|
Name |
Accession |
Description |
Interval |
E-value |
| COG3397 |
COG3397 |
Predicted carbohydrate-binding protein, contains CBM5 and CBM33 domains [General function ... |
29-311 |
3.27e-98 |
|
Predicted carbohydrate-binding protein, contains CBM5 and CBM33 domains [General function prediction only];
Pssm-ID: 442624 [Multi-domain] Cd Length: 294 Bit Score: 293.15 E-value: 3.27e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 29 VPALGLVLTTGEKAEAHGTPMKPASRTFLCWQDGLTATGeikPVNPACKSAAQQsGTTPFYNWFSVLRSDGAGRTRGFVP 108
Cdd:COG3397 13 LAALLALLLAAGPASAHGYVESPASRAYLCYLDGGEDAA---PQNPACWAAVAA-GPQAQYEWQSVLREGPKGFPQAGIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 109 DGELCSGGNTNFTGFNKPSADWPVTHLTEGATIDFSYNAWAAHPGW-FYVYVTKDGYDPTKALTWADMEASPFLSIDHPA 187
Cdd:COG3397 89 DGQLCSAGRARFSGLDLQRGDWPKTPVTAGANFTFTWTATAPHATTyWRYYITKQGWDPTQPLTWSDLELVPFCTVTDPG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 188 LNGSpgtveADYRWTGALPEGKDGRHVIYMVWQRSDSQETFYSCSDVVFDGGNGEVTGVKDGSGSTPTEPPPGACTATRT 267
Cdd:COG3397 169 ARPG-----GTYTHTVNLPAGRSGRHVIYAVWQRSDTAEAFYNCSDVNFGGGGGTPPWTAAGTSVEITTPPTPPPPSTPA 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 503919370 268 TT-----GSWNGGYQSEVKVTNSGTVPMLGWMVEWTQPTGQSVASLWSG 311
Cdd:COG3397 244 TTptpstTTTGSGGATTVATSTTAGGAVTTTTTVVNTGAGATGGEAATT 292
|
|
| LPMO_10 |
pfam03067 |
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with ... |
45-234 |
9.12e-79 |
|
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with a wide variety of cellulose binding domains. This is a family of two very closely related proteins that together act as both a C1- and a C4-oxidising lytic polysaccharide mono-oxygenase, degrading cellulose. This domain is also found in baculoviral spheroidins and spindolins, protein of unknown function.
Pssm-ID: 460793 [Multi-domain] Cd Length: 184 Bit Score: 239.21 E-value: 9.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 45 HGTPMKPASRTFLCWQDGltaTGEIKPVNPACKSAAQQSGTTPFYNWFSVLRSDGaGRTRGFVPDGELCSGGNTNFTGFN 124
Cdd:pfam03067 1 HGYVTSPPSRQYLCREGP---EGGEAPNNPACRAAVAAGGTQAQYEWNSVEGPKG-GRHQAGIPDGGLCSAGDPNFSGLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 125 KPSADWPVTHLTEGATIDFSYNAWAAH-PGWFYVYVTKDGYDPTKALTWADMEASPFLSIDHPalnGSPGTVEADYRWTG 203
Cdd:pfam03067 77 LPRTDWPKTTYTAGQTITFTWTLTAPHkTGYFEFYITKPGWDPTKPLTWSDLELGPFATVTDP---GQQPPAGGAYYITV 153
|
170 180 190
....*....|....*....|....*....|.
gi 503919370 204 ALPEGKDGRHVIYMVWQRSDSQETFYSCSDV 234
Cdd:pfam03067 154 TLPSGRSGRHVILQVWQRSDTGEAFYNCSDV 184
|
|
| LPMO_AA10 |
cd21177 |
lytic polysaccharide monooxygenase (LPMO) auxiliary activity family 10 (AA10); AA10 proteins ... |
45-235 |
1.09e-59 |
|
lytic polysaccharide monooxygenase (LPMO) auxiliary activity family 10 (AA10); AA10 proteins are copper-dependent lytic polysaccharide monooxygenases (LPMOs), which may act on chitin or cellulose. The family used to be called CBM33. Activities in this family include lytic cellulose monooxygenase (C1-hydroxylating) (EC 1.14.99.54), lytic cellulose monooxygenase (C4-dehydrogenating) (EC 1.14.99.56), lytic chitin monooxygenase (EC 1.14.99.53), and lytic xylan monooxygenase/xylan oxidase (glycosidic bond-cleaving) (EC 1.14.99.-). Also included are viral chitin-binding glycoproteins such as fusolin and spheroidin-like proteins.
