|
Name |
Accession |
Description |
Interval |
E-value |
| CBM9_like_1 |
cd00005 |
DOMON-like type 9 carbohydrate binding module of xylanases; Family 9 carbohydrate-binding ... |
719-901 |
3.56e-76 |
|
DOMON-like type 9 carbohydrate binding module of xylanases; Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
:
Pssm-ID: 187674 Cd Length: 185 Bit Score: 247.53 E-value: 3.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 719 IEKATKATVKIDGEADSEWDKAVAIPLTINLGAS--VTADAKVLWDDENLYVYATVKDRVLNKDSGEAYQQDSLEVFIDE 796
Cdd:cd00005 1 VATAKYGTPVIDGEVDDVWAKAEEITTDKKVSGTdgATATARTLWDEDNLYVLAEVKDPVLNKASANPWEQDSVEIFVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 797 NNAKTESYDDDDKQYRINYVNEHSFNGKKcLEENVRSAAKETEDGYVIEAAFKWTDIQPKEGDRIGLEFQINDADASGAR 876
Cdd:cd00005 81 NNAKTSSYEDDDAQYRVNFDNEQSFGGGA-IAERFTSATKLTDGGYVVEAAIPLKTITPAAGTVIGFDLQVNDADDGGKR 159
|
170 180
....*....|....*....|....*
gi 1469754418 877 IGTLSWNDETGMGWSKSSVYGTIEL 901
Cdd:cd00005 160 IGVANWNDPTGNGYQDTSRFGVLLL 184
|
|
| XynA |
COG3693 |
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]; |
189-570 |
6.72e-74 |
|
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism];
:
Pssm-ID: 442908 Cd Length: 328 Bit Score: 246.73 E-value: 6.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 189 GTGIMLSEITDDTLMKLVEKHFNAVTFGNELKPDAlfnyklensvktktvqfdgqdlevpvVNDAGDSLDFSRADAMVDk 268
Cdd:COG3693 30 GTAVNAGQLDDPAYRELLAREFNSVTPENEMKWGS--------------------------IEPERGEFNFSAADAIVA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 269 ileWNAAHpdrKIRIRGHVLVWHSQTQEWFFHENydiskpyVDKETMNRRLEWYISSVFDHYfgeaangkyDGLFYGWDV 348
Cdd:COG3693 83 ---FAKAN---GMKVRGHTLVWHSQTPDWVFEDA-------LSKEELRARLEEHITTVVGRY---------KGKIYAWDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 349 VNEAV-IGNTYRtdtvspaeslneirhgnNSSWWHVYKsNEFIINAFKYANKYAPkNVELYYNDFG-ETDNIKSEGIIKL 426
Cdd:COG3693 141 VNEAIdDDGSLR-----------------NSPWYQALG-PDYIADAFRWAREADP-DAKLFYNDYNiEGGPAKRDAYLEL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 427 ISDVKsAEGTRLDAFGMQAHYSVDSFSAAQFKTVAKKYAEAAGKVQLTELDFQASAAYKSGAASkdseYTKMAYCHKQLF 506
Cdd:COG3693 202 VKDLK-ARGVPIDGVGLQGHLGLDYPSPEEIEAALDRFAALGLPIHITELDVRVLPLPDLTEED----DAAQADRYRDLF 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469754418 507 DAAKDLKkngtNVAGITVWGVIEPNSWLhsqsnvgggADGSKQCPLLFDGKYKAKPAYWAYVDA 570
Cdd:COG3693 277 DAFLSHP----AVTGVTFWGLTDGYSWR---------PGFRTGYPLLFDEDYQPKPAYDAVLDA 327
|
|
| CBM86 |
cd20907 |
carbohydrate binding module family 86; This family describes what is most likely a ... |
29-156 |
1.03e-47 |
|
carbohydrate binding module family 86; This family describes what is most likely a xylan-binding module such as found in the Xyn10A protein of Roseburia intestinalis L1-82, which is involved in the extracellular capture and breakdown of xylan.
