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Conserved domains on  [gi|538260974]
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Chain B, 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  30 NGVITRY-RYPVLTAAHtpvfwrydlneetnpflMERIGMNATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGId 108
Cdd:COG2152    1 NGILKRYpGNPILTPND-----------------MPRWEVNAVFNPGAVRFNGKFLLLYRVEGRDGKSHLGLARSDDGI- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 109 NFRFWEYPVTLPEDVVPATNVYDMRLTAHeDGWIYGIFCAErhddnapigdlSSATATAGIARTKDLKNWERLPDLkTKS 188
Cdd:COG2152   63 NFRRDDEPILFPETDYEDTGVEDPRITKI-DGRYYITYTAY-----------SGAGARIGLARTKDFKTWERLGLI-FPP 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 189 QQRNVVLHPEFVDGKYALYTRPQDGFidTGSGGGIGWALIDDITHAEvGEEKIIDKRYyHTIKEVKNGEGPHPIKTPQGW 268
Cdd:COG2152  130 DNKDAVLFPEKINGKYALLHRPSDGF--HTGGPDIWISYSPDLEHWG-DHRIVMGPRP-GTWDSLKIGAGPPPIKTEEGW 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 269 LHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIASPAGYFMAPVGE-ERIGDVSNVLFSNGWIADDDGKVFIYYASSDTRM 347
Cdd:COG2152  206 LLIYHGVRNTAAGLVYRLGAALLDLEDPSKVIARSPEPILEPEEEyERVGDVPNVVFPCGAVVDEDGTVYIYYGAADTRI 285
                        330
                 ....*....|....*....
gi 538260974 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  30 NGVITRY-RYPVLTAAHtpvfwrydlneetnpflMERIGMNATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGId 108
Cdd:COG2152    1 NGILKRYpGNPILTPND-----------------MPRWEVNAVFNPGAVRFNGKFLLLYRVEGRDGKSHLGLARSDDGI- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 109 NFRFWEYPVTLPEDVVPATNVYDMRLTAHeDGWIYGIFCAErhddnapigdlSSATATAGIARTKDLKNWERLPDLkTKS 188
Cdd:COG2152   63 NFRRDDEPILFPETDYEDTGVEDPRITKI-DGRYYITYTAY-----------SGAGARIGLARTKDFKTWERLGLI-FPP 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 189 QQRNVVLHPEFVDGKYALYTRPQDGFidTGSGGGIGWALIDDITHAEvGEEKIIDKRYyHTIKEVKNGEGPHPIKTPQGW 268
Cdd:COG2152  130 DNKDAVLFPEKINGKYALLHRPSDGF--HTGGPDIWISYSPDLEHWG-DHRIVMGPRP-GTWDSLKIGAGPPPIKTEEGW 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 269 LHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIASPAGYFMAPVGE-ERIGDVSNVLFSNGWIADDDGKVFIYYASSDTRM 347
Cdd:COG2152  206 LLIYHGVRNTAAGLVYRLGAALLDLEDPSKVIARSPEPILEPEEEyERVGDVPNVVFPCGAVVDEDGTVYIYYGAADTRI 285
                        330
                 ....*....|....*....
gi 538260974 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  67 GMNATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGIDNFRFWEYPVT--LPEDVVPATNVYDMRLTAHEDgWIYG 144
Cdd:cd08993    2 PANSVFNAGAVKFNGKYLLLFRVEDLNGRSFLGLAESDDGIHFTVEPEPILTpdEPFEPYEETGVYDPRITKIDD-TYYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 145 IFCAERHDdnapigdlssaTATAGIARTKDLKNWERLPDLkTKSQQRNVVLHPEFVDGKYALYTRPQDGFIdtGSGGGIG 224
Cdd:cd08993   81 TFAADSDH-----------GPRIGLARTKDFKTFERLELI-SEPDNRNGVLFPEKINGKYARLDRPSDGGH--TSGGDIW 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 225 WALIDDITHaeVGEEKIIDKRYYHTIKEVKNGEGPHPIKTPQGWLHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIASPA 304
Cdd:cd08993  147 ISYSPDLIH--WGNSRLVMGPRPGPWDNDKIGPGAPPIKTEEGWLLIYHGVRTTCSGFVYRLGAALLDLEDPSKVIARSR 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 538260974 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974   75 GAIKWDGKYLMLVRVEGADRKSFF-AVAESPNGIDNFRFWEyPVTLPEDVVPATNVYDMRLTAHEDGWiYGIFCAErhdd 153
