NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|521095578|ref|WP_020426481|]
View 

glycoside hydrolase family 130 protein [Paenibacillus riograndensis]

Protein Classification

glycoside hydrolase family 130 protein( domain architecture ID 13035677)

glycoside hydrolase family 130 (GH130) protein may function as a phosphorylase or hydrolase for beta-mannosides; involved in the bacterial utilization of mannans or N-linked glycans

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GH130_Lin0857-like cd18612
Glycoside hydrolase family 130 such as Listeria innocua beta-1,2-mannobiose phosphorylase; ...
 24-339 4.34e-168

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: 468.53  E-value: 4.34e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  24 FRVLGVFNAGVAQFGDEIILLLRIAEaplsdradevlvprlneagtdvlverydktdpgydfsdsrfiardgqtvmltsl 103
Cdd:cd18612    1 LEVIGVFNPGAARYGDEIILLLRVAE------------------------------------------------------ 26

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 104 sHLRVARSKDGIHFDIEPQPALFPEHALEAWGIEDPRVTQIGDIYYITYSSASARGVGAGLAETRDFRTFKRRGLMLAPE 183
Cdd:cd18612   27 -HLRLARSRDGIHFTVDEKPALFPEGPYEAFGIEDPRITRIDDTYYITYTAVSEYGIATALASTKDFKTFERHGVIFPPE 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 184 NKDVMIFPDKINGKYYALHRPVPKSFGSPEMWIAESPDLDHWGNHRFLMGLSEQGWDSARMGGGAVPIRTERGWLALYHG 263
Cdd:cd18612  106 NKDVVIFPEKINGKYYALHRPVPSGFGKPEIWIAESPDLLHWGNHRHLAGPRPGMWDSGRIGAGAVPIKTEKGWLEIYHG 185

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521095578 264 ADSKHRYCMGAVLLDLDDPAKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGALLLDQTVRMYYGAADEVMAVADIP 339
Cdd:cd18612  186 ADENNRYCLGALLLDLEDPSKVIARSEEPILEPEAPYEKEGFFGNVVFTCGAVVEGDTLLIYYGAADTSIAVAEFS 261
 
Name Accession Description Interval E-value
GH130_Lin0857-like cd18612
Glycoside hydrolase family 130 such as Listeria innocua beta-1,2-mannobiose phosphorylase; ...
 24-339 4.34e-168

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: 468.53  E-value: 4.34e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  24 FRVLGVFNAGVAQFGDEIILLLRIAEaplsdradevlvprlneagtdvlverydktdpgydfsdsrfiardgqtvmltsl 103
Cdd:cd18612    1 LEVIGVFNPGAARYGDEIILLLRVAE------------------------------------------------------ 26

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 104 sHLRVARSKDGIHFDIEPQPALFPEHALEAWGIEDPRVTQIGDIYYITYSSASARGVGAGLAETRDFRTFKRRGLMLAPE 183
Cdd:cd18612   27 -HLRLARSRDGIHFTVDEKPALFPEGPYEAFGIEDPRITRIDDTYYITYTAVSEYGIATALASTKDFKTFERHGVIFPPE 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 184 NKDVMIFPDKINGKYYALHRPVPKSFGSPEMWIAESPDLDHWGNHRFLMGLSEQGWDSARMGGGAVPIRTERGWLALYHG 263
Cdd:cd18612  106 NKDVVIFPEKINGKYYALHRPVPSGFGKPEIWIAESPDLLHWGNHRHLAGPRPGMWDSGRIGAGAVPIKTEKGWLEIYHG 185

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521095578 264 ADSKHRYCMGAVLLDLDDPAKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGALLLDQTVRMYYGAADEVMAVADIP 339
Cdd:cd18612  186 ADENNRYCLGALLLDLEDPSKVIARSEEPILEPEAPYEKEGFFGNVVFTCGAVVEGDTLLIYYGAADTSIAVAEFS 261
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
1-348 2.33e-141