Pssm-ID: 410624 [Multi-domain] Cd Length: 180 Bit Score: 190.21 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 45 HGTPMKPASRTFLCWQDGLTAtgeikPVNPACKSAAQQSGTTPFYNWFSVlRSDGAGRTRGFVPDGELCSGGNTNFTGFN 124
Cdd:cd21177 1 HGYVSSPPSRAYLCALGGGEG-----PPNPACGAAQYEPQSVEGPDWNGV-DYNDDGFPVAGPPDGKLCSAGNGRFAGLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 125 KPSADWPVTHLTEGATIDFSYNAWAAH-PGWFYVYVTKDGYDPTKaLTWADMEASPFLSIDHPALNGSPGTveadYRWTG 203
Cdd:cd21177 75 EQSGDWPKTPVKPGGTFTFTWTATAPHkTSYWRYYITKPGWDPNQ-LTLAWFDLEPFCTVDGPGGQLPGGT----YTHTV 149
|
170 180 190
....*....|....*....|....*....|..
gi 503919370 204 ALPEgKDGRHVIYMVWQRSDSQETFYSCSDVV 235
Cdd:cd21177 150 TLPA-RSGYHVIYAVWQRADTGEAFYNCSDVD 180
|
|
| CBD_II |
smart00637 |
CBD_II domain; |
269-347 |
3.21e-18 |
|
CBD_II domain;
Pssm-ID: 214754 [Multi-domain] Cd Length: 92 Bit Score: 78.60 E-value: 3.21e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503919370 269 TGSWNGGYQSEVKVTNSGTVPMLGWMVEWTQPTGQSVASLWSGDMTTQGQEVMVHNAGWNGSLDPGESTTFGYVSQGGA 347
Cdd:smart00637 1 TSDWGSGFTANVTVTNTGSSAINGWTLTFDLPGGQTVTNSWNATVSQSGGHVTATNASWNGTIAPGGSVSFGFQGKTGS 79
|
|
| PRK13211 |
PRK13211 |
N-acetylglucosamine-binding protein GbpA; |
42-255 |
5.78e-17 |
|
N-acetylglucosamine-binding protein GbpA;
Pssm-ID: 237309 [Multi-domain] Cd Length: 478 Bit Score: 81.59 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 42 AEAHGTPMKPASRTFLCwqdglTATGEIKPVNpaCkSAAQqsgttpfYNWFSVLRSDGAgrTRGFVPDGELCSGGNTNFT 121
Cdd:PRK13211 21 ALAHGYVSSPESRAYLC-----KLGAGEKNTN--C-GAVQ-------YEPQSVEGPSGF--PESGPPDGKIASAGNAQFS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 122 GFNKPSAD-WPVTHLTEGATiDFSYNAWAAHP--GWFYvYVTKDGYDPTKALTWADMEASPFLSID-HPALNGSPGTVEA 197
Cdd:PRK13211 84 PLDEQTADrWVKRPIKAGPN-TFEWTFTANHVtrNWRY-YITKQDWNPNQPLTRDSFDLTPFCVVDgGMVQPPKRVSHEC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503919370 198 DyrwtgaLPEgKDGRHVIYMVWQRSDSQETFYSCSDVVFDGGNGEVTGVKDGSGSTPT 255
Cdd:PRK13211 162 N------VPE-RTGYQVILAVWEVGDTANSFYNVIDVNFDGGGGVVPEWSKVGQINPS 212
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG3397 |
COG3397 |
Predicted carbohydrate-binding protein, contains CBM5 and CBM33 domains [General function ... |
29-311 |
3.27e-98 |
|
Predicted carbohydrate-binding protein, contains CBM5 and CBM33 domains [General function prediction only];
Pssm-ID: 442624 [Multi-domain] Cd Length: 294 Bit Score: 293.15 E-value: 3.27e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 29 VPALGLVLTTGEKAEAHGTPMKPASRTFLCWQDGLTATGeikPVNPACKSAAQQsGTTPFYNWFSVLRSDGAGRTRGFVP 108
Cdd:COG3397 13 LAALLALLLAAGPASAHGYVESPASRAYLCYLDGGEDAA---PQNPACWAAVAA-GPQAQYEWQSVLREGPKGFPQAGIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 109 DGELCSGGNTNFTGFNKPSADWPVTHLTEGATIDFSYNAWAAHPGW-FYVYVTKDGYDPTKALTWADMEASPFLSIDHPA 187
Cdd:COG3397 89 DGQLCSAGRARFSGLDLQRGDWPKTPVTAGANFTFTWTATAPHATTyWRYYITKQGWDPTQPLTWSDLELVPFCTVTDPG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 188 LNGSpgtveADYRWTGALPEGKDGRHVIYMVWQRSDSQETFYSCSDVVFDGGNGEVTGVKDGSGSTPTEPPPGACTATRT 267
Cdd:COG3397 169 ARPG-----GTYTHTVNLPAGRSGRHVIYAVWQRSDTAEAFYNCSDVNFGGGGGTPPWTAAGTSVEITTPPTPPPPSTPA 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 503919370 268 TT-----GSWNGGYQSEVKVTNSGTVPMLGWMVEWTQPTGQSVASLWSG 311
Cdd:COG3397 244 TTptpstTTTGSGGATTVATSTTAGGAVTTTTTVVNTGAGATGGEAATT 292
|
|
| LPMO_10 |
pfam03067 |
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with ... |
45-234 |
9.12e-79 |
|
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with a wide variety of cellulose binding domains. This is a family of two very closely related proteins that together act as both a C1- and a C4-oxidising lytic polysaccharide mono-oxygenase, degrading cellulose. This domain is also found in baculoviral spheroidins and spindolins, protein of unknown function.
Pssm-ID: 460793 [Multi-domain] Cd Length: 184 Bit Score: 239.21 E-value: 9.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 45 HGTPMKPASRTFLCWQDGltaTGEIKPVNPACKSAAQQSGTTPFYNWFSVLRSDGaGRTRGFVPDGELCSGGNTNFTGFN 124
Cdd:pfam03067 1 HGYVTSPPSRQYLCREGP---EGGEAPNNPACRAAVAAGGTQAQYEWNSVEGPKG-GRHQAGIPDGGLCSAGDPNFSGLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 125 KPSADWPVTHLTEGATIDFSYNAWAAH-PGWFYVYVTKDGYDPTKALTWADMEASPFLSIDHPalnGSPGTVEADYRWTG 203
Cdd:pfam03067 77 LPRTDWPKTTYTAGQTITFTWTLTAPHkTGYFEFYITKPGWDPTKPLTWSDLELGPFATVTDP---GQQPPAGGAYYITV 153
|
170 180 190
....*....|....*....|....*....|.
gi 503919370 204 ALPEGKDGRHVIYMVWQRSDSQETFYSCSDV 234
Cdd:pfam03067 154 TLPSGRSGRHVILQVWQRSDTGEAFYNCSDV 184
|
|
| LPMO_AA10 |
cd21177 |
lytic polysaccharide monooxygenase (LPMO) auxiliary activity family 10 (AA10); AA10 proteins ... |
45-235 |
1.09e-59 |
|
lytic polysaccharide monooxygenase (LPMO) auxiliary activity family 10 (AA10); AA10 proteins are copper-dependent lytic polysaccharide monooxygenases (LPMOs), which may act on chitin or cellulose. The family used to be called CBM33. Activities in this family include lytic cellulose monooxygenase (C1-hydroxylating) (EC 1.14.99.54), lytic cellulose monooxygenase (C4-dehydrogenating) (EC 1.14.99.56), lytic chitin monooxygenase (EC 1.14.99.53), and lytic xylan monooxygenase/xylan oxidase (glycosidic bond-cleaving) (EC 1.14.99.-). Also included are viral chitin-binding glycoproteins such as fusolin and spheroidin-like proteins.
Pssm-ID: 410624 [Multi-domain] Cd Length: 180 Bit Score: 190.21 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 45 HGTPMKPASRTFLCWQDGLTAtgeikPVNPACKSAAQQSGTTPFYNWFSVlRSDGAGRTRGFVPDGELCSGGNTNFTGFN 124
Cdd:cd21177 1 HGYVSSPPSRAYLCALGGGEG-----PPNPACGAAQYEPQSVEGPDWNGV-DYNDDGFPVAGPPDGKLCSAGNGRFAGLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 125 KPSADWPVTHLTEGATIDFSYNAWAAH-PGWFYVYVTKDGYDPTKaLTWADMEASPFLSIDHPALNGSPGTveadYRWTG 203
Cdd:cd21177 75 EQSGDWPKTPVKPGGTFTFTWTATAPHkTSYWRYYITKPGWDPNQ-LTLAWFDLEPFCTVDGPGGQLPGGT----YTHTV 149
|
170 180 190
....*....|....*....|....*....|..
gi 503919370 204 ALPEgKDGRHVIYMVWQRSDSQETFYSCSDVV 235
Cdd:cd21177 150 TLPA-RSGYHVIYAVWQRADTGEAFYNCSDVD 180
|
|
| CBM_2 |
pfam00553 |
Cellulose binding domain; Two tryptophan residues are involved in cellulose binding. Cellulose ... |
262-351 |
2.84e-22 |
|
Cellulose binding domain; Two tryptophan residues are involved in cellulose binding. Cellulose binding domain found in bacteria.
Pssm-ID: 425748 [Multi-domain] Cd Length: 101 Bit Score: 89.81 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 262 CTATRTTTGSWNGGYQSEVKVTNSGTVPMLGWMVEWTQPTGQSVASLWSGDMTTQGQEVMVHNAGWNGSLDPGESTTFGY 341
Cdd:pfam00553 1 CTATYAVTNQWGTGFTANVTITNTGSSPINGWTVSWTYPAGQRVTQSWNATVSQSGNPVTATNVSWNGTIAPGGSASFGF 80
|
90
....*....|
gi 503919370 342 VSQGGAPDSA 351
Cdd:pfam00553 81 QGSGTGSNSA 90
|
|
| CBD_II |
smart00637 |
CBD_II domain; |
269-347 |
3.21e-18 |
|
CBD_II domain;
Pssm-ID: 214754 [Multi-domain] Cd Length: 92 Bit Score: 78.60 E-value: 3.21e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503919370 269 TGSWNGGYQSEVKVTNSGTVPMLGWMVEWTQPTGQSVASLWSGDMTTQGQEVMVHNAGWNGSLDPGESTTFGYVSQGGA 347
Cdd:smart00637 1 TSDWGSGFTANVTVTNTGSSAINGWTLTFDLPGGQTVTNSWNATVSQSGGHVTATNASWNGTIAPGGSVSFGFQGKTGS 79
|
|
| PRK13211 |
PRK13211 |
N-acetylglucosamine-binding protein GbpA; |
42-255 |
5.78e-17 |
|
N-acetylglucosamine-binding protein GbpA;
Pssm-ID: 237309 [Multi-domain] Cd Length: 478 Bit Score: 81.59 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 42 AEAHGTPMKPASRTFLCwqdglTATGEIKPVNpaCkSAAQqsgttpfYNWFSVLRSDGAgrTRGFVPDGELCSGGNTNFT 121
Cdd:PRK13211 21 ALAHGYVSSPESRAYLC-----KLGAGEKNTN--C-GAVQ-------YEPQSVEGPSGF--PESGPPDGKIASAGNAQFS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 122 GFNKPSAD-WPVTHLTEGATiDFSYNAWAAHP--GWFYvYVTKDGYDPTKALTWADMEASPFLSID-HPALNGSPGTVEA 197
Cdd:PRK13211 84 PLDEQTADrWVKRPIKAGPN-TFEWTFTANHVtrNWRY-YITKQDWNPNQPLTRDSFDLTPFCVVDgGMVQPPKRVSHEC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503919370 198 DyrwtgaLPEgKDGRHVIYMVWQRSDSQETFYSCSDVVFDGGNGEVTGVKDGSGSTPT 255
Cdd:PRK13211 162 N------VPE-RTGYQVILAVWEVGDTANSFYNVIDVNFDGGGGVVPEWSKVGQINPS 212
|
|
| CelA1 |
COG5297 |
Cellulase/cellobiase CelA1 [Carbohydrate transport and metabolism]; |
98-341 |
1.08e-16 |
|
Cellulase/cellobiase CelA1 [Carbohydrate transport and metabolism];
Pssm-ID: 444099 [Multi-domain] Cd Length: 301 Bit Score: 79.48 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 98 DGAGRTRGFVPDGELCSGGNTNFTGFNKPSADWPVTHLTEGATIDFSYNAWAAHPGWFYVYVTKDGYDPTKALTWADMEA 177
Cdd:COG5297 38 AASASGSASGSSASGAGAGAGAAASGADTGSGGGAGAGAGVGVGAGGAAGGAGGSAGVAGAASAAGAAGAAATSSGATSS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 178 SPFLSIDHPALNGSPGTVEADYRWTGALPEGKDGrhVIYMVWQRSDSQETFYSCSDVVFDGGNGEVTGVKDGSGSTPTEP 257
Cdd:COG5297 118 SSSGTSSGGGGGSSSSTSDTTTSSATSGSSTSTS--SPTTGSTSTTTGGGIANQPTAVWDRIAAITATVRAHLDAALAAP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 258 PPGA-CTATRTTTGSWNGGYQSEVKVTNSGTVPMLGWMVEWTQPTGQSVASLWSGDMTTQGQEVMVHNAGWNGSLDPGES 336
Cdd:COG5297 196 LPGRdCGVTYSVYSDWGSGYTAAVTVTNPGSLPLNGWTLAWDLPGGAGVTNAWGFTLNQSGYTVTATNVSWNGTLAPGGS 275
|
....*
gi 503919370 337 TTFGY 341
Cdd:COG5297 276 VSFGF 280
|
|
| gp37 |
PHA03387 |
spherodin-like protein; Provisional |
44-237 |
4.19e-16 |
|
spherodin-like protein; Provisional
Pssm-ID: 177623 Cd Length: 267 Bit Score: 77.36 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 44 AHGTPMKPASRTFLCWQDG---LTATGEIKPvNPACKSAAQqsgtTPFYNWFSVLRSDGAGRT----------------- 103
Cdd:PHA03387 19 SHGYLSYPAARQYKCFRDGnfwWPDNGDNIP-DPACRNAYK----TVYAKYRSAGESSGVAANaaqymfqqyyeyaalag 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 104 ----------RGFVPDgELCSGGNTN----F---TGFNKPSADWPVTHLT-----EGATIDFSYNAWAAH-PGWFYVYVT 160
Cdd:PHA03387 94 pnyddfehikRNVVPH-TLCAAGANDrsavFgdkSGMDEPFPNWRPDTLYknkyqSGHQTNLHFCPTAVHePSYFEVFVT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 161 KDGYDPTKALTWADMEaspFLSIDHPALNGSPGTVEAD-----YRWTGALPEgKDGRHVIYMVWQRSDSQ-ETFYSCSDV 234
Cdd:PHA03387 173 KPEYDYRNELTWNDLE---LIGGNGSQLVPNDGSDELCassqvYSIPVRVPF-RSGKFVLYVRWQRIDVVgEGFYNCADV 248
|
...
gi 503919370 235 VFD 237
Cdd:PHA03387 249 VFD 251
|
|
| Fusolin-like |
cd21178 |
fusolin and similar proteins; Fusolin is a protein found in spindles of insect poxviruses that ... |
45-236 |
1.67e-14 |
|
fusolin and similar proteins; Fusolin is a protein found in spindles of insect poxviruses that resembles the lytic polysaccharide monooxygenases of chitinovorous bacteria and may function to disrupt the chitin-rich peritrophic matrix that protects insects against oral infections. Thus, it is a component of the virus occlusion bodies (which are large proteinaceous polyhedra) that protect the virus from the outside environment for extended periods until they are ingested by insect larvae.
Pssm-ID: 410625 Cd Length: 227 Bit Score: 71.98 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 45 HGTPMKPASRTFLCWQDG---LTATGEIKPvNPACKSAAQqsgtTPFYNWFSVLRSDGAGR------------------- 102
Cdd:cd21178 1 HGYLSYPLARQRRCYVDGdfwWPDDGDGIP-DPACRAAYQ----HVYNKYLSNGGSEGQAAaaaqymfqqyaeyaalagp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 103 --------TRGFVPDgELCSGGNTN----F---TGFNKPSADWPVTHLTEGATIDFSYNAWAAH-PGWFYVYVTKDGYDP 166
Cdd:cd21178 76 nyedlehiRNNVVPH-YLCAAGATDrsrpFgdkSGMDVPSGSWRPTTIPLRVPIELYFCPTAIHePSYFEVYITKPEFDV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503919370 167 TK-ALTWADMEA-----SPFLSIDHPALNGSPGTVeadYRWTGALPEgKDGRHVIYMVWQRSD-SQETFYSCSDVVF 236
Cdd:cd21178 155 GKdKVTWSDLELiysntSNLVPNNPDDECCDNSLV---YRIPVPIPY-RSNQFVLYVRWQREDpVGEGFYNCADVVF 227
|
|
| CBM49 |
pfam09478 |
Carbohydrate binding domain CBM49; This domain is found at the C terminal of cellulases and in ... |
265-344 |
3.56e-04 |
|
Carbohydrate binding domain CBM49; This domain is found at the C terminal of cellulases and in vitro binding studies have shown it to binds to crystalline cellulose.
Pssm-ID: 286553 Cd Length: 80 Bit Score: 38.84 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 265 TRTTTGSWNGG----YQSEVKVTNSGTVPMLGW---MVEWTQPtgqsvasLWSgdmTTQGQEVMVHNAGWNGSLDPGEST 337
Cdd:pfam09478 4 SQTITSSWIDNgvtyYQYSVTITNNGSKTIKSLtisIDNLYGP-------IWG---VEKVSGNTYSFPSWLPSLPPGASF 73
|
....*..
gi 503919370 338 TFGYVSQ 344
Cdd:pfam09478 74 SFGYIQQ 80
|
|
| CBM49 |
smart01063 |
Carbohydrate binding domain CBM49; This domain is found at the C terminal of cellulases and in ... |
267-346 |
5.03e-03 |
|
Carbohydrate binding domain CBM49; This domain is found at the C terminal of cellulases and in vitro binding studies have shown it to binds to crystalline cellulose.
Pssm-ID: 215005 [Multi-domain] Cd Length: 84 Bit Score: 35.71 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919370 267 TTTGSWNGG----YQSEVKVTNSGTVPMLGWMVEwTQPTGQSVASLWSGDMTTQGQevmVHNAGWNGSLDPGESTTFGYV 342
Cdd:smart01063 5 TITSSWVDNnvtyTQYDVTITNNGNKPIKSITIG-TDNNLRDSGSIWNVERLSNGS---LTLPSYQNSIAPGSSYTFGYI 80
|
....
gi 503919370 343 SQGG 346
Cdd:smart01063 81 IKGS 84
|
|
| |
