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Conserved domains on  [gi|538260973|pdb|3WAT|A]
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Chain A, 4-O-beta-D-mannosyl-D-glucose phosphorylase

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
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
30-366 2.43e-152

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


:

Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 431.87  E-value: 2.43e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A       30 NGVITRY-RYPVLTAAHtpvfwrydlneetnpflMERIGMNATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGId 108
Cdd:COG2152   1 NGILKRYpGNPILTPND-----------------MPRWEVNAVFNPGAVRFNGKFLLLYRVEGRDGKSHLGLARSDDGI- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      109 NFRFWEYPVTLPEDVVPATNVYDMRLTAHeDGWIYGIFCAErhddnapigdlSSATATAGIARTKDLKNWERLPDLkTKS 188
Cdd:COG2152  63 NFRRDDEPILFPETDYEDTGVEDPRITKI-DGRYYITYTAY-----------SGAGARIGLARTKDFKTWERLGLI-FPP 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      189 QQRNVVLHPEFVDGKYALYTRPQDGFidTGSGGGIGWALIDDITHAEvGEEKIIDKRYyHTIKEVKNGEGPHPIKTPQGW 268
Cdd:COG2152 130 DNKDAVLFPEKINGKYALLHRPSDGF--HTGGPDIWISYSPDLEHWG-DHRIVMGPRP-GTWDSLKIGAGPPPIKTEEGW 205

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      269 LHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIASPAGYFMAPVGE-ERIGDVSNVLFSNGWIADDDGKVFIYYASSDTRM 347
Cdd:COG2152 206 LLIYHGVRNTAAGLVYRLGAALLDLEDPSKVIARSPEPILEPEEEyERVGDVPNVVFPCGAVVDEDGTVYIYYGAADTRI 285

                       330
                ....*....|....*....
3WAT_A      348 HVATSTIERLVDYCLHTPQ 366
Cdd:COG2152 286 ALATATLDELLDYLKNTPE 304
 
Name Accession Description Interval E-value
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
30-366 2.43e-152

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


Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 431.87  E-value: 2.43e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A       30 NGVITRY-RYPVLTAAHtpvfwrydlneetnpflMERIGMNATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGId 108
Cdd:COG2152   1 NGILKRYpGNPILTPND-----------------MPRWEVNAVFNPGAVRFNGKFLLLYRVEGRDGKSHLGLARSDDGI- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      109 NFRFWEYPVTLPEDVVPATNVYDMRLTAHeDGWIYGIFCAErhddnapigdlSSATATAGIARTKDLKNWERLPDLkTKS 188
Cdd:COG2152  63 NFRRDDEPILFPETDYEDTGVEDPRITKI-DGRYYITYTAY-----------SGAGARIGLARTKDFKTWERLGLI-FPP 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      189 QQRNVVLHPEFVDGKYALYTRPQDGFidTGSGGGIGWALIDDITHAEvGEEKIIDKRYyHTIKEVKNGEGPHPIKTPQGW 268
Cdd:COG2152 130 DNKDAVLFPEKINGKYALLHRPSDGF--HTGGPDIWISYSPDLEHWG-DHRIVMGPRP-GTWDSLKIGAGPPPIKTEEGW 205

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      269 LHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIASPAGYFMAPVGE-ERIGDVSNVLFSNGWIADDDGKVFIYYASSDTRM 347
Cdd:COG2152 206 LLIYHGVRNTAAGLVYRLGAALLDLEDPSKVIARSPEPILEPEEEyERVGDVPNVVFPCGAVVDEDGTVYIYYGAADTRI 285

                       330
                ....*....|....*....
3WAT_A      348 HVATSTIERLVDYCLHTPQ 366
Cdd:COG2152 286 ALATATLDELLDYLKNTPE 304
GH130 cd08993
Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) ...
 67-358 1.50e-115