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


Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 402.60  E-value: 2.33e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578   1 MNIKRSAQNPVIRIEDvapsRPDFRVLGVFNAGVAQFGDEIILLLRIAEAPlsdradevlvprlneagtdvlverydktd 80
Cdd:COG2152    2 GILKRYPGNPILTPND----MPRWEVNAVFNPGAVRFNGKFLLLYRVEGRD----------------------------- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  81 pgydfsdsrfiardgqtvmltSLSHLRVARSKDGIHFDIEPQPALFPEHALEAWGIEDPRVTQIGDIYYITYSSASARGV 160
Cdd:COG2152   49 ---------------------GKSHLGLARSDDGINFRRDDEPILFPETDYEDTGVEDPRITKIDGRYYITYTAYSGAGA 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 161 GAGLAETRDFRTFKRRGLMLAPENKDVMIFPDKINGKYYALHRPVPK-SFGSPEMWIAESPDLDHWGNHRFLMGLSEQGW 239
Cdd:COG2152  108 RIGLARTKDFKTWERLGLIFPPDNKDAVLFPEKINGKYALLHRPSDGfHTGGPDIWISYSPDLEHWGDHRIVMGPRPGTW 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 240 DSARMGGGAVPIRTERGWLALYHGAD---SKHRYCMGAVLLDLDDPAKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGAL 316
Cdd:COG2152  188 DSLKIGAGPPPIKTEEGWLLIYHGVRntaAGLVYRLGAALLDLEDPSKVIARSPEPILEPEEEYERVGDVPNVVFPCGAV 267

                        330       340       350
                 ....*....|....*....|....*....|...
gi 521095578 317 L-LDQTVRMYYGAADEVMAVADIPLEDIYNTLL 348
Cdd:COG2152  268 VdEDGTVYIYYGAADTRIALATATLDELLDYLK 300
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 102-347 1.85e-65

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: 209.65  E-value: 1.85e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  102 SLSHLRV--ARSKDGIHFDIEPQPALFPEHALEAWGIEDPRVTQIGDIYYITYSSASARGVGAGLAETRDFRTFKRRGLM 179
Cdd:pfam04041  62 DIASFRIglEDSYDGIKKTLEPEPIFWPRDKQEFWGVEDPRVVKINSTYYMTYTGRDYKYWRIEVGTTKDFLTWARLPVK 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  180 LAPEN--------KDVMIFPDKINGKYYALHRPvpksfgsPEMWIAESPDLDHWGNHRFLMGLSEQGWDSA----RMGGG 247
Cdd:pfam04041 142 IALFEkrydsiktSDGNAFPVKIKGKYLMYHRV-------GDIWLAVSPDLVHWENRLEPLGSPRPIMFPNpfetKIGWG 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  248 AVPIRTERGWLALYHGAD-SKHRYCMGAVLLDLDDpaKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGALLLDQTVRMYY 326
Cdd:pfam04041 215 TPPVETKEGWLVLIHGVDtEDLVYRVGAALLDLEG--KVLARTPEYILEPEEEYEEYGDRPNVVFPCGALVDGERVIIYY 292

                         250       260
                  ....*....|....*....|.
gi 521095578  327 GAADEVMAVADIPLEDIYNTL 347
Cdd:pfam04041 293 GAADTAIGLAEIPEEEIMNLL 313
 
Name Accession Description Interval E-value
GH130_Lin0857-like cd18612
Glycoside hydrolase family 130 such as Listeria innocua beta-1,2-mannobiose phosphorylase; ...
 24-339 4.34e-168

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: 468.53  E-value: 4.34e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  24 FRVLGVFNAGVAQFGDEIILLLRIAEaplsdradevlvprlneagtdvlverydktdpgydfsdsrfiardgqtvmltsl 103
Cdd:cd18612    1 LEVIGVFNPGAARYGDEIILLLRVAE------------------------------------------------------ 26

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 104 sHLRVARSKDGIHFDIEPQPALFPEHALEAWGIEDPRVTQIGDIYYITYSSASARGVGAGLAETRDFRTFKRRGLMLAPE 183
Cdd:cd18612   27 -HLRLARSRDGIHFTVDEKPALFPEGPYEAFGIEDPRITRIDDTYYITYTAVSEYGIATALASTKDFKTFERHGVIFPPE 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 184 NKDVMIFPDKINGKYYALHRPVPKSFGSPEMWIAESPDLDHWGNHRFLMGLSEQGWDSARMGGGAVPIRTERGWLALYHG 263
Cdd:cd18612  106 NKDVVIFPEKINGKYYALHRPVPSGFGKPEIWIAESPDLLHWGNHRHLAGPRPGMWDSGRIGAGAVPIKTEKGWLEIYHG 185