:
Pssm-ID: 411019 Cd Length: 127 Bit Score: 166.00 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 29 KKTTYTADQLEVDWGNASYERTDGVWKVTFNNQYDQVKWRLPETIDMSTVKSVTFNVKDQKGSVSLKVYKrEQTEADGAN 108
Cdd:cd20907 1 KTKEFTADKLTLAFGGAWYSSADGSGKLTFAKQYQEYKYDLPETLDMSQVKSVTFKVKDQKGNIALKLYD-TGGDMTEVN 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1469754418 109 TQYGLTGKEEYSISPTGEGDMEAVGLMTTDDTGSGSAISLVSVTVETD 156
Cdd:cd20907 80 ANYGLNGQDEYTINPNYDGKVRAIGIMAMGSNEYDAPVSITSVTVELD 127
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CBM9_like_1 |
cd00005 |
DOMON-like type 9 carbohydrate binding module of xylanases; Family 9 carbohydrate-binding ... |
719-901 |
3.56e-76 |
|
DOMON-like type 9 carbohydrate binding module of xylanases; Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
Pssm-ID: 187674 Cd Length: 185 Bit Score: 247.53 E-value: 3.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 719 IEKATKATVKIDGEADSEWDKAVAIPLTINLGAS--VTADAKVLWDDENLYVYATVKDRVLNKDSGEAYQQDSLEVFIDE 796
Cdd:cd00005 1 VATAKYGTPVIDGEVDDVWAKAEEITTDKKVSGTdgATATARTLWDEDNLYVLAEVKDPVLNKASANPWEQDSVEIFVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 797 NNAKTESYDDDDKQYRINYVNEHSFNGKKcLEENVRSAAKETEDGYVIEAAFKWTDIQPKEGDRIGLEFQINDADASGAR 876
Cdd:cd00005 81 NNAKTSSYEDDDAQYRVNFDNEQSFGGGA-IAERFTSATKLTDGGYVVEAAIPLKTITPAAGTVIGFDLQVNDADDGGKR 159
|
170 180
....*....|....*....|....*
gi 1469754418 877 IGTLSWNDETGMGWSKSSVYGTIEL 901
Cdd:cd00005 160 IGVANWNDPTGNGYQDTSRFGVLLL 184
|
|
| XynA |
COG3693 |
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]; |
189-570 |
6.72e-74 |
|
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism];
Pssm-ID: 442908 Cd Length: 328 Bit Score: 246.73 E-value: 6.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 189 GTGIMLSEITDDTLMKLVEKHFNAVTFGNELKPDAlfnyklensvktktvqfdgqdlevpvVNDAGDSLDFSRADAMVDk 268
Cdd:COG3693 30 GTAVNAGQLDDPAYRELLAREFNSVTPENEMKWGS--------------------------IEPERGEFNFSAADAIVA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 269 ileWNAAHpdrKIRIRGHVLVWHSQTQEWFFHENydiskpyVDKETMNRRLEWYISSVFDHYfgeaangkyDGLFYGWDV 348
Cdd:COG3693 83 ---FAKAN---GMKVRGHTLVWHSQTPDWVFEDA-------LSKEELRARLEEHITTVVGRY---------KGKIYAWDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 349 VNEAV-IGNTYRtdtvspaeslneirhgnNSSWWHVYKsNEFIINAFKYANKYAPkNVELYYNDFG-ETDNIKSEGIIKL 426
Cdd:COG3693 141 VNEAIdDDGSLR-----------------NSPWYQALG-PDYIADAFRWAREADP-DAKLFYNDYNiEGGPAKRDAYLEL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 427 ISDVKsAEGTRLDAFGMQAHYSVDSFSAAQFKTVAKKYAEAAGKVQLTELDFQASAAYKSGAASkdseYTKMAYCHKQLF 506
Cdd:COG3693 202 VKDLK-ARGVPIDGVGLQGHLGLDYPSPEEIEAALDRFAALGLPIHITELDVRVLPLPDLTEED----DAAQADRYRDLF 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469754418 507 DAAKDLKkngtNVAGITVWGVIEPNSWLhsqsnvgggADGSKQCPLLFDGKYKAKPAYWAYVDA 570
Cdd:COG3693 277 DAFLSHP----AVTGVTFWGLTDGYSWR---------PGFRTGYPLLFDEDYQPKPAYDAVLDA 327
