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Conserved domains on  [gi|446622360|ref|WP_000699706|]
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MULTISPECIES: colanic acid biosynthesis fucosyltransferase WcaI [Enterobacteriaceae]

Protein Classification

glycosyltransferase WbuB( domain architecture ID 11499288)

glycosyltransferase WbuB involved in synthesis of O-antigen

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
wcaI TIGR04007
colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl ...
1-407 0e+00

colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species.


:

Pssm-ID: 188522 [Multi-domain]  Cd Length: 407  Bit Score: 873.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360    1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKREEGAATVWRCPLYVPKQPST 80
Cdd:TIGR04007   1 MKILVYGINYSPELTGIGKYTGEMVEWMARQGHEVRVITAPPYYPQWKVGENYSAWRYRREEGAATVWRCPLYVPKQPST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   81 LKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVA 160
Cdd:TIGR04007  81 LKRLLHLGSFALSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGMAGKGKGGKVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  161 QLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQHVADADVDALRNQLGLPDNKKIILYSGNI 240
Cdd:TIGR04007 161 RLASAFERSGLHNVDNVSTISRSMMNKAQEKGVAAEKVIFFPNWSEVARFRDVKDADVEALRSQLGLPDDKKIILYSGNI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  241 GEKQGLENVIEAADRLRDEPLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAADAV 320
Cdd:TIGR04007 241 GEKQGLENVIDAAARLTDRPWIFAIVGQGGGKARLEKMARERGLTNVKFFPLQPYEALPALLKMGDCHLVVQKRGAADAV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  321 LPSKLTNILAVGGNAVITAEAHTELGQLCETFPGIAVCVEPESVEALVAGIRQALLLPKHNTVAREYAERTLDKENVLRQ 400
Cdd:TIGR04007 321 LPSKLTNILAVGGNAVITAEPHTELGQLCITYPGIAVCVEPESVDALVAGIVQALAMPKNNTVAREYAERTLEKENVLRQ 400

                  ....*..
gi 446622360  401 FINDIRG 407
Cdd:TIGR04007 401 FIADIRG 407
 
Name Accession Description Interval E-value
wcaI TIGR04007
colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl ...
1-407 0e+00

colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species.


Pssm-ID: 188522 [Multi-domain]  Cd Length: 407  Bit Score: 873.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360    1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKREEGAATVWRCPLYVPKQPST 80
Cdd:TIGR04007   1 MKILVYGINYSPELTGIGKYTGEMVEWMARQGHEVRVITAPPYYPQWKVGENYSAWRYRREEGAATVWRCPLYVPKQPST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   81 LKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVA 160
Cdd:TIGR04007  81 LKRLLHLGSFALSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGMAGKGKGGKVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  161 QLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQHVADADVDALRNQLGLPDNKKIILYSGNI 240
Cdd:TIGR04007 161 RLASAFERSGLHNVDNVSTISRSMMNKAQEKGVAAEKVIFFPNWSEVARFRDVKDADVEALRSQLGLPDDKKIILYSGNI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  241 GEKQGLENVIEAADRLRDEPLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAADAV 320
Cdd:TIGR04007 241 GEKQGLENVIDAAARLTDRPWIFAIVGQGGGKARLEKMARERGLTNVKFFPLQPYEALPALLKMGDCHLVVQKRGAADAV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  321 LPSKLTNILAVGGNAVITAEAHTELGQLCETFPGIAVCVEPESVEALVAGIRQALLLPKHNTVAREYAERTLDKENVLRQ 400
Cdd:TIGR04007 321 LPSKLTNILAVGGNAVITAEPHTELGQLCITYPGIAVCVEPESVDALVAGIVQALAMPKNNTVAREYAERTLEKENVLRQ 400

                  ....*..
gi 446622360  401 FINDIRG 407
Cdd:TIGR04007 401 FIADIRG 407
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
1-407 0e+00