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521095578 264 ADSKHRYCMGAVLLDLDDPAKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGALLLDQTVRMYYGAADEVMAVADIP 339
Cdd:cd18612  186 ADENNRYCLGALLLDLEDPSKVIARSEEPILEPEAPYEKEGFFGNVVFTCGAVVEGDTLLIYYGAADTSIAVAEFS 261
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
1-348 2.33e-141

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


Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 402.60  E-value: 2.33e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578   1 MNIKRSAQNPVIRIEDvapsRPDFRVLGVFNAGVAQFGDEIILLLRIAEAPlsdradevlvprlneagtdvlverydktd 80
Cdd:COG2152    2 GILKRYPGNPILTPND----MPRWEVNAVFNPGAVRFNGKFLLLYRVEGRD----------------------------- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  81 pgydfsdsrfiardgqtvmltSLSHLRVARSKDGIHFDIEPQPALFPEHALEAWGIEDPRVTQIGDIYYITYSSASARGV 160
Cdd:COG2152   49 ---------------------GKSHLGLARSDDGINFRRDDEPILFPETDYEDTGVEDPRITKIDGRYYITYTAYSGAGA 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 161 GAGLAETRDFRTFKRRGLMLAPENKDVMIFPDKINGKYYALHRPVPK-SFGSPEMWIAESPDLDHWGNHRFLMGLSEQGW 239
Cdd:COG2152  108 RIGLARTKDFKTWERLGLIFPPDNKDAVLFPEKINGKYALLHRPSDGfHTGGPDIWISYSPDLEHWGDHRIVMGPRPGTW 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 240 DSARMGGGAVPIRTERGWLALYHGAD---SKHRYCMGAVLLDLDDPAKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGAL 316
Cdd:COG2152  188 DSLKIGAGPPPIKTEEGWLLIYHGVRntaAGLVYRLGAALLDLEDPSKVIARSPEPILEPEEEYERVGDVPNVVFPCGAV 267

                        330       340       350
                 ....*....|....*....|....*....|...
gi 521095578 317 L-LDQTVRMYYGAADEVMAVADIPLEDIYNTLL 348
Cdd:COG2152  268 VdEDGTVYIYYGAADTRIALATATLDELLDYLK 300
GH130 cd08993
Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) ...
 24-343 2.40e-113

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: 330.58  E-value: 2.40e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  24 FRVLGVFNAGVAQFGDEIILLLRiaeaplsdradevlvprlneagtdvlVERYDKTdpgydfsdsrfiardgqtvmltsl 103
Cdd:cd08993    1 YPANSVFNAGAVKFNGKYLLLFR--------------------------VEDLNGR------------------------ 30

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 104 SHLRVARSKDGIHFDIEPQPALFPE---HALEAWGIEDPRVTQIGDIYYITYSSASARGVGAGLAETRDFRTFKRRGLML 180
Cdd:cd08993   31 SFLGLAESDDGIHFTVEPEPILTPDepfEPYEETGVYDPRITKIDDTYYITFAADSDHGPRIGLARTKDFKTFERLELIS 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 181 APENKDVMIFPDKINGKYYALHRPVPKSFGSP-EMWIAESPDLDHWGNHRFLMGLSEQGWDSARMGGGAVPIRTERGWLA 259
Cdd:cd08993  111 EPDNRNGVLFPEKINGKYARLDRPSDGGHTSGgDIWISYSPDLIHWGNSRLVMGPRPGPWDNDKIGPGAPPIKTEEGWLL 190

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 260 LYHGAD---SKHRYCMGAVLLDLDDPAKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGALLL-DQTVRMYYGAADEVMAV 335
Cdd:cd08993  191 IYHGVRttcSGFVYRLGAALLDLEDPSKVIARSREPILAPEEPYERVGDVPNVVFPCGAIVEeDGEVKIYYGAADTVICL 270


