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Conserved domains on  [gi|1830960328|ref|WP_168252254|]
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GH36-type glycosyl hydrolase domain-containing protein [Rhizobium ruizarguesonis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3459 COG3459
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
497-1295 0e+00

Cellobiose phosphorylase [Carbohydrate transport and metabolism];


:

Pssm-ID: 442682 [Multi-domain]  Cd Length: 794  Bit Score: 1247.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  497 NGLGGFAADGHEYVVRvdalkpqAPTlPPAPWTNVIANPHFGCLTTEAGLGYTWAENSQMNRLTPWSNDPVTDAPGEVLY 576
Cdd:COG3459      1 NGYGGFDDDGREYVIT-------GPD-TPAPWINVLANPDFGFLVSETGGGYSWYKNSRENRLTRWRNDPVSDPPGEYFY 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  577 LRDEETSDTWTPTPLPLG-PGAVVTVRHGQGYSRYTSFSRHLSQELTVSVAPNDPVKIMRLRLSNEDTRVRHVTAIYFAE 655
Cdd:COG3459     73 LRDEETGDYWSPTWQPVRkPLDEYECRHGFGYTRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  656 WVLGTQREQTAARVVC----ERDARSGAIVARNPWAGDFAGRLAFAAASQPARSTTSDRTEFLGKYGSVFQPAALGRTDL 731
Cdd:COG3459    153 WVLGNARDDTANFQVTlstgEVDPEGGAILARNPYNERFNGRVAFFAVSEPVSSFTGDREEFLGRYGSLANPAALERGKL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  732 AERFGPLLDPCAALMVDISLRPSESREIVFILGQAADLDEVSRLVHEHTDLERAAASLSAASRQWDDILNSIQVSTPDTG 811
Cdd:COG3459    233 SNSVGAGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARYRDPDAVDAALAEVKAYWDELLGAVQVETPDPA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  812 LNLMMNRWLLYQVLACRMWARTSNYQSGGAYGFRDQLQDVMALVYSVPSEARSHILRSAARQFEEGDVQHWWHPPSGVGV 891
Cdd:COG3459    313 LDLMVNGWLLYQTLACRLWARSAFYQSGGAYGFRDQLQDSMALVHARPELAREQILLAASRQFPEGDVQHWWHPPTGRGV 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  892 RTRITDDLYFLPLVVHHYVSTTGDAQLLDEIVPFITSPVLRDDQEEDFNQPATSEQSGTVYEHCVRALEHGY-RLGSHGL 970
Cdd:COG3459    393 RTRFSDDLLWLPYAVAAYIKETGDFSILDEVVPFLDGPPLPPGEEDAYDLPTVSGEEATLYEHCKRAIDFSLnRLGPHGL 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  971 PLMGTGDWNDGMNKVGAGGKGESVWNGWLYLTVLKSFAEISASRGDQSRAAWCGERVEALRIAIEANAWDGGWYRRAYFD 1050
Cdd:COG3459    473 PLIGRGDWNDGMNLVGEGGKGESVWLAWFLYYALKEFAPLAEARGDEERAERYRAEAEELREAIEKHAWDGEWYRRAYFD 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1051 DGTPLGSSLNDECQIDAIPQAWAVISGEADAERASQAMRAVHDRLVRPEDRLIKLFDPPFDDGVLQPGYIKGYVPGIREN 1130
Cdd:COG3459    553 DGTPLGSKENEECKIDLIAQSWAVLSGAADPERARKAMDSVDKYLVTEYGGLILLLTPPFDKYDPDPGYIKGYPPGVREN 632
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1131 GGQYTHAATWVVWATALQGDGELALKLWNLINPIYHGatkDQVERYKVEPYAVAADIYGAPPHTGRGGWTWYTGSASWLY 1210
Cdd:COG3459    633 GGQYTHAAPWAIMAEALLGDGDRAYELYSMINPINHN---DEADRYKVEPYVYAADVYGVDPHFGRGGWSWYTGSAGWMY 709
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1211 RVALEAILGFRQEGRFLRFEPCVPAGWPAYEIAYRYGSATYRIHFDNSKGIGRGVQSVTLDGEPVANESVPLAQDARTHD 1290
Cdd:COG3459    710 RAATEYILGIRPEGDGLRIDPCIPSDWPGFSVTRRFRGAVYHITVKNPDGVSKGVKSITVDGKPIEGNLIPLVDDGKEHE 789

                   ....*
gi 1830960328 1291 VHVII 1295
Cdd:COG3459    790 VEVVL 794
GH94N_ChvB_NdvB_2_like cd11753
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ...
23-296 8.92e-120

Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This second of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.


:

Pssm-ID: 213069 [Multi-domain]  Cd Length: 336  Bit Score: 375.71  E-value: 8.92e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   23 VALLSNDGYSVLVTAAGAGYGMWQGLDITRWREDSTRDCWGQFCYVRDLTDNDLWSIGRQPLFRPSNIYEHAFYGDRAEL 102
Cdd:cd11753     63 VHLLSNGRYSVMLTASGSGYSRWNDLAVTRWREDATRDNWGSFIYLRDVDSGKVWSATYQPTRDPPDEYEVVFSEDRAEF 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  103 SCHAGDIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLELTSYAEVCLYNRSADMAHPGFAKLFVETQFDEATGALFARR 182
Cdd:cd11753    143 RRRDGGIETTTEVVVSPEDDAEIRRVTLTNLSRRPRELEVTSYAEVVLAPPAADEAHPAFSKLFVQTEFLPEQGALLATR 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  183 RPRAAGEKATWAVHVSSSNLQPAQAAQYETDRLRFLGRGRTTANPMAFDAGAPLSGTTGPVLDPIFCLRRTVRLAPGADA 262
Cdd:cd11753    223 RPRSPDEPPPWAAHFVAVEGEAVGPLQYETDRARFIGRGRSLANPAAMDDGAPLSGTVGAVLDPIFSLRRRVRLPPGETA 302
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1830960328  263 RVAFVTGAADDQSAVQFIAKRYAEIDAVEQAFSD 296
Cdd:cd11753    303 RVTFVTGVADSREEALELADKYRDPSAVERAFEL 336
 
Name Accession Description Interval E-value
COG3459 COG3459
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
497-1295 0e+00

