|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_hydro_10 |
pfam00331 |
Glycosyl hydrolase family 10; |
525-855 |
1.24e-116 |
|
Glycosyl hydrolase family 10;
:
Pssm-ID: 425613 Cd Length: 310 Bit Score: 368.54 E-value: 1.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 525 LKDVYKNDF-LIGNAISAEDLEG--TRLELLKMHHDVVTAGNAMKPDALQPTKGNFTFTAADAMIDKVLAEGMKMHGHVL 601
Cdd:pfam00331 1 LKDAAKAKGkYFGTAVSAGELLGnsQYTAILKAEFNQVTPENEMKWDALEPSRGNFTFANADRIVNFAKQNGMAVRGHTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 602 VWHQQSPAWLNTKKDDNNNtvplgrdeALDNLRTHIQTVMKHFGNKVISWDVVNEAMNDNPSNpadykaSLRQTPWYQAI 681
Cdd:pfam00331 81 VWHSQLPDWVFNINGSKAD--------LLQVLENHITTVVGHYKGKIYAWDVVNEAFDDDGSG------GLRSSVWYQVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 682 GSDYVEQAFLAAREVLDenpswNIKLYYNDYNEDNQN-KATAIYNMVKDINDRYaaahngkLLIDGVGMQGHYNINTN-P 759
Cdd:pfam00331 147 GEDYIEIAFRAAREADP-----DAKLYYNDYNIEEDGaKRDAVYNLVKDLKAKG-------VPIDGIGFQSHLSAGGPsI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 760 DNVKLSLEKFISLGVEVSVSELDVTAGNNYTLPENLAvgQAYLYAQLFKLYKEHADhIARVTFWGMDDNTSWRAE---NN 836
Cdd:pfam00331 215 SNIRAALQRFAALGLEVAITELDIRGPDPSDEEALQA--QAARYKEVFKACLAVPN-CTGITVWGVTDKYSWLSGffpGA 291
|
330
....*....|....*....
gi 62990090 837 PLLFDKNLQAKPAYYGVID 855
Cdd:pfam00331 292 PLLFDSNYQPKPAYNAVVD 310
|
|
| CBM9_like_1 |
cd00005 |
DOMON-like type 9 carbohydrate binding module of xylanases; Family 9 carbohydrate-binding ... |
873-1054 |
2.05e-92 |
|
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: 296.45 E-value: 2.05e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 873 AEAQYGTPVIDGTVDSIWSNAQAMPVNRYQMAWQGATGTAKALWDDQNLYVLIQVSDSQLNKANENAWEQDSVEVFLDQN 952
Cdd:cd00005 2 ATAKYGTPVIDGEVDDVWAKAEEITTDKKVSGTDGATATARTLWDEDNLYVLAEVKDPVLNKASANPWEQDSVEIFVDEN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 953 NGKTTFYQNDDGQYRVNFDNETSFSPASIAAGFESQTKKTANSYTVELKIPLTAVTPANQKKLGFDVQINDATDG-ARTS 1031
Cdd:cd00005 82 NAKTSSYEDDDAQYRVNFDNEQSFGGGAIAERFTSATKLTDGGYVVEAAIPLKTITPAAGTVIGFDLQVNDADDGgKRIG 161
|
170 180
....*....|....*....|...
gi 62990090 1032 VAAWNDTTGNGYQDTSVYGELTL 1054
Cdd:cd00005 162 VANWNDPTGNGYQDTSRFGVLLL 184
|
|
| CBM_4_9 |
pfam02018 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
361-498 |
9.04e-15 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
:
Pssm-ID: 396553 Cd Length: 134 Bit Score: 72.48 E-value: 9.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 361 TFEDQTAGGFTGRaGTETLTVTNESNHtaDGSYSLKVEGRTTSWHGPSLRVEKYVDKGYEYKVTAWVKLLSPETsTKLEL 440
Cdd:pfam02018 8 TFEDGGLDGWKAR-GGSGKATVDVTSY--NGTYSLKVSGRTATWDGQIIDITIRLEKGTTYTVSFWVKASSGPP-QTVSV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 62990090 441 ASQvGDGGSANYPTPTTQAWQARrlpaaDGWVQLQGNYRYNSvGGEYLTIYVQSSNAT 498
Cdd:pfam02018 84 TLQ-ITDASGNYDTVADEKVVLT-----GEWTKLEGTFTIPK-TASTVELYVELPDST 134
|
|
| SLH |
pfam00395 |
S-layer homology domain; |
1288-1329 |
2.47e-08 |
|
S-layer homology domain;
:
Pssm-ID: 459798 [Multi-domain] Cd Length: 42 Bit Score: 51.05 E-value: 2.47e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 62990090 1288 FGDLAKVPWAKEAIDAMASRGVIKGTGENTFSPAASIKRADF 1329
Cdd:pfam00395 1 FKDVKSVAAWAEAVAALAELGIISGYPDGTFRPNEPITRAEA 42
|
|
| SLH |
pfam00395 |
S-layer homology domain; |
1350-1391 |
4.28e-07 |
|
S-layer homology domain;
:
Pssm-ID: 459798 [Multi-domain] Cd Length: 42 Bit Score: 47.59 E-value: 4.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 62990090 1350 FSDVPANAYYYNELAVAKQLGIATGFEDNTFKPDSSISRQDM 1391
Cdd:pfam00395 1 FKDVKSVAAWAEAVAALAELGIISGYPDGTFRPNEPITRAEA 42
|
|
| CBM_4_9 super family |
cl19911 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
53-165 |
6.86e-07 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
The actual alignment was detected with superfamily member pfam02018:
Pssm-ID: 418717 Cd Length: 134 Bit Score: 50.14 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 53 GGASLTQVTGKVFDGNNdgsALYVSNRANTWDAAdFKFADIGLQNGKTYTVTVKGYVDQDATVPSGAQAFLQAVDSNNYG 132
Cdd:pfam02018 21 GGSGKATVDVTSYNGTY---SLKVSGRTATWDGQ-IIDITIRLEKGTTYTVSFWVKASSGPPQTVSVTLQITDASGNYDT 96
|
90 100 110
....*....|....*....|....*....|....
gi 62990090 133 FLASANFAAGTAFTLTKEFTVDTSVST-QLRVQS 165
Cdd:pfam02018 97 VADEKVVLTGEWTKLEGTFTIPKTASTvELYVEL 130
|
|
| CBM_4_9 super family |
cl19911 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
208-320 |
1.68e-06 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
The actual alignment was detected with superfamily member pfam02018:
Pssm-ID: 418717 Cd Length: 134 Bit Score: 48.98 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 208 GGANLAQVADKVFDGNddgKALYVSNRANTWDAAdFKFADIGLQNGKTYTVTVKGYVDQDATVPSGAQAFLQAVDSNNYG 287
Cdd:pfam02018 21 GGSGKATVDVTSYNGT---YSLKVSGRTATWDGQ-IIDITIRLEKGTTYTVSFWVKASSGPPQTVSVTLQITDASGNYDT 96
|
90 100 110
....*....|....*....|....*....|....
gi 62990090 288 FLASANFAARSAFTLTKEFTVDTSVTT-QLRVQS 320
Cdd:pfam02018 97 VADEKVVLTGEWTKLEGTFTIPKTASTvELYVEL 130
|
|
| SLH |
pfam00395 |
S-layer homology domain; |
1415-1456 |
1.10e-05 |
|
S-layer homology domain;
:
Pssm-ID: 459798 [Multi-domain] Cd Length: 42 Bit Score: 43.73 E-value: 1.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 62990090 1415 FSDAASVAGYAqDSVAALVKAGVVQGSGSK-LAPNDQLTRAEA 1456
Cdd:pfam00395 1 FKDVKSVAAWA-EAVAALAELGIISGYPDGtFRPNEPITRAEA 42
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_hydro_10 |
pfam00331 |
Glycosyl hydrolase family 10; |
525-855 |
1.24e-116 |
|
Glycosyl hydrolase family 10;
Pssm-ID: 425613 Cd Length: 310 Bit Score: 368.54 E-value: 1.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 525 LKDVYKNDF-LIGNAISAEDLEG--TRLELLKMHHDVVTAGNAMKPDALQPTKGNFTFTAADAMIDKVLAEGMKMHGHVL 601
Cdd:pfam00331 1 LKDAAKAKGkYFGTAVSAGELLGnsQYTAILKAEFNQVTPENEMKWDALEPSRGNFTFANADRIVNFAKQNGMAVRGHTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 602 VWHQQSPAWLNTKKDDNNNtvplgrdeALDNLRTHIQTVMKHFGNKVISWDVVNEAMNDNPSNpadykaSLRQTPWYQAI 681
Cdd:pfam00331 81 VWHSQLPDWVFNINGSKAD--------LLQVLENHITTVVGHYKGKIYAWDVVNEAFDDDGSG------GLRSSVWYQVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 682 GSDYVEQAFLAAREVLDenpswNIKLYYNDYNEDNQN-KATAIYNMVKDINDRYaaahngkLLIDGVGMQGHYNINTN-P 759
Cdd:pfam00331 147 GEDYIEIAFRAAREADP-----DAKLYYNDYNIEEDGaKRDAVYNLVKDLKAKG-------VPIDGIGFQSHLSAGGPsI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 760 DNVKLSLEKFISLGVEVSVSELDVTAGNNYTLPENLAvgQAYLYAQLFKLYKEHADhIARVTFWGMDDNTSWRAE---NN 836
Cdd:pfam00331 215 SNIRAALQRFAALGLEVAITELDIRGPDPSDEEALQA--QAARYKEVFKACLAVPN-CTGITVWGVTDKYSWLSGffpGA 291
|
330
....*....|....*....