|
|
| Glyco_10 |
smart00633 |
Glycosyl hydrolase family 10; |
255-566 |
7.97e-68 |
|
Glycosyl hydrolase family 10;
Pssm-ID: 214750 Cd Length: 263 Bit Score: 227.89 E-value: 7.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 255 DSLDFSRADAMVDkileWNAAHpdrKIRIRGHVLVWHSQTQEWFFHENYDiskpyvDKETMNRRLEWYISSVFDHYfgea 334
Cdd:smart00633 11 GQFNFSGADAIVN----FAKEN---GIKVRGHTLVWHSQTPDWVFNLNIS------GKETLLARLENHIKTVVGRY---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 335 aNGKYdglfYGWDVVNEAVIGNTyrtdtvspaeslneIRHGNNSSWWHVYKsNEFIINAFKYANKYAPkNVELYYNDFG- 413
Cdd:smart00633 74 -KGKI----YAWDVVNEAIHDNG--------------SGLRRSSVWYQILG-EDYIEKAFRYAREADP-DAKLFYNDYNt 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 414 ETDNIKSEGIIKLISDVKsAEGTRLDAFGMQAHYSVDSFSAAQFKTVAKKYAEAAGKVQLTELDFqasaaykSGAASKDS 493
Cdd:smart00633 133 EEPNAKRQAIYELVKKLK-AKGVPIDGIGLQSHLSLGGPNIAEIRAALDRFASLGLEIWITELDI-------SGPPNPEE 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469754418 494 EYTKMAYCHKQLFDAAKDLKkngtNVAGITVWGVIEPNSWLhsqsnvgggadGSKQCPLLFDGKYKAKPAYWA 566
Cdd:smart00633 205 NLQAQAADYEEVFKACLAHP----AVTGVTVWGVTDGYSWL-----------DGFGAPLLFDANYQPKPAYWA 262
|
|
| Glyco_hydro_10 |
pfam00331 |
Glycosyl hydrolase family 10; |
189-569 |
1.95e-62 |
|
Glycosyl hydrolase family 10;
Pssm-ID: 425613 Cd Length: 310 Bit Score: 214.46 E-value: 1.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 189 GTGIMLSEITD-DTLMKLVEKHFNAVTFGNELKPDALFNYKlensvktktvqfdgqdlevpvvndagDSLDFSRADamvd 267
Cdd:pfam00331 13 GTAVSAGELLGnSQYTAILKAEFNQVTPENEMKWDALEPSR--------------------------GNFTFANAD---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 268 KILEWNAAHpdrKIRIRGHVLVWHSQTQEWFFHENYDiskpyvdKETMNRRLEWYISSVFDHYFGEaangkydglFYGWD 347
Cdd:pfam00331 63 RIVNFAKQN---GMAVRGHTLVWHSQLPDWVFNINGS-------KADLLQVLENHITTVVGHYKGK---------IYAWD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 348 VVNEAV---IGNTYRtdtvspaeslneirhgnNSSWWHVYkSNEFIINAFKYANKYAPkNVELYYNDFG-ETDNIKSEGI 423
Cdd:pfam00331 124 VVNEAFdddGSGGLR-----------------SSVWYQVL-GEDYIEIAFRAAREADP-DAKLYYNDYNiEEDGAKRDAV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 424 IKLISDVKSAeGTRLDAFGMQAHYSVDSFSAAQFKTVAKKYAEAAGKVQLTELDFQASAAYKSGAASkdseytKMAYCHK 503
Cdd:pfam00331 185 YNLVKDLKAK-GVPIDGIGFQSHLSAGGPSISNIRAALQRFAALGLEVAITELDIRGPDPSDEEALQ------AQAARYK 257
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469754418 504 QLFDAAKDLKkngtNVAGITVWGVIEPNSWLHSQSNVGggadgskqcPLLFDGKYKAKPAYWAYVD 569
Cdd:pfam00331 258 EVFKACLAVP----NCTGITVWGVTDKYSWLSGFFPGA---------PLLFDSNYQPKPAYNAVVD 310
|
|
| CBM9_1 |
pfam06452 |
Carbohydrate family 9 binding domain-like; CBM9_1 is a C-terminal domain on bacterial xylanase ... |
729-901 |
1.19e-53 |
|
Carbohydrate family 9 binding domain-like; CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallization reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.