Cdd:pfam04041  44 KELHVYPRVVMGYYKYVSDIASFRiGLEDSYDGIKKTLEPE-PIFWPRDKQEFWGVEDPRVVKINSTY-YMTYTGR---- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  154 napigdlSSATATAGIARTKDLKNWERLPDL-------KTKSQQRNVVLHPEFVDGKYALYTRPQDGFIDTGsgggigwa 226
Cdd:pfam04041 118 -------DYKYWRIEVGTTKDFLTWARLPVKialfekrYDSIKTSDGNAFPVKIKGKYLMYHRVGDIWLAVS-------- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  227 liDDITHAEVGEEKIIDKR--YYHTIKEVKNGEGPHPIKTPQGWLHLAHGVrncaAGLRYVLYMYMTSLDDPTRLIASPA 304
Cdd:pfam04041 183 --PDLVHWENRLEPLGSPRpiMFPNPFETKIGWGTPPVETKEGWLVLIHGV----DTEDLVYRVGAALLDLEGKVLARTP 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 538260974  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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  30 NGVITRY-RYPVLTAAHtpvfwrydlneetnpflMERIGMNATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGId 108
Cdd:COG2152    1 NGILKRYpGNPILTPND-----------------MPRWEVNAVFNPGAVRFNGKFLLLYRVEGRDGKSHLGLARSDDGI- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 109 NFRFWEYPVTLPEDVVPATNVYDMRLTAHeDGWIYGIFCAErhddnapigdlSSATATAGIARTKDLKNWERLPDLkTKS 188
Cdd:COG2152   63 NFRRDDEPILFPETDYEDTGVEDPRITKI-DGRYYITYTAY-----------SGAGARIGLARTKDFKTWERLGLI-FPP 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 189 QQRNVVLHPEFVDGKYALYTRPQDGFidTGSGGGIGWALIDDITHAEvGEEKIIDKRYyHTIKEVKNGEGPHPIKTPQGW 268
Cdd:COG2152  130 DNKDAVLFPEKINGKYALLHRPSDGF--HTGGPDIWISYSPDLEHWG-DHRIVMGPRP-GTWDSLKIGAGPPPIKTEEGW 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 269 LHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIASPAGYFMAPVGE-ERIGDVSNVLFSNGWIADDDGKVFIYYASSDTRM 347
Cdd:COG2152  206 LLIYHGVRNTAAGLVYRLGAALLDLEDPSKVIARSPEPILEPEEEyERVGDVPNVVFPCGAVVDEDGTVYIYYGAADTRI 285
                        330
                 ....*....|....*....
gi 538260974 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  67 GMNATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGIDNFRFWEYPVT--LPEDVVPATNVYDMRLTAHEDgWIYG 144
Cdd:cd08993    2 PANSVFNAGAVKFNGKYLLLFRVEDLNGRSFLGLAESDDGIHFTVEPEPILTpdEPFEPYEETGVYDPRITKIDD-TYYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 145 IFCAERHDdnapigdlssaTATAGIARTKDLKNWERLPDLkTKSQQRNVVLHPEFVDGKYALYTRPQDGFIdtGSGGGIG 224
Cdd:cd08993   81 TFAADSDH-----------GPRIGLARTKDFKTFERLELI-SEPDNRNGVLFPEKINGKYARLDRPSDGGH--TSGGDIW 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 225 WALIDDITHaeVGEEKIIDKRYYHTIKEVKNGEGPHPIKTPQGWLHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIASPA 304
Cdd:cd08993  147 ISYSPDLIH--WGNSRLVMGPRPGPWDNDKIGPGAPPIKTEEGWLLIYHGVRTTCSGFVYRLGAALLDLEDPSKVIARSR 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 538260974 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  66 IGMNATLNAGAIKWDGKYLMLVRVEGAD-RKSFFAVAESPNGIDNFRFWEYPVTLP-EDVVPATNVYDMRLTAHEDgWIY 143
Cdd:cd18607    1 WESAAVFNPGAILHDGKYHLLYRAVGKGtRRSSIGYARSKDGIHFERLDEPPLYPPpENPYEKGGCEDPRITKIDD-TYY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 144 GIFCAERHDdnapigdlssaTATAGIARTKDLKNWERLPDLKT-KSQQRNVVLHPEFVDGKYALYTRPQdgfidtgsGGG 222
Cdd:cd18607   80 MTYTAYDGF-----------GPRLALATTKDLKNWERHGLAFPpAPENKNGVIFPEKINGKYAMLHRPD--------GPD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 223 IGWALIDDITHaeVGEEKIIDKRYYHTIKEVKNGEGPHPIKTPQGWLHLAHGVRNCAAGLRYVLYMYMTSLDDPTRLIAS 302