                 ....*...
gi 521095578 336 ADIPLEDI 343
Cdd:cd08993  271 ATATIDDL 278
GH130 cd18607
Glycoside hydrolase family 130; Members of the glycosyl hydrolase family 130, as classified by ...
 94-338 2.03e-100

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: 297.30  E-value: 2.03e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  94 DGQTVML-------TSLSHLRVARSKDGIHFDIEPQPALFP--EHALEAWGIEDPRVTQIGDIYYITYSSASARGVGAGL 164
Cdd:cd18607   15 DGKYHLLyravgkgTRRSSIGYARSKDGIHFERLDEPPLYPppENPYEKGGCEDPRITKIDDTYYMTYTAYDGFGPRLAL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 165 AETRDFRTFKRRGLM--LAPENKDVMIFPDKINGKYYALHRPVPksfgsPEMWIAESPDLDHWGNHRFLMGLSEQGWDSA 242
Cdd:cd18607   95 ATTKDLKNWERHGLAfpPAPENKNGVIFPEKINGKYAMLHRPDG-----PDIWLATSDDLIHWGDHKPLLKPRKGTWDSA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 243 RMGGGAVPIRTERGWLALYHGADSK---HRYCMGAVLLDLDDPAKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGALLLD 319
Cdd:cd18607  170 KVGAGPPPIKTKKGWLLLYHGVNETaagNRYRLGAALLDLNDPTRVLYRSDKPILEPEEDYEKSGYVPNVVFPCGAVAID 249

                        250       260
                 ....*....|....*....|
gi 521095578 320 Q-TVRMYYGAADEVMAVADI 338
Cdd:cd18607  250 GdELKLYYGAADTKVAVATV 269
GH130 cd18615
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 24-336 5.73e-94

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: 281.04  E-value: 5.73e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  24 FRVLGVFNAGVAQFGDEIILLLRiaeaplsdradevlvprlneagtdvlVErydktdpgydfsdsrfiARDGqtvmltsL 103
Cdd:cd18615    3 YPANAVFNPGAAKLGGETLLLVR--------------------------VE-----------------DRRG-------F 32

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 104 SHLRVARSKDGIH-FDIEPQPALFPE---HALEAWGIEDPRVTQIGDI--YYITYSSASARGVGAGLAETRDFRTFKRRG 177
Cdd:cd18615   33 SHLTVARSADGVTnWKIDPKPTLEPDpedYPEEMWGIEDPRITWLEELgrYAITYTAYSPAGPGVSLATTKDFKTFERLG 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 178 LMLAPENKDVMIFPDKINGKYYALHRPVPKsfGSPEMWIAESPDLDHWGNHRFLMGLSEQG-WDSARMGGGAVPIRTERG 256
Cdd:cd18615  113 LVMPPEDKDAALFPRRINGRWALLHRPVSA--GRAHIWISFSPDLKHWGDHRPVLPARRGPwWDAVKVGLGPPPIETPEG 190

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 257 WLALYHG---ADSKHRYCMGAVLLDLDDPAKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGALLL--DQTVRMYYGAADE 331
Cdd:cd18615  191 WLIIYHGvkeTASGSIYRVGLALLDLEDPTKVIRRSDEWVLGPEEPYERIGDVPNVVFPCGAILDedGDELRLYYGAADT 270


                 ....*
gi 521095578 332 VMAVA 336
Cdd:cd18615  271 CIALA 275
GH130 cd18614
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 104-340 6.22e-94

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: 280.84  E-value: 6.22e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 104 SHLRVARSKDGIHFD-IEPQPALFP-EHALEAWGIEDPRVTQIGDIYYITY---SSASARGVGAGLAETRDFRTFKRRG- 177
Cdd:cd18614   31 SRLGYASSKDGIHFDeRLDEPVYVPkKSGGENGGCEDPRITKIDDTYYMTYtayDGWPPPRVALTSISTKDFLNFKWNWv 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 178 ---LMLAPE--NKDVMIFPDKINGKYYALHRPvpksfgSPEMWIAESPDLD---HWGNHRFLMGLSEQGWDSARMGGGAV 249
Cdd:cd18614  111 ippLISPPGvdDKDAVLFPEKINGKYALLHRI------GPDIWIDYSDDLDfgkNWIDSKIILEPRPGMWDSRKIGAGAP 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 250 PIRTERGWLALYHGADSK-HRYCMGAVLLDLDDPAKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGALLLDQTVRMYYGA 328
Cdd:cd18614  185 PIKTKKGWLLIYHGVDDDdRVYRLGAALLDLEDPTKVIARSPEPILEPEEDYEKEGLVPNVVFPCGAVVKDDTLFVYYGG 264