Pssm-ID: 428950 Cd Length: 180 Bit Score: 184.86 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 729 IDGEADSEWDKAVAIPLTINLGASVTADA----KVLWDDENLYVYATVKDRVLNKDSGEAYQQDSLEVFIDENNAKTESY 804
Cdd:pfam06452 1 IDGTVDAVWSNAQSLTIFKLWTGTVSSDAsgtfKALWDDDNLYVLAEVTDDVLNDGSTNPWEDDSVEIFIDENNGKTTEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 805 DDDDKQYRINYVNEHSFN-GKKCLEENVRSAAKETEDGYVIEAAFKWTDIQ-PKEGDRIGLEFQINDADASGARIGTLSW 882
Cdd:pfam06452 81 GANDFQYRVNYNNETSFDpGNGLIAAGFTSASKVSDGGYIVEAKIPLKTITtPANNKVIGFDVQINDDDDGGTRQGKITW 160
|
170
....*....|....*....
gi 1469754418 883 NDETGMGWSKSSVYGTIEL 901
Cdd:pfam06452 161 NDPTGNAWQDPSVFGTVTL 179
|
|
| CBM86 |
cd20907 |
carbohydrate binding module family 86; This family describes what is most likely a ... |
29-156 |
1.03e-47 |
|
carbohydrate binding module family 86; This family describes what is most likely a xylan-binding module such as found in the Xyn10A protein of Roseburia intestinalis L1-82, which is involved in the extracellular capture and breakdown of xylan.
Pssm-ID: 411019 Cd Length: 127 Bit Score: 166.00 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 29 KKTTYTADQLEVDWGNASYERTDGVWKVTFNNQYDQVKWRLPETIDMSTVKSVTFNVKDQKGSVSLKVYKrEQTEADGAN 108
Cdd:cd20907 1 KTKEFTADKLTLAFGGAWYSSADGSGKLTFAKQYQEYKYDLPETLDMSQVKSVTFKVKDQKGNIALKLYD-TGGDMTEVN 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1469754418 109 TQYGLTGKEEYSISPTGEGDMEAVGLMTTDDTGSGSAISLVSVTVETD 156
Cdd:cd20907 80 ANYGLNGQDEYTINPNYDGKVRAIGIMAMGSNEYDAPVSITSVTVELD 127
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CBM9_like_1 |
cd00005 |
DOMON-like type 9 carbohydrate binding module of xylanases; Family 9 carbohydrate-binding ... |
719-901 |
3.56e-76 |
|
DOMON-like type 9 carbohydrate binding module of xylanases; Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
Pssm-ID: 187674 Cd Length: 185 Bit Score: 247.53 E-value: 3.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 719 IEKATKATVKIDGEADSEWDKAVAIPLTINLGAS--VTADAKVLWDDENLYVYATVKDRVLNKDSGEAYQQDSLEVFIDE 796
Cdd:cd00005 1 VATAKYGTPVIDGEVDDVWAKAEEITTDKKVSGTdgATATARTLWDEDNLYVLAEVKDPVLNKASANPWEQDSVEIFVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 797 NNAKTESYDDDDKQYRINYVNEHSFNGKKcLEENVRSAAKETEDGYVIEAAFKWTDIQPKEGDRIGLEFQINDADASGAR 876
Cdd:cd00005 81 NNAKTSSYEDDDAQYRVNFDNEQSFGGGA-IAERFTSATKLTDGGYVVEAAIPLKTITPAAGTVIGFDLQVNDADDGGKR 159
|
170 180
....*....|....*....|....*
gi 1469754418 877 IGTLSWNDETGMGWSKSSVYGTIEL 901
Cdd:cd00005 160 IGVANWNDPTGNGYQDTSRFGVLLL 184
|
|
| XynA |
COG3693 |
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]; |
189-570 |
6.72e-74 |
|
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism];
Pssm-ID: 442908 Cd Length: 328 Bit Score: 246.73 E-value: 6.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 189 GTGIMLSEITDDTLMKLVEKHFNAVTFGNELKPDAlfnyklensvktktvqfdgqdlevpvVNDAGDSLDFSRADAMVDk 268
Cdd:COG3693 30 GTAVNAGQLDDPAYRELLAREFNSVTPENEMKWGS--------------------------IEPERGEFNFSAADAIVA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 269 ileWNAAHpdrKIRIRGHVLVWHSQTQEWFFHENydiskpyVDKETMNRRLEWYISSVFDHYfgeaangkyDGLFYGWDV 348
Cdd:COG3693 83 ---FAKAN---GMKVRGHTLVWHSQTPDWVFEDA-------LSKEELRARLEEHITTVVGRY---------KGKIYAWDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 349 VNEAV-IGNTYRtdtvspaeslneirhgnNSSWWHVYKsNEFIINAFKYANKYAPkNVELYYNDFG-ETDNIKSEGIIKL 426
Cdd:COG3693 141 VNEAIdDDGSLR-----------------NSPWYQALG-PDYIADAFRWAREADP-DAKLFYNDYNiEGGPAKRDAYLEL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 427 ISDVKsAEGTRLDAFGMQAHYSVDSFSAAQFKTVAKKYAEAAGKVQLTELDFQASAAYKSGAASkdseYTKMAYCHKQLF 506
Cdd:COG3693 202 VKDLK-ARGVPIDGVGLQGHLGLDYPSPEEIEAALDRFAALGLPIHITELDVRVLPLPDLTEED----DAAQADRYRDLF 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469754418 507 DAAKDLKkngtNVAGITVWGVIEPNSWLhsqsnvgggADGSKQCPLLFDGKYKAKPAYWAYVDA 570
Cdd:COG3693 277 DAFLSHP----AVTGVTFWGLTDGYSWR---------PGFRTGYPLLFDEDYQPKPAYDAVLDA 327
|
|
| Glyco_10 |
smart00633 |
Glycosyl hydrolase family 10; |
255-566 |
7.97e-68 |
|
Glycosyl hydrolase family 10;
Pssm-ID: 214750 Cd Length: 263 Bit Score: 227.89 E-value: 7.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 255 DSLDFSRADAMVDkileWNAAHpdrKIRIRGHVLVWHSQTQEWFFHENYDiskpyvDKETMNRRLEWYISSVFDHYfgea 334
Cdd:smart00633 11 GQFNFSGADAIVN----FAKEN---GIKVRGHTLVWHSQTPDWVFNLNIS------GKETLLARLENHIKTVVGRY---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 335 aNGKYdglfYGWDVVNEAVIGNTyrtdtvspaeslneIRHGNNSSWWHVYKsNEFIINAFKYANKYAPkNVELYYNDFG- 413
Cdd:smart00633 74 -KGKI----YAWDVVNEAIHDNG--------------SGLRRSSVWYQILG-EDYIEKAFRYAREADP-DAKLFYNDYNt 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 414 ETDNIKSEGIIKLISDVKsAEGTRLDAFGMQAHYSVDSFSAAQFKTVAKKYAEAAGKVQLTELDFqasaaykSGAASKDS 493
Cdd:smart00633 133 EEPNAKRQAIYELVKKLK-AKGVPIDGIGLQSHLSLGGPNIAEIRAALDRFASLGLEIWITELDI-------SGPPNPEE 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469754418 494 EYTKMAYCHKQLFDAAKDLKkngtNVAGITVWGVIEPNSWLhsqsnvgggadGSKQCPLLFDGKYKAKPAYWA 566
Cdd:smart00633 205 NLQAQAADYEEVFKACLAHP----AVTGVTVWGVTDGYSWL-----------DGFGAPLLFDANYQPKPAYWA 262
|
|
| Glyco_hydro_10 |
pfam00331 |
Glycosyl hydrolase family 10; |
189-569 |
1.95e-62 |
|
Glycosyl hydrolase family 10;
Pssm-ID: 425613 Cd Length: 310 Bit Score: 214.46 E-value: 1.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 189 GTGIMLSEITD-DTLMKLVEKHFNAVTFGNELKPDALFNYKlensvktktvqfdgqdlevpvvndagDSLDFSRADamvd 267
Cdd:pfam00331 13 GTAVSAGELLGnSQYTAILKAEFNQVTPENEMKWDALEPSR--------------------------GNFTFANAD---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 268 KILEWNAAHpdrKIRIRGHVLVWHSQTQEWFFHENYDiskpyvdKETMNRRLEWYISSVFDHYFGEaangkydglFYGWD 347
Cdd:pfam00331 63 RIVNFAKQN---GMAVRGHTLVWHSQLPDWVFNINGS-------KADLLQVLENHITTVVGHYKGK---------IYAWD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 348 VVNEAV---IGNTYRtdtvspaeslneirhgnNSSWWHVYkSNEFIINAFKYANKYAPkNVELYYNDFG-ETDNIKSEGI 423
Cdd:pfam00331 124 VVNEAFdddGSGGLR-----------------SSVWYQVL-GEDYIEIAFRAAREADP-DAKLYYNDYNiEEDGAKRDAV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 424 IKLISDVKSAeGTRLDAFGMQAHYSVDSFSAAQFKTVAKKYAEAAGKVQLTELDFQASAAYKSGAASkdseytKMAYCHK 503
Cdd:pfam00331 185 YNLVKDLKAK-GVPIDGIGFQSHLSAGGPSISNIRAALQRFAALGLEVAITELDIRGPDPSDEEALQ------AQAARYK 257
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469754418 504 QLFDAAKDLKkngtNVAGITVWGVIEPNSWLHSQSNVGggadgskqcPLLFDGKYKAKPAYWAYVD 569
Cdd:pfam00331 258 EVFKACLAVP----NCTGITVWGVTDKYSWLSGFFPGA---------PLLFDSNYQPKPAYNAVVD 310
|
|
| CBM9_1 |
pfam06452 |
Carbohydrate family 9 binding domain-like; CBM9_1 is a C-terminal domain on bacterial xylanase ... |
729-901 |
1.19e-53 |
|
Carbohydrate family 9 binding domain-like; CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallization reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.