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: 337.52  E-value: 1.50e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A       67 GMNATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGIDNFRFWEYPVT--LPEDVVPATNVYDMRLTAHEDgWIYG 144
Cdd:cd08993   2 PANSVFNAGAVKFNGKYLLLFRVEDLNGRSFLGLAESDDGIHFTVEPEPILTpdEPFEPYEETGVYDPRITKIDD-TYYI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      145 IFCAERHDdnapigdlssaTATAGIARTKDLKNWERLPDLkTKSQQRNVVLHPEFVDGKYALYTRPQDGFIdtGSGGGIG 224
Cdd:cd08993  81 TFAADSDH-----------GPRIGLARTKDFKTFERLELI-SEPDNRNGVLFPEKINGKYARLDRPSDGGH--TSGGDIW 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      225 WALIDDITHaeVGEEKIIDKRYYHTIKEVKNGEGPHPIKTPQGWLHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIASPA 304
Cdd:cd08993 147 ISYSPDLIH--WGNSRLVMGPRPGPWDNDKIGPGAPPIKTEEGWLLIYHGVRTTCSGFVYRLGAALLDLEDPSKVIARSR 224

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
3WAT_A      305 GYFMAPVGE-ERIGDVSNVLFSNGWIADDDGKVFIYYASSDTRMHVATSTIERLV 358
Cdd:cd08993 225 EPILAPEEPyERVGDVPNVVFPCGAIVEEDGEVKIYYGAADTVICLATATIDDLV 279
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 75-361 5.18e-21

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: 92.55  E-value: 5.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A         75 GAIKWDGKYLMLVRVEGADRKSFF-AVAESPNGIDNFRFWEyPVTLPEDVVPATNVYDMRLTAHEDGWiYGIFCAErhdd 153
Cdd:pfam04041  44 KELHVYPRVVMGYYKYVSDIASFRiGLEDSYDGIKKTLEPE-PIFWPRDKQEFWGVEDPRVVKINSTY-YMTYTGR---- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A        154 napigdlSSATATAGIARTKDLKNWERLPDL-------KTKSQQRNVVLHPEFVDGKYALYTRPQDGFIDTGsgggigwa 226
Cdd:pfam04041 118 -------DYKYWRIEVGTTKDFLTWARLPVKialfekrYDSIKTSDGNAFPVKIKGKYLMYHRVGDIWLAVS-------- 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A        227 liDDITHAEVGEEKIIDKR--YYHTIKEVKNGEGPHPIKTPQGWLHLAHGVrncaAGLRYVLYMYMTSLDDPTRLIASPA 304
Cdd:pfam04041 183 --PDLVHWENRLEPLGSPRpiMFPNPFETKIGWGTPPVETKEGWLVLIHGV----DTEDLVYRVGAALLDLEGKVLARTP 256

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
3WAT_A        305 GYFMAPVGE-ERIGDVSNVLFSNGWIADDDgKVFIYYASSDTRMHVATSTIERLVDYC 361
Cdd:pfam04041 257 EYILEPEEEyEEYGDRPNVVFPCGALVDGE-RVIIYYGAADTAIGLAEIPEEEIMNLL 313
 
Name Accession Description Interval E-value
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
30-366 2.43e-152

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


Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 431.87  E-value: 2.43e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A       30 NGVITRY-RYPVLTAAHtpvfwrydlneetnpflMERIGMNATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGId 108
Cdd:COG2152   1 NGILKRYpGNPILTPND-----------------MPRWEVNAVFNPGAVRFNGKFLLLYRVEGRDGKSHLGLARSDDGI- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      109 NFRFWEYPVTLPEDVVPATNVYDMRLTAHeDGWIYGIFCAErhddnapigdlSSATATAGIARTKDLKNWERLPDLkTKS 188
Cdd:COG2152  63 NFRRDDEPILFPETDYEDTGVEDPRITKI-DGRYYITYTAY-----------SGAGARIGLARTKDFKTWERLGLI-FPP 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      189 QQRNVVLHPEFVDGKYALYTRPQDGFidTGSGGGIGWALIDDITHAEvGEEKIIDKRYyHTIKEVKNGEGPHPIKTPQGW 268
Cdd:COG2152 130 DNKDAVLFPEKINGKYALLHRPSDGF--HTGGPDIWISYSPDLEHWG-DHRIVMGPRP-GTWDSLKIGAGPPPIKTEEGW 205