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 731.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKRE-EGAATVWRCPLYVPKQPS 79
Cdd:PRK10307   1 MKILVYGINYAPELTGIGKYTGEMAEWLAARGHEVRVITAPPYYPQWRVGEGYSAWRYRREsEGGVTVWRCPLYVPKQPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  80 TLKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMlglGLAGKGKGGKV 159
Cdd:PRK10307  81 GLKRLLHLGSFALSSFFPLLAQRRWRPDRVIGVVPTLFCAPGARLLARLSGARTWLHIQDYEVDAA---FGLGLLKGGKV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 160 AQLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQHVADADVDALRNQLGLPDNKKIILYSGN 239
Cdd:PRK10307 158 ARLATAFERSLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVARFQPVADADVDALRAQLGLPDGKKIVLYSGN 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 240 IGEKQGLENVIEAADRLRDEP-LIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAAD 318
Cdd:PRK10307 238 IGEKQGLELVIDAARRLRDRPdLIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLPALLKMADCHLLPQKAGAAD 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 319 AVLPSKLTNILAVGGNAVITAEAHTELGQLCEtfpGIAVCVEPESVEALVAGI----RQALLLPKHNTVAREYAERTLDK 394
Cdd:PRK10307 318 LVLPSKLTNMLASGRNVVATAEPGTELGQLVE---GIGVCVEPESVEALVAAIaalaRQALLRPKLGTVAREYAERTLDK 394
                        410
                 ....*....|...
gi 446622360 395 ENVLRQFINDIRG 407
Cdd:PRK10307 395 ENVLRQFIADIRG 407
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
2-402 2.58e-80

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: 252.26  E-value: 2.58e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWqvgenYSAWRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03794    1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLG-----RIFAGATETKDGIRVIRVKLGPIKKNGLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  82 KRLLHLGSFAVSSFFPLMAqRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVAQ 161
Cdd:cd03794   76 RRLLNYLSFALAALLKLLV-REERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLLKLLK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 162 LataFERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQhvaDADVDALRnQLGLPDNKKIILYSGNIG 241
Cdd:cd03794  155 K---LERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFK---PPPKDELR-KKLGLDDKFVVVYAGNIG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 242 EKQGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAA-DA 319
Cdd:cd03794  228 KAQGLETLLEAAERLKRRPDIrFLFVGDGDEKERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLVPLKDNPAnRG 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 320 VLPSKLTNILAVGGNAVITAEAHTELGQLCEtfpGIAVCVEPESVEALVAGIRQALLlpkhNTV--------AREYAERT 391
Cdd:cd03794  308 SSPSKLFEYMAAGKPILASDDGGSDLAVEIN---GCGLVVEPGDPEALADAILELLD----DPElrramgenGRELAEEK 380
                        410
                 ....*....|.
gi 446622360 392 LDKENVLRQFI 402
Cdd:cd03794  381 FSREKLADRLL 391
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
230-390 1.16e-23

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: 96.19  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  230 NKKIILYSGNIGEKQGLENVIEAADRLR--DEPLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPL-QSYDALPALLKMgd 306
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKekNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGfVSDEDLPELLKI-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  307 CHLVVQKrgAADAVLPSKLTNILAVGGnAVITAEAHTELGQLCETFPGiaVCVEPESVEALVAGIRQALLLPKHNTVARE 386
Cdd:pfam00534  79 ADVFVLP--SRYEGFGIVLLEAMACGL-PVIASDVGGPPEVVKDGETG--FLVKPNNAEALAEAIDKLLEDEELRERLGE 153

                  ....
gi 446622360  387 YAER 390
Cdd:pfam00534 154 NARK 157
 
Name Accession Description Interval E-value
wcaI TIGR04007
colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl ...
1-407 0e+00

colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species.


Pssm-ID: 188522 [Multi-domain]  Cd Length: 407  Bit Score: 873.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360    1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKREEGAATVWRCPLYVPKQPST 80
Cdd:TIGR04007   1 MKILVYGINYSPELTGIGKYTGEMVEWMARQGHEVRVITAPPYYPQWKVGENYSAWRYRREEGAATVWRCPLYVPKQPST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   81 LKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVA 160
Cdd:TIGR04007  81 LKRLLHLGSFALSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGMAGKGKGGKVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  161 QLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQHVADADVDALRNQLGLPDNKKIILYSGNI 240
Cdd:TIGR04007 161 RLASAFERSGLHNVDNVSTISRSMMNKAQEKGVAAEKVIFFPNWSEVARFRDVKDADVEALRSQLGLPDDKKIILYSGNI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  241 GEKQGLENVIEAADRLRDEPLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAADAV 320
Cdd:TIGR04007 241 GEKQGLENVIDAAARLTDRPWIFAIVGQGGGKARLEKMARERGLTNVKFFPLQPYEALPALLKMGDCHLVVQKRGAADAV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  321 LPSKLTNILAVGGNAVITAEAHTELGQLCETFPGIAVCVEPESVEALVAGIRQALLLPKHNTVAREYAERTLDKENVLRQ 400
Cdd:TIGR04007 321 LPSKLTNILAVGGNAVITAEPHTELGQLCITYPGIAVCVEPESVDALVAGIVQALAMPKNNTVAREYAERTLEKENVLRQ 400

                  ....*..
gi 446622360  401 FINDIRG 407
Cdd:TIGR04007 401 FIADIRG 407
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
1-407 0e+00

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 731.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKRE-EGAATVWRCPLYVPKQPS 79
Cdd:PRK10307   1 MKILVYGINYAPELTGIGKYTGEMAEWLAARGHEVRVITAPPYYPQWRVGEGYSAWRYRREsEGGVTVWRCPLYVPKQPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  80 TLKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMlglGLAGKGKGGKV 159
Cdd:PRK10307  81 GLKRLLHLGSFALSSFFPLLAQRRWRPDRVIGVVPTLFCAPGARLLARLSGARTWLHIQDYEVDAA---FGLGLLKGGKV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 160 AQLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQHVADADVDALRNQLGLPDNKKIILYSGN 239
Cdd:PRK10307 158 ARLATAFERSLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVARFQPVADADVDALRAQLGLPDGKKIVLYSGN 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 240 IGEKQGLENVIEAADRLRDEP-LIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAAD 318
Cdd:PRK10307 238 IGEKQGLELVIDAARRLRDRPdLIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLPALLKMADCHLLPQKAGAAD 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 319 AVLPSKLTNILAVGGNAVITAEAHTELGQLCEtfpGIAVCVEPESVEALVAGI----RQALLLPKHNTVAREYAERTLDK 394
Cdd:PRK10307 318 LVLPSKLTNMLASGRNVVATAEPGTELGQLVE---GIGVCVEPESVEALVAAIaalaRQALLRPKLGTVAREYAERTLDK 394
                        410
                 ....*....|...
gi 446622360 395 ENVLRQFINDIRG 407
Cdd:PRK10307 395 ENVLRQFIADIRG 407
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
2-402 2.58e-80

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: 252.26  E-value: 2.58e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWqvgenYSAWRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03794    1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLG-----RIFAGATETKDGIRVIRVKLGPIKKNGLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  82 KRLLHLGSFAVSSFFPLMAqRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVAQ 161
Cdd:cd03794   76 RRLLNYLSFALAALLKLLV-REERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLLKLLK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 162 LataFERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQhvaDADVDALRnQLGLPDNKKIILYSGNIG 241
Cdd:cd03794  155 K---LERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFK---PPPKDELR-KKLGLDDKFVVVYAGNIG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 242 EKQGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAA-DA 319
Cdd:cd03794  228 KAQGLETLLEAAERLKRRPDIrFLFVGDGDEKERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLVPLKDNPAnRG 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 320 VLPSKLTNILAVGGNAVITAEAHTELGQLCEtfpGIAVCVEPESVEALVAGIRQALLlpkhNTV--------AREYAERT 391
Cdd:cd03794  308 SSPSKLFEYMAAGKPILASDDGGSDLAVEIN---GCGLVVEPGDPEALADAILELLD----DPElrramgenGRELAEEK 380
                        410
                 ....*....|.
gi 446622360 392 LDKENVLRQFI 402
Cdd:cd03794  381 FSREKLADRLL 391
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
230-390 1.16e-23

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: 96.19  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  230 NKKIILYSGNIGEKQGLENVIEAADRLR--DEPLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPL-QSYDALPALLKMgd 306
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKekNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGfVSDEDLPELLKI-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  307 CHLVVQKrgAADAVLPSKLTNILAVGGnAVITAEAHTELGQLCETFPGiaVCVEPESVEALVAGIRQALLLPKHNTVARE 386
Cdd:pfam00534  79 ADVFVLP--SRYEGFGIVLLEAMACGL-PVIASDVGGPPEVVKDGETG--FLVKPNNAEALAEAIDKLLEDEELRERLGE 153

                  ....
gi 446622360  387 YAER 390
Cdd:pfam00534 154 NARK 157
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
15-204 4.28e-20

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 86.30  E-value: 4.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   15 TGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQvgenysawrykREEGAATVWRCPL-YVPKQPSTLKRLLHLGSFAvs 93
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPE-----------LVGDGVRVHRLPVpPRPSPLADLAALRRLRRLL-- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   94 sffplmaqRRWKPDRIIGVVPTLFctPGMRLLAKLSGARTVLHIQDYEVDamlglglagkGKGGKVAQLATAFERSGLHN 173
Cdd:pfam13579  68 --------RAERPDVVHAHSPTAG--LAARLARRRRGVPLVVTVHGLALD----------YGSGWKRRLARALERRLLRR 127
                         170       180       190
                  ....*....|....*....|....*....|.
gi 446622360  174 VDNVSTISRSMMNKAIEKGVAADNIIFFPNW 204
Cdd:pfam13579 128 ADAVVVVSEAEAELLRALGVPAARVVVVPNG 158
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
2-406 3.20e-19

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: 88.36  E-value: 3.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYypqwqvgenysawRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03801    1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADP-------------GEPPEELEDGVIVPLLPSLAALLRA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  82 KRLLHLGSFAVssffplmaqRRWKPDRIIgvVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKggkvaq 161
Cdd:cd03801   68 RRLLRELRPLL---------RLRKFDVVH--AHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRL------ 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 162 LATAFERsgLHNVDNVSTISRSMMNKAIEKGVA-ADNIIFFPNWSEIARFQhvadadvDALRNQLGLPDNKKIILYSGNI 240
Cdd:cd03801  131 LARAEAL--LRRADAVIAVSEALRDELRALGGIpPEKIVVIPNGVDLERFS-------PPLRRKLGIPPDRPVLLFVGRL 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 241 GEKQGLENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDChlvvqkrgaad 318
Cdd:cd03801  202 SPRKGVDLLLEALAKLLRRgpDVRLVIVGGDGPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADV----------- 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 319 AVLPSKLTNIlavgGNAVITAEAH------TELGQLCETFP--GIAVCVEPESVEALVAGIRQAL----LLPKHNTVARE 386
Cdd:cd03801  271 FVLPSRYEGF----GLVVLEAMAAglpvvaTDVGGLPEVVEdgEGGLVVPPDDVEALADALLRLLadpeLRARLGRAARE 346
                        410       420
                 ....*....|....*....|
gi 446622360 387 YAERTLDKENVLRQFINDIR 406
Cdd:cd03801  347 RVAERFSWERVAERLLDLYR 366
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
15-375 8.93e-18

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: 83.97  E-value: 8.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  15 TGIGKYTGEMVEWLAAQGHEVRVITAPPYYPqwqvgenySAWRYKREEGAATVWRCPLYVPKQPStlKRLLHLGSFAVSS 94
Cdd:cd03798   14 PGRGIFVRRQVRALSRRGVDVEVLAPAPWGP--------AAARLLRKLLGEAVPPRDGRRLLPLK--PRLRLLAPLRAPS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  95 FFPLMAQ-RRWKPDRI--IGVVPTLFctpGMRLLAKLSGARTVL-----HIQDYEVDamlglglagkgkggkvaQLATAF 166
Cdd:cd03798   84 LAKLLKRrRRGPPDLIhaHFAYPAGF---AAALLARLYGVPYVVtehgsDINVFPPR-----------------SLLRKL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 167 ERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQHVADAdvdalrnqLGLPDNKKIILYSGNIGEKQGL 246
Cdd:cd03798  144 LRWALRRAARVIAVSKALAEELVALGVPRDRVDVIPNGVDPARFQPEDRG--------LGLPLDAFVILFVGRLIPRKGI 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 247 ENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGLRN-MQFFPLQSYDALPALLKmgdchlvvqkrgAADA-VLP 322
Cdd:cd03798  216 DLLLEAFARLAKArpDVVLLIVGDGPLREALRALAEDLGLGDrVTFTGRLPHEQVPAYYR------------ACDVfVLP 283
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446622360 323 SkltniLAVG-GNAVITAEA------HTELGQLCE--TFPGIAVCVEPESVEALVAGIRQAL 375
Cdd:cd03798  284 S-----RHEGfGLVLLEAMAcglpvvATDVGGIPEvvGDPETGLLVPPGDADALAAALRRAL 340
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
26-390 7.16e-15

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: 75.39  E-value: 7.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  26 EWLAAQGHEVRVITapPYYPQWQVGENYSAWRYKREEGAATVWRCpLYVPKQPSTLKRLlhlgsfavssffplmaqRRWK 105
Cdd:cd03817   25 RALEKRGHEVYVIT--PSDPGAEDEEEVVRYRSFSIPIRKYHRQH-IPFPFKKAVIDRI-----------------KELG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 106 PDRI-------IGVVptlfctpGMRLlAKLSGARTV--LHIQdYEVDAmLGLGLAGKGKGGKVAQLATAFersgLHNVDN 176
Cdd:cd03817   85 PDIIhthtpfsLGKL-------GLRI-ARKLKIPIVhtYHTM-YEDYL-HYIPKGKLLVKAVVRKLVRRF----YNHTDA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 177 VSTISRSMMNKAIEKGVAaDNIIFFPNWSEIARFQHVADadvDALRNQLGLPDNKKIILYSGNIGEKQGLENVIEAADRL 256
Cdd:cd03817  151 VIAPSEKIKDTLREYGVK-GPIEVIPNGIDLDKFEKPLN---TEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAEL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 257 RDEPLIFA-IVGQGGGKARLEKMAQQRGL-RNMQFFPLQSYDALPALLKMGDCH----------LVVQKrgAADAVLPsk 324
Cdd:cd03817  227 KKEPNIKLvIVGDGPEREELKELARELGLaDKVIFTGFVPREELPEYYKAADLFvfasttetqgLVYLE--AMAAGLP-- 302
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446622360 325 ltnILAVGGNAVITAEAHTELGQLCETfpgiavcvEPESVEALVAGIRQAL-LLPKHNTVAREYAER 390
Cdd:cd03817  303 ---VVAAKDPAASELVEDGENGFLFEP--------NDETLAEKLLHLRENLeLLRKLSKNAEISARE 358
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
7-379 2.80e-10

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: 61.23  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   7 GINYSPE---LTGIGKYTGEMVEWLAAQGHEVRVITAPPYypqwqvgenysawryKREEGAATVWRCPLYVPKQPSTLKR 83
Cdd:cd03809    3 LIDGRSLaqrLTGIGRYTRELLKALAKNDPDESVLAVPPL---------------PGELLRLLREYPELSLGVIKIKLWR 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  84 LLHLgsfavssffplmaQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVAQLA 163
Cdd:cd03809   68 ELAL-------------LRWLQILLPKKDKPDLLHSPHNTAPLLLKGCPQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPI 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 164 TafersgLHNVDNVSTISRSMMNKAIEK-GVAADNIIFFPNwsEIARFQHVADADvDALRNQLGLPDnkKIILYSGNIGE 242
Cdd:cd03809  135 S------LRRADAIITVSEATRDDIIKFyGVPPEKIVVIPL--GVDPSFFPPESA-AVLIAKYLLPE--PYFLYVGTLEP 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 243 KQGLENVIEAADRLRDE--PLIFAIVGQGGGK-ARLEKMAQQRGLR-NMQFFPLQSYDALPALLKmgdchlvvqkrgAAD 318
Cdd:cd03809  204 RKNHERLLKAFALLKKQggDLKLVIVGGKGWEdEELLDLVKKLGLGgRVRFLGYVSDEDLPALYR------------GAR 271
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446622360 319 A-VLPSkltniLAVG-----------GNAVITA--EAHTELGqlcetfPGIAVCVEPESVEALVAGIRQALLLPK 379
Cdd:cd03809  272 AfVFPS-----LYEGfglpvleamacGTPVIASniSVLPEVA------GDAALYFDPLDPESIADAILRLLEDPS 335
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
164-395 9.50e-10

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: 59.69  E-value: 9.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 164 TAFERSGLHNVDNVSTISRSMMNKAIEKGVAADnIIFFPNWSEIARFqHVADADvdalRNQLGLPDNKKIILYSGNIGEK 243
Cdd:cd03821  143 HLIERRNLNNAALVHFTSEQEADELRRFGLEPP-IAVIPNGVDIPEF-DPGLRD----RRKHNGLEDRRIILFLGRIHPK 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 244 QGLENVIEAADRLRDEPL--IFAIVGQGGGkARLEKMAQQR--GLRNMQFFPLQSY-DALPALLKMGDCHlvvqkrgaad 318
Cdd:cd03821  217 KGLDLLIRAARKLAEQGRdwHLVIAGPDDG-AYPAFLQLQSslGLGDRVTFTGPLYgEAKWALYASADLF---------- 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 319 aVLPSKLTNI-------LAVGGNAVITAEAHtelgqLCETF-PGIAVCVEPEsVEALVAGIRQALLLPKHNTVAREYAER 390
Cdd:cd03821  286 -VLPSYSENFgnvvaeaLACGLPVVITDKCG-----LSELVeAGCGVVVDPN-VSSLAEALAEALRDPADRKRLGEMARR 358

                 ....*
gi 446622360 391 TLDKE 395
Cdd:cd03821  359 ARQVE 363
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
190-388 4.92e-08

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: 54.25  E-value: 4.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 190 EKGVAADNIIFFPNWSEIARFqHVADADVDALRNQLGLPDNKKIILYSGNIGEKQGLENVIEAADRLRDEP--LIFAIVG 267
Cdd:cd03807  150 EQGYAKNKIVVIYNGIDLFKL-SPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHpdLRLLLVG 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 268 QGGGKARLEKMAQQRGLRNMQFFPLQSYDaLPALLKmgdchlvvqkrgAADA-VLPSK---LTNILA------------- 330
Cdd:cd03807  229 RGPERPNLERLLLELGLEDRVHLLGERSD-VPALLP------------AMDIfVLSSRtegFPNALLeamacglpvvatd 295
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446622360 331 VGGNAVItaeahtelgqLCetfPGIAVCVEPESVEALVAGIRQALLLPKHNTVAREYA 388
Cdd:cd03807  296 VGGAAEL----------VD---DGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAA 340
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
8-379 5.21e-08

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: 54.28  E-value: 5.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   8 INYSPELTGIGKYTGEMVEWLAAQGHEVRVITAppyypqwqvgenysawrykreeGAATVWRCPLYVPKQPSTLKRLLHL 87
Cdd:cd03819    4 LTPALEIGGAETYILDLARALAERGHRVLVVTA----------------------GGPLLPRLRQIGIGLPGLKVPLLRA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  88 GSFAVSSFFPLmaqRRWKPDrIIGV---VPTLFCtpgmRLLAKLSGARTVLHIQDyevdamlglglagkgkGGKVAQLAT 164
Cdd:cd03819   62 LLGNVRLARLI---RRERID-LIHAhsrAPAWLG----WLASRLTGVPLVTTVHG----------------SYLATYHPK 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 165 AFERSGLHNVDNVSTISRSMMNKAIEK-GVAADNIIFFPNWSEIARFQHVADAdvdALRNQLGLPDNKKIILYSGNIGEK 243
Cdd:cd03819  118 DFALAVRARGDRVIAVSELVRDHLIEAlGVDPERIRVIPNGVDTDRFPPEAEA---EERAQLGLPEGKPVVGYVGRLSPE 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 244 QGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKMAQQRGLRNmQFFPLQSYDALPALlkMGDCHLVvqkrgaadaVLP 322
Cdd:cd03819  195 KGWLLLVDAAAELKDEPDFrLLVAGDGPERDEIRRLVERLGLRD-RVTFTGFREDVPAA--LAASDVV---------VLP 262
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446622360 323 SkLTNILavgGNAVITAEAH------TELGQLCETFPG--IAVCVEPESVEALVAGIRQALLLPK 379
Cdd:cd03819  263 S-LHEEF---GRVALEAMACgtpvvaTDVGGAREIVVHgrTGLLVPPGDAEALADAIRAAKLLPE 323
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
2-278 6.37e-08

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: 54.22  E-value: 6.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVIT-APPYYPQWQVGENYSAWRykreegaatvWRCPLY------V 74
Cdd:cd03814    1 RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVApGPFDEAESAEGRVVSVPS----------FPLPFYpeyrlaL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  75 PKQPSTLKR-------LLHLGSFAVSSFFPLMAQRRWKPDrIIGVVPTLFCTP----GMRLLAKLS---------GARTV 134
Cdd:cd03814   71 PLPRRVRRLikefqpdIIHIATPGPLGLAALRAARRLGLP-VVTSYHTDFPEYlsyyTLGPLSWLAwaylrwfhnPFDTT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 135 LhiqdyevdamlglglagkgkggkVAQLATAFERSGlHNVDNVSTISRsmmnkaiekGVaaDNIIFFPnwseiaRFQHva 214
Cdd:cd03814  150 L-----------------------VPSPSIARELEG-HGFERVRLWPR---------GV--DTELFHP------SRRD-- 186
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446622360 215 dadvDALRNQLGlPDNKKIILYSGNIGEKQGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKM 278
Cdd:cd03814  187 ----AALRRRLG-PPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVrLVVVGDGPARAELEAR 246
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
191-391 1.01e-07

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: 53.54  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 191 KGVAADNIIFFPNWSEIARFQHVADadvdalRNQLGLPDNKKIILYSGNIGEKQGLENVIEAADRLRDE--PLIFAIVG- 267
Cdd:cd03822  153 KLIPAVNIEVIPHGVPEVPQDPTTA------LKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEfpDVRLVIAGe 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 268 ------QGGGKARLEKMAQQRGLRNMQFFPLQSY--DALPALLKMgdCHLVVQ-----KRGAADAVlpskltnILAVG-G 333
Cdd:cd03822  227 lhpslaRYEGERYRKAAIEELGLQDHVDFHNNFLpeEEVPRYISA--ADVVVLpylntEQSSSGTL-------SYAIAcG 297
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446622360 334 NAVITaeahTELGQLCETFPGIA-VCVEPESVEALVAGIRQALLLPKHntvAREYAERT 391
Cdd:cd03822  298 KPVIS----TPLRHAEELLADGRgVLVPFDDPSAIAEAILRLLEDDER---RQAIAERA 349
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
2-310 1.60e-07

