRGINPLKDLKALFKLYKLLKKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  81 NLDFIQSAAHKSNTFGILAAKWAKIPYRFALVEGLGSFYIDQGFKanlvRFVINSLYKLSFKFAHQFIFVNESNAEFMRN 160
Cdd:cd03808    81 KPDIVHCHTPKPGILGRLAARLAGVPKVIYTVHGLGFVFTEGKLL----RLLYLLLEKLALLFTDKVIFVNEDDRDLAIK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 161 LGL-KENKICVIKSVGINLKKFFPIYVEsekkelfwknlNIDKKPIVLMIARALWHKGVKEFYESATMLKDKAN---FVL 236
Cdd:cd03808   157 KGIiKKKKTVLIPGSGVDLDRFQYSPES-----------LPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPnvrFLL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 237 VGGRDENPSCASL--EFLNSGAVHYLGARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNA 314
Cdd:cd03808   226 VGDGELENPSEILieKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDG 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1835265595 315 YDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDALQ-YDENIIAQRYL 366
Cdd:cd03808   306 VNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEkFDEEKVVNKLL 358
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-369 7.52e-45

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 158.08  E-value: 7.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595   2 RIGFLSH-----AGASIYHFRMpIIKALKDRKDEVFVIVPQDEYTQKLRDLGLKVIvyefsraslNPFVVLKNFFYLAKV 76
Cdd:cd03801     1 KILLLSPelpppVGGAERHVRE-LARALAARGHDVTVLTPADPGEPPEELEDGVIV---------PLLPSLAALLRARRL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  77 LKNLNL-------DFIQSAAHKSNTFGILAAKWAKIPYRFAL-VEGLGSFYIDQGFKANLVRFVINSLyklsfKFAHQFI 148
Cdd:cd03801    71 LRELRPllrlrkfDVVHAHGLLAALLAALLALLLGAPLVVTLhGAEPGRLLLLLAAERRLLARAEALL-----RRADAVI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 149 FVNESNAEFMRNL-GLKENKICVIkSVGINLKKFFPiyvesekkELFWKNLNIDKKPIVLMIARALWHKGVKEFYESATM 227
Cdd:cd03801   146 AVSEALRDELRALgGIPPEKIVVI-PNGVDLERFSP--------PLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAK 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 228 LKDKAN---FVLVGGRDENPSC-ASLEFLNSGAVHYLGARS--DIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVV 301
Cdd:cd03801   217 LLRRGPdvrLVIVGGDGPLRAElEELELGLGDRVRFLGFVPdeELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVA 296

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835265595 302 SDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDALQ-YDENIIAQRYLKLY 369
Cdd:cd03801   297 TDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAErFSWERVAERLLDLY 365
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 202-352 2.50e-38

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 134.71  E-value: 2.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 202 KKPIVLMIARALWHKGVKEFYESATMLK---DKANFVLVGG--RDENPSCASLEFLNSGAVHYLGARS--DIVELLQNCD 274
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKeknPNLKLVIAGDgeEEKRLKKLAEKLGLGDNVIFLGFVSdeDLPELLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835265595 275 IFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQD 352
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 30-370 2.21e-33

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 127.43  E-value: 2.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  30 EVFVIVPQDEYTQKLRDLGLKVIVyefsrASLNPFVVLKNFFYLAKVLKNLNLDFIQSAAHKSNTFGILAAKWAKIPYRF 109
Cdd:cd03807    33 VVISLTGDGVLGEELLAAGVPVVC-----LGLSSGKDPGVLLRLAKLIRKRNPDVVHTWMYHADLIGGLAAKLAGGVKVI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 110 ALVEGLGSFYidqgfkaNLVRFVInSLYKLSFKFAHQFIFVNESNAEFMRNLGLKENKICVIKSvGINLKKFFPiyvESE 189
Cdd:cd03807   108 WSVRSSNIPQ-------RLTRLVR-KLCLLLSKFSPATVANSSAVAEFHQEQGYAKNKIVVIYN-GIDLFKLSP---DDA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 190 KKELFWKNLNIDKKPIVLMIARALW-HKGVKEFYESATMLKDK---ANFVLVGGRDENPSCASL--EFLNSGAVHYLGAR 263
Cdd:cd03807   176 SRARARRRLGLAEDRRVIGIVGRLHpVKDHSDLLRAAALLVEThpdLRLLLVGRGPERPNLERLllELGLEDRVHLLGER 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 264 SDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKtKNAKDLSEKISLLLEDEKLRL 343
Cdd:cd03807   256 SDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDGTGFLVPA-GDPQALADAIRALLEDPEKRA 334