Pssm-ID: 428950 Cd Length: 180 Bit Score: 184.86 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 729 IDGEADSEWDKAVAIPLTINLGASVTADA----KVLWDDENLYVYATVKDRVLNKDSGEAYQQDSLEVFIDENNAKTESY 804
Cdd:pfam06452 1 IDGTVDAVWSNAQSLTIFKLWTGTVSSDAsgtfKALWDDDNLYVLAEVTDDVLNDGSTNPWEDDSVEIFIDENNGKTTEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 805 DDDDKQYRINYVNEHSFN-GKKCLEENVRSAAKETEDGYVIEAAFKWTDIQ-PKEGDRIGLEFQINDADASGARIGTLSW 882
Cdd:pfam06452 81 GANDFQYRVNYNNETSFDpGNGLIAAGFTSASKVSDGGYIVEAKIPLKTITtPANNKVIGFDVQINDDDDGGTRQGKITW 160
|
170
....*....|....*....
gi 1469754418 883 NDETGMGWSKSSVYGTIEL 901
Cdd:pfam06452 161 NDPTGNAWQDPSVFGTVTL 179
|
|
| CBM86 |
cd20907 |
carbohydrate binding module family 86; This family describes what is most likely a ... |
29-156 |
1.03e-47 |
|
carbohydrate binding module family 86; This family describes what is most likely a xylan-binding module such as found in the Xyn10A protein of Roseburia intestinalis L1-82, which is involved in the extracellular capture and breakdown of xylan.
Pssm-ID: 411019 Cd Length: 127 Bit Score: 166.00 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 29 KKTTYTADQLEVDWGNASYERTDGVWKVTFNNQYDQVKWRLPETIDMSTVKSVTFNVKDQKGSVSLKVYKrEQTEADGAN 108
Cdd:cd20907 1 KTKEFTADKLTLAFGGAWYSSADGSGKLTFAKQYQEYKYDLPETLDMSQVKSVTFKVKDQKGNIALKLYD-TGGDMTEVN 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1469754418 109 TQYGLTGKEEYSISPTGEGDMEAVGLMTTDDTGSGSAISLVSVTVETD 156
Cdd:cd20907 80 ANYGLNGQDEYTINPNYDGKVRAIGIMAMGSNEYDAPVSITSVTVELD 127
|
|
| CBM9_like_4 |
cd09619 |
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) ... |
729-897 |
3.02e-24 |
|
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains.
Pssm-ID: 187677 Cd Length: 187 Bit Score: 100.97 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 729 IDGEADSEWDKAVAIPLTINLG--------ASVTADAKVLWDDENLYVYATVKDRVL--NKDSGEAYQQDSLEVFIDENN 798
Cdd:cd09619 4 IDGTLEAAWYPGSILPLEAKGLiddtgpsaTDLSATFAAMWDDTNLYVLVDVTDDTLrnDLDGKDHWRGDAVEIFIDPDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 799 AKTESYDDDDKQYRINY---VNEHSFNGKKCLEENVRSAAKETEDGYVIEAAFKWTDI--QPKEGDRIGLEFQINDADAS 873
Cdd:cd09619 84 NKLATYTANDFQLGFRPndeTGQPEGWNHTTPAPGIRVASTPRYGGYTVEAAIPWSTLgiTPAANLLLGFDVAINDDDTG 163
|
170 180
....*....|....*....|....
gi 1469754418 874 GARIGTLSWNDETGMGWSKSSVYG 897
Cdd:cd09619 164 GTRDQQIAWNAKDDQNWSNPSLFG 187
|
|
| DOMON_like |
cd00241 |
Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of ... |
748-877 |
4.20e-12 |
|
Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.
Pssm-ID: 187675 Cd Length: 158 Bit Score: 65.28 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 748 NLGASVTADAKVLWDDENLYVYATVKDRVLNKD--SGEAYQQDSLEVFIDENNAKTESYD----------DDDKQYRINY 815
Cdd:cd00241 13 GGPGDLSATVKLAWDGEYLYFLVEVTDDVLRDTaaLSLVWDGDGVELFFDPDNDGTDGNAfgygidlygfSVDLADGSGT 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469754418 816 VNEHSFNGKKcleENVRSAAKETEDGYVIEAAFKWTD---IQPKEGDRIGLEFQINDADASGARI 877
Cdd:cd00241 93 AADYGTEGGR---EGVSSSAKKGGGGYTVEFAIPLAAldgLDPGKGKGYGFAFAINDGSADDRRH 154
|
|
| CBM9_like_5 |
cd09621 |
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) ... |
755-901 |
3.43e-11 |
|
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.