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      269 LHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIASPAGYFMAPVGE-ERIGDVSNVLFSNGWIADDDGKVFIYYASSDTRM 347
Cdd:COG2152 206 LLIYHGVRNTAAGLVYRLGAALLDLEDPSKVIARSPEPILEPEEEyERVGDVPNVVFPCGAVVDEDGTVYIYYGAADTRI 285

                       330
                ....*....|....*....
3WAT_A      348 HVATSTIERLVDYCLHTPQ 366
Cdd:COG2152 286 ALATATLDELLDYLKNTPE 304
GH130 cd08993
Glycosyl hydrolase family 130; This subfamily contains glycosyl hydrolase family 130 (GH130) ...
 67-358 1.50e-115

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: 337.52  E-value: 1.50e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A       67 GMNATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGIDNFRFWEYPVT--LPEDVVPATNVYDMRLTAHEDgWIYG 144
Cdd:cd08993   2 PANSVFNAGAVKFNGKYLLLFRVEDLNGRSFLGLAESDDGIHFTVEPEPILTpdEPFEPYEETGVYDPRITKIDD-TYYI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      145 IFCAERHDdnapigdlssaTATAGIARTKDLKNWERLPDLkTKSQQRNVVLHPEFVDGKYALYTRPQDGFIdtGSGGGIG 224
Cdd:cd08993  81 TFAADSDH-----------GPRIGLARTKDFKTFERLELI-SEPDNRNGVLFPEKINGKYARLDRPSDGGH--TSGGDIW 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      225 WALIDDITHaeVGEEKIIDKRYYHTIKEVKNGEGPHPIKTPQGWLHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIASPA 304
Cdd:cd08993 147 ISYSPDLIH--WGNSRLVMGPRPGPWDNDKIGPGAPPIKTEEGWLLIYHGVRTTCSGFVYRLGAALLDLEDPSKVIARSR 224

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
3WAT_A      305 GYFMAPVGE-ERIGDVSNVLFSNGWIADDDGKVFIYYASSDTRMHVATSTIERLV 358
Cdd:cd08993 225 EPILAPEEPyERVGDVPNVVFPCGAIVEEDGEVKIYYGAADTVICLATATIDDLV 279
GH130 cd18607
Glycoside hydrolase family 130; Members of the glycosyl hydrolase family 130, as classified by ...
 66-352 2.74e-108

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: 318.88  E-value: 2.74e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A       66 IGMNATLNAGAIKWDGKYLMLVRVEGAD-RKSFFAVAESPNGIDNFRFWEYPVTLP-EDVVPATNVYDMRLTAHEDgWIY 143
Cdd:cd18607   1 WESAAVFNPGAILHDGKYHLLYRAVGKGtRRSSIGYARSKDGIHFERLDEPPLYPPpENPYEKGGCEDPRITKIDD-TYY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      144 GIFCAERHDdnapigdlssaTATAGIARTKDLKNWERLPDLKT-KSQQRNVVLHPEFVDGKYALYTRPQdgfidtgsGGG 222
Cdd:cd18607  80 MTYTAYDGF-----------GPRLALATTKDLKNWERHGLAFPpAPENKNGVIFPEKINGKYAMLHRPD--------GPD 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      223 IGWALIDDITHaeVGEEKIIDKRYYHTIKEVKNGEGPHPIKTPQGWLHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIAS 302
Cdd:cd18607 141 IWLATSDDLIH--WGDHKPLLKPRKGTWDSAKVGAGPPPIKTKKGWLLLYHGVNETAAGNRYRLGAALLDLNDPTRVLYR 218

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
3WAT_A      303 PAGYFMAPVGEERI-GDVSNVLFSNGWIADDDGKVFIYYASSDTRMHVATS 352
Cdd:cd18607 219 SDKPILEPEEDYEKsGYVPNVVFPCGAVAIDGDELKLYYGAADTKVAVATV 269
GH130 cd18615
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 69-352 3.56e-40

