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Conserved domains on  [gi|1663150213|gb|QCT77870|]
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glycosidase [Bacteroides fragilis]

Protein Classification

glycoside hydrolase family 130 protein( domain architecture ID 10173007)

glycoside hydrolase family 130 protein is involved in the bacterial utilization of mannans or N-linked glycans.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH130 cd08993
Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) ...
 42-323 9.01e-163

Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), among others that have yet to be characterized. They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. This family includes Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) and beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2), enzymes that phosphorolyze beta-mannosidic linkages at the non-reducing ends of their substrates, and have substantially diverse substrate specificity that are determined by three loop regions.


:

Pssm-ID: 350107 [Multi-domain]  Cd Length: 279  Bit Score: 455.00  E-value: 9.01e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  42 PTSNSIFNSAVVPFKDGYAGVFRCDDTNRRMRLHVGFSKDAVHWDINEEPLKFQCDDAEVGTWVYGYDPRVCFIEDRYYV 121
Cdd:cd08993     1 YPANSVFNAGAVKFNGKYLLLFRVEDLNGRSFLGLAESDDGIHFTVEPEPILTPDEPFEPYEETGVYDPRITKIDDTYYI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 122 TWCNGY-HGPTIGVAYTYDFVTFHQLENAFIPFNRNGVLFPRKINGRFAMLSRPSDNGHTPFGDIFYSESPDMEFWGRHR 200
Cdd:cd08993    81 TFAADSdHGPRIGLARTKDFKTFERLELISEPDNRNGVLFPEKINGKYARLDRPSDGGHTSGGDIWISYSPDLIHWGNSR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 201 HVMSPapfEDSAWQCTKIGAGPIPIETSEGWLLIYHGVLASCNGFVYSFGSALLDIDQPWKVKFRSGPYLISPQKDYECM 280
Cdd:cd08993   161 LVMGP---RPGPWDNDKIGPGAPPIKTEEGWLLIYHGVRTTCSGFVYRLGAALLDLEDPSKVIARSREPILAPEEPYERV 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1663150213 281 GDVPNVCFPCAALHDsETGRIAIYYGCADTVTGLAFGYIPEII 323
Cdd:cd08993   238 GDVPNVVFPCGAIVE-EDGEVKIYYGAADTVICLATATIDDLV 279
 
Name Accession Description Interval E-value
GH130 cd08993
Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) ...
 42-323 9.01e-163

Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), among others that have yet to be characterized. They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. This family includes Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) and beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2), enzymes that phosphorolyze beta-mannosidic linkages at the non-reducing ends of their substrates, and have substantially diverse substrate specificity that are determined by three loop regions.


Pssm-ID: 350107 [Multi-domain]  Cd Length: 279  Bit Score: 455.00  E-value: 9.01e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  42 PTSNSIFNSAVVPFKDGYAGVFRCDDTNRRMRLHVGFSKDAVHWDINEEPLKFQCDDAEVGTWVYGYDPRVCFIEDRYYV 121
Cdd:cd08993     1 YPANSVFNAGAVKFNGKYLLLFRVEDLNGRSFLGLAESDDGIHFTVEPEPILTPDEPFEPYEETGVYDPRITKIDDTYYI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 122 TWCNGY-HGPTIGVAYTYDFVTFHQLENAFIPFNRNGVLFPRKINGRFAMLSRPSDNGHTPFGDIFYSESPDMEFWGRHR 200
Cdd:cd08993    81 TFAADSdHGPRIGLARTKDFKTFERLELISEPDNRNGVLFPEKINGKYARLDRPSDGGHTSGGDIWISYSPDLIHWGNSR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 201 HVMSPapfEDSAWQCTKIGAGPIPIETSEGWLLIYHGVLASCNGFVYSFGSALLDIDQPWKVKFRSGPYLISPQKDYECM 280
Cdd:cd08993   161 LVMGP---RPGPWDNDKIGPGAPPIKTEEGWLLIYHGVRTTCSGFVYRLGAALLDLEDPSKVIARSREPILAPEEPYERV 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1663150213 281 GDVPNVCFPCAALHDsETGRIAIYYGCADTVTGLAFGYIPEII 323
Cdd:cd08993   238 GDVPNVVFPCGAIVE-EDGEVKIYYGAADTVICLATATIDDLV 279
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
24-331 8.39e-157

Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];


Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 440.73  E-value: 8.39e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  24 KDVVWRCSANPIIPRDLLP--TSNSIFNSAVVPFKDGYAGVFRCDDTNRRMRLHVGFSKDAVHWDINEEPLKFQCDDAEV 101
Cdd:COG2152     1 NGILKRYPGNPILTPNDMPrwEVNAVFNPGAVRFNGKFLLLYRVEGRDGKSHLGLARSDDGINFRRDDEPILFPETDYED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 102 GtwvYGYDPRVCFIEDRYYVTWCN-GYHGPTIGVAYTYDFVTFHQLENAFIPFNRNGVLFPRKINGRFAMLSRPSDNGHT 180
Cdd:COG2152    81 T---GVEDPRITKIDGRYYITYTAySGAGARIGLARTKDFKTWERLGLIFPPDNKDAVLFPEKINGKYALLHRPSDGFHT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 181 PFGDIFYSESPDMEFWGRHRHVMSPAPfedSAWQCTKIGAGPIPIETSEGWLLIYHGVLASCNGFVYSFGSALLDIDQPW 260
Cdd:COG2152   158 GGPDIWISYSPDLEHWGDHRIVMGPRP---GTWDSLKIGAGPPPIKTEEGWLLIYHGVRNTAAGLVYRLGAALLDLEDPS 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1663150213 261 KVKFRSGPYLISPQKDYECMGDVPNVCFPCAALHDsETGRIAIYYGCADTVTGLAFGYIPEIIEFTKRTSI 331
Cdd:COG2152   235 KVIARSPEPILEPEEEYERVGDVPNVVFPCGAVVD-EDGTVYIYYGAADTRIALATATLDELLDYLKNTPE 304
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 12-328 4.92e-72

beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the CAZy GH130 family. Several have been characterized as mannosylglucose phosphorylase. This enzyme is part of the mannan catalytic pathway and feeds into the glycolysis cycle. Specifically it catalyzes the reversible phosphorolysis of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine. This family was noted to belong to the Beta fructosidase superfamily in.


Pssm-ID: 397932 [Multi-domain]  Cd Length: 315  Bit Score: 225.83  E-value: 4.92e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  12 PAMPWEERPAGCKDVVWRCSANPIIPRdllptsnSIFNSAVVPFKDG------YAGVFRCDDTN-RRMRLHVGFSKDAVH 84
Cdd:pfam04041   6 PTIDILERPSYITGKDSRITNPVRNPV-------AVFNPAVVLYEKElhvyprVVMGYYKYVSDiASFRIGLEDSYDGIK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  85 WDINEEPLKFQCDDAEVgtwvYG-YDPRVCFIEDRYYVTWCN-GYHGPTIGVAYTYDFVTFHQLENAFIPFN-------- 154
Cdd:pfam04041  79 KTLEPEPIFWPRDKQEF----WGvEDPRVVKINSTYYMTYTGrDYKYWRIEVGTTKDFLTWARLPVKIALFEkrydsikt 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 155 RNGVLFPRKINGRFAMLSRpsdnghtpFGDIFYSESPDMEFWGRH-------RHVMSPAPFEdsawqcTKIGAGPIPIET 227
Cdd:pfam04041 155 SDGNAFPVKIKGKYLMYHR--------VGDIWLAVSPDLVHWENRleplgspRPIMFPNPFE------TKIGWGTPPVET 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 228 SEGWLLIYHGVlaSCNGFVYSFGSALLDIDQpwKVKFRSGPYLISPQKDYECMGDVPNVCFPCAALHDSEtgRIAIYYGC 307
Cdd:pfam04041 221 KEGWLVLIHGV--DTEDLVYRVGAALLDLEG--KVLARTPEYILEPEEEYEEYGDRPNVVFPCGALVDGE--RVIIYYGA 294

                         330       340
                  ....*....|....*....|.
gi 1663150213 308 ADTVTGLAFGYIPEIIEFTKR 328
Cdd:pfam04041 295 ADTAIGLAEIPEEEIMNLLKE 315
 
Name Accession Description Interval E-value
GH130 cd08993
Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) ...
 42-323 9.01e-163

Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), among others that have yet to be characterized. They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. This family includes Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) and beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2), enzymes that phosphorolyze beta-mannosidic linkages at the non-reducing ends of their substrates, and have substantially diverse substrate specificity that are determined by three loop regions.