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: 52.72  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   2 KILVYGINYSPELT-GIGKYTGEMVEWLAAQGHEVRVITAPPYyPQWQVGENYSAWRYKReegaatvwrcPLYVPKQPST 80
Cdd:cd03823    1 KILLVNSLYPPQRVgGAEISVHDLAEALVAEGHEVAVLTAGVG-PPGQATVARSVVRYRR----------APDETLPLAL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  81 LKRLLHLGSFAVSSFFPLMAQ--RRWKPDRI-----IGVvptlfctpGMRLL--AKLSGARTVLHIQDYEVDAMlglgla 151
Cdd:cd03823   70 KRRGYELFETYNPGLRRLLARllEDFRPDVVhthnlSGL--------GASLLdaARDLGIPVVHTLHDYWLLCP------ 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 152 gkgkggkvaqlatafeRSGL--HNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARfqhvadadvdALRNQLGLPD 229
Cdd:cd03823  136 ----------------RQFLfkKGGDAVLAPSRFTANLHEANGLFSARISVIPNAVEPDL----------APPPRRRPGT 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 230 NKKIILYSGNIGEKQGLENVIEAADRLRDEPLIFAIVgqggGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHL 309
Cdd:cd03823  190 ERLRFGYIGRLTEEKGIDLLVEAFKRLPREDIELVIA----GHGPLSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLV 265

                 .
gi 446622360 310 V 310
Cdd:cd03823  266 V 266
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
2-291 8.32e-07

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: 50.43  E-value: 8.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   2 KILVygINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAppyypqwqvgeNYSAWRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03811    1 KILF--VIPSLSGGGAERVLLNLANALDKRGYDVTLVLL-----------RDEGDLDKQLNGDVKLIRLLIRVLKLIKLG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  82 KRLLHLgsfavssFFPLMAQRRwKPDRIIGvvptlFCTPGMRLLAKLSGARTVLHIqdYEVDAMLGLGLAgkgkggkvaQ 161
Cdd:cd03811   68 LLKAIL-------KLKRILKRA-KPDVVIS-----FLGFATYIVAKLAAARSKVIA--WIHSSLSKLYYL---------K 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 162 LATAFERSGLHNVDNVSTISRSMMNKAIEKG-VAADNIIFFPNwseiarFQHVADADVDALRNQLGLPDNKKIILYSGNI 240
Cdd:cd03811  124 KKLLLKLKLYKKADKIVCVSKGIKEDLIRLGpSPPEKIEVIYN------PIDIDRIRALAKEPILNEPEDGPVILAVGRL 197
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446622360 241 GEKQGLENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGLRNMQFFP 291
Cdd:cd03811  198 DPQKGHDLLIEAFAKLRKKypDVKLVILGDGPLREELEKLAKELGLAERVIFL 250
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
16-203 8.05e-06

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 45.99  E-value: 8.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   16 GIGKYTGEMVEWLAAQGHEVRVIT---APPYYPQWQVGENYSAWRYKREEGaatvwrcPLYVPKQPSTLKRLLhlgsfav 92
Cdd:pfam13439   2 GVERYVLELARALARRGHEVTVVTpggPGPLAEEVVRVVRVPRVPLPLPPR-------LLRSLAFLRRLRRLL------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360   93 ssffplmaqRRWKPDRIIGVVPTLFCTpGMRLLAKLSGARTV--LHiqdyevdAMLGLGLAGKGKGGKVAQLATAFERSG 170
Cdd:pfam13439  68 ---------RRERPDVVHAHSPFPLGL-AALAARLRLGIPLVvtYH-------GLFPDYKRLGARLSPLRRLLRRLERRL 130
                         170       180       190
                  ....*....|....*....|....*....|....
gi 446622360  171 LHNVDNVSTISRSMMNKAIEK-GVAADNIIFFPN 203
Cdd:pfam13439 131 LRRADRVIAVSEAVADELRRLyGVPPEKIRVIPN 164
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
180-335 3.28e-05

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: 45.52  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 180 ISRSMMNKAIEKGVAADNIIFFPNWSEIARFqHVADADVDALRnqlglpdnkkiILYSGNIGEKQGLENVIEA----ADR 255
Cdd:cd05844  150 VSGFIRDRLLARGLPAERIHVHYIGIDPAKF-APRDPAERAPT-----------ILFVGRLVEKKGCDVLIEAfrrlAAR 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 256 LRDEPLIfaIVGQGGGKARLEKMAqqRGLRNMQFFPLQSYDALPALLkmgdchlvvqkRGAADAVLPSkltnILAVGGNA 335
Cdd:cd05844  218 HPTARLV--IAGDGPLRPALQALA--AALGRVRFLGALPHAEVQDWM-----------RRAEIFCLPS----VTAASGDS 278
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
159-401 5.93e-05