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: 143.91  E-value: 3.56e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A       69 NATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGIDNFRFWEYPVTLPEDVVPATNVY---DMRLTAHEDGWIYGI 145
Cdd:cd18615   6 NAVFNPGAAKLGGETLLLVRVEDRRGFSHLTVARSADGVTNWKIDPKPTLEPDPEDYPEEMWgieDPRITWLEELGRYAI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      146 FCaerhddnapigdlsSATATAG----IARTKDLKNWERL-----PDLKtksqqrNVVLHPEFVDGKYALYTRPqdgfiD 216
Cdd:cd18615  86 TY--------------TAYSPAGpgvsLATTKDFKTFERLglvmpPEDK------DAALFPRRINGRWALLHRP-----V 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      217 TGSGGGIGWALIDDITHAEvGEEKIIDKRYYHTIKEVKNGEGPHPIKTPQGWLHLAHGVRNCAAGLRYVLYMYMTSLDDP 296
Cdd:cd18615 141 SAGRAHIWISFSPDLKHWG-DHRPVLPARRGPWWDAVKVGLGPPPIETPEGWLIIYHGVKETASGSIYRVGLALLDLEDP 219

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
3WAT_A      297 TRLIASPAGYFMAPVGE-ERIGDVSNVLFSNGWIAD-DDGKVFIYYASSDTRMHVATS 352
Cdd:cd18615 220 TKVIRRSDEWVLGPEEPyERIGDVPNVVFPCGAILDeDGDELRLYYGAADTCIALATA 277
GH130_Lin0857-like cd18612
Glycoside hydrolase family 130 such as Listeria innocua beta-1,2-mannobiose phosphorylase; ...
 63-351 1.73e-33

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: 125.31  E-value: 1.73e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A       63 MERIGmnaTLNAGAIKWDGKYLMLVRVegADrksFFAVAESPNGIdNFRFWEYPVTLPEDVVPATNVYDMRLTAHEDGWi 142
Cdd:cd18612   1 LEVIG---VFNPGAARYGDEIILLLRV--AE---HLRLARSRDGI-HFTVDEKPALFPEGPYEAFGIEDPRITRIDDTY- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      143 YGIFCAerhddnapigdLSSATATAGIARTKDLKNWERL-----PDLKtksqqrNVVLHPEFVDGKYALYTRPqdgfidt 217
Cdd:cd18612  71 YITYTA-----------VSEYGIATALASTKDFKTFERHgvifpPENK------DVVIFPEKINGKYYALHRP------- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      218 gSGGGIG----W-ALIDDITHAevGEEKIIDKRYYHTIKEVKNGEGPHPIKTPQGWLHLAHGV-RNCaaglRYVLYMYMT 291
Cdd:cd18612 127 -VPSGFGkpeiWiAESPDLLHW--GNHRHLAGPRPGMWDSGRIGAGAVPIKTEKGWLEIYHGAdENN----RYCLGALLL 199

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
3WAT_A      292 SLDDPTRLIASPAGYFMAPVGE-ERIGDVSNVLFSNGWIADDDgKVFIYYASSDTRMHVAT 351
Cdd:cd18612 200 DLEDPSKVIARSEEPILEPEAPyEKEGFFGNVVFTCGAVVEGD-TLLIYYGAADTSIAVAE 259
GH130 cd18614
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 69-351 4.04e-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: 350126 [Multi-domain]  Cd Length: 276  Bit Score: 122.14  E-value: 4.04e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A       69 NATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGIDNFRFWEYPVtlpedVVPATNVY------DMRLTaHEDGWI 142
Cdd:cd18614   4 KAVFNPAAIYEDGKVHLLYRAVGEDNISRLGYASSKDGIHFDERLDEPV-----YVPKKSGGenggceDPRIT-KIDDTY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      143 YGIFCAerHDDNAPIGdlssatATAGIARTKDLKNWERL---PDLKTKSQ--QRNVVLHPEFVDGKYALYTRPqdgfidt 217
Cdd:cd18614  78 YMTYTA--YDGWPPPR------VALTSISTKDFLNFKWNwviPPLISPPGvdDKDAVLFPEKINGKYALLHRI------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      218 gsGGGIGWALIDDITHAE--VGEEKIIDKRYYHtIKEVKNGEGPHPIKTPQGWLHLAHGVrnCAAGLRYVLYMYMTSLDD 295
Cdd:cd18614 143 --GPDIWIDYSDDLDFGKnwIDSKIILEPRPGM-WDSRKIGAGAPPIKTKKGWLLIYHGV--DDDDRVYRLGAALLDLED 217