Pssm-ID: 350107 [Multi-domain]  Cd Length: 279  Bit Score: 455.00  E-value: 9.01e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  42 PTSNSIFNSAVVPFKDGYAGVFRCDDTNRRMRLHVGFSKDAVHWDINEEPLKFQCDDAEVGTWVYGYDPRVCFIEDRYYV 121
Cdd:cd08993     1 YPANSVFNAGAVKFNGKYLLLFRVEDLNGRSFLGLAESDDGIHFTVEPEPILTPDEPFEPYEETGVYDPRITKIDDTYYI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 122 TWCNGY-HGPTIGVAYTYDFVTFHQLENAFIPFNRNGVLFPRKINGRFAMLSRPSDNGHTPFGDIFYSESPDMEFWGRHR 200
Cdd:cd08993    81 TFAADSdHGPRIGLARTKDFKTFERLELISEPDNRNGVLFPEKINGKYARLDRPSDGGHTSGGDIWISYSPDLIHWGNSR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 201 HVMSPapfEDSAWQCTKIGAGPIPIETSEGWLLIYHGVLASCNGFVYSFGSALLDIDQPWKVKFRSGPYLISPQKDYECM 280
Cdd:cd08993   161 LVMGP---RPGPWDNDKIGPGAPPIKTEEGWLLIYHGVRTTCSGFVYRLGAALLDLEDPSKVIARSREPILAPEEPYERV 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1663150213 281 GDVPNVCFPCAALHDsETGRIAIYYGCADTVTGLAFGYIPEII 323
Cdd:cd08993   238 GDVPNVVFPCGAIVE-EDGEVKIYYGAADTVICLATATIDDLV 279
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
24-331 8.39e-157

Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];


Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 440.73  E-value: 8.39e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  24 KDVVWRCSANPIIPRDLLP--TSNSIFNSAVVPFKDGYAGVFRCDDTNRRMRLHVGFSKDAVHWDINEEPLKFQCDDAEV 101
Cdd:COG2152     1 NGILKRYPGNPILTPNDMPrwEVNAVFNPGAVRFNGKFLLLYRVEGRDGKSHLGLARSDDGINFRRDDEPILFPETDYED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 102 GtwvYGYDPRVCFIEDRYYVTWCN-GYHGPTIGVAYTYDFVTFHQLENAFIPFNRNGVLFPRKINGRFAMLSRPSDNGHT 180
Cdd:COG2152    81 T---GVEDPRITKIDGRYYITYTAySGAGARIGLARTKDFKTWERLGLIFPPDNKDAVLFPEKINGKYALLHRPSDGFHT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 181 PFGDIFYSESPDMEFWGRHRHVMSPAPfedSAWQCTKIGAGPIPIETSEGWLLIYHGVLASCNGFVYSFGSALLDIDQPW 260
Cdd:COG2152   158 GGPDIWISYSPDLEHWGDHRIVMGPRP---GTWDSLKIGAGPPPIKTEEGWLLIYHGVRNTAAGLVYRLGAALLDLEDPS 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1663150213 261 KVKFRSGPYLISPQKDYECMGDVPNVCFPCAALHDsETGRIAIYYGCADTVTGLAFGYIPEIIEFTKRTSI 331
Cdd:COG2152   235 KVIARSPEPILEPEEEYERVGDVPNVVFPCGAVVD-EDGTVYIYYGAADTRIALATATLDELLDYLKNTPE 304
GH130 cd18615
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 45-317 1.14e-83

Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350127 [Multi-domain]  Cd Length: 277  Bit Score: 254.07  E-value: 1.14e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  45 NSIFNSAVVPFKDGYAGVFRCDDTNRRMRLHVGFSKDAVH-WDINEEPLkFQCDDAEVGTWVYGY-DPRVCFIED--RYY 120
Cdd:cd18615     6 NAVFNPGAAKLGGETLLLVRVEDRRGFSHLTVARSADGVTnWKIDPKPT-LEPDPEDYPEEMWGIeDPRITWLEElgRYA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 121 VTWCN-GYHGPTIGVAYTYDFVTFHQLENAFIPFNRNGVLFPRKINGRFAMLSRPSDNGHtpfGDIFYSESPDMEFWGRH 199
Cdd:cd18615    85 ITYTAySPAGPGVSLATTKDFKTFERLGLVMPPEDKDAALFPRRINGRWALLHRPVSAGR---AHIWISFSPDLKHWGDH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 200 RHVMSPAPfeDSAWQCTKIGAGPIPIETSEGWLLIYHGVLASCNGFVYSFGSALLDIDQPWKVKFRSGPYLISPQKDYEC 279
Cdd:cd18615   162 RPVLPARR--GPWWDAVKVGLGPPPIETPEGWLIIYHGVKETASGSIYRVGLALLDLEDPTKVIRRSDEWVLGPEEPYER 239