Cellobiose phosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 442682 [Multi-domain]  Cd Length: 794  Bit Score: 1247.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  497 NGLGGFAADGHEYVVRvdalkpqAPTlPPAPWTNVIANPHFGCLTTEAGLGYTWAENSQMNRLTPWSNDPVTDAPGEVLY 576
Cdd:COG3459      1 NGYGGFDDDGREYVIT-------GPD-TPAPWINVLANPDFGFLVSETGGGYSWYKNSRENRLTRWRNDPVSDPPGEYFY 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  577 LRDEETSDTWTPTPLPLG-PGAVVTVRHGQGYSRYTSFSRHLSQELTVSVAPNDPVKIMRLRLSNEDTRVRHVTAIYFAE 655
Cdd:COG3459     73 LRDEETGDYWSPTWQPVRkPLDEYECRHGFGYTRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  656 WVLGTQREQTAARVVC----ERDARSGAIVARNPWAGDFAGRLAFAAASQPARSTTSDRTEFLGKYGSVFQPAALGRTDL 731
Cdd:COG3459    153 WVLGNARDDTANFQVTlstgEVDPEGGAILARNPYNERFNGRVAFFAVSEPVSSFTGDREEFLGRYGSLANPAALERGKL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  732 AERFGPLLDPCAALMVDISLRPSESREIVFILGQAADLDEVSRLVHEHTDLERAAASLSAASRQWDDILNSIQVSTPDTG 811
Cdd:COG3459    233 SNSVGAGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARYRDPDAVDAALAEVKAYWDELLGAVQVETPDPA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  812 LNLMMNRWLLYQVLACRMWARTSNYQSGGAYGFRDQLQDVMALVYSVPSEARSHILRSAARQFEEGDVQHWWHPPSGVGV 891
Cdd:COG3459    313 LDLMVNGWLLYQTLACRLWARSAFYQSGGAYGFRDQLQDSMALVHARPELAREQILLAASRQFPEGDVQHWWHPPTGRGV 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  892 RTRITDDLYFLPLVVHHYVSTTGDAQLLDEIVPFITSPVLRDDQEEDFNQPATSEQSGTVYEHCVRALEHGY-RLGSHGL 970
Cdd:COG3459    393 RTRFSDDLLWLPYAVAAYIKETGDFSILDEVVPFLDGPPLPPGEEDAYDLPTVSGEEATLYEHCKRAIDFSLnRLGPHGL 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  971 PLMGTGDWNDGMNKVGAGGKGESVWNGWLYLTVLKSFAEISASRGDQSRAAWCGERVEALRIAIEANAWDGGWYRRAYFD 1050
Cdd:COG3459    473 PLIGRGDWNDGMNLVGEGGKGESVWLAWFLYYALKEFAPLAEARGDEERAERYRAEAEELREAIEKHAWDGEWYRRAYFD 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1051 DGTPLGSSLNDECQIDAIPQAWAVISGEADAERASQAMRAVHDRLVRPEDRLIKLFDPPFDDGVLQPGYIKGYVPGIREN 1130
Cdd:COG3459    553 DGTPLGSKENEECKIDLIAQSWAVLSGAADPERARKAMDSVDKYLVTEYGGLILLLTPPFDKYDPDPGYIKGYPPGVREN 632
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1131 GGQYTHAATWVVWATALQGDGELALKLWNLINPIYHGatkDQVERYKVEPYAVAADIYGAPPHTGRGGWTWYTGSASWLY 1210
Cdd:COG3459    633 GGQYTHAAPWAIMAEALLGDGDRAYELYSMINPINHN---DEADRYKVEPYVYAADVYGVDPHFGRGGWSWYTGSAGWMY 709
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1211 RVALEAILGFRQEGRFLRFEPCVPAGWPAYEIAYRYGSATYRIHFDNSKGIGRGVQSVTLDGEPVANESVPLAQDARTHD 1290
Cdd:COG3459    710 RAATEYILGIRPEGDGLRIDPCIPSDWPGFSVTRRFRGAVYHITVKNPDGVSKGVKSITVDGKPIEGNLIPLVDDGKEHE 789

                   ....*
gi 1830960328 1291 VHVII 1295
Cdd:COG3459    790 VEVVL 794
GH94N_ChvB_NdvB_1_like cd11756
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ...
492-779 5.67e-147

First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This first of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.


Pssm-ID: 213072 [Multi-domain]  Cd Length: 284  Bit Score: 445.80  E-value: 5.67e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  492 DLQYWNGLGGFAADGHEYVVRvdaLKPQAPTlpPAPWTNVIANPHFGCLTTEAGLGYTWAENSQMNRLTPWSNDPVTDAP 571
Cdd:cd11756      1 DLQFFNGYGGFSPDGREYVIV---LGPGKRT--PAPWINVIANPGFGFLVSESGSGYTWAENSRENRLTPWSNDPVSDPP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  572 GEVLYLRDEETSDTWTPTPLPLGPGAVVTVRHGQGYSRYTSFSRHLSQELTVSVAPNDPVKIMRLRLSNEDTRVRHVTAI 651
Cdd:cd11756     76 GEALYLRDEETGEVWSPTPLPIRGGGPYRVRHGFGYSRFEHRSHGIEQELTVFVPRDDPVKISRLRLRNTSGRPRRLSVT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  652 YFAEWVLGTQREQTAARVVCERDARSGAIVARNPWAGDFAGRLAFAAASQPARSTTSDRTEFLGKYGSVFQPAALGRTDL 731
Cdd:cd11756    156 YYAEWVLGVNREKTAPHIVTEYDEETGALLARNPYNEDFGGRVAFLAVSGGPRSFTGDRREFIGRNGSLANPAALKRGRL 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1830960328  732 AERFGPLLDPCAALMVDISLRPSESREIVFILGQAADLDEVSRLVHEH 779
Cdd:cd11756    236 SGRTGAGLDPCAALQVDLELAPGEEKEIVFLLGEADDAEEARALIRRY 283
Glyco_hydro_36 pfam17167
Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the ...
796-1221 1.95e-138

Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the superfamily of enzymes referred to as GH36. UniProtKB:Q76IQ9 is a chitobiose phosphorylase that catalyzes the reversible phosphorolysis of chitobiose into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration. The full-length enzyme comprises a beta sandwich domain and an (alpha/alpha)(6) barrel domain. The alpha-helical barrel component of the domain, this family, is the catalytic region.


Pssm-ID: 465366  Cd Length: 425  Bit Score: 428.84  E-value: 1.95e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  796 WDDILNSIQVSTPDTGLNLMMNRWLLYQVLACRMWART-SNYQSGGA--YGFRDQLQDVMALVYSVPSEARSHILRSAAR 872
Cdd:pfam17167    2 WDSRLEKFQVKTPDESLDTMINIWNLYQCEICFVWSRFaSFIESGGRtgYGFRDTAQDIIGVPHMNPEMTRKRILDLASG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  873 QFEEGDVQHWWHPPSGvGVRTRITDDLYFLPLVVHhYVSTTGDAQLLDE--IVPFITSPVLRDDQEEDFNQ--PATSEQS 948
Cdd:pfam17167   82 QFKAGYGLHLFDPDWD-DIKPSKSPTVLPTPYDND-KIHGIGDTCSDDHlwLVPTIEAYVKETGDFSFLDEviPYSDGKK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  949 GTVYEHCVRALEHGYR-LGSHGLPLMGTGDWNDGMNKvgagGKGESVWNGWLYLTVLKSFAEISASRGDQSRAAWCGERV 1027
Cdd:pfam17167  160 ATVYEHLKKAIDFSLEyLGQHGIPLGGRADWNDCLNL----GGGESVFVSFLLYLALQEFIEIAKFKGDDEDAEWYEKMA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1028 EALRIAIEANAWDGGWYRRAYFDDGTPLGSSLNDECQIDAIPQAWAVISGEADAERASQAMRAVHDRLVRPedRLIKLFD 1107
Cdd:pfam17167  236 DKVREAIEKYAWDGEWYIRAYTKDGDKIGSKQNEEGKIHLESQSWAVLSGIGKDERAKKAMDSVEKYLFTE--YGLHLNQ 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1108 PPFDDGVLQPGYIKGYVPGIRENGGQYTHAATWVVWATALQGDGELALKLWNLINPIYHgatKDQVERYKVEPYAVAADI 1187
Cdd:pfam17167  314 PPFSTPNLDIGFITRYYPGVKENGGIFCHPNPWVIVAETKLGRGDRAMKLYDAINPANQ---NDIIETRKAEPYVYAQFV 390
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1830960328 1188 YGA-PPHTGRGGWTWYTGSASWLYRVALEAILGFR 1221
Cdd:pfam17167  391 MGKdHPDHGRANHPWLTGTAGWAYVAITEGILGLR 425
GH94N_ChvB_NdvB_2_like cd11753
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ...
23-296 8.92e-120

Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This second of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.