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
3WAT_A      296 PTRLIASPAGYFMAPVGE-ERIGDVSNVLFSNGWIADDDgKVFIYYASSDTRMHVAT 351
Cdd:cd18614 218 PTKVIARSPEPILEPEEDyEKEGLVPNVVFPCGAVVKDD-TLFVYYGGADKVIGVAT 273
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 75-361 5.18e-21

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: 92.55  E-value: 5.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A         75 GAIKWDGKYLMLVRVEGADRKSFF-AVAESPNGIDNFRFWEyPVTLPEDVVPATNVYDMRLTAHEDGWiYGIFCAErhdd 153
Cdd:pfam04041  44 KELHVYPRVVMGYYKYVSDIASFRiGLEDSYDGIKKTLEPE-PIFWPRDKQEFWGVEDPRVVKINSTY-YMTYTGR---- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A        154 napigdlSSATATAGIARTKDLKNWERLPDL-------KTKSQQRNVVLHPEFVDGKYALYTRPQDGFIDTGsgggigwa 226
Cdd:pfam04041 118 -------DYKYWRIEVGTTKDFLTWARLPVKialfekrYDSIKTSDGNAFPVKIKGKYLMYHRVGDIWLAVS-------- 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A        227 liDDITHAEVGEEKIIDKR--YYHTIKEVKNGEGPHPIKTPQGWLHLAHGVrncaAGLRYVLYMYMTSLDDPTRLIASPA 304
Cdd:pfam04041 183 --PDLVHWENRLEPLGSPRpiMFPNPFETKIGWGTPPVETKEGWLVLIHGV----DTEDLVYRVGAALLDLEGKVLARTP 256

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
3WAT_A        305 GYFMAPVGE-ERIGDVSNVLFSNGWIADDDgKVFIYYASSDTRMHVATSTIERLVDYC 361
Cdd:pfam04041 257 EYILEPEEEyEEYGDRPNVVFPCGALVDGE-RVIIYYGAADTAIGLAEIPEEEIMNLL 313
GH130_BT3780-like cd18610
Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624; This ...
 70-352 5.21e-15

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: 74.93  E-value: 5.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A       70 ATLNAGAIKWDGKYLMLVRVEGADRK----SFFAVAESPNGIdNFrfweypVTLPEDVVPATNVY-------DMRLTAHE 138
Cdd:cd18610  14 DVFNPAAIVRDGKVYLLYRAEDASGNgngtSRIGLAVSDDGL-HF------TRLPEPVLYPEEDYewpggceDPRIVEIE 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      139 DGWIYGIFCAerhddnapigdLSSATATAGIARTKDLKNWERLP------------DLKTKS-----QQRNVVLhpefVD 201
Cdd:cd18610  87 DGTYYMTYTA-----------YDGKTARLCLATSTDLVHWTKHGpafpdadggkyrDLWSKSgaivpELKGAAK----IN 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      202 GKYALYtrpqdgFIDTGsgggIGWALIDDITHAEVGEekiiDKRYYHTIKEVKNGE--------GPHPIKTPQGWLHLAH 273
Cdd:cd18610 152 GKYWMY------WGESN----IYLATSDDLIHWTPVE----DDGSLRPVLSPRPGKfdsdlvepGPPPILTDGGILLIYN 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      274 GVRNCAAGLRYVLYMYMTS-----LDDPTRLIASPAGYFMAPV-GEERIGDVSNVLFSNGWIaDDDGKVFIYYASSDTRM 347
Cdd:cd18610 218 GANDGGGGPGYPKGTYSAGqalfdANDPTKLLARLDKPFLEPEtPYEKEGQVNNVVFVEGLV-YFKGKWLLYYGTADSKI 296


                ....*
3WAT_A      348 HVATS 352
Cdd:cd18610 297 GVATA 301
GH130 cd18613
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 195-357 8.79e-14