                         330       340
                  ....*....|....*....|....*...
gi 1835265595 344 NLAKNAAQD-ALQYDENIIAQRYLKLYD 370
Cdd:cd03807   335 RLGRAARERiANEFSIDAMVRRYETLYY 362
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 7-372 8.35e-29

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 115.17  E-value: 8.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595   7 SHAGASIYHFRMpiIKALKDRKDEVFVIVPQDEYTQKLRDL--GLKVIVYEFSRASLNPF--VVLKNFFYLAKVLKNLNL 82
Cdd:cd03798    12 NSPGRGIFVRRQ--VRALSRRGVDVEVLAPAPWGPAAARLLrkLLGEAVPPRDGRRLLPLkpRLRLLAPLRAPSLAKLLK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  83 DFIQSA-----AHKSNTFGILAAK---WAKIPYrfaLVEGLGSfYIDQGFKANLVRFVINSLYKLsfkfAHQFIFVNESN 154
Cdd:cd03798    90 RRRRGPpdlihAHFAYPAGFAAALlarLYGVPY---VVTEHGS-DINVFPPRSLLRKLLRWALRR----AARVIAVSKAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 155 AEFMRNLGLKENKICVIKSvGINLKKFFPIYVESEKKElfwknlnidKKPIVLMIARALWHKGVKEFYESATMLKDKAN- 233
Cdd:cd03798   162 AEELVALGVPRDRVDVIPN-GVDPARFQPEDRGLGLPL---------DAFVILFVGRLIPRKGIDLLLEAFARLAKARPd 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 234 --FVLVG-GRDENPSCASLEFLNSGA-VHYLGARS--DIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGC 307
Cdd:cd03798   232 vvLLIVGdGPLREALRALAEDLGLGDrVTFTGRLPheQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGI 311

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835265595 308 VEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDALQYDENIIAQRYLKLYDRV 372
Cdd:cd03798   312 PEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
203-338 1.95e-28

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 107.98  E-value: 1.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 203 KPIVLMIAR-ALWHKGVKEFYESATMLKDK---ANFVLVGGRDEnpscASLEFLNSG---AVHYLGARSDIVELLQNCDI 275
Cdd:pfam13692   1 RPVILFVGRlHPNVKGVDYLLEAVPLLRKRdndVRLVIVGDGPE----EELEELAAGledRVIFTGFVEDLAELLAAADV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835265595 276 FVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNaYDGLWAKTKNAKDLSEKISLLLED 338
Cdd:pfam13692  77 FVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDG-ENGLLVPPGDPEALAEAILRLLED 138
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 20-351 2.70e-28

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 113.22  E-value: 2.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  20 IIKALKDRKDEVFVIVPQDEYTQKLRDLGLKVIVYEFsraslNPFVVLKNFFYLAKVLKNLNLDFIQSAAHKSNTFGILA 99
Cdd:cd03819    20 LARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLKV-----PLLRALLGNVRLARLIRRERIDLIHAHSRAPAWLGWLA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 100 AKWAKIPYRFAlVEGLGSFYIDQGFKANLVRFvinslyklsfkFAHQFIFVNESNAEFM-RNLGLKENKICVIKSvGINL 178
Cdd:cd03819    95 SRLTGVPLVTT-VHGSYLATYHPKDFALAVRA-----------RGDRVIAVSELVRDHLiEALGVDPERIRVIPN-GVDT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 179 KKFFPiyvESEKKELFWKNLNiDKKPIVLMIARaLWH-KGVKEFYESATMLKDKANFVL--VGGRDENPSCASL--EFLN 253
Cdd:cd03819   162 DRFPP---EAEAEERAQLGLP-EGKPVVGYVGR-LSPeKGWLLLVDAAAELKDEPDFRLlvAGDGPERDEIRRLveRLGL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 254 SGAVHYLGARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKIS 333
Cdd:cd03819   237 RDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALADAIR 316

                         330
                  ....*....|....*...
gi 1835265595 334 LLLEDEKLRLNLAKNAAQ 351
Cdd:cd03819   317 AAKLLPEAREKLQAAAAL 334
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 20-358 4.23e-28