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 44.78  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 159 VAQLATAFERSGLHNvdNVSTISRSMMNKAIEKGVAAD-NIIFFPNWSEIARFQHvadADVDALRNQLGLPDNKKIILYS 237
Cdd:PRK15484 125 VMHMHNAFEPELLDK--NAKIIVPSQFLKKFYEERLPNaDISIVPNGFCLETYQS---NPQPNLRQQLNISPDETVLLYA 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 238 GNIGEKQGLENVIEAADRLRDEP--LIFAIVGQGGGKARLEKMAQQRGLRNM--------------------QFFPLQSY 295
Cdd:PRK15484 200 GRISPDKGILLLMQAFEKLATAHsnLKLVVVGDPTASSKGEKAAYQKKVLEAakrigdrcimlggqppekmhNYYPLADL 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 296 DALPALLKMGDCHLVVQKRGAADAVLPSKLTNIlavggnavitaeahTELGQLCETFPGIAvcvEPESVEALVAGIRQAL 375
Cdd:PRK15484 280 VVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGI--------------TEFVLEGITGYHLA---EPMTSDSIISDINRTL 342
                        250       260
                 ....*....|....*....|....*....
gi 446622360 376 LLPKHNTVAREYAERTLDK---ENVLRQF 401
Cdd:PRK15484 343 ADPELTQIAEQAKDFVFSKyswEGVTQRF 371
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
231-307 1.48e-04

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: 43.42  E-value: 1.48e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446622360 231 KKIILYSGNIGEKQGLENVIEAADRLrDEPLIfaIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDC 307
Cdd:cd03795  191 KKIFLFIGRLVYYKGLDYLIEAAQYL-NYPIV--IGGEGPLKPDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDV 264
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
231-375 6.62e-04

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 39.80  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360  231 KKIILYSGNIGEKQ-GLENVIEAADRLRDEP--LIFAIVGqGGGKARLEKMAqqRGLRNmQFFPLQSYDALPALLKMGDC 307
Cdd:pfam13692   1 RPVILFVGRLHPNVkGVDYLLEAVPLLRKRDndVRLVIVG-DGPEEELEELA--AGLED-RVIFTGFVEDLAELLAAADV 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446622360  308 hlvvqkrgaadAVLPSKLTNIlavgGNAVITAEAH------TELGQLCETFPGIA-VCVEPESVEALVAGIRQAL 375
Cdd:pfam13692  77 -----------FVLPSLYEGF----GLKLLEAMAAglpvvaTDVGGIPELVDGENgLLVPPGDPEALAEAILRLL 136
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
168-309 1.47e-03

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: 40.41  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 168 RSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQHVADadvDALRNQLGLPDNKKIILYSGNIGEKQGLE 247
Cdd:cd04962  136 RFSINKSDRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPA---GALKRRLLAPPDEKVVIHVSNFRPVKRID 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446622360 248 NVIEAADRLRDE-PLIFAIVGQGGGKARLEKMAQQRGLRNMQFFpLQSYDALPALLKMGDCHL 309
Cdd:cd04962  213 DVVRVFARVRRKiPAKLLLVGDGPERVPAEELARELGVEDRVLF-LGKQDDVEELLSIADLFL 274
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
216-386 1.63e-03

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: 40.30  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 216 ADVDALRNQLGLPDNKKIILYSGNIGEKQGLENVIEAA--DRLRDEPLIFAIVG--QGGGKAR----LEKMAQQRGLRNM 287
Cdd:cd03800  205 DRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFaqLPELRELANLVLVGgpSDDPLSMdreeLAELAEELGLIDR 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446622360 288 -QFFPLQSYDALPALLKmgdchlvvqkrgAADA-VLPSK-----LTNILA-----------VGGNAVITAEAHTelGQLc 349
Cdd:cd03800  285 vRFPGRVSRDDLPELYR------------AADVfVVPSLyepfgLTAIEAmacgtpvvataVGGLQDIVRDGRT--GLL- 349
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446622360 350 etfpgiavcVEPESVEALVAGIRQALLLPKHNTVARE 386
Cdd:cd03800  350 ---------VDPHDPEALAAALRRLLDDPALWQRLSR 377
 
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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