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1663150213 280 MGDVPNVCFPCAALHDSETGRIAIYYGCADTVTGLAFG 317
Cdd:cd18615   240 IGDVPNVVFPCGAILDEDGDELRLYYGAADTCIALATA 277
GH130 cd18607
Glycoside hydrolase family 130; Members of the glycosyl hydrolase family 130, as classified by ...
 44-316 1.49e-77

Glycoside hydrolase family 130; Members of the glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350119 [Multi-domain]  Cd Length: 269  Bit Score: 238.37  E-value: 1.49e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  44 SNSIFNSAVVPFKDGYAGVFRC-DDTNRRMRLHVGFSKDAVHWDINEEPLKFQCDDAEVGTWvYGYDPRVCFIEDRYYVT 122
Cdd:cd18607     3 SAAVFNPGAILHDGKYHLLYRAvGKGTRRSSIGYARSKDGIHFERLDEPPLYPPPENPYEKG-GCEDPRITKIDDTYYMT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 123 WC--NGyHGPTIGVAYTYDFVTFHQLENAFI--PFNRNGVLFPRKINGRFAMLSRPSdnghtpFGDIFYSESPDMEFWGR 198
Cdd:cd18607    82 YTayDG-FGPRLALATTKDLKNWERHGLAFPpaPENKNGVIFPEKINGKYAMLHRPD------GPDIWLATSDDLIHWGD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 199 HRHVMSP-APFEDSAwqctKIGAGPIPIETSEGWLLIYHGVLASCNGFVYSFGSALLDIDQPWKVKFRSGPYLISPQKDY 277
Cdd:cd18607   155 HKPLLKPrKGTWDSA----KVGAGPPPIKTKKGWLLLYHGVNETAAGNRYRLGAALLDLNDPTRVLYRSDKPILEPEEDY 230

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1663150213 278 ECMGDVPNVCFPCAALHDsETGRIAIYYGCADTVTGLAF 316
Cdd:cd18607   231 EKSGYVPNVVFPCGAVAI-DGDELKLYYGAADTKVAVAT 268
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 12-328 4.92e-72

beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the CAZy GH130 family. Several have been characterized as mannosylglucose phosphorylase. This enzyme is part of the mannan catalytic pathway and feeds into the glycolysis cycle. Specifically it catalyzes the reversible phosphorolysis of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine. This family was noted to belong to the Beta fructosidase superfamily in.


Pssm-ID: 397932 [Multi-domain]  Cd Length: 315  Bit Score: 225.83  E-value: 4.92e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  12 PAMPWEERPAGCKDVVWRCSANPIIPRdllptsnSIFNSAVVPFKDG------YAGVFRCDDTN-RRMRLHVGFSKDAVH 84
Cdd:pfam04041   6 PTIDILERPSYITGKDSRITNPVRNPV-------AVFNPAVVLYEKElhvyprVVMGYYKYVSDiASFRIGLEDSYDGIK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  85 WDINEEPLKFQCDDAEVgtwvYG-YDPRVCFIEDRYYVTWCN-GYHGPTIGVAYTYDFVTFHQLENAFIPFN-------- 154
Cdd:pfam04041  79 KTLEPEPIFWPRDKQEF----WGvEDPRVVKINSTYYMTYTGrDYKYWRIEVGTTKDFLTWARLPVKIALFEkrydsikt 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 155 RNGVLFPRKINGRFAMLSRpsdnghtpFGDIFYSESPDMEFWGRH-------RHVMSPAPFEdsawqcTKIGAGPIPIET 227
Cdd:pfam04041 155 SDGNAFPVKIKGKYLMYHR--------VGDIWLAVSPDLVHWENRleplgspRPIMFPNPFE------TKIGWGTPPVET 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 228 SEGWLLIYHGVlaSCNGFVYSFGSALLDIDQpwKVKFRSGPYLISPQKDYECMGDVPNVCFPCAALHDSEtgRIAIYYGC 307
Cdd:pfam04041 221 KEGWLVLIHGV--DTEDLVYRVGAALLDLEG--KVLARTPEYILEPEEEYEEYGDRPNVVFPCGALVDGE--RVIIYYGA 294