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 112.84  E-value: 4.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  20 IIKALKDRKDEVFVIVPQDE-YTQKLRDLGLKVIVYEFSRASLNPFVVLKNFFYLAKVLKNLNLDFIQS-AAHKSNTFGI 97
Cdd:cd03811    21 LANALDKRGYDVTLVLLRDEgDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILKRAKPDVVISfLGFATYIVAK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  98 LAAKWAKIPYRfalvegLGSFYIDQGFKANLVrfvinSLYKLSFKFAHQFIFVNESNAE-FMRNLGLKENKICVIKSvGI 176
Cdd:cd03811   101 LAAARSKVIAW------IHSSLSKLYYLKKKL-----LLKLKLYKKADKIVCVSKGIKEdLIRLGPSPPEKIEVIYN-PI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 177 NLKKFFPiyvESEKKELFWKnlniDKKPIVLMIARALWHKGVKEFYESATMLKDK---ANFVLVGGRDENPSCASL-EFL 252
Cdd:cd03811   169 DIDRIRA---LAKEPILNEP----EDGPVILAVGRLDPQKGHDLLIEAFAKLRKKypdVKLVILGDGPLREELEKLaKEL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 253 N-SGAVHYLGARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGlWAKTKNAKDLSEK 331
Cdd:cd03811   242 GlAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENG-LLVPDGDAAALAG 320

                         330       340
                  ....*....|....*....|....*..
gi 1835265595 332 ISLLLEDEKLRLNLAKNAAQDALQYDE 358
Cdd:cd03811   321 ILAALLQKKLDAALRERLAKAQEAVFR 347
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 269-374 1.55e-26

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 102.38  E-value: 1.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 269 LLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKN 348
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                          90       100
                  ....*....|....*....|....*..
gi 1835265595 349 AAQDALQ-YDENIIAQRYLKLYDRVIK 374
Cdd:COG0438    97 ARERAEErFSWEAIAERLLALYEELLA 123
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 112-370 1.26e-24

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 104.72  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 112 VEGLGSFYIDQGFKANLVRFvINSLYKLSFKFAHQFIFVNESNAEFMRNLGLKENKICVIKSvGINLKKFFPIYVESEKK 191
Cdd:cd03813   214 IEILQSTWIMGYIKKLWIRF-FERLGKLAYQQADKIISLYEGNRRRQIRLGADPDKTRVIPN-GIDIQRFAPAREERPEK 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 192 ElfwknlnidkKPIVLMIARALWHKGVKEFYESATMLKDK---ANFVLVGGRDENPS----C----ASLEFLNSgaVHYL 260
Cdd:cd03813   292 E----------PPVVGLVGRVVPIKDVKTFIRAFKLVRRAmpdAEGWLIGPEDEDPEyaqeCkrlvASLGLENK--VKFL 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 261 GaRSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYD-----GLWAKTKNAKDLSEKISLL 335
Cdd:cd03813   360 G-FQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIYGADDalgqaGLVVPPADPEALAEALIKL 438

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1835265595 336 LEDEKLRLNLAKNAAQDALQY--DENIIAqRYLKLYD 370
Cdd:cd03813   439 LRDPELRQAFGEAGRKRVEKYytLEGMID-SYRKLYL 474
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 147-372 6.20e-24

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 101.25  E-value: 6.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 147 FIFVNESN---AEFMRNLGLKENKICVIKSvGINLKKFFPIYVESEKKELfwknlNIDK-KPIVLMIARAL--WHKGVKE 220
Cdd:cd03825   139 LTIVAPSRwlaDMVRRSPLLKGLPVVVIPN-GIDTEIFAPVDKAKARKRL-----GIPQdKKVILFGAESVtkPRKGFDE 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 221 FYESATMLKDKANFVLV--GGRDENpscaslEFLNSGAVHYLGARSD---IVELLQNCDIFVLPSYKEGFPVSVLEAKAC 295
Cdd:cd03825   213 LIEALKLLATKDDLLLVvfGKNDPQ------IVILPFDIISLGYIDDdeqLVDIYSAADLFVHPSLADNLPNTLLEAMAC 286

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835265595 296 GKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDA-LQYDENIIAQRYLKLYDRV 372
Cdd:cd03825   287 GTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAeNHFDQRVQAQRYLELYKDL 364
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 49-365 7.70e-23