                        250
                 ....*....|..
gi 521095578 329 ADEVMAVADIPL 340
Cdd:cd18614  265 ADKVIGVATAPL 276
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 102-347 1.85e-65

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: 209.65  E-value: 1.85e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  102 SLSHLRV--ARSKDGIHFDIEPQPALFPEHALEAWGIEDPRVTQIGDIYYITYSSASARGVGAGLAETRDFRTFKRRGLM 179
Cdd:pfam04041  62 DIASFRIglEDSYDGIKKTLEPEPIFWPRDKQEFWGVEDPRVVKINSTYYMTYTGRDYKYWRIEVGTTKDFLTWARLPVK 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  180 LAPEN--------KDVMIFPDKINGKYYALHRPvpksfgsPEMWIAESPDLDHWGNHRFLMGLSEQGWDSA----RMGGG 247
Cdd:pfam04041 142 IALFEkrydsiktSDGNAFPVKIKGKYLMYHRV-------GDIWLAVSPDLVHWENRLEPLGSPRPIMFPNpfetKIGWG 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  248 AVPIRTERGWLALYHGAD-SKHRYCMGAVLLDLDDpaKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGALLLDQTVRMYY 326
Cdd:pfam04041 215 TPPVETKEGWLVLIHGVDtEDLVYRVGAALLDLEG--KVLARTPEYILEPEEEYEEYGDRPNVVFPCGALVDGERVIIYY 292

                         250       260
                  ....*....|....*....|.
gi 521095578  327 GAADEVMAVADIPLEDIYNTL 347
Cdd:pfam04041 293 GAADTAIGLAEIPEEEIMNLL 313
GH130 cd18611
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 102-338 9.41e-57

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: 186.19  E-value: 9.41e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 102 SLSHLRVARSKDGIHFDIEPQPaLFPEHALEAWGIEDPRVTQIGDIYYITYSSAS-----ARGVGAGLAETRDFRTFKRR 176
Cdd:cd18611   37 GLSTIGYAESKDGVHFENRRQL-IKPEEEWEKYGCEDPRVTKIDGKYYIFYTALSgypfgPEGIKVAVAITKDFKTIEEK 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 177 GLmLAPEN-KDVMIFPDKINGKYYAL---H--RPVPK----SFGSPE-MWIAESPD--LDHWGNHRflmgLSEQGWDSAR 243
Cdd:cd18611  116 HL-VTPFNaKAMALFPEKINGKYAALltvNtdNPPAKialaYFDKIEdLWSPEYWDkwYANLDDHA----LPLRRSEHDH 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 244 MGGGAVPIRTERGWLALY----HGADSKHRYCMGAVLLDLDDPAKVIARSRVPVLEPEAAYEVNGFFGKVVFSCGALLLD 319
Cdd:cd18611  191 VEVGAPPIKTKDGWLLIYsyiqNYFSGERVFGIEAALLDLNDPRKIIGRTKGPLLVPEEEYELYGLVPNIVFPSGALIEG 270

                        250
                 ....*....|....*....
gi 521095578 320 QTVRMYYGAADEVMAVADI 338
Cdd:cd18611  271 DKLHIYYGAADTVCCLASV 289
GH130 cd18613
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 91-343 1.97e-53