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: 71.38  E-value: 8.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      195 LHPEFVDGKYALYTRpQDG---FIdtgsgggigwALIDDITHAEVGEeKIIDKRYYHTIKEVKNGeGPhPIKTPQGWLHL 271
Cdd:cd18613 154 LFPRKIGGRYAMLSR-QDGeniYL----------MFSDDLYFWDEAE-LILKPRYPWEFVQIGNC-GS-PIETDEGWLVL 219

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      272 AHGV---RncaaglRYVLYMYMTSLDDPTRLIASPAGYFMAPVGEERIGDVSNVLFSNGWIADDDgKVFIYYASSDTRMH 348
Cdd:cd18613 220 THGVgpmR------RYSIGAILLDLDDPTKVIGRLREPLLSPDEEEREGYVPNVVYSCGALVHGD-RLILPYGMSDSATG 292


                ....*....
3WAT_A      349 VATSTIERL 357
Cdd:cd18613 293 FATVDLDEL 301
GH130 cd18611
Glycosyl hydrolase family 130; uncharacterized; This subfamily contains glycosyl hydrolase ...
 70-345 2.99e-09

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: 57.53  E-value: 2.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A       70 ATLNAGAIKWDGKYLMLVRVEGADRK--------SFFAVAESPNGIdNF----RF------WEYpvtlpedvvpatnvY- 130
Cdd:cd18611   5 AVFNGSVIKDGGKYHLLYRALSSPQEidgpklglSTIGYAESKDGV-HFenrrQLikpeeeWEK--------------Yg 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      131 --DMRLTAHEDgwIYGIF-CAerhddnapIGD--LSSATATAGIARTKDLKNWErlpdlktksqQRNVV---------LH 196
Cdd:cd18611  70 ceDPRVTKIDG--KYYIFyTA--------LSGypFGPEGIKVAVAITKDFKTIE----------EKHLVtpfnakamaLF 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      197 PEFVDGKY-ALYTrpqdgfIDTGS-GGGIGWALIDDIT-----------HAEVGEEKIIDKRYYHTIKEVkngeGPHPIK 263
Cdd:cd18611 130 PEKINGKYaALLT------VNTDNpPAKIALAYFDKIEdlwspeywdkwYANLDDHALPLRRSEHDHVEV----GAPPIK 199

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      264 TPQGWLHLAHGVRNcaaglryvlymYMTS------------LDDPTRLIASPAGYFMAPVGE-ERIGDVSNVLFSNGWIA 330
Cdd:cd18611 200 TKDGWLLIYSYIQN-----------YFSGervfgieaalldLNDPRKIIGRTKGPLLVPEEEyELYGLVPNIVFPSGALI 268

                       330
                ....*....|....*
3WAT_A      331 DDDgKVFIYYASSDT 345
Cdd:cd18611 269 EGD-KLHIYYGAADT 282
GH43_62_32_68_117_130 cd08772
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 129-340 6.26e-03

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: 37.96  E-value: 6.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      129 VYDMRLTAHEDGWiYGIFCAerhdDNAPigDLSSATATAGIARTKDLKNWERLPDLKTKSQQ-------RNVVLHPEFVD 201
Cdd:cd08772  58 AFDPEVVYIEGTY-YLTYCS----DDLG--DILRHGQHIGVAYSKDPKGPWTRKDAPLIEPPnayspknRDPVLFPRKIG 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3WAT_A      202 GKYALYTRPQDGFIDtgsGGGIGWALIDD----ITHAEVGEEKIIdkryyhtikeVKNGEGPHPIKTPQGWLHLAHGVrn 277
Cdd:cd08772 131 KYYLLNVPSDNGHTR---FGKIAIAESPD*lhwINHSFVYNYNEQ----------GKVGEGPSLWKTKGGWYLIYHAN-- 195

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3WAT_A      278 caaglRYVLYMYMTS-----LDDPTRLIASPAGYFMApvgeERIGDVSNVLFSNGWIADDDGKVFIYY 340
Cdd:cd08772 196 -----TLTGYGYGFGyalgdLDDPSKVLYRSRPEEEY----ETVGFKPNVVAPAAFLCDSTGIVAIIG 254
 
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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