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 98.08  E-value: 7.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  49 LKVIVYEFSRASLNPFvvlKNFFYLAKVLKNLNLDFIQSAAHKSNTFgiLAAKWAKIPYrfaLVEGLGSFYIDQGFKANL 128
Cdd:cd03820    58 LGDRKYSHFKLLLKYF---KKVRRLRKYLKNNKPDVVISFRTSLLTF--LALIGLKSKL---IVWEHNNYEAYNKGLRRL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 129 VRFvinslyKLSFKFAHQFIFVNEsnAEFMRNLGLKENKICVIKsvgiNLKKFfpiyvesekkELFWKNLNIDKKpIVLM 208
Cdd:cd03820   130 LLR------RLLYKRADKIVVLTE--ADKLKKYKQPNSNVVVIP----NPLSF----------PSEEPSTNLKSK-RILA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 209 IARALWHKGVKEFYESATMLKDKA---NFVLVG-GRDEnpscASLEFLN-----SGAVHYLGARSDIVELLQNCDIFVLP 279
Cdd:cd03820   187 VGRLTYQKGFDLLIEAWALIAKKHpdwKLRIYGdGPER----EELEKLIdklglEDRVKLLGPTKNIAEEYANSSIFVLS 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 280 SYKEGFPVSVLEAKACGKAIVVSDCE-GCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDALQYDE 358
Cdd:cd03820   263 SRYEGFPMVLLEAMAYGLPIISFDCPtGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSI 342


                  ....*..
gi 1835265595 359 NIIAQRY 365
Cdd:cd03820   343 EKIIKQW 349
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 20-367 4.32e-21

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 93.20  E-value: 4.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  20 IIKALKDRKDEVFVIVPQDEYTQKLRDLGLKVIVYEFSRASLNPFVVLKNFFYLAKVLKNLNLDFIQSAahkSNTFGILA 99
Cdd:cd03809    23 LLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLLHSP---HNTAPLLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 100 AKwAK--------IPYRFALveglgsfyidqgFKANLVRFVINSLYKLSFKFAHQFIFVNESNA-EFMRNLGLKENKICV 170
Cdd:cd03809   100 KG-CPqvvtihdlIPLRYPE------------FFPKRFRLYYRLLLPISLRRADAIITVSEATRdDIIKFYGVPPEKIVV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 171 IKSvGINlkkffPIYVESEKKELFwKNLNIDKKPIVLMIARALWHKGVKEFYESATMLKDKA---NFVLVGGR---DENP 244
Cdd:cd03809   167 IPL-GVD-----PSFFPPESAAVL-IAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGgdlKLVIVGGKgweDEEL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 245 SCASLEFLNSGAVHYLG--ARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAydGLWAKT 322
Cdd:cd03809   240 LDLVKKLGLGGRVRFLGyvSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDA--ALYFDP 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1835265595 323 KNAKDLSEKISLLLEDEKLRLNLAKNAAQDALQYDENIIAQRYLK 367
Cdd:cd03809   318 LDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 153-365 5.36e-21

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 92.72  E-value: 5.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 153 SNAEFMRNLglkENKICVIKSvGINLKKFfPIYVESEKKelfwKNLNIDKKPIVLMIARALWHKGVKEFYESATMLKdkA 232
Cdd:cd03795   150 ETSPTLREF---KNKVRVIPL-GIDKNVY-NIPRVDFEN----IKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYLN--Y 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 233 NFVLVGGRDENPSCASL-EFLNSGAVHYLGARSD--IVELLQNCDIFVLPSY--KEGFPVSVLEAKACGKAIVVSDCEGC 307
Cdd:cd03795   219 PIVIGGEGPLKPDLEAQiELNLLDNVKFLGRVDDeeKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVISTNIGTG 298

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835265595 308 VEAIS-NAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQdalQYDENIIAQRY 365
Cdd:cd03795   299 VPYVNnNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKK---RFEELFTAEKM 354
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 155-366 2.81e-19

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 88.45  E-value: 2.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 155 AEFMRNL-GLKENKICVIkSVGINLKKFFPIyvesEKKELFWKNLNID-KKPIVLMIARALWHKG----VKEFYESATmL 228
Cdd:cd03800   175 ADELISLyGADPSRINVV-PPGVDLERFFPV----DRAEARRARLLLPpDKPVVLALGRLDPRKGidtlVRAFAQLPE-L 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 229 KDKANFVLVGG-RDENPSCASLE-------FLNSGAVHYLGA--RSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKA 298
Cdd:cd03800   249 RELANLVLVGGpSDDPLSMDREElaelaeeLGLIDRVRFPGRvsRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTP 328

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835265595 299 IVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDALQ-YDENIIAQRYL 366
Cdd:cd03800   329 VVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAhYTWESVADQLL 397
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 22-372 4.27e-18

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 84.64  E-value: 4.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  22 KALKDRKDEVFVIVPQdeYTQKLRDLGLKVIVYEFS--RASLNPFVVLKNFFYLAKVLKNLNLDFIQSaaHKSNTFGILA 99
Cdd:cd03817    25 RALEKRGHEVYVITPS--DPGAEDEEEVVRYRSFSIpiRKYHRQHIPFPFKKAVIDRIKELGPDIIHT--HTPFSLGKLG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 100 AKWA---KIP----YRFALVEGLGSFYIDQGFKANLVRFVINSLYKlsfkFAHQFIFVNESNAEFMRNLGLKeNKICVIk 172
Cdd:cd03817   101 LRIArklKIPivhtYHTMYEDYLHYIPKGKLLVKAVVRKLVRRFYN----HTDAVIAPSEKIKDTLREYGVK-GPIEVI- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 173 SVGINLKKFFPIYVESEKKELFWKnlniDKKPIVLMIARALWHKGVKEFYESATMLKDKAN--FVLVGgrdENPSCASLE 250
Cdd:cd03817   175 PNGIDLDKFEKPLNTEERRKLGLP----PDEPILLYVGRLAKEKNIDFLLRAFAELKKEPNikLVIVG---DGPEREELK 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 251 FLN-----SGAVHYLGA--RSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGlWAKTK 323
Cdd:cd03817   248 ELArelglADKVIFTGFvpREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENG-FLFEP 326

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1835265595 324 NAKDLSEKISLLLEDEKLRLNLAKNAAQDALQYDeniIAQRYLKLYDRV 372
Cdd:cd03817   327 NDETLAEKLLHLRENLELLRKLSKNAEISAREFA---FAKSVEKLYEEV 372
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 123-366 4.42e-18

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 84.70  E-value: 4.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 123 GFKANLVRFVINSLYKLSFKFAHQFIFVNESNAEFMRNLGLKENKICVIKSvGINLKKFFPIYVESEKKElfwknlNIDK 202
Cdd:cd03794   143 VLKKGSLLKLLKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPN-WADLEEFKPPPKDELRKK------LGLD 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 203 KPIVLMIARALWHK-GVKEFYESATMLKDKAN--FVLVGGRDENPSCASLEFLNSGA-VHYLGA--RSDIVELLQNCDIF 276
Cdd:cd03794   216 DKFVVVYAGNIGKAqGLETLLEAAERLKRRPDirFLFVGDGDEKERLKELAKARGLDnVTFLGRvpKEEVPELLSAADVG 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 277 VLP-----SYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQ 351
Cdd:cd03794   296 LVPlkdnpANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRE 375

                         250
                  ....*....|....*.
gi 1835265595 352 DAL-QYDENIIAQRYL 366
Cdd:cd03794   376 LAEeKFSREKLADRLL 391
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 148-366 2.30e-16

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 79.72  E-value: 2.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 148 IFVNESNAEFMRNLGLkENKICVIKSvGINLKKFFPiyvESEKKELFWKnlnIDKKPIVLMIARALWHKGVKEFYESATM 227
Cdd:cd03821   157 HFTSEQEADELRRFGL-EPPIAVIPN-GVDIPEFDP---GLRDRRKHNG---LEDRRIILFLGRIHPKKGLDLLIRAARK 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 228 LKDKAN---FVLVGGRDENPSCA---SLEFLNSGAVHYLGARSD--IVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAI 299
Cdd:cd03821   229 LAEQGRdwhLVIAGPDDGAYPAFlqlQSSLGLGDRVTFTGPLYGeaKWALYASADLFVLPSYSENFGNVVAEALACGLPV 308

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835265595 300 VVSD-CEGCveAISNAYDGLWAKTkNAKDLSEKISLLLED----EKLRLNlAKNAAQDALQYDENIIAQRYL 366
Cdd:cd03821   309 VITDkCGLS--ELVEAGCGVVVDP-NVSSLAEALAEALRDpadrKRLGEM-ARRARQVEENFSWEAVAGQLG 376
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 229-372 8.19e-16

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 77.78  E-value: 8.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 229 KDKANFVLVG-GRDENPSCASLEFLN-SGAVHYLGARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEG 306
Cdd:cd04962   224 KIPAKLLLVGdGPERVPAEELARELGvEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGG 303

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835265595 307 CVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDAL-QYDENIIAQRYLKLYDRV 372
Cdd:cd04962   304 IPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAeRFDPERIVPQYEAYYRRL 370
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 175-363 1.05e-15

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 77.72  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 175 GINLKKFFPiyveSEKKELFWKNLNIDKKPIVLMIARALWHKGVKEFYESATMLKDKANF--VLVGgrdENPSCASLEFL 252
Cdd:cd03814   174 GVDTELFHP----SRRDAALRRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVrlVVVG---DGPARAELEAR 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 253 NSgAVHYLGARS--DIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSE 330
Cdd:cd03814   247 GP-DVIFTGFLTgeELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAA 325

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1835265595 331 KISLLLEDEKLRLNLAKNAAQDALQYD-ENIIAQ 363
Cdd:cd03814   326 ALRALLEDPELRRRMAARARAEAERYSwEAFLDN 359
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 16-303 1.97e-14

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 73.86  E-value: 1.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  16 FRMPIIKALKDRKDEVFVIV---PQDEYTQKLRDLGLKVIVYEFsraslNPFVVLKNFFYLAKVLKNLNLDFIQSAAHKS 92
Cdd:cd03812    17 FLMNLYRKLDKSKIEFDFLAtsdDKGEYDEELEELGGKIFYIPP-----KKKNIIKYFIKLLKLIKKEKYDIVHVHGSSS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  93 NTFGILAAKWAKIPYRFAlveglgSFYIDQGFKANLVRFVINSLYKLSFKFAHQFIFVNESNAEFMrnLGLKENKICVIK 172
Cdd:cd03812    92 NGIILLLAAKAGVPVRIA------HSHNTKDSSIKLRKIRKNVLKKLIERLSTKYLACSEDAGEWL--FGEVENGKFKVI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 173 SVGINLKKF-FPIYVESEKKELfwknLNIDKKPIVLMIARALWHKG----VKEFYEsatMLKDKANF--VLVG-GRDENP 244
Cdd:cd03812   164 PNGIDIEKYkFNKEKRRKRRKL----LILEDKLVLGHVGRFNEQKNhsflIDIFEE---LKKKNPNVklVLVGeGELKEK 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835265595 245 --SCASLEFLNSgAVHYLGARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSD 303
Cdd:cd03812   237 ikEKVKELGLED-KVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSD 296
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 215-369 2.03e-14

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 73.52  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 215 HKGVKEFYESATMLKDK-ANFVLVGGRDENPsCASLEFLnsGAVHYLGA--RSDIVELLQNCDIFVLPS-YKEGFPVSVL 290
Cdd:cd03823   203 EKGIDLLVEAFKRLPREdIELVIAGHGPLSD-ERQIEGG--RRIAFLGRvpTDDIKDFYEKIDVLVVPSiWPEPFGLVVR 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835265595 291 EAKACGKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLrLNLAKNAAQDALQYDENiiAQRYLKLY 369
Cdd:cd03823   280 EAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPAL-LERLRAGAEPPRSTESQ--AEEYLKLY 355
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 190-318 4.36e-14

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 70.90  E-value: 4.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 190 KKELFWKNLNIDKKPIVLMIARALWHKGVKEFYESATMLK---DKANFVLVGGRDENP---SCASLEFLNSGAVHYLG-- 261
Cdd:cd01635    97 ELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKarlPDLVLVLVGGGGEREeeeALAAALGLLERVVIIGGlv 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835265595 262 ARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGL 318
Cdd:cd01635   177 DDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 257-369 3.14e-11

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 64.00  E-value: 3.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 257 VHYLGARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLwaKTKNAKDLSEKIS-LL 335
Cdd:cd04951   247 VILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHNYVV--PVSDPQLLAEKIKeIF 324

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1835265595 336 LEDEKLRLNLAKNAAQDALQYDENIIAQRYLKLY 369
Cdd:cd04951   325 DMSDEERDILGNKNEYIAKNFSINTIVNEWERLY 358
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 145-350 2.18e-10

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 61.31  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 145 HQFIFVneSNAEFMRN----LGLKENKICVIkSVGINLKKFFPIYVESEKkelfwknlnidkkPIVLMIARALWHKGVKE 220
Cdd:cd05844   143 PAALFV--AVSGFIRDrllaRGLPAERIHVH-YIGIDPAKFAPRDPAERA-------------PTILFVGRLVEKKGCDV 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 221 FYESATMLKDK---ANFVLVGgrdENPSCASLEFLNSGA--VHYLGA--RSDIVELLQNCDIFVLPSY------KEGFPV 287
Cdd:cd05844   207 LIEAFRRLAARhptARLVIAG---DGPLRPALQALAAALgrVRFLGAlpHAEVQDWMRRAEIFCLPSVtaasgdSEGLGI 283

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835265595 288 SVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAA 350
Cdd:cd05844   284 VLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAAR 346
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
20-171 1.20e-09

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 56.77  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  20 IIKALKDRKDEVFVIVPQDEYTQKLRDLGLKVIVYEFSRASLNPFVVLKNFFYLAKVLKNLNLDFIQSAAHKSNTFGILA 99
Cdd:pfam13439  10 LARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSPFPLGLAALA 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835265595 100 AKWA-KIPyrfaLVE---GLGSFYIDQGFKANLVRFVINSLYKLSFKFAHQFIFVNESNAEFMR-NLGLKENKICVI 171
Cdd:pfam13439  90 ARLRlGIP----LVVtyhGLFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRrLYGVPPEKIRVI 162
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 175-369 1.56e-09

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 58.94  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 175 GINLKKFFPiyVESEKKELFwknlnIDKKPIVLMIARALWHKGVKEFYESATMLKDK---ANFVLVGGRDenPSCASLEf 251
Cdd:cd03822   166 GVPEVPQDP--TTALKRLLL-----PEGKKVILTFGFIGPGKGLEILLEALPELKAEfpdVRLVIAGELH--PSLARYE- 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 252 lnsgAVHYLGARS-------------------DIVELLQNCDIFVLPSYKEGFPVS--VLEAKACGKAIVVSDCEGcVEA 310
Cdd:cd03822   236 ----GERYRKAAIeelglqdhvdfhnnflpeeEVPRYISAADVVVLPYLNTEQSSSgtLSYAIACGKPVISTPLRH-AEE 310

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835265595 311 ISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDALQYDENIIAQRYLKLY 369
Cdd:cd03822   311 LLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLF 369
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 232-371 1.64e-08

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 55.87  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 232 ANFVLVGG---------RDENPSCASLEFLNSGAVHYLG--ARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIV 300
Cdd:TIGR04047 225 AQLVIAGGatlfdydayRREFRARAAELGVDPGPVVITGpvPDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVV 304

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835265595 301 VSDCEGCVEAIsNAYDGLWAKTKNAKDLSEKISLLLEDEkLRLNLAKNAAQDALQYDENIIAQRYLKLYDR 371
Cdd:TIGR04047 305 ASDIAPFTEYL-GRFDAAWADPSDPDSIADALALALDPA-RRPALRAAGPELAARYTWDASARAHLEFYRR 373
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 204-369 2.19e-07

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 52.37  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 204 PIVLMIARALW-HKGVKEFYESATML---KDKANFVLVGGRD-----ENPSCASL--EFLNSGA-----VHYLG--ARSD 265
Cdd:cd03818   214 PVITYVARNLEpYRGFHVFMRALPRIqarRPDARVVVVGGDGvsygsPPPDGGSWkqKMLAELGvdlerVHFVGkvPYDQ 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 266 IVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNL 345
Cdd:cd03818   294 YVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAAL 373

                         170       180
                  ....*....|....*....|....
gi 1835265595 346 AKNAAQDALQYDeniIAQRYLKLY 369
Cdd:cd03818   374 RRAARRTVERSD---SLDVCLARY 394
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 160-361 1.05e-06

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 50.14  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 160 NLGLKENKIcVIKSVGINLKKFfpiyvesekkELFWKNLNIDKKPIVLMIARALWHKGVKEFYESATMLKDK-ANF---V 235
Cdd:cd03799   142 ALGCDEKKI-IVHRSGIDCNKF----------RFKPRYLPLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKyPNIeyqI 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 236 LVGGRDENPSCASLEFLNSG-AVHYLGARS--DIVELLQNCDIFVLPSY------KEGFPVSVLEAKACGKAIVVSDCEG 306
Cdd:cd03799   211 IGDGDLKEQLQQLIQELNIGdCVKLLGWKPqeEIIEILDEADIFIAPSVtaadgdQDGPPNTLKEAMAMGLPVISTEHGG 290

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1835265595 307 CVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNA-AQDALQYDENII 361
Cdd:cd03799   291 IPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGrARVEEEYDINKL 346
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
20-171 8.02e-06

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 45.47  E-value: 8.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595  20 IIKALKDRKDEVFVIVPQDEY-TQKLRDLGLKVIVYEFSRASLnPFVVLKNFFYLAKVLKNLNLDFIQSAAHKSNTFGIL 98
Cdd:pfam13579  10 LARALAALGHEVRVVTPGGPPgRPELVGDGVRVHRLPVPPRPS-PLADLAALRRLRRLLRAERPDVVHAHSPTAGLAARL 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835265595  99 AAKWAKIPYRFALVEGLgsFYIDQGFKANLVRFvinsLYKLSFKFAHQFIFVNESNAEFMRNLGLKENKICVI 171
Cdd:pfam13579  89 ARRRRGVPLVVTVHGLA--LDYGSGWKRRLARA----LERRLLRRADAVVVVSEAEAELLRALGVPAARVVVV 155
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 257-363 2.11e-05

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 45.76  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 257 VHYLGARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCE-GCVEAISNAYDGLWAKTKNAKDLSEKISLL 335
Cdd:cd04949   219 VFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIEL 298

                          90       100
                  ....*....|....*....|....*....
gi 1835265595 336 LEDEKLRLNLAKNAAQDALQY-DENIIAQ 363
Cdd:cd04949   299 LNDPEKLQQFSEESYKIAEKYsTENVMEK 327
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 196-372 1.86e-04

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 43.08  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 196 KNLNID-KKPIVLMIARALWHKGVKEFYESATMLKDKAN---FVLVG-GRDENPScASLEF-------LNSGAVHYL--- 260
Cdd:cd03792   189 KPFVIDpERPYILQVARFDPSKDPLGVIDAYKLFKRRAEepqLVICGhGAVDDPE-GSVVYeevmeyaGDDHDIHVLrlp 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 261 GARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGlWAKTKNAKDlSEKISLLLEDEK 340
Cdd:cd03792   268 PSDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETG-FLVNSVEGA-AVRILRLLTDPE 345

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835265595 341 LRLNLAKNAAQDAL-QYDENIIAQRYLKLYDRV 372
Cdd:cd03792   346 LRRKMGLAAREHVRdNFLITGNLRAWLYLIAKL 378
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
275-356 2.43e-04

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 39.51  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 275 IFVLPSYKEGFP-VSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKtkNAKDLSEKISLLLEDEKLRLNLAKNAAQDA 353
Cdd:pfam13524   1 IVLNPSRRPDSPnMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERV 78


                  ...
gi 1835265595 354 LQY 356
Cdd:pfam13524  79 LAE 81
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 257-318 1.04e-03

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 40.91  E-value: 1.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835265595 257 VHYLG--ARSDIVELLQN--CDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGL 318
Cdd:cd04946   285 VNFTGevSNKEVKQLYKEndVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGL 350
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 274-357 1.10e-03

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 40.85  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 274 DIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGlwaKTK------NAKDLSEKISLLLEDEKLRLNLAK 347
Cdd:PLN02871  333 DVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPDQEG---KTGflytpgDVDDCVEKLETLLADPELRERMGA 409

                          90
                  ....*....|
gi 1835265595 348 NAAQDALQYD 357
Cdd:PLN02871  410 AAREEVEKWD 419
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
6-151 2.09e-03

Glycosyl transferase 4-like;


Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 38.07  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595   6 LSHAGASIyhFRMPIIKALKDRKDEVFVIVPQDEYTQKLRDLGLKVIVYEFSRASLNPFVvlkNFFYLAKVLKNLNLDFI 85
Cdd:pfam13477   4 LLANADSI--HTLRWADALADRGYDVHVISSKGPAKDELIAEGIHVHRLKVPRKGPLGYL---KAFRLKKLIKKIKPDVV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835265595  86 QSAAHKS-NTFGILAAKWAK-IPYrfaLVEGLGSFYIDQGFKANLVRFvinsLYKLSFKFAHQFIFVN 151
Cdd:pfam13477  79 HVHYAKPyGLLAGLAARLSGfPPV---VLSAWGLDVYKFPNKSRLKKL----LLKLNLKKATLIISTS 139
PHA01630 PHA01630
putative group 1 glycosyl transferase
 265-322 3.37e-03

putative group 1 glycosyl transferase


Pssm-ID: 164861  Cd Length: 331  Bit Score: 39.00  E-value: 3.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835265595 265 DIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKT 322
Cdd:PHA01630  202 DIYSLFAGCDILFYPVRGGAFEIPVIEALALGLDVVVTEKGAWSEWVLSNLDVYWIKS 259
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
158-342 3.67e-03

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 38.92  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 158 MRNLGLKENKICVIksvginlkkFFPIyvesEKKELFWKNLNIDKKPIVLMIARALW--HKGVKEFYESATMLKDKANFV 235
Cdd:PRK09922  148 MMARGISAQRISVI---------YNPV----EIKTIIIPPPERDKPAVFLYVGRLKFegQKNVKELFDGLSQTTGEWQLH 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835265595 236 LVGGRDENPSCASL-EFLN-SGAVHYLGARSDIVELLQ----NCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDC-EGCV 308
Cdd:PRK09922  215 IIGDGSDFEKCKAYsRELGiEQRIIWHGWQSQPWEVVQqkikNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDCmSGPR 294

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1835265595 309 EAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLR 342
Cdd:PRK09922  295 DIIKPGLNGELYTPGNIDEFVGKLNKVISGEVKY 328
 
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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