Pssm-ID: 213069 [Multi-domain]  Cd Length: 336  Bit Score: 375.71  E-value: 8.92e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   23 VALLSNDGYSVLVTAAGAGYGMWQGLDITRWREDSTRDCWGQFCYVRDLTDNDLWSIGRQPLFRPSNIYEHAFYGDRAEL 102
Cdd:cd11753     63 VHLLSNGRYSVMLTASGSGYSRWNDLAVTRWREDATRDNWGSFIYLRDVDSGKVWSATYQPTRDPPDEYEVVFSEDRAEF 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  103 SCHAGDIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLELTSYAEVCLYNRSADMAHPGFAKLFVETQFDEATGALFARR 182
Cdd:cd11753    143 RRRDGGIETTTEVVVSPEDDAEIRRVTLTNLSRRPRELEVTSYAEVVLAPPAADEAHPAFSKLFVQTEFLPEQGALLATR 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  183 RPRAAGEKATWAVHVSSSNLQPAQAAQYETDRLRFLGRGRTTANPMAFDAGAPLSGTTGPVLDPIFCLRRTVRLAPGADA 262
Cdd:cd11753    223 RPRSPDEPPPWAAHFVAVEGEAVGPLQYETDRARFIGRGRSLANPAAMDDGAPLSGTVGAVLDPIFSLRRRVRLPPGETA 302
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1830960328  263 RVAFVTGAADDQSAVQFIAKRYAEIDAVEQAFSD 296
Cdd:cd11753    303 RVTFVTGVADSREEALELADKYRDPSAVERAFEL 336
Glyco_transf_36 pfam06165
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose ...
19-269 3.07e-82

Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-). Many members of this family contain two copies of this domain.


Pssm-ID: 461842 [Multi-domain]  Cd Length: 247  Bit Score: 269.36  E-value: 3.07e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   19 PSSAVALLSNDGYSVLVTAAGAGYGMWQGLD---ITRWREDSTRDCWGQFCYVRDLTDNDLWSIGRQPlFRPSNIYE--H 93
Cdd:pfam06165    1 PAPWINVLSNGDYGVLISNTGGGYSWYKNSRenrLTRWRNDPVRDPPGEYIYIRDEESGEVWSPTWQP-VRKPLDYEvrH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   94 AFygDRAELSCHAGDIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLELTSYAEVCLYNRSADMAHPGFAKLFVETQFDE 173
Cdd:pfam06165   80 GL--GYTRFEREDGGIETELTVFVPPEDPVEIRRLTLTNTSDRERRLSVTSYVEWVLGNAAADLAHPAFSRLFSQTEIVT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  174 ATGALFARRRPRAAGEKATWAVHVSSsnlqpAQAAQYETDRLRFLGRGRTTANPMAFDAGaPLSGTTGPVLDPIFCLRRT 253
Cdd:pfam06165  158 ELGAILAARNPRSEEFRNRYAFHAVS-----GPVDSYETDREEFIGRGGSLANPAALERG-PLSNSVGAGLDPCAALQVR 231
                          250
                   ....*....|....*.
gi 1830960328  254 VRLAPGADARVAFVTG 269
Cdd:pfam06165  232 IELAPGETKEVVFILG 247
COG3459 COG3459
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
26-301 3.52e-46

Cellobiose phosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 442682 [Multi-domain]  Cd Length: 794  Bit Score: 179.57  E-value: 3.52e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   26 LSNDGYSVLVTAAGAGYgMWQGlD-----ITRWREDSTRDCWGQFCYVRDLTDNDLWSIGRQPLFRPSNIYE--HAF-Yg 97
Cdd:COG3459     28 LANPDFGFLVSETGGGY-SWYK-NsrenrLTRWRNDPVSDPPGEYFYLRDEETGDYWSPTWQPVRKPLDEYEcrHGFgY- 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   98 drAELSCHAGDIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLELTSYAEVCLYNRSADMAHpgFAKLFVETQFDEATGA 177
Cdd:COG3459    105 --TRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLGNARDDTAN--FQVTLSTGEVDPEGGA 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  178 LFARRRPRAAGEKATWAVHVSssnlqpAQAAQYETDRLRFLGRGRTTANPMAFDAGaPLSGTTGPVLDPIFCLRRTVRLA 257
Cdd:COG3459    181 ILARNPYNERFNGRVAFFAVS------EPVSSFTGDREEFLGRYGSLANPAALERG-KLSNSVGAGLDPCAALQVDIELA 253
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1830960328  258 PGADARVAFVTGAADDQSAVQFIAKRYAEIDAVEQAFsDASRRY 301
Cdd:COG3459    254 PGEEKELVFLLGQGENKEEARALIARYRDPDAVDAAL-AEVKAY 296
CBM_X smart01068
Putative carbohydrate binding domain;
497-567 4.51e-21

Putative carbohydrate binding domain;


Pssm-ID: 215008 [Multi-domain]  Cd Length: 62  Bit Score: 87.63  E-value: 4.51e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830960328   497 NGLGGFAADGHEYVVRVDalkpqaPTLPPAPWTNVIANPHFGCLTTEAGLGYT-WAENSqmnrLTPWSNDPV 567
Cdd:smart01068    1 NGLGGFDDDGREYVRTLD------GPDTPAPWINVLSNGRYGVMVSASGSGYSrWADNS----LTRWRNDPV 62
CBM_X smart01068
Putative carbohydrate binding domain;
1-58 3.62e-14

Putative carbohydrate binding domain;


Pssm-ID: 215008 [Multi-domain]  Cd Length: 62  Bit Score: 68.37  E-value: 3.62e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830960328     1 MATSTADAPRHDSIAELN----PSSAVALLSNDGYSVLVTAAGAGYGMWQGLDITRWREDST 58
Cdd:smart01068    1 NGLGGFDDDGREYVRTLDgpdtPAPWINVLSNGRYGVMVSASGSGYSRWADNSLTRWRNDPV 62
 
Name Accession Description Interval E-value
COG3459 COG3459
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
497-1295 0e+00