Pssm-ID: 187679 Cd Length: 188 Bit Score: 63.11 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 755 ADAKVLWDDENLYVYATVKDRV--LNKDSGEAYQQDSLEVFID---ENNAKTESYD------DDDKQ--YRINYVNehSF 821
Cdd:cd09621 30 AKVWLGWDADNLYLAARVTDDRhsQPFTGADIWKGDSIQLALDlpgQKGGADGFWElglartDDGGAlvWRWNAPA--GF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 822 NGKKCL----EENVRSAAKETedgyVIEAAFKWTDI---QPKEGDRIGLEFQINDADASGaRIGTLSWNDETGMGWSkSS 894
Cdd:cd09621 108 DPAAAAaairLETSRDEAKVT----VYEAAIPWAELgltGPAAGDGFRFNLLVNDNDGGG-REGWIEWAPGIGESKD-PA 181
|
....*..
gi 1469754418 895 VYGTIEL 901
Cdd:cd09621 182 LFPLVTL 188
|
|
| CBM9_like_3 |
cd09620 |
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) ... |
729-868 |
2.40e-08 |
|
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains.
Pssm-ID: 187678 Cd Length: 200 Bit Score: 55.08 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 729 IDGEAD-SEWDKAVAIPLTINLGASVTAD----AKVLWDDENLYVYATVKDR----VLNKDSGEAYQQDSLEVFIDenna 799
Cdd:cd09620 1 IDGKLDePAWQAAPWVELFVDIGGGPPPKpqtrVRLLYDDEYLYLAFEVEDDdiwaTYTERDDPVWEDDVVEVFID---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 800 ktesYDDDDKQY----------------RINYVNEHSFNGKKCLEENVRSAA--------KETEDGYVIEAAFKWTDIQP 855
Cdd:cd09620 77 ----PDGDGPNYyefevnplgtvldafiRRPRDGGGDRDNRQPDSAGLESAVsidgtlndSDGDKGWTVELAIPFAALAK 152
|
170
....*....|....*
gi 1469754418 856 KEGDR--IGLEFQIN 868
Cdd:cd09620 153 AAGGPplPGDVWRAN 167
|
|
| CBM9_like_2 |
cd09618 |
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) ... |
723-883 |
6.84e-05 |
|
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized subfamily are typically found at the N-terminus of longer proteins that lack additional annotation with domain footprints.
Pssm-ID: 187676 Cd Length: 186 Bit Score: 44.55 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 723 TKATVKIDGEADSE-WDKAVAIPLTI----NLG--ASVTADAKVLWDDENLYVYATVKDRVLNK---------DSGEayQ 786
Cdd:cd09618 7 ISGPPVIDGVLDEAvWQQAPVATDFVqrepNDGgpAPERTEVRVLYDDEALYVAAVCYDPEPDKiraqllrrdDDGE--N 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469754418 787 QDSLEVFIDENNAKTESYD---------DDDKQYRINYVNEhSFNGKkcleenVRSAAKETEDGYVIEAAFKWTDI--QP 855
Cdd:cd09618 85 DDRFGVALDTFNDRRNAYQfgvnpagvqRDALEFDGNNEDF-SWDAV------WESATKITDDGWTAEMAIPFSSLrfPK 157
|
170 180
....*....|....*....|....*...
gi 1469754418 856 KEGDRIGLEFQINDADasgaRIGTLSWN 883
Cdd:cd09618 158 GSVQTWGINFYRNIPR----TNERSSWP 181
|
|
| |