Cdd:cd18607  141 IWLATSDDLIH--WGDHKPLLKPRKGTWDSAKVGAGPPPIKTKKGWLLLYHGVNETAAGNRYRLGAALLDLNDPTRVLYR 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 538260974 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  69 NATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGIDNFRFWEYPVTLPEDVVPATNVY---DMRLTAHEDGWIYGI 145
Cdd:cd18615    6 NAVFNPGAAKLGGETLLLVRVEDRRGFSHLTVARSADGVTNWKIDPKPTLEPDPEDYPEEMWgieDPRITWLEELGRYAI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 146 FCaerhddnapigdlsSATATAG----IARTKDLKNWERL-----PDLKtksqqrNVVLHPEFVDGKYALYTRPqdgfiD 216
Cdd:cd18615   86 TY--------------TAYSPAGpgvsLATTKDFKTFERLglvmpPEDK------DAALFPRRINGRWALLHRP-----V 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 217 TGSGGGIGWALIDDITHAEvGEEKIIDKRYYHTIKEVKNGEGPHPIKTPQGWLHLAHGVRNCAAGLRYVLYMYMTSLDDP 296
Cdd:cd18615  141 SAGRAHIWISFSPDLKHWG-DHRPVLPARRGPWWDAVKVGLGPPPIETPEGWLIIYHGVKETASGSIYRVGLALLDLEDP 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 538260974 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  63 MERIGmnaTLNAGAIKWDGKYLMLVRVegADrksFFAVAESPNGIdNFRFWEYPVTLPEDVVPATNVYDMRLTAHEDGWi 142
Cdd:cd18612    1 LEVIG---VFNPGAARYGDEIILLLRV--AE---HLRLARSRDGI-HFTVDEKPALFPEGPYEAFGIEDPRITRIDDTY- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 143 YGIFCAerhddnapigdLSSATATAGIARTKDLKNWERL-----PDLKtksqqrNVVLHPEFVDGKYALYTRPqdgfidt 217
Cdd:cd18612   71 YITYTA-----------VSEYGIATALASTKDFKTFERHgvifpPENK------DVVIFPEKINGKYYALHRP------- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 218 gSGGGIG----W-ALIDDITHAevGEEKIIDKRYYHTIKEVKNGEGPHPIKTPQGWLHLAHGV-RNCaaglRYVLYMYMT 291
Cdd:cd18612  127 -VPSGFGkpeiWiAESPDLLHW--GNHRHLAGPRPGMWDSGRIGAGAVPIKTEKGWLEIYHGAdENN----RYCLGALLL 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 538260974 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  69 NATLNAGAIKWDGKYLMLVRVEGADRKSFFAVAESPNGIDNFRFWEYPVtlpedVVPATNVY------DMRLTaHEDGWI 142
Cdd:cd18614    4 KAVFNPAAIYEDGKVHLLYRAVGEDNISRLGYASSKDGIHFDERLDEPV-----YVPKKSGGenggceDPRIT-KIDDTY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 143 YGIFCAerHDDNAPIGdlssatATAGIARTKDLKNWERL---PDLKTKSQ--QRNVVLHPEFVDGKYALYTRPqdgfidt 217
Cdd:cd18614   78 YMTYTA--YDGWPPPR------VALTSISTKDFLNFKWNwviPPLISPPGvdDKDAVLFPEKINGKYALLHRI------- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 218 gsGGGIGWALIDDITHAE--VGEEKIIDKRYYHtIKEVKNGEGPHPIKTPQGWLHLAHGVrnCAAGLRYVLYMYMTSLDD 295
Cdd:cd18614  143 --GPDIWIDYSDDLDFGKnwIDSKIILEPRPGM-WDSRKIGAGAPPIKTKKGWLLIYHGV--DDDDRVYRLGAALLDLED 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 538260974 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974   75 GAIKWDGKYLMLVRVEGADRKSFF-AVAESPNGIDNFRFWEyPVTLPEDVVPATNVYDMRLTAHEDGWiYGIFCAErhdd 153
Cdd:pfam04041  44 KELHVYPRVVMGYYKYVSDIASFRiGLEDSYDGIKKTLEPE-PIFWPRDKQEFWGVEDPRVVKINSTY-YMTYTGR---- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  154 napigdlSSATATAGIARTKDLKNWERLPDL-------KTKSQQRNVVLHPEFVDGKYALYTRPQDGFIDTGsgggigwa 226
Cdd:pfam04041 118 -------DYKYWRIEVGTTKDFLTWARLPVKialfekrYDSIKTSDGNAFPVKIKGKYLMYHRVGDIWLAVS-------- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  227 liDDITHAEVGEEKIIDKR--YYHTIKEVKNGEGPHPIKTPQGWLHLAHGVrncaAGLRYVLYMYMTSLDDPTRLIASPA 304