Cellobiose phosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 442682 [Multi-domain]  Cd Length: 794  Bit Score: 1247.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  497 NGLGGFAADGHEYVVRvdalkpqAPTlPPAPWTNVIANPHFGCLTTEAGLGYTWAENSQMNRLTPWSNDPVTDAPGEVLY 576
Cdd:COG3459      1 NGYGGFDDDGREYVIT-------GPD-TPAPWINVLANPDFGFLVSETGGGYSWYKNSRENRLTRWRNDPVSDPPGEYFY 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  577 LRDEETSDTWTPTPLPLG-PGAVVTVRHGQGYSRYTSFSRHLSQELTVSVAPNDPVKIMRLRLSNEDTRVRHVTAIYFAE 655
Cdd:COG3459     73 LRDEETGDYWSPTWQPVRkPLDEYECRHGFGYTRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  656 WVLGTQREQTAARVVC----ERDARSGAIVARNPWAGDFAGRLAFAAASQPARSTTSDRTEFLGKYGSVFQPAALGRTDL 731
Cdd:COG3459    153 WVLGNARDDTANFQVTlstgEVDPEGGAILARNPYNERFNGRVAFFAVSEPVSSFTGDREEFLGRYGSLANPAALERGKL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  732 AERFGPLLDPCAALMVDISLRPSESREIVFILGQAADLDEVSRLVHEHTDLERAAASLSAASRQWDDILNSIQVSTPDTG 811
Cdd:COG3459    233 SNSVGAGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARYRDPDAVDAALAEVKAYWDELLGAVQVETPDPA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  812 LNLMMNRWLLYQVLACRMWARTSNYQSGGAYGFRDQLQDVMALVYSVPSEARSHILRSAARQFEEGDVQHWWHPPSGVGV 891
Cdd:COG3459    313 LDLMVNGWLLYQTLACRLWARSAFYQSGGAYGFRDQLQDSMALVHARPELAREQILLAASRQFPEGDVQHWWHPPTGRGV 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  892 RTRITDDLYFLPLVVHHYVSTTGDAQLLDEIVPFITSPVLRDDQEEDFNQPATSEQSGTVYEHCVRALEHGY-RLGSHGL 970
Cdd:COG3459    393 RTRFSDDLLWLPYAVAAYIKETGDFSILDEVVPFLDGPPLPPGEEDAYDLPTVSGEEATLYEHCKRAIDFSLnRLGPHGL 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  971 PLMGTGDWNDGMNKVGAGGKGESVWNGWLYLTVLKSFAEISASRGDQSRAAWCGERVEALRIAIEANAWDGGWYRRAYFD 1050
Cdd:COG3459    473 PLIGRGDWNDGMNLVGEGGKGESVWLAWFLYYALKEFAPLAEARGDEERAERYRAEAEELREAIEKHAWDGEWYRRAYFD 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1051 DGTPLGSSLNDECQIDAIPQAWAVISGEADAERASQAMRAVHDRLVRPEDRLIKLFDPPFDDGVLQPGYIKGYVPGIREN 1130
Cdd:COG3459    553 DGTPLGSKENEECKIDLIAQSWAVLSGAADPERARKAMDSVDKYLVTEYGGLILLLTPPFDKYDPDPGYIKGYPPGVREN 632
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1131 GGQYTHAATWVVWATALQGDGELALKLWNLINPIYHGatkDQVERYKVEPYAVAADIYGAPPHTGRGGWTWYTGSASWLY 1210
Cdd:COG3459    633 GGQYTHAAPWAIMAEALLGDGDRAYELYSMINPINHN---DEADRYKVEPYVYAADVYGVDPHFGRGGWSWYTGSAGWMY 709
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1211 RVALEAILGFRQEGRFLRFEPCVPAGWPAYEIAYRYGSATYRIHFDNSKGIGRGVQSVTLDGEPVANESVPLAQDARTHD 1290
Cdd:COG3459    710 RAATEYILGIRPEGDGLRIDPCIPSDWPGFSVTRRFRGAVYHITVKNPDGVSKGVKSITVDGKPIEGNLIPLVDDGKEHE 789

                   ....*
gi 1830960328 1291 VHVII 1295
Cdd:COG3459    790 VEVVL 794
GH94N_ChvB_NdvB_1_like cd11756
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ...
492-779 5.67e-147

First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This first of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.


Pssm-ID: 213072 [Multi-domain]  Cd Length: 284  Bit Score: 445.80  E-value: 5.67e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  492 DLQYWNGLGGFAADGHEYVVRvdaLKPQAPTlpPAPWTNVIANPHFGCLTTEAGLGYTWAENSQMNRLTPWSNDPVTDAP 571
Cdd:cd11756      1 DLQFFNGYGGFSPDGREYVIV---LGPGKRT--PAPWINVIANPGFGFLVSESGSGYTWAENSRENRLTPWSNDPVSDPP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  572 GEVLYLRDEETSDTWTPTPLPLGPGAVVTVRHGQGYSRYTSFSRHLSQELTVSVAPNDPVKIMRLRLSNEDTRVRHVTAI 651
Cdd:cd11756     76 GEALYLRDEETGEVWSPTPLPIRGGGPYRVRHGFGYSRFEHRSHGIEQELTVFVPRDDPVKISRLRLRNTSGRPRRLSVT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  652 YFAEWVLGTQREQTAARVVCERDARSGAIVARNPWAGDFAGRLAFAAASQPARSTTSDRTEFLGKYGSVFQPAALGRTDL 731
Cdd:cd11756    156 YYAEWVLGVNREKTAPHIVTEYDEETGALLARNPYNEDFGGRVAFLAVSGGPRSFTGDRREFIGRNGSLANPAALKRGRL 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1830960328  732 AERFGPLLDPCAALMVDISLRPSESREIVFILGQAADLDEVSRLVHEH 779
Cdd:cd11756    236 SGRTGAGLDPCAALQVDLELAPGEEKEIVFLLGEADDAEEARALIRRY 283
Glyco_hydro_36 pfam17167
Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the ...
796-1221 1.95e-138

Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the superfamily of enzymes referred to as GH36. UniProtKB:Q76IQ9 is a chitobiose phosphorylase that catalyzes the reversible phosphorolysis of chitobiose into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration. The full-length enzyme comprises a beta sandwich domain and an (alpha/alpha)(6) barrel domain. The alpha-helical barrel component of the domain, this family, is the catalytic region.


Pssm-ID: 465366  Cd Length: 425  Bit Score: 428.84  E-value: 1.95e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  796 WDDILNSIQVSTPDTGLNLMMNRWLLYQVLACRMWART-SNYQSGGA--YGFRDQLQDVMALVYSVPSEARSHILRSAAR 872
Cdd:pfam17167    2 WDSRLEKFQVKTPDESLDTMINIWNLYQCEICFVWSRFaSFIESGGRtgYGFRDTAQDIIGVPHMNPEMTRKRILDLASG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  873 QFEEGDVQHWWHPPSGvGVRTRITDDLYFLPLVVHhYVSTTGDAQLLDE--IVPFITSPVLRDDQEEDFNQ--PATSEQS 948
Cdd:pfam17167   82 QFKAGYGLHLFDPDWD-DIKPSKSPTVLPTPYDND-KIHGIGDTCSDDHlwLVPTIEAYVKETGDFSFLDEviPYSDGKK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  949 GTVYEHCVRALEHGYR-LGSHGLPLMGTGDWNDGMNKvgagGKGESVWNGWLYLTVLKSFAEISASRGDQSRAAWCGERV 1027
Cdd:pfam17167  160 ATVYEHLKKAIDFSLEyLGQHGIPLGGRADWNDCLNL----GGGESVFVSFLLYLALQEFIEIAKFKGDDEDAEWYEKMA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1028 EALRIAIEANAWDGGWYRRAYFDDGTPLGSSLNDECQIDAIPQAWAVISGEADAERASQAMRAVHDRLVRPedRLIKLFD 1107
Cdd:pfam17167  236 DKVREAIEKYAWDGEWYIRAYTKDGDKIGSKQNEEGKIHLESQSWAVLSGIGKDERAKKAMDSVEKYLFTE--YGLHLNQ 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328 1108 PPFDDGVLQPGYIKGYVPGIRENGGQYTHAATWVVWATALQGDGELALKLWNLINPIYHgatKDQVERYKVEPYAVAADI 1187
Cdd:pfam17167  314 PPFSTPNLDIGFITRYYPGVKENGGIFCHPNPWVIVAETKLGRGDRAMKLYDAINPANQ---NDIIETRKAEPYVYAQFV 390
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1830960328 1188 YGA-PPHTGRGGWTWYTGSASWLYRVALEAILGFR 1221
Cdd:pfam17167  391 MGKdHPDHGRANHPWLTGTAGWAYVAITEGILGLR 425
GH94N_ChvB_NdvB_2_like cd11753
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ...
23-296 8.92e-120

Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This second of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.