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: 178.08  E-value: 1.97e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  91 IARDGQTVMLtslshLRVARSKDGIHFDIEPQPA---LFPEHALEAWGIEDPRVTQIGD-----IYYITYSSASARGVGA 162
Cdd:cd18613   52 IDPGGEIRLI-----RWLADSNYELRFPADVDLServLFPVTPAESNGIEDARFVRFTDddgsvTYYATYTAYDGRAIRP 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 163 GLAETRDFRTFKRRGLM-LAPENKDVMIFPDKINGKYYALHRPVPKSfgspeMWIAESPDLDHWGNHRFLMGlSEQGWDS 241
Cdd:cd18613  127 QLLETRDFRTFKVRPLTgPAARNKGMALFPRKIGGRYAMLSRQDGEN-----IYLMFSDDLYFWDEAELILK-PRYPWEF 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 242 ARMGGGAVPIRTERGWLALYHGADSKHRYCMGAVLLDLDDPAKVIARSRVPVLEPeAAYEVNGFFGKVVFSCGALLLDQT 321
Cdd:cd18613  201 VQIGNCGSPIETDEGWLVLTHGVGPMRRYSIGAILLDLDDPTKVIGRLREPLLSP-DEEEREGYVPNVVYSCGALVHGDR 279

                        250       260
                 ....*....|....*....|..
gi 521095578 322 VRMYYGAADEVMAVADIPLEDI 343
Cdd:cd18613  280 LILPYGMSDSATGFATVDLDEL 301
GH130_BT3780-like cd18610
Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624; This ...
 91-336 6.32e-53

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: 176.62  E-value: 6.32e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578  91 IARDGQTVML----------TSLSHLRVARSKDGIHFDIEPQPALFPEHALEaW--GIEDPRVTQIGD-IYYITYSS--- 154
Cdd:cd18610   21 IVRDGKVYLLyraedasgngNGTSRIGLAVSDDGLHFTRLPEPVLYPEEDYE-WpgGCEDPRIVEIEDgTYYMTYTAydg 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 155 ASARgvgAGLAETRDFRTFKRRGLMLA---------PENKDVMIFP-----DKINGKYYALhrpvpksFGSPEMWIAESP 220
Cdd:cd18610  100 KTAR---LCLATSTDLVHWTKHGPAFPdadggkyrdLWSKSGAIVPelkgaAKINGKYWMY-------WGESNIYLATSD 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 221 DLDHW------GNHRFLMGLSEQGWDSARMGGGAVPIRTERGWLALYHGADS--------KHRYCMGAVLLDLDDPAKVI 286
Cdd:cd18610  170 DLIHWtpveddGSLRPVLSPRPGKFDSDLVEPGPPPILTDGGILLIYNGANDggggpgypKGTYSAGQALFDANDPTKLL 249

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 521095578 287 ARSRVPVLEPEAAYEVNGFFGKVVFSCGALLLDQTVRMYYGAADEVMAVA 336
Cdd:cd18610  250 ARLDKPFLEPETPYEKEGQVNNVVFVEGLVYFKGKWLLYYGTADSKIGVA 299
GH43_62_32_68_117_130 cd08772
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 109-329 1.38e-23

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: 97.67  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 109 ARSKDGIHFDIEPQPALF-PEHALEAWGIEDPRVTQIGDIYYITYSSASARGVGA-----GLAETRDFRTFKRRGLMLAP 182
Cdd:cd08772   30 ARSKDLIHWEEEPPAIVArGGGSYDTSYAFDPEVVYIEGTYYLTYCSDDLGDILRhgqhiGVAYSKDPKGPWTRKDAPLI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521095578 183 E--------NKDVMIFPDKINGKYYaLHRPVPKSFGS-PEMWIAESPDLDHWGNHRFLMGLSEQGWDSARMGggavPIRT 253
Cdd:cd08772  110 EppnayspkNRDPVLFPRKIGKYYL-LNVPSDNGHTRfGKIAIAESPD*LHWINHSFVYNYNEQGKVGEGPS----LWKT 184

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521095578 254 ERGWLALYHGADSKHR-YCMGAVLLDLDDPAKVIARSRvpvlePEAAYEVNGFFGKVVFSCGALLLDQTVRMYYGAA 329
Cdd:cd08772  185 KGGWYLIYHANTLTGYgYGFGYALGDLDDPSKVLYRSR-----PEEEYETVGFKPNVVAPAAFLCDSTGIVAIIGHA 256
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH