NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1553137927|ref|WP_127594867|]
View 

glycoside hydrolase family 16 protein [Paenibacillus lautus]

Protein Classification

glycoside hydrolase family 16 protein( domain architecture ID 10114982)

glycoside hydrolase family 16 protein similar to lichenase (also known as 1,3-1,4-beta-glucanase) which specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GH16_lichenase cd02175
lichenase, member of glycosyl hydrolase family 16; Lichenase, also known as 1,3-1, ...
 37-254 2.62e-108

lichenase, member of glycosyl hydrolase family 16; Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure.


:

Pssm-ID: 185684 [Multi-domain]  Cd Length: 212  Bit Score: 311.51  E-value: 2.62e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  37 FNEPLNGTNPNLFYTSDGWANGPDFGVGWKAANQEFSNGIMALRLDNAGCpascSGKSYASGEYATHLKYGYGRVEARIK 116
Cdd:cd02175     1 FFEDFNSLDTGRWYKSDGWSNGGPFNCTWSADNVEFSDGGLALTLTNDTY----GEKPYACGEYRTRGFYGYGRYEVRMK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 117 AAKGTGLVTSLFTYSGQATGTSNDEIDIEILGKDTTKMETNYFTNGVGQHSTIINLGFDASLDFHNYAFEWSPSSIKWYV 196
Cdd:cd02175    77 PAKGSGVVSSFFTYTGPYDGDPHDEIDIEFLGKDTTKVQFNYYTNGVGGHEKLIDLGFDASEGFHTYAFEWEPDSIRWYV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1553137927 197 DGQLVHTENGSRGALPTSPGHIMVNLWSGSGpAEIWTGTFNYpGSPVRAYYDWIKFTP 254
Cdd:cd02175   157 DGELVHEATATDPNIPDTPGKIMMNLWPGDG-VDDWLGPFDG-GTPLTAEYDWVSYTP 212
 
Name Accession Description Interval E-value
GH16_lichenase cd02175
lichenase, member of glycosyl hydrolase family 16; Lichenase, also known as 1,3-1, ...
 37-254 2.62e-108

lichenase, member of glycosyl hydrolase family 16; Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure.


Pssm-ID: 185684 [Multi-domain]  Cd Length: 212  Bit Score: 311.51  E-value: 2.62e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  37 FNEPLNGTNPNLFYTSDGWANGPDFGVGWKAANQEFSNGIMALRLDNAGCpascSGKSYASGEYATHLKYGYGRVEARIK 116
Cdd:cd02175     1 FFEDFNSLDTGRWYKSDGWSNGGPFNCTWSADNVEFSDGGLALTLTNDTY----GEKPYACGEYRTRGFYGYGRYEVRMK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 117 AAKGTGLVTSLFTYSGQATGTSNDEIDIEILGKDTTKMETNYFTNGVGQHSTIINLGFDASLDFHNYAFEWSPSSIKWYV 196
Cdd:cd02175    77 PAKGSGVVSSFFTYTGPYDGDPHDEIDIEFLGKDTTKVQFNYYTNGVGGHEKLIDLGFDASEGFHTYAFEWEPDSIRWYV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1553137927 197 DGQLVHTENGSRGALPTSPGHIMVNLWSGSGpAEIWTGTFNYpGSPVRAYYDWIKFTP 254
Cdd:cd02175   157 DGELVHEATATDPNIPDTPGKIMMNLWPGDG-VDDWLGPFDG-GTPLTAEYDWVSYTP 212
BglS COG2273
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism];
11-254 9.66e-56

Beta-glucanase, GH16 family [Carbohydrate transport and metabolism];


Pssm-ID: 441874 [Multi-domain]  Cd Length: 259  Bit Score: 179.41  E-value: 9.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  11 MTTMLMAGSLLCGLLVPIQASAA------DVAFNEPLNGTNPNL---FYTSDGWANGPDFGVGWKAANQEFSNGIMALRL 81
Cdd:COG2273     1 MKLLLLLALLLAALAAAGAASSApaaagwTLVFSDEFDGTSLDTskwTYDTGGPGWGNGELQYYTDENVSVENGNLVITA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  82 DNAgcPASCSGKSYASGEYATHLK--YGYGRVEARIKAAKGTGLVTSLFTYSGQATGT--SNDEIDI-EILGKDTTKMET 156
Cdd:COG2273    81 RKE--PYGGGGRPYTSGRITTKGKfsFTYGRFEARAKLPKGQGLWPAFWMLGGDIDGGwpASGEIDImEFVGKDPNKVHG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 157 NYFT---NGVGQHSTIINLGFDASLDFHNYAFEWSPSSIKWYVDGQLVHTENGSRGALPT---SPGHIMVNLWSGSGpae 230
Cdd:COG2273   159 NVHYggyNGGEGIGASYDLPFDASDDFHTYAVEWTPDSIRWYVDGVLVHTVTPADVGGPWpfdQPFYLILNLAVGGN--- 235

                         250       260
                  ....*....|....*....|....
gi 1553137927 231 iWTGTFNYPGSPVRAYYDWIKFTP 254
Cdd:COG2273   236 -WPGAPDTTGFPATMEVDYVRVYQ 258
Glyco_hydro_16 pfam00722
Glycosyl hydrolases family 16;
65-251 3.88e-46

Glycosyl hydrolases family 16;


Pssm-ID: 395585 [Multi-domain]  Cd Length: 168  Bit Score: 151.59  E-value: 3.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  65 WKAANQEFSNGIMALRLDNagcpascsgksYASGEYATHLKYGYGRVEARIKAAKGTGLVTSLFTYSGqaTGTSNDEIDI 144
Cdd:pfam00722   1 WGGDNVSVSNGGLTLTLDK-----------YTGSGFQSKFYYLYGKVEARIKAARGAGVVTAFYLSSE--DWDDHDEIDF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 145 EILGKDTTKMETNYFTNGVGQH-STIINLGFDASLDFHNYAFEWSPSSIKWYVDGQLVHT---ENGSRGALPTSPGHIMV 220
Cdd:pfam00722  68 EFLGNDTGQVQTNVYGNGKGNRgEQRFSLWFDPTADFHTYSILWNPDKITWYVDGVPVRTlknNDAGGVPYPQTPMRLYV 147

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1553137927 221 NLWSGSGPAeiwtgtfnypGSPVRAYYDWIK 251
Cdd:pfam00722 148 SLWPGGDWA----------TPGGGVKIDWAG 168
PLN03161 PLN03161
Probable xyloglucan endotransglucosylase/hydrolase protein; Provisional
 108-198 5.75e-13

Probable xyloglucan endotransglucosylase/hydrolase protein; Provisional


Pssm-ID: 178706 [Multi-domain]  Cd Length: 291  Bit Score: 67.23  E-value: 5.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 108 YGRVEARIKAAKG--TGLVTSLFTYSgqaTGTSNDEIDIEILGKDTTK---METNYFTNGVGQHSTIINLGFDASLDFHN 182
Cdd:PLN03161   69 FGSIEMLIKLVPGnsAGTVTAYYLSS---TGSRHDEIDFEFLGNVSGQpytIHTNIYTQGNGSREQQFRPWFDPTADFHN 145

                          90
                  ....*....|....*.
gi 1553137927 183 YAFEWSPSSIKWYVDG 198
Cdd:PLN03161  146 YTIHWNPSEVVWYVDG 161
 
Name Accession Description Interval E-value
GH16_lichenase cd02175
lichenase, member of glycosyl hydrolase family 16; Lichenase, also known as 1,3-1, ...
 37-254 2.62e-108

lichenase, member of glycosyl hydrolase family 16; Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure.


Pssm-ID: 185684 [Multi-domain]  Cd Length: 212  Bit Score: 311.51  E-value: 2.62e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  37 FNEPLNGTNPNLFYTSDGWANGPDFGVGWKAANQEFSNGIMALRLDNAGCpascSGKSYASGEYATHLKYGYGRVEARIK 116
Cdd:cd02175     1 FFEDFNSLDTGRWYKSDGWSNGGPFNCTWSADNVEFSDGGLALTLTNDTY----GEKPYACGEYRTRGFYGYGRYEVRMK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 117 AAKGTGLVTSLFTYSGQATGTSNDEIDIEILGKDTTKMETNYFTNGVGQHSTIINLGFDASLDFHNYAFEWSPSSIKWYV 196
Cdd:cd02175    77 PAKGSGVVSSFFTYTGPYDGDPHDEIDIEFLGKDTTKVQFNYYTNGVGGHEKLIDLGFDASEGFHTYAFEWEPDSIRWYV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1553137927 197 DGQLVHTENGSRGALPTSPGHIMVNLWSGSGpAEIWTGTFNYpGSPVRAYYDWIKFTP 254
Cdd:cd02175   157 DGELVHEATATDPNIPDTPGKIMMNLWPGDG-VDDWLGPFDG-GTPLTAEYDWVSYTP 212
BglS COG2273
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism];
11-254 9.66e-56

Beta-glucanase, GH16 family [Carbohydrate transport and metabolism];


Pssm-ID: 441874 [Multi-domain]  Cd Length: 259  Bit Score: 179.41  E-value: 9.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  11 MTTMLMAGSLLCGLLVPIQASAA------DVAFNEPLNGTNPNL---FYTSDGWANGPDFGVGWKAANQEFSNGIMALRL 81
Cdd:COG2273     1 MKLLLLLALLLAALAAAGAASSApaaagwTLVFSDEFDGTSLDTskwTYDTGGPGWGNGELQYYTDENVSVENGNLVITA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  82 DNAgcPASCSGKSYASGEYATHLK--YGYGRVEARIKAAKGTGLVTSLFTYSGQATGT--SNDEIDI-EILGKDTTKMET 156
Cdd:COG2273    81 RKE--PYGGGGRPYTSGRITTKGKfsFTYGRFEARAKLPKGQGLWPAFWMLGGDIDGGwpASGEIDImEFVGKDPNKVHG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 157 NYFT---NGVGQHSTIINLGFDASLDFHNYAFEWSPSSIKWYVDGQLVHTENGSRGALPT---SPGHIMVNLWSGSGpae 230
Cdd:COG2273   159 NVHYggyNGGEGIGASYDLPFDASDDFHTYAVEWTPDSIRWYVDGVLVHTVTPADVGGPWpfdQPFYLILNLAVGGN--- 235

                         250       260
                  ....*....|....*....|....
gi 1553137927 231 iWTGTFNYPGSPVRAYYDWIKFTP 254
Cdd:COG2273   236 -WPGAPDTTGFPATMEVDYVRVYQ 258
Glyco_hydro_16 pfam00722
Glycosyl hydrolases family 16;
65-251 3.88e-46

Glycosyl hydrolases family 16;


Pssm-ID: 395585 [Multi-domain]  Cd Length: 168  Bit Score: 151.59  E-value: 3.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  65 WKAANQEFSNGIMALRLDNagcpascsgksYASGEYATHLKYGYGRVEARIKAAKGTGLVTSLFTYSGqaTGTSNDEIDI 144
Cdd:pfam00722   1 WGGDNVSVSNGGLTLTLDK-----------YTGSGFQSKFYYLYGKVEARIKAARGAGVVTAFYLSSE--DWDDHDEIDF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 145 EILGKDTTKMETNYFTNGVGQH-STIINLGFDASLDFHNYAFEWSPSSIKWYVDGQLVHT---ENGSRGALPTSPGHIMV 220
Cdd:pfam00722  68 EFLGNDTGQVQTNVYGNGKGNRgEQRFSLWFDPTADFHTYSILWNPDKITWYVDGVPVRTlknNDAGGVPYPQTPMRLYV 147

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1553137927 221 NLWSGSGPAeiwtgtfnypGSPVRAYYDWIK 251
Cdd:pfam00722 148 SLWPGGDWA----------TPGGGVKIDWAG 168
Glyco_hydrolase_16 cd00413
glycosyl hydrolase family 16; The O-Glycosyl hydrolases are a widespread group of enzymes that ...
 55-253 6.95e-45

glycosyl hydrolase family 16; The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.


Pssm-ID: 185683 [Multi-domain]  Cd Length: 210  Bit Score: 149.89  E-value: 6.95e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  55 WANGPDFGVGWKAANQEFSN-GIMALRLDnagcPASCSGKSYASGEYATHLKYGYGRVEARIKAAKGTGLVTSLFTYSGQ 133
Cdd:cd00413    17 DGPSWGGNMTNSPNNVYVENdGGLTLRTD----RDQTDGPYSSAEIDSQKNNYTYGYYEARAKLAGGPGAVSAFWTYSDD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 134 ATGTSNDEIDIEILGKDTTKMETNYFTNGVG-----QHSTIINLGFDASLDFHNYAFEWSPSSIKWYVDGQLVHTengSR 208
Cdd:cd00413    93 DDPPDGGEIDIEFLGRDPTTVQTNVHWPGYGagattGEEKSVHLPFDPADDFHTYRVDWTPGEITFYVDGVLVAT---IT 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1553137927 209 GALPTSPGHIMVNLWSGSGpaeiWTGTFNYPGSPVRAYYDWIKFT 253
Cdd:cd00413   170 NQVPDDPMNIILNLWSDGG----WWWGGPPPGAPAYMEIDWVRVY 210
GH16_fungal_CRH1_transglycosylase cd02183
glycosylphosphatidylinositol-glucanosyltransferase; Group of fungal GH16 members related to ...
 108-256 1.32e-26

glycosylphosphatidylinositol-glucanosyltransferase; Group of fungal GH16 members related to Saccharomyces cerevisiae Crh1p. Chr1p and Crh2p are transglycosylases that are required for the linkage of chitin to beta(1-3)glucose branches of beta(1-6)glucan, an important step in the assembly of new cell wall. Both have been shown to be glycosylphosphatidylinositol (GPI)-anchored. A third homologous protein, Crr1p, functions in the formation of the spore wall. They belongs to the family 16 of glycosyl hydrolases that includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.


Pssm-ID: 185692 [Multi-domain]  Cd Length: 203  Bit Score: 102.24  E-value: 1.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 108 YGRVEARIKAAKGTGLVTSLFTYSgqATGtsnDEIDIEILGKDTTKMETNYFTNGVGQ---HSTIINLGFDASLDFHNYA 184
Cdd:cd02183    47 YGKVEVTMKAAPGQGIVSSFVLQS--DDL---DEIDWEWVGGDLTQVQTNYFGKGNTTtydRGGYHPVPNPQTEEFHTYT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 185 FEWSPSSIKWYVDGQLVHT----ENGSRGALPTSPGHIMVNLWSGSGP-AEIWT-----GTFNYPGSPVRAYYDWIKFTP 254
Cdd:cd02183   122 IDWTKDRITWYIDGKVVRTltkaDTTGGYGYPQTPMRLQIGIWAGGDPsNAPGTiewagGETDYDKGPFTMYVKSVTVTD 201


                  ..
gi 1553137927 255 AN 256
Cdd:cd02183   202 YS 203
GH16_XET cd02176
Xyloglucan endotransglycosylase, member of glycosyl hydrolase family 16; Xyloglucan ...
 60-226 6.75e-22

Xyloglucan endotransglycosylase, member of glycosyl hydrolase family 16; Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Xyloglucan is a soluble hemicellulose with a backbone of beta-1,4-linked glucose units, partially substituted with alpha-1,6-linked xylopyranose branches. It binds noncovalently to cellulose, cross-linking the adjacent cellulose microfibrils, giving it a key structural role as a matrix polymer. Therefore, XET plays an important role in all plant processes that require cell wall remodeling.


Pssm-ID: 185685 [Multi-domain]  Cd Length: 263  Bit Score: 91.11  E-value: 6.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  60 DFGVGWKAANQEFSNG--IMALRLDnagcpascsgKSYASGeYATHLKYGYGRVEARIKAAKG--TGLVTSLFTYSGQat 135
Cdd:cd02176     9 NFFVTWGPDHIRVSNDgtSVQLTLD----------QSSGSG-FKSKNKYLFGFFSMRIKLPPGdsAGTVTAFYLSSQG-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 136 GTSNDEIDIEILGKDTTK---METNYFTNGVGQHSTIINLGFDASLDFHNYAFEWSPSSIKWYVDGQLV-----HTENGS 207
Cdd:cd02176    76 PDNHDEIDFEFLGNVTGQpytLQTNVFANGVGGREQRIYLWFDPTADFHTYSILWNPHQIVFYVDDVPIrvfknNEALGV 155

                         170       180
                  ....*....|....*....|
gi 1553137927 208 rgALPTS-PGHIMVNLWSGS 226
Cdd:cd02176   156 --PYPSSqPMGVYASIWDGS 173
GH16_laminarinase_like cd08023
Laminarinase, member of the glycosyl hydrolase family 16; Laminarinase, also known as glucan ...
 91-252 1.60e-17

Laminarinase, member of the glycosyl hydrolase family 16; Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.


Pssm-ID: 185693 [Multi-domain]  Cd Length: 235  Bit Score: 78.82  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  91 SGKSYASGEYATHLKYG--YGRVEARIKAAKGTG------LVTSLFTYSG-QATGtsndEIDI-EILGKDTTKMETNYFT 160
Cdd:cd08023    60 DGYPYTSGRITTKGKFSftYGRVEARAKLPKGQGtwpafwMLGENIKYVGwPASG----EIDImEYVGNEPNTVYGTLHG 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 161 NGV-----GQHSTIINLGFDASLDFHNYAFEWSPSSIKWYVDGQLVHT-----ENGSRGALPTSPGHIMVNL-WSGSGPA 229
Cdd:cd08023   136 GATndgnnGSGGSYTLPTDDLSDDFHTYAVEWTPDKITFYVDGKLYFTytnpnTDNGGQWPFDQPFYLILNLaVGGNWPG 215

                         170       180
                  ....*....|....*....|...
gi 1553137927 230 EIWTGTFNypgsPVRAYYDWIKF 252
Cdd:cd08023   216 PPDDDTPF----PATMEVDYVRV 234
PLN03161 PLN03161
Probable xyloglucan endotransglucosylase/hydrolase protein; Provisional
 108-198 5.75e-13

Probable xyloglucan endotransglucosylase/hydrolase protein; Provisional


Pssm-ID: 178706 [Multi-domain]  Cd Length: 291  Bit Score: 67.23  E-value: 5.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 108 YGRVEARIKAAKG--TGLVTSLFTYSgqaTGTSNDEIDIEILGKDTTK---METNYFTNGVGQHSTIINLGFDASLDFHN 182
Cdd:PLN03161   69 FGSIEMLIKLVPGnsAGTVTAYYLSS---TGSRHDEIDFEFLGNVSGQpytIHTNIYTQGNGSREQQFRPWFDPTADFHN 145

                          90
                  ....*....|....*.
gi 1553137927 183 YAFEWSPSSIKWYVDG 198
Cdd:PLN03161  146 YTIHWNPSEVVWYVDG 161
GH16_beta_agarase cd02178
Beta-agarase, member of glycosyl hydrolase family 16; Beta-agarase is a glycosyl hydrolase ...
 65-250 6.24e-12

Beta-agarase, member of glycosyl hydrolase family 16; Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.


Pssm-ID: 185687  Cd Length: 258  Bit Score: 63.91  E-value: 6.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  65 WKAANQEFSNGIMALRLDNAGCPASCSGKSYASGEYATHLKYGYGRVEARIKAAKGTgLVTSLFTYSGQATGTSndEIDI 144
Cdd:cd02178    55 FSADNVSVEDGNLVLSATRHPGTELGNGYKVTTGSITSKEKVKYGYFEARAKASNLP-MSSAFWLLSDTKDSTT--EIDI 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 145 -EILGKDT-----TKMETNY-------FTNGVGQH-STIINLGFDASLDFHNYAFEW-SPSSIKWYVDGQLVHTENGSRG 209
Cdd:cd02178   132 lEHYGGDReewfaTRMNSNThvfirdpEQDYQPKDdGSWYYNPTELADDFHVYGVYWkDPDTIRFYIDGVLVRTVENSEI 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1553137927 210 ALPTsPGHImvnlwsgsgPAEIW--TGTFNYPGSPVRA----------YYDWI 250
Cdd:cd02178   212 TDGT-GFDQ---------PMYIIidTETYDWRGEPTDEeladdskntfYVDYV 254
GH16_kappa_carrageenase cd02177
Kappa-carrageenase, member of glycosyl hydrolase family 16; Kappa-carrageenase is a glycosyl ...
 57-201 5.42e-06

Kappa-carrageenase, member of glycosyl hydrolase family 16; Kappa-carrageenase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of kappa-carrageenans, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Carrageenans are linear chains of galactose units linked by alternating D-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Depending on the position and number of sulfate ester modifications they are subdivided into kappa-, iota-, and lambda-carrageenases, kappa being modified once. Carrageenans form thermo-reversible gels widely used for industrial applications. Kappa-carrageenases exist in bacteria belonging to at least three phylogenetically distant branches, including pseudoalteromonas, planctomycetes, and baceroidetes. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.


Pssm-ID: 185686  Cd Length: 269  Bit Score: 46.51  E-value: 5.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927  57 NGPDFGVgWKAANQE---FSNGIMAL---RLDNAGCPASCSGKS-----YASGEYATHLKYGYGRVEARIKAAK-GTGLV 124
Cdd:cd02177    31 TGENTGA-WKWNNEKnvvISNGILELtmrRNANNTTFWDQQQVPdgptyFTSGIFKSYAKGTYGYYEARIKGADiFPGVC 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553137927 125 TSLFTYS------GQATGTSNDEIDIEILGKDTTKMETNYFTNGVGQHSTIINLG---------------------FDAS 177
Cdd:cd02177   110 PSFWLYSdidysvANEGEVVYSEIDVVELQQFDWYHQDDIRDMDHNLHAIVKENGqgvwkrpkmyppteqlnyhrpFDPS 189

                         170       180
                  ....*....|....*....|....
gi 1553137927 178 LDFHNYAFEWSPSSIKWYVDGQLV 201
Cdd:cd02177   190 KDFHTYGCNVNQDEIIWYVDGVEV 213
GH16_beta_GRP cd02179
beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1, ...
 179-229 8.81e-04

beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.


Pssm-ID: 185688 [Multi-domain]  Cd Length: 321  Bit Score: 40.06  E-value: 8.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1553137927 179 DFHNYAFEWSPSSIKWYVDGQLVHTENGSRGALPTSPGHIMVNLW-SGSGPA 229
Cdd:cd02179   201 DFHVYTLEWKPDGITLMVDGEEYGEIEPGEGGYSEAANNPAASRWlGGTVMA 252
GH16_CCF cd08024
Coelomic cytolytic factor, member of glycosyl hydrolase family 16; Subgroup of glucanases of ...
 179-227 1.76e-03

Coelomic cytolytic factor, member of glycosyl hydrolase family 16; Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.


Pssm-ID: 185694  Cd Length: 330  Bit Score: 39.15  E-value: 1.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1553137927 179 DFHNYAFEWSPSSIKWYVDGQL---VHTENGS---RGALPTSPGHimvNLWSGSG 227
Cdd:cd08024   206 DFHTYGLDWTPDHIRFYVDDRLiltLDVPGQGfweFGGFSGTPID---NPWAGGG 257
GH16_Strep_laminarinase_like cd02182
Streptomyces laminarinase-like, member of glycosyl hydrolase family 16; Proteins similar to ...
 179-242 6.40e-03

Streptomyces laminarinase-like, member of glycosyl hydrolase family 16; Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel.


Pssm-ID: 185691  Cd Length: 259  Bit Score: 36.91  E-value: 6.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1553137927 179 DFHNYAFEW-----SPSSIKWYVDGQLVHTENGSR-------GALPTSPGHIMVNLWSGSgpaeiwtgtfNYPGSP 242
Cdd:cd02182   173 GFHTYAVEIdrtngDAESIRWYLDGVVYHTVTGARvgdettwQALAHHPLFIILNVAVGG----------NWPGAP 238
 
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