Pssm-ID: 213069 [Multi-domain]  Cd Length: 336  Bit Score: 375.71  E-value: 8.92e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   23 VALLSNDGYSVLVTAAGAGYGMWQGLDITRWREDSTRDCWGQFCYVRDLTDNDLWSIGRQPLFRPSNIYEHAFYGDRAEL 102
Cdd:cd11753     63 VHLLSNGRYSVMLTASGSGYSRWNDLAVTRWREDATRDNWGSFIYLRDVDSGKVWSATYQPTRDPPDEYEVVFSEDRAEF 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  103 SCHAGDIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLELTSYAEVCLYNRSADMAHPGFAKLFVETQFDEATGALFARR 182
Cdd:cd11753    143 RRRDGGIETTTEVVVSPEDDAEIRRVTLTNLSRRPRELEVTSYAEVVLAPPAADEAHPAFSKLFVQTEFLPEQGALLATR 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  183 RPRAAGEKATWAVHVSSSNLQPAQAAQYETDRLRFLGRGRTTANPMAFDAGAPLSGTTGPVLDPIFCLRRTVRLAPGADA 262
Cdd:cd11753    223 RPRSPDEPPPWAAHFVAVEGEAVGPLQYETDRARFIGRGRSLANPAAMDDGAPLSGTVGAVLDPIFSLRRRVRLPPGETA 302
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1830960328  263 RVAFVTGAADDQSAVQFIAKRYAEIDAVEQAFSD 296
Cdd:cd11753    303 RVTFVTGVADSREEALELADKYRDPSAVERAFEL 336
Glyco_transf_36 pfam06165
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose ...
525-764 4.10e-91

Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-). Many members of this family contain two copies of this domain.


Pssm-ID: 461842 [Multi-domain]  Cd Length: 247  Bit Score: 294.01  E-value: 4.10e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  525 PAPWTNVIANPHFGCLTTEAGLGYTWAENSQMNRLTPWSNDPVTDAPGEVLYLRDEETSDTWTPTPLPLGPGAVVTVRHG 604
Cdd:pfam06165    1 PAPWINVLSNGDYGVLISNTGGGYSWYKNSRENRLTRWRNDPVRDPPGEYIYIRDEESGEVWSPTWQPVRKPLDYEVRHG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  605 QGYSRYTSFSRHLSQELTVSVAPNDPVKIMRLRLSNEDTRVRHVTAIYFAEWVLGT----------QREQTAARVVCERD 674
Cdd:pfam06165   81 LGYTRFEREDGGIETELTVFVPPEDPVEIRRLTLTNTSDRERRLSVTSYVEWVLGNaaadlahpafSRLFSQTEIVTELG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  675 ArsgAIVARNPWAGDFAGRLAFAAASQPARSTTSDRTEFLGKYGSVFQPAALGRTDLAERFGPLLDPCAALMVDISLRPS 754
Cdd:pfam06165  161 A---ILAARNPRSEEFRNRYAFHAVSGPVDSYETDREEFIGRGGSLANPAALERGPLSNSVGAGLDPCAALQVRIELAPG 237
                          250
                   ....*....|
gi 1830960328  755 ESREIVFILG 764
Cdd:pfam06165  238 ETKEVVFILG 247
Glyco_transf_36 pfam06165
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose ...
19-269 3.07e-82

Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-). Many members of this family contain two copies of this domain.


Pssm-ID: 461842 [Multi-domain]  Cd Length: 247  Bit Score: 269.36  E-value: 3.07e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   19 PSSAVALLSNDGYSVLVTAAGAGYGMWQGLD---ITRWREDSTRDCWGQFCYVRDLTDNDLWSIGRQPlFRPSNIYE--H 93
Cdd:pfam06165    1 PAPWINVLSNGDYGVLISNTGGGYSWYKNSRenrLTRWRNDPVRDPPGEYIYIRDEESGEVWSPTWQP-VRKPLDYEvrH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   94 AFygDRAELSCHAGDIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLELTSYAEVCLYNRSADMAHPGFAKLFVETQFDE 173
Cdd:pfam06165   80 GL--GYTRFEREDGGIETELTVFVPPEDPVEIRRLTLTNTSDRERRLSVTSYVEWVLGNAAADLAHPAFSRLFSQTEIVT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  174 ATGALFARRRPRAAGEKATWAVHVSSsnlqpAQAAQYETDRLRFLGRGRTTANPMAFDAGaPLSGTTGPVLDPIFCLRRT 253
Cdd:pfam06165  158 ELGAILAARNPRSEEFRNRYAFHAVS-----GPVDSYETDREEFIGRGGSLANPAALERG-PLSNSVGAGLDPCAALQVR 231
                          250
                   ....*....|....*.
gi 1830960328  254 VRLAPGADARVAFVTG 269
Cdd:pfam06165  232 IELAPGETKEVVFILG 247
COG3459 COG3459
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
26-301 3.52e-46

Cellobiose phosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 442682 [Multi-domain]  Cd Length: 794  Bit Score: 179.57  E-value: 3.52e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   26 LSNDGYSVLVTAAGAGYgMWQGlD-----ITRWREDSTRDCWGQFCYVRDLTDNDLWSIGRQPLFRPSNIYE--HAF-Yg 97
Cdd:COG3459     28 LANPDFGFLVSETGGGY-SWYK-NsrenrLTRWRNDPVSDPPGEYFYLRDEETGDYWSPTWQPVRKPLDEYEcrHGFgY- 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   98 drAELSCHAGDIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLELTSYAEVCLYNRSADMAHpgFAKLFVETQFDEATGA 177
Cdd:COG3459    105 --TRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLGNARDDTAN--FQVTLSTGEVDPEGGA 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  178 LFARRRPRAAGEKATWAVHVSssnlqpAQAAQYETDRLRFLGRGRTTANPMAFDAGaPLSGTTGPVLDPIFCLRRTVRLA 257
Cdd:COG3459    181 ILARNPYNERFNGRVAFFAVS------EPVSSFTGDREEFLGRYGSLANPAALERG-KLSNSVGAGLDPCAALQVDIELA 253
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1830960328  258 PGADARVAFVTGAADDQSAVQFIAKRYAEIDAVEQAFsDASRRY 301
Cdd:COG3459    254 PGEEKELVFLLGQGENKEEARALIARYRDPDAVDAAL-AEVKAY 296
GH94N_like_4 cd11751
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The ...
565-771 1.95e-35

Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. The GH64N domain, as represented by this model, is found near the N-terminus of GH94 members and related proteins with uncharacterized specificities.