                         330       340
                  ....*....|....*....|.
gi 1663150213 308 ADTVTGLAFGYIPEIIEFTKR 328
Cdd:pfam04041 295 ADTAIGLAEIPEEEIMNLLKE 315
GH130_Lin0857-like cd18612
Glycoside hydrolase family 130 such as Listeria innocua beta-1,2-mannobiose phosphorylase; ...
 47-315 1.14e-70

Glycoside hydrolase family 130 such as Listeria innocua beta-1,2-mannobiose phosphorylase; This subfamily contains the glycosyl hydrolase family 130 (GH130), as classified by the carbohydrate-active enzymes database (CAZY), enzymes that are phosphorylases and hydrolases for beta-mannosides, and includes Listeria innocua beta-1,2-mannobiose phosphorylase (Lin0857). hey possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Structure of Lin0857 shows beta-1,2-mannotriose bound in a U-shape, interacting with a phosphate analog at both ends. Lin0857 has a unique dimer structure connected by a loop, with a significant open-close loop displacement observed for substrate entry. A long loop, which is exclusively present in Lin0857, covers the active site to limit the pocket size.


Pssm-ID: 350124 [Multi-domain]  Cd Length: 261  Bit Score: 220.46  E-value: 1.14e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  47 IFNSAVVPFKDGYAGVFRCDDTNRRMRlhvgfSKDAVHWDINEEPLKFQCDDAEVgtwvYGY-DPRVCFIEDRYYVTwcn 125
Cdd:cd18612     6 VFNPGAARYGDEIILLLRVAEHLRLAR-----SRDGIHFTVDEKPALFPEGPYEA----FGIeDPRITRIDDTYYIT--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 126 gY-----HGPTIGVAYTYDFVTFHQLENAFIPFNRNGVLFPRKINGRFAMLSRPSDNGhtpFG--DIFYSESPDMEFWGR 198
Cdd:cd18612    74 -YtavseYGIATALASTKDFKTFERHGVIFPPENKDVVIFPEKINGKYYALHRPVPSG---FGkpEIWIAESPDLLHWGN 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 199 HRHVMSPAPfedSAWQCTKIGAGPIPIETSEGWLLIYHGVLASCngfVYSFGSALLDIDQPWKVKFRSGPYLISPQKDYE 278
Cdd:cd18612   150 HRHLAGPRP---GMWDSGRIGAGAVPIKTEKGWLEIYHGADENN---RYCLGALLLDLEDPSKVIARSEEPILEPEAPYE 223

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1663150213 279 CMGDVPNVCFPCAALHDSetGRIAIYYGCADTVTGLA 315
Cdd:cd18612   224 KEGFFGNVVFTCGAVVEG--DTLLIYYGAADTSIAVA 258
GH130 cd18614
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 109-315 1.07e-58

Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350126 [Multi-domain]  Cd Length: 276  Bit Score: 190.32  E-value: 1.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 109 DPRVCFIEDRYYVTWC--NGYHGPTIGVAY--TYDFVTFH-------QLENAFIPfNRNGVLFPRKINGRFAMLsrpsdn 177
Cdd:cd18614    67 DPRITKIDDTYYMTYTayDGWPPPRVALTSisTKDFLNFKwnwvippLISPPGVD-DKDAVLFPEKINGKYALL------ 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 178 gHTPFGDIFYSESPDMEF---WGRHRHVMSPAPFEdsaWQCTKIGAGPIPIETSEGWLLIYHGVlaSCNGFVYSFGSALL 254
Cdd:cd18614   140 -HRIGPDIWIDYSDDLDFgknWIDSKIILEPRPGM---WDSRKIGAGAPPIKTKKGWLLIYHGV--DDDDRVYRLGAALL 213

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1663150213 255 DIDQPWKVKFRSGPYLISPQKDYECMGDVPNVCFPC-AALHDsetGRIAIYYGCADTVTGLA 315
Cdd:cd18614   214 DLEDPTKVIARSPEPILEPEEDYEKEGLVPNVVFPCgAVVKD---DTLFVYYGGADKVIGVA 272
GH43_62_32_68_117_130 cd08772
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 48-306 1.58e-42

Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.


Pssm-ID: 350091 [Multi-domain]  Cd Length: 257  Bit Score: 147.74  E-value: 1.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  48 FNSAVVPFKDGYAGVFRCDDTNRRMRLHVGFSKDAVHWDINEEPLKFQCDDAEvGTWVYgYDPRVCFIEDRYYVTWCNGY 127
Cdd:cd08772     1 FDPSVVPYNGEYHLFFTIGPKNTRPFLGHARSKDLIHWEEEPPAIVARGGGSY-DTSYA-FDPEVVYIEGTYYLTYCSDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 128 ------HGPTIGVAYTYDFVTF--------HQLENAFIPFNRNGVLFPRKInGRFAMLSRPSDNGHTPFGDIFYSESPDM 193
Cdd:cd08772    79 lgdilrHGQHIGVAYSKDPKGPwtrkdaplIEPPNAYSPKNRDPVLFPRKI-GKYYLLNVPSDNGHTRFGKIAIAESPD* 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 194 EFWGRHRHVMSPapfedsaWQCTKIGAGPIPIETSEGWLLIYHGVlaSCNGFVYSFGSALLDIDQPWKVKFRSgpyliSP 273
Cdd:cd08772   158 LHWINHSFVYNY-------NEQGKVGEGPSLWKTKGGWYLIYHAN--TLTGYGYGFGYALGDLDDPSKVLYRS-----RP 223

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1663150213 274 QKDYECMGDVPNVCFPCAALHDSeTGRIAIYYG 306
Cdd:cd08772   224 EEEYETVGFKPNVVAPAAFLCDS-TGIVAIIGH 255
GH130 cd18613
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 109-323 6.97e-34

Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350125  Cd Length: 302  Bit Score: 126.08  E-value: 6.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 109 DPR-VCFIED----RYYVTWcNGYHGPTIG--VAYTYDFVTFHqlenaFIPFNRNGV------LFPRKINGRFAMLSRpS 175
Cdd:cd18613    97 DARfVRFTDDdgsvTYYATY-TAYDGRAIRpqLLETRDFRTFK-----VRPLTGPAArnkgmaLFPRKIGGRYAMLSR-Q 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 176 DNghtpfGDIFYSESPDMEFWGRHRHVMSPApfedSAWQCTKIGAGPIPIETSEGWLLIYHGVlascnGFV--YSFGSAL 253
Cdd:cd18613   170 DG-----ENIYLMFSDDLYFWDEAELILKPR----YPWEFVQIGNCGSPIETDEGWLVLTHGV-----GPMrrYSIGAIL 235

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1663150213 254 LDIDQPWKVKFRSGPYLISPQKDyECMGDVPNVCFPCAAL-HDsetGRIAIYYGCADTVTGLAFGYIPEII 323
Cdd:cd18613   236 LDLDDPTKVIGRLREPLLSPDEE-EREGYVPNVVYSCGALvHG---DRLILPYGMSDSATGFATVDLDELL 302
GH130 cd18611
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 48-315 1.03e-32

Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), most of which are as yet uncharacterized. GH130 enzymes are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350123 [Multi-domain]  Cd Length: 289  Bit Score: 122.63  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  48 FNSAVVPFKDGYAGVFRC-----DDTNRRMRLHV---GFSKDAVHWDINEEPLKFQCDdaevgtW-VYG-YDPRVCFIED 117
Cdd:cd18611     7 FNGSVIKDGGKYHLLYRAlsspqEIDGPKLGLSTigyAESKDGVHFENRRQLIKPEEE------WeKYGcEDPRVTKIDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 118 RYYV------TWCNGYHGPTIGVAYTYDFVTFHqlENAFI-PFN-RNGVLFPRKINGRFAML------SRPSDNGHTPFG 183
Cdd:cd18611    81 KYYIfytalsGYPFGPEGIKVAVAITKDFKTIE--EKHLVtPFNaKAMALFPEKINGKYAALltvntdNPPAKIALAYFD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 184 DIfySESPDMEFWGR-----HRHVMspaPFEDSAWQCTKIGAgpIPIETSEGWLLIYHGVLascNGF----VYSFGSALL 254
Cdd:cd18611   159 KI--EDLWSPEYWDKwyanlDDHAL---PLRRSEHDHVEVGA--PPIKTKDGWLLIYSYIQ---NYFsgerVFGIEAALL 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1663150213 255 DIDQPWKVKFRSGPYLISPQKDYECMGDVPNVCFPCAALhdSETGRIAIYYGCADTVTGLA 315
Cdd:cd18611   229 DLNDPRKIIGRTKGPLLVPEEEYELYGLVPNIVFPSGAL--IEGDKLHIYYGAADTVCCLA 287
GH130_BT3780-like cd18610
Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624; This ...
 44-315 9.69e-27

Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624; This subfamily contains glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), and includes Bacteroides enzymes, BT3780 and BACOVA_03624. Members of this family possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. GH130 enzymes have also been shown to target beta-1,2- and beta-1,4-mannosidic linkages where these phosphorylases mediate bond cleavage by a single displacement reaction in which phosphate functions as the catalytic nucleophile. However, some lack the conserved basic residues that bind the phosphate nucleophile, as observed for the Bacteroides enzymes, BT3780 and BACOVA_03624, which are indeed beta-mannosidases that hydrolyze beta-1,2-mannosidic linkages through an inverting mechanism.


Pssm-ID: 350122 [Multi-domain]  Cd Length: 301  Bit Score: 106.90  E-value: 9.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213  44 SNSIFNSAVVPFKDGYAGVFRCDDTNRRM----RLHVGFSKDAVHWDINEEPLKFQCDDAEvgtWVYGY-DPRVCFIED- 117
Cdd:cd18610    12 SKDVFNPAAIVRDGKVYLLYRAEDASGNGngtsRIGLAVSDDGLHFTRLPEPVLYPEEDYE---WPGGCeDPRIVEIEDg 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 118 RYYVTWcNGYHG--PTIGVAYTYDFVTFHQLENAF---------IPFNRNGVLFPR-----KINGRFAMLsrpsdnghtp 181
Cdd:cd18610    89 TYYMTY-TAYDGktARLCLATSTDLVHWTKHGPAFpdadggkyrDLWSKSGAIVPElkgaaKINGKYWMY---------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 182 FGD--IFYSESPD------MEFWGRHRHVMSPAPFEDSAWQctkIGAGPIPIETSEGWLLIYHGVLASCNG-----FVYS 248
Cdd:cd18610   158 WGEsnIYLATSDDlihwtpVEDDGSLRPVLSPRPGKFDSDL---VEPGPPPILTDGGILLIYNGANDGGGGpgypkGTYS 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1663150213 249 FGSALLDIDQPWKVKFRSGPYLISPQKDYECMGDVPNVCFpCAALHDSEtGRIAIYYGCADTVTGLA 315
Cdd:cd18610   235 AGQALFDANDPTKLLARLDKPFLEPETPYEKEGQVNNVVF-VEGLVYFK-GKWLLYYGTADSKIGVA 299
Tachylectin pfam14517
Tachylectin; This family of lectins binds N-acetylglucosamine and N-acetylgalactosamine and ...
 150-232 7.92e-03

Tachylectin; This family of lectins binds N-acetylglucosamine and N-acetylgalactosamine and may be involved in innate immunity. It has a five-bladed beta-propeller structure with five carbohydrate-binding sites, one per beta sheet.


Pssm-ID: 464197 [Multi-domain]  Cd Length: 228  Bit Score: 37.04  E-value: 7.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663150213 150 FIPFNRNGVLFPRKINGRFAMLSRPSDnGHTPFGDifYSESPDMEFWGRHRHVMSPAPfEDSAWQCTKIG--AGPIPIET 227
Cdd:pfam14517 133 SLFFDPDGVLYAITSTGKLVKGRPPAE-SDSDWLQ--NATLVSGEGWRDSRHIISFSP-GGNVWCVSKDNgyRYPPPTAG 208


                  ....*
gi 1663150213 228 SEGWL 232
Cdd:pfam14517 209 APGWL 213
 
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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