Cdd:pfam04041 183 --PDLVHWENRLEPLGSPRpiMFPNPFETKIGWGTPPVETKEGWLVLIHGV----DTEDLVYRVGAALLDLEGKVLARTP 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 538260974  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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  70 ATLNAGAIKWDGKYLMLVRVEGADRK----SFFAVAESPNGIdNFrfweypVTLPEDVVPATNVY-------DMRLTAHE 138
Cdd:cd18610   14 DVFNPAAIVRDGKVYLLYRAEDASGNgngtSRIGLAVSDDGL-HF------TRLPEPVLYPEEDYewpggceDPRIVEIE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 139 DGWIYGIFCAerhddnapigdLSSATATAGIARTKDLKNWERLP------------DLKTKS-----QQRNVVLhpefVD 201
Cdd:cd18610   87 DGTYYMTYTA-----------YDGKTARLCLATSTDLVHWTKHGpafpdadggkyrDLWSKSgaivpELKGAAK----IN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 202 GKYALYtrpqdgFIDTGsgggIGWALIDDITHAEVGEekiiDKRYYHTIKEVKNGE--------GPHPIKTPQGWLHLAH 273
Cdd:cd18610  152 GKYWMY------WGESN----IYLATSDDLIHWTPVE----DDGSLRPVLSPRPGKfdsdlvepGPPPILTDGGILLIYN 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 274 GVRNCAAGLRYVLYMYMTS-----LDDPTRLIASPAGYFMAPV-GEERIGDVSNVLFSNGWIaDDDGKVFIYYASSDTRM 347
Cdd:cd18610  218 GANDGGGGPGYPKGTYSAGqalfdANDPTKLLARLDKPFLEPEtPYEKEGQVNNVVFVEGLV-YFKGKWLLYYGTADSKI 296

                 ....*
gi 538260974 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 195 LHPEFVDGKYALYTRpQDG---FIdtgsgggigwALIDDITHAEVGEeKIIDKRYYHTIKEVKNGeGPhPIKTPQGWLHL 271
Cdd:cd18613  154 LFPRKIGGRYAMLSR-QDGeniYL----------MFSDDLYFWDEAE-LILKPRYPWEFVQIGNC-GS-PIETDEGWLVL 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 272 AHGV---RncaaglRYVLYMYMTSLDDPTRLIASPAGYFMAPVGEERIGDVSNVLFSNGWIADDDgKVFIYYASSDTRMH 348
Cdd:cd18613  220 THGVgpmR------RYSIGAILLDLDDPTKVIGRLREPLLSPDEEEREGYVPNVVYSCGALVHGD-RLILPYGMSDSATG 292

                 ....*....
gi 538260974 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974  70 ATLNAGAIKWDGKYLMLVRVEGADRK--------SFFAVAESPNGIdNF----RF------WEYpvtlpedvvpatnvY- 130
Cdd:cd18611    5 AVFNGSVIKDGGKYHLLYRALSSPQEidgpklglSTIGYAESKDGV-HFenrrQLikpeeeWEK--------------Yg 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 131 --DMRLTAHEDgwIYGIF-CAerhddnapIGD--LSSATATAGIARTKDLKNWErlpdlktksqQRNVV---------LH 196
Cdd:cd18611   70 ceDPRVTKIDG--KYYIFyTA--------LSGypFGPEGIKVAVAITKDFKTIE----------EKHLVtpfnakamaLF 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 197 PEFVDGKY-ALYTrpqdgfIDTGS-GGGIGWALIDDIT-----------HAEVGEEKIIDKRYYHTIKEVkngeGPHPIK 263
Cdd:cd18611  130 PEKINGKYaALLT------VNTDNpPAKIALAYFDKIEdlwspeywdkwYANLDDHALPLRRSEHDHVEV----GAPPIK 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 264 TPQGWLHLAHGVRNcaaglryvlymYMTS------------LDDPTRLIASPAGYFMAPVGE-ERIGDVSNVLFSNGWIA 330
Cdd:cd18611  200 TKDGWLLIYSYIQN-----------YFSGervfgieaalldLNDPRKIIGRTKGPLLVPEEEyELYGLVPNIVFPSGALI 268
                        330
                 ....*....|....*
gi 538260974 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 129 VYDMRLTAHEDGWiYGIFCAerhdDNAPigDLSSATATAGIARTKDLKNWERLPDLKTKSQQ-------RNVVLHPEFVD 201
Cdd:cd08772   58 AFDPEVVYIEGTY-YLTYCS----DDLG--DILRHGQHIGVAYSKDPKGPWTRKDAPLIEPPnayspknRDPVLFPRKIG 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538260974 202 GKYALYTRPQDGFIDtgsGGGIGWALIDD----ITHAEVGEEKIIdkryyhtikeVKNGEGPHPIKTPQGWLHLAHGVrn 277
Cdd:cd08772  131 KYYLLNVPSDNGHTR---FGKIAIAESPD*lhwINHSFVYNYNEQ----------GKVGEGPSLWKTKGGWYLIYHAN-- 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 538260974 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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