Pssm-ID: 213067  Cd Length: 223  Bit Score: 134.80  E-value: 1.95e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  565 DPVTDAPGEVLYLRDEETSDTWTPTPLPLG-PGAVVTVRHGQGYSRYTSFSRHLSQELTVSVAPNDPVKIMRLRLSNEDT 643
Cdd:cd11751      2 DLIKDNWGKYFYIRDDDTGEVWSATYKPLKtEPEDYECVHGIGYSEFTSEYNGIRSSLTVFVPKDDPVEIWSLTLRNTSD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  644 RVRHVTAIYFAEWVLG---------------TQREQTAARVVCERDARSGAIVARNPWAgDFAGRLAFAAASQPARSTTS 708
Cdd:cd11751     82 RERRLSVFSYFEWELGgfpdehrefhklfieTSFDRELNGIYARKYLWGFPDEKGRHNN-RNWPYVAFHAASEPVVSYDG 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830960328  709 DRTEFLGKYGSVFQPAALGRTDLAERFGPLLDPCAALMVDISLRPSESREIVFILGQAADLDE 771
Cdd:cd11751    161 DKESFIGMYGSEENPDAVAMGGLSNSVGRFEDAIGVLQHEVTLEPGEEKTIHFTLGAAESGEE 223
GH94N_ChBP_like cd11755
N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins; The glycoside ...
500-784 1.66e-34

N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes chitobiose phosphorylase (EC:2.4.1.-). This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Chitobiose phosphorylase catalyzes the reversible phosphate dependent hydrolysis of chitobiose [(GlcNAc)2] into alpha-GlcNAc-1-phosphate and GlcNAc. In some organisms, ChBP may be involved in the production of GlcNac-6-phosphate in intracellular pathways.


Pssm-ID: 213071 [Multi-domain]  Cd Length: 300  Bit Score: 134.67  E-value: 1.66e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  500 GGFAADGHEYVV-RVDAlkpqaptlpPAPWTNVIANPHFGCLTTEAGLGYTWAENSQMNRLTPW-SNDPVTDAPGEVLYL 577
Cdd:cd11755      4 GYFDDENREYVItRPDT---------PTPWTNYLGSGEYGAIISNNAGGYSFYKSPANGRITRFrFNSVPMDRPGRYVYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  578 RDEETSDTWTPTPLPLGP---GAVVTVRHGQGYSRYTSFSRHLSQELTVSVAPNDPVKIMRLRLSNEDTRVRHVTAIYFA 654
Cdd:cd11755     75 RDNESGDYWSASWQPVGKpldEYKYECRHGTGYTTIESEYKGIAAETTYFVPLDQDYEIWDVKITNTSSRKRKLSVFSYA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  655 E---------------WVLGTQREQTAARVVCerdarsgAIVARNPWAG--DFAGRLAFAAASQPARSTTSDRTEFLGKY 717
Cdd:cd11755    155 EfsfhwnaeqdqqnlqYSLYISRTSYKDGIIE-------YDNYYNLDDDpnGDERYRFFTSAGAEVDGFDGSRDRFIGPY 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1830960328  718 GSVFQPAALGRTDLAERFGPLLDPCAALMVDISLRPSESREIVFILGQAADlDEVSRLVHEHTDLER 784
Cdd:cd11755    228 RSESNPIAVERGKCSNSLATGGNHCGALQSDITLAPGEEKEIIFILGVGNR-EEGRAIRAKYSDPEA 293
GH94N_ChvB_NdvB_1_like cd11756
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ...
26-284 4.17e-33

First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This first of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.


Pssm-ID: 213072 [Multi-domain]  Cd Length: 284  Bit Score: 129.93  E-value: 4.17e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   26 LSNDGYSVLVTAAGAGY------GMWQgldITRWREDSTRDCWGQFCYVRDLTDNDLWSIGRQPLfRPSNIYE--HAF-Y 96
Cdd:cd11756     36 IANPGFGFLVSESGSGYtwaensRENR---LTPWSNDPVSDPPGEALYLRDEETGEVWSPTPLPI-RGGGPYRvrHGFgY 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   97 gdrAELSCHAGDIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLELTSYAEVCLYNRSADMAhpgfakLFVETQFDEATG 176
Cdd:cd11756    112 ---SRFEHRSHGIEQELTVFVPRDDPVKISRLRLRNTSGRPRRLSVTYYAEWVLGVNREKTA------PHIVTEYDEETG 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  177 ALFARRRPRA--AGEKA--TWAVHVSSsnlqpaqaaqYETDRLRFLGRGRTTANPMAFDAGaPLSGTTGPVLDPIFCLRR 252
Cdd:cd11756    183 ALLARNPYNEdfGGRVAflAVSGGPRS----------FTGDRREFIGRNGSLANPAALKRG-RLSGRTGAGLDPCAALQV 251
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1830960328  253 TVRLAPGADARVAFVTGAADDQSAVQFIAKRY 284
Cdd:cd11756    252 DLELAPGEEKEIVFLLGEADDAEEARALIRRY 283
GH94N_like_4 cd11751
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The ...
56-273 3.97e-28

Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. The GH64N domain, as represented by this model, is found near the N-terminus of GH94 members and related proteins with uncharacterized specificities.


Pssm-ID: 213067  Cd Length: 223  Bit Score: 113.61  E-value: 3.97e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   56 DSTRDCWGQFCYVRDLTDNDLWSIGRQPLFRPSNIYE--HAFYGDRAELSCHagDIEIVSKICVAPDVDVEVRMLTVTNH 133
Cdd:cd11751      2 DLIKDNWGKYFYIRDDDTGEVWSATYKPLKTEPEDYEcvHGIGYSEFTSEYN--GIRSSLTVFVPKDDPVEIWSLTLRNT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  134 GTRERTLELTSYAEVCLYNRSADmaHPGFAKLFVETQFDEATGALFARRR----PRAAGEKAT--WAVHVSSSNLQPAQA 207
Cdd:cd11751     80 SDRERRLSVFSYFEWELGGFPDE--HREFHKLFIETSFDRELNGIYARKYlwgfPDEKGRHNNrnWPYVAFHAASEPVVS 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1830960328  208 aqYETDRLRFLGRGRTTANPMAFDAGApLSGTTGPVLDPIFCLRRTVRLAPGADARVAFVTGAADD 273
Cdd:cd11751    158 --YDGDKESFIGMYGSEENPDAVAMGG-LSNSVGRFEDAIGVLQHEVTLEPGEEKTIHFTLGAAES 220
GH94N_ChBP_like cd11755
N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins; The glycoside ...
24-294 1.29e-24

N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes chitobiose phosphorylase (EC:2.4.1.-). This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Chitobiose phosphorylase catalyzes the reversible phosphate dependent hydrolysis of chitobiose [(GlcNAc)2] into alpha-GlcNAc-1-phosphate and GlcNAc. In some organisms, ChBP may be involved in the production of GlcNac-6-phosphate in intracellular pathways.


Pssm-ID: 213071 [Multi-domain]  Cd Length: 300  Bit Score: 105.78  E-value: 1.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   24 ALLSND--GYSVLVTAAgagYGMwqgldITRWREDSTR-DCWGQFCYVRDLTDNDLWSIGRQPLFRPSNIYEHafygdra 100
Cdd:cd11755     35 AIISNNagGYSFYKSPA---NGR-----ITRFRFNSVPmDRPGRYVYLRDNESGDYWSASWQPVGKPLDEYKY------- 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  101 elSCHAG-----------DIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLELTSYAEVCLY-NRSADMAHPGFAKLFVE 168
Cdd:cd11755    100 --ECRHGtgyttieseykGIAAETTYFVPLDQDYEIWDVKITNTSSRKRKLSVFSYAEFSFHwNAEQDQQNLQYSLYISR 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  169 TQFDEatGALFARRRPRAAGEKATWAVHV--SSSNlqpAQAAQYETDRLRFLGRGRTTANPMAFDAGApLSGTTGPVLDP 246
Cdd:cd11755    178 TSYKD--GIIEYDNYYNLDDDPNGDERYRffTSAG---AEVDGFDGSRDRFIGPYRSESNPIAVERGK-CSNSLATGGNH 251
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1830960328  247 IFCLRRTVRLAPGADARVAFVTGAADDQSAVQFIAKrYAEIDAVEQAF 294
Cdd:cd11755    252 CGALQSDITLAPGEEKEIIFILGVGNREEGRAIRAK-YSDPEAVDAEF 298
GH94N_CBP_like cd11754
N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside ...
508-764 7.89e-24

N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20) or cellobiose:phosphate alpha-D-glucosyltransferase, or CepA. This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Cellobiose phosphorylase participates in the degradation of cellulose, it catalyzes the phosphate dependent hydrolysis of cellobiose into alpha-D-glucose-1-phosphate and D-glucose, a reversible reaction.


Pssm-ID: 213070 [Multi-domain]  Cd Length: 303  Bit Score: 103.47  E-value: 7.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  508 EYVVrvdalkpqapTLP--PAPWTNVIANPHFGCLTTEAGLGYTWAENSQMNRLTPWS-NDPVTDAPGEVLYLRDEET-- 582
Cdd:cd11754     12 EYVI----------TTPdtPLPWINYLGSEDFFSLISNTAGGYSFYKDARLRRLTRYRyNNVPLDNGGRYFYIKDGGTvw 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  583 SDTWTPTPLPLGPgavVTVRHGQGYSRYTSFSRHLSQELTVSVAPNDPVKIMRLRLSNEDTRVRHVTAIYFAEWVL---- 658
Cdd:cd11754     82 NPGWKPVKTPLDS---YECRHGLGYTRITGEKNGIEAEVLYFVPLGENAEIWRLTLTNTSDSPKKLKLFSFVEFCLwnal 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  659 --GT--QREQTAARVVCErdarSGAIV-------ARNPWagdfagrlAFAAASQPARSTTSDRTEFLGKYGSVFQPAAL- 726
Cdd:cd11754    159 ddMTnfQRNLSTGEVEVE----GSVIYhkteyreRRNHY--------AFFAVNAPIDGFDTDRDAFLGLYNGFDEPQAVl 226
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1830960328  727 -GRTDLAERFGplLDPCAALMVDISLRPSESREIVFILG 764
Cdd:cd11754    227 eGKSTNSVAHG--WSPIGSHHVELTLAPGESKELIFVLG 263
GH94N_ChvB_NdvB_2_like cd11753
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ...
521-781 6.61e-23

Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This second of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.


Pssm-ID: 213069 [Multi-domain]  Cd Length: 336  Bit Score: 101.45  E-value: 6.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  521 PTLPPAPWTNVIANPHFGCLTTEAGLGYTWAENSQMNRltpWSNDPVTDAPGEVLYLRDEETSDTWTPTPLPLG-PGAVV 599
Cdd:cd11753     55 TPDTALPEVHLLSNGRYSVMLTASGSGYSRWNDLAVTR---WREDATRDNWGSFIYLRDVDSGKVWSATYQPTRdPPDEY 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  600 TVRHGQGYSRytsFSRH---LSQELTVSVAPNDPVKIMRLRLSNEDTRVRHVTAIYFAEWVLGTQREQTAAR------VV 670
Cdd:cd11753    132 EVVFSEDRAE---FRRRdggIETTTEVVVSPEDDAEIRRVTLTNLSRRPRELEVTSYAEVVLAPPAADEAHPafsklfVQ 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  671 CERDARSGAIVA-RNPWAGDFAGRLAF---AAASQPARSTT--SDRTEFLGKYGSVFQPAALG-RTDLAERFGPLLDPCA 743
Cdd:cd11753    209 TEFLPEQGALLAtRRPRSPDEPPPWAAhfvAVEGEAVGPLQyeTDRARFIGRGRSLANPAAMDdGAPLSGTVGAVLDPIF 288
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1830960328  744 ALMVDISLRPSESREIVFILGQAADLDEVSRLVHEHTD 781
Cdd:cd11753    289 SLRRRVRLPPGETARVTFVTGVADSREEALELADKYRD 326
CBM_X smart01068
Putative carbohydrate binding domain;
497-567 4.51e-21

Putative carbohydrate binding domain;


Pssm-ID: 215008 [Multi-domain]  Cd Length: 62  Bit Score: 87.63  E-value: 4.51e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830960328   497 NGLGGFAADGHEYVVRVDalkpqaPTLPPAPWTNVIANPHFGCLTTEAGLGYT-WAENSqmnrLTPWSNDPV 567
Cdd:smart01068    1 NGLGGFDDDGREYVRTLD------GPDTPAPWINVLSNGRYGVMVSASGSGYSrWADNS----LTRWRNDPV 62
GH94N_like cd11746
N-terminal domain of glycoside hydrolase family 94 and related domains; The glycoside ...
67-269 4.02e-20

N-terminal domain of glycoside hydrolase family 94 and related domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. This GH64N domain also occurs in tandem repeat arrangements (not at the N-terminus) in cyclic beta 1-2 glucan synthetase and related proteins, and as a standalone domain in distantly related proteins of unknown function.


Pssm-ID: 213062  Cd Length: 179  Bit Score: 89.10  E-value: 4.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   67 YVRDLTDNDLWSIGRQPLFRPSNIYEhaFYGDRAELSCHAGDIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLELTSYA 146
Cdd:cd11746      2 YFYLSDDGDKWSLGWQPVRREAEHYE--VRLGYVTFENEYNGIEAETTIFVPPDDPGEIQRVKLTNTGDRPRELTLFPYF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  147 EVCLynrsadmahpgFAKLFVETQFDEATGALFARRRPRaagekatwavhvSSSNLQPAQAAQyETDRLRFLGRGRTT-A 225
Cdd:cd11746     80 EWCL-----------PDALFQGTSYDPEGGAVNCTTYYS------------YNIGARPAFYAT-SFKPDDFDGDGGRTlA 135
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1830960328  226 NPMAFDAGAPlSGTTGPVLDPIFCLRRTVRLAPGADARVAFVTG 269
Cdd:cd11746    136 NPLAVVAGQL-SNTVGRVEDPIAALAIRFALEPGESKRYTFALG 178
GH94N_CBP_like cd11754
N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside ...
26-296 1.71e-17

N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20) or cellobiose:phosphate alpha-D-glucosyltransferase, or CepA. This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Cellobiose phosphorylase participates in the degradation of cellulose, it catalyzes the phosphate dependent hydrolysis of cellobiose into alpha-D-glucose-1-phosphate and D-glucose, a reversible reaction.


Pssm-ID: 213070 [Multi-domain]  Cd Length: 303  Bit Score: 84.60  E-value: 1.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   26 LSNDGYSVLVTAAGAGYGMWQG---LDITRWR-EDSTRDCWGQFCYVRDltDNDLWSIGRQPLFRPSNIYEhafygdrae 101
Cdd:cd11754     28 LGSEDFFSLISNTAGGYSFYKDarlRRLTRYRyNNVPLDNGGRYFYIKD--GGTVWNPGWKPVKTPLDSYE--------- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  102 lsCHAG-----------DIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLELTSYAEVCLYNRSADMAHpgFAKLF---- 166
Cdd:cd11754     97 --CRHGlgytritgeknGIEAEVLYFVPLGENAEIWRLTLTNTSDSPKKLKLFSFVEFCLWNALDDMTN--FQRNLstge 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  167 VE---------TQFDEatgalfarRRPRAAgekatwavhVSSSNlqpAQAAQYETDRLRFLGRGRTTANPMAFDAGAPls 237
Cdd:cd11754    173 VEvegsviyhkTEYRE--------RRNHYA---------FFAVN---APIDGFDTDRDAFLGLYNGFDEPQAVLEGKS-- 230
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830960328  238 gtTGPVLD---PIFCLRRTVRLAPGADARVAFVTGAADDQSAVQFIAK-------------RYAEIDAVEQAFSD 296
Cdd:cd11754    231 --TNSVAHgwsPIGSHHVELTLAPGESKELIFVLGYVENPDDEKWESPgvinkkpakelieRFATPEAVDAAFAE 303
GH94N_like cd11746
N-terminal domain of glycoside hydrolase family 94 and related domains; The glycoside ...
576-765 1.00e-15

N-terminal domain of glycoside hydrolase family 94 and related domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. This GH64N domain also occurs in tandem repeat arrangements (not at the N-terminus) in cyclic beta 1-2 glucan synthetase and related proteins, and as a standalone domain in distantly related proteins of unknown function.


Pssm-ID: 213062  Cd Length: 179  Bit Score: 76.39  E-value: 1.00e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  576 YLRDEETSDTWTPTPLPlgpgAVVTVRHGQGYSRYTSFSRH---LSQELTVSVAPNDPVKIMRLRLSNEDTRVRHVTAIY 652
Cdd:cd11746      2 YFYLSDDGDKWSLGWQP----VRREAEHYEVRLGYVTFENEyngIEAETTIFVPPDDPGEIQRVKLTNTGDRPRELTLFP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  653 FAEWVLGtqreqTAARVVCERDARSGAIVARNPWAGDFAGRLAFAAASQparsTTSDrteFLGKYGSVFQ-PAALGRTDL 731
Cdd:cd11746     78 YFEWCLP-----DALFQGTSYDPEGGAVNCTTYYSYNIGARPAFYATSF----KPDD---FDGDGGRTLAnPLAVVAGQL 145
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1830960328  732 AERFGPLLDPCAALMVDISLRPSESREIVFILGQ 765
Cdd:cd11746    146 SNTVGRVEDPIAALAIRFALEPGESKRYTFALGI 179
CBM_X smart01068
Putative carbohydrate binding domain;
1-58 3.62e-14

Putative carbohydrate binding domain;


Pssm-ID: 215008 [Multi-domain]  Cd Length: 62  Bit Score: 68.37  E-value: 3.62e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830960328     1 MATSTADAPRHDSIAELN----PSSAVALLSNDGYSVLVTAAGAGYGMWQGLDITRWREDST 58
Cdd:smart01068    1 NGLGGFDDDGREYVRTLDgpdtPAPWINVLSNGRYGVMVSASGSGYSRWADNSLTRWRNDPV 62
GH94N_like_3 cd11750
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The ...
500-771 9.13e-10

Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. The GH64N domain, as represented by this model, is found at the N-terminus of GH94 members with uncharacterized specificities.


Pssm-ID: 213066 [Multi-domain]  Cd Length: 282  Bit Score: 61.34  E-value: 9.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  500 GGFAADGHEYVVrvdalkpqapTLP--PAPWTNVIANPHFGCLTTEAGLGYTWAENSQMNRLTPW-SNDPVTDAPGEVLY 576
Cdd:cd11750      2 GYFDDANKEYVI----------TTPktPIKWINYVGTLDFGGFVDHTGGSLVCKGDPALNRITKYiAQLPSSDFKGSTIY 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  577 LR--DEETSDTWTPTPLP-LGPGAVVTVRHGQGYSRYTSFSRHLSQELTVSVAPNDPVKIMRLRLSNEDTRVRHVTAI-- 651
Cdd:cd11750     72 IRvkDGDNYKIFSPFYVPtLDKYDKYECHVGLGYSRIIAEAYGIRTEITIFVPEGDQVLLQDIKVTNIRDKPVEVDVIpv 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  652 ----YF--------AEWVLGTQR----EQTAARVVCERDARSGAIVARNpwagdfagrlaFAAASQPARSTTSDRTEFLG 715
Cdd:cd11750    152 veytHFdalkqltnADWVPQTMTskahQEENGHTVLEQYAFMKRDYAVN-----------YFTSNRPVSSFEGDRRSFLG 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1830960328  716 K--YGSVFQPAALGRTDLAERFGPLLDPCAALMVDIS-LRPSESREIVFILGQAADLDE 771
Cdd:cd11750    221 QneYGTWANPLSLQNDELSNYECLRGDNIGALMHHLGwLAPGETKRVITQLGQEESLKA 279
GH94N_NdvB_like cd11748
Glycoside hydrolase family 94 N-terminal-like domain of NdvB-like proteins; The glycoside ...
571-779 1.42e-08

Glycoside hydrolase family 94 N-terminal-like domain of NdvB-like proteins; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel)]. The GH64N domain, as represented by this model, is found at the N-terminus of largely uncharacterized proteins, some members from Xanthomonas campestris and related organisms are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.


Pssm-ID: 213064 [Multi-domain]  Cd Length: 294  Bit Score: 57.71  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  571 PGEVLYLRDEETSDTWT----PTPLPL-------GPGAVVTVRHGQGysrytsfsrhLSQELTVSVAPNDPVKIMRLRLS 639
Cdd:cd11748     74 PGRFFYVKDEDTGELFSapyePVRRPPdsfafsvGKNDIRWVVEQDG----------LEVELTLSLPVDDPAELWEVKVR 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328  640 NEDTRVRHVTAI-YF----AEWVlgtqrEQTAarvvcERDARSGAIVAR--NPW--AGDFAGR-----LAFAAASQPARS 705
Cdd:cd11748    144 NLSDRARKLSLYpYFpvgyMSWM-----NQSA-----RYDEGLNAIVASsvTPYqkVEDYFKNkdlkdKTFLLADRKPDS 213
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1830960328  706 TTSDRTEFLGKyGSVFQPAALGRTDLAERFGPLLDPCAALMVDISLRPSESREIVFILGQAADLDEVSRLVHEH 779
Cdd:cd11748    214 WEARQEAFEGE-GGLHNPSALQAPTLANGDARYETPAAVMQYRLTLDPGETEQYRFVFGPAKDEAEIAQLRARY 286
GH94N_NdvB_like cd11748
Glycoside hydrolase family 94 N-terminal-like domain of NdvB-like proteins; The glycoside ...
63-145 3.68e-04

Glycoside hydrolase family 94 N-terminal-like domain of NdvB-like proteins; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel)]. The GH64N domain, as represented by this model, is found at the N-terminus of largely uncharacterized proteins, some members from Xanthomonas campestris and related organisms are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.


Pssm-ID: 213064 [Multi-domain]  Cd Length: 294  Bit Score: 44.23  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830960328   63 GQFCYVRDLTDNDLWSIGRQPLFRPSNIYEHAFYGDRAELSCHAGDIEIVSKICVAPDVDVEVRMLTVTNHGTRERTLEL 142
Cdd:cd11748     75 GRFFYVKDEDTGELFSAPYEPVRRPPDSFAFSVGKNDIRWVVEQDGLEVELTLSLPVDDPAELWEVKVRNLSDRARKLSL 154

                   ...
gi 1830960328  143 TSY 145
Cdd:cd11748    155 YPY 157
 
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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