gi 62990090 837 PLLFDKNLQAKPAYYGVID 855
Cdd:pfam00331 292 PLLFDSNYQPKPAYNAVVD 310
|
|
| XynA |
COG3693 |
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]; |
505-855 |
2.32e-116 |
|
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism];
Pssm-ID: 442908 Cd Length: 328 Bit Score: 368.45 E-value: 2.32e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 505 DISFESTGSGPvgiQKDLAPLKDVYKN-DFLIGNAISAEDL-EGTRLELLKMHHDVVTAGNAMKPDALQPTKGNFTFTAA 582
Cdd:COG3693 1 ALALAALDAAA---APGAASLKDLAADkGFLFGTAVNAGQLdDPAYRELLAREFNSVTPENEMKWGSIEPERGEFNFSAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 583 DAMIDKVLAEGMKMHGHVLVWHQQSPAWLNTKKddnnntvpLGRDEALDNLRTHIQTVMKHFGNKVISWDVVNEAMNDNP 662
Cdd:COG3693 78 DAIVAFAKANGMKVRGHTLVWHSQTPDWVFEDA--------LSKEELRARLEEHITTVVGRYKGKIYAWDVVNEAIDDDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 663 snpadykaSLRQTPWYQAIGSDYVEQAFLAAREVLdenpsWNIKLYYNDYN-EDNQNKATAIYNMVKDINDRYAaahngk 741
Cdd:COG3693 150 --------SLRNSPWYQALGPDYIADAFRWAREAD-----PDAKLFYNDYNiEGGPAKRDAYLELVKDLKARGV------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 742 lLIDGVGMQGHYNINT-NPDNVKLSLEKFISLGVEVSVSELDVTAGNNYTLPENLAVGQAYLYAQLFKLYKEHaDHIARV 820
Cdd:COG3693 211 -PIDGVGLQGHLGLDYpSPEEIEAALDRFAALGLPIHITELDVRVLPLPDLTEEDDAAQADRYRDLFDAFLSH-PAVTGV 288
|
330 340 350
....*....|....*....|....*....|....*...
gi 62990090 821 TFWGMDDNTSWRA---ENNPLLFDKNLQAKPAYYGVID 855
Cdd:COG3693 289 TFWGLTDGYSWRPgfrTGYPLLFDEDYQPKPAYDAVLD 326
|
|
| Glyco_10 |
smart00633 |
Glycosyl hydrolase family 10; |
565-853 |
2.97e-100 |
|
Glycosyl hydrolase family 10;
Pssm-ID: 214750 Cd Length: 263 Bit Score: 321.49 E-value: 2.97e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 565 MKPDALQPTKGNFTFTAADAMIDKVLAEGMKMHGHVLVWHQQSPAWLNTKKDDnnntvplGRDEALDNLRTHIQTVMKHF 644
Cdd:smart00633 1 MKWDSTEPSRGQFNFSGADAIVNFAKENGIKVRGHTLVWHSQTPDWVFNLNIS-------GKETLLARLENHIKTVVGRY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 645 GNKVISWDVVNEAMNDNPSNpadykaSLRQTPWYQAIGSDYVEQAFLAAREVLDenpswNIKLYYNDYNEDNQN-KATAI 723
Cdd:smart00633 74 KGKIYAWDVVNEAIHDNGSG------LRRSSVWYQILGEDYIEKAFRYAREADP-----DAKLFYNDYNTEEPNaKRQAI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 724 YNMVKDINDRYAaahngklLIDGVGMQGHYNIN-TNPDNVKLSLEKFISLGVEVSVSELDVTAGNNytlPENLAVGQAYL 802
Cdd:smart00633 143 YELVKKLKAKGV-------PIDGIGLQSHLSLGgPNIAEIRAALDRFASLGLEIWITELDISGPPN---PEENLQAQAAD 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 62990090 803 YAQLFKLYKEHaDHIARVTFWGMDDNTSWRA-ENNPLLFDKNLQAKPAYYGV 853
Cdd:smart00633 213 YEEVFKACLAH-PAVTGVTVWGVTDGYSWLDgFGAPLLFDANYQPKPAYWAI 263
|
|
| CBM9_like_1 |
cd00005 |
DOMON-like type 9 carbohydrate binding module of xylanases; Family 9 carbohydrate-binding ... |
873-1054 |
2.05e-92 |
|
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: 296.45 E-value: 2.05e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 873 AEAQYGTPVIDGTVDSIWSNAQAMPVNRYQMAWQGATGTAKALWDDQNLYVLIQVSDSQLNKANENAWEQDSVEVFLDQN 952
Cdd:cd00005 2 ATAKYGTPVIDGEVDDVWAKAEEITTDKKVSGTDGATATARTLWDEDNLYVLAEVKDPVLNKASANPWEQDSVEIFVDEN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 953 NGKTTFYQNDDGQYRVNFDNETSFSPASIAAGFESQTKKTANSYTVELKIPLTAVTPANQKKLGFDVQINDATDG-ARTS 1031
Cdd:cd00005 82 NAKTSSYEDDDAQYRVNFDNEQSFGGGAIAERFTSATKLTDGGYVVEAAIPLKTITPAAGTVIGFDLQVNDADDGgKRIG 161
|
170 180
....*....|....*....|...
gi 62990090 1032 VAAWNDTTGNGYQDTSVYGELTL 1054
Cdd:cd00005 162 VANWNDPTGNGYQDTSRFGVLLL 184
|
|
| CBM9_1 |
pfam06452 |
Carbohydrate family 9 binding domain-like; CBM9_1 is a C-terminal domain on bacterial xylanase ... |
882-1054 |
2.84e-75 |
|
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: 247.65 E-value: 2.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 882 IDGTVDSIWSNAQAMPVNRYQMAWQ--GATGTAKALWDDQNLYVLIQVSDSQLNKANENAWEQDSVEVFLDQNNGKTTFY 959
Cdd:pfam06452 1 IDGTVDAVWSNAQSLTIFKLWTGTVssDASGTFKALWDDDNLYVLAEVTDDVLNDGSTNPWEDDSVEIFIDENNGKTTEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 960 QNDDGQYRVNFDNETSFSPAS--IAAGFESQTKKTANSYTVELKIPLTAV-TPANQKKLGFDVQIND-ATDGARTSVAAW 1035
Cdd:pfam06452 81 GANDFQYRVNYNNETSFDPGNglIAAGFTSASKVSDGGYIVEAKIPLKTItTPANNKVIGFDVQINDdDDGGTRQGKITW 160
|
170
....*....|....*....
gi 62990090 1036 NDTTGNGYQDTSVYGELTL 1054
Cdd:pfam06452 161 NDPTGNAWQDPSVFGTVTL 179
|
|
| CBM_4_9 |
pfam02018 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
361-498 |
9.04e-15 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
Pssm-ID: 396553 Cd Length: 134 Bit Score: 72.48 E-value: 9.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 361 TFEDQTAGGFTGRaGTETLTVTNESNHtaDGSYSLKVEGRTTSWHGPSLRVEKYVDKGYEYKVTAWVKLLSPETsTKLEL 440
Cdd:pfam02018 8 TFEDGGLDGWKAR-GGSGKATVDVTSY--NGTYSLKVSGRTATWDGQIIDITIRLEKGTTYTVSFWVKASSGPP-QTVSV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 62990090 441 ASQvGDGGSANYPTPTTQAWQARrlpaaDGWVQLQGNYRYNSvGGEYLTIYVQSSNAT 498
Cdd:pfam02018 84 TLQ-ITDASGNYDTVADEKVVLT-----GEWTKLEGTFTIPK-TASTVELYVELPDST 134
|
|
| SLH |
pfam00395 |
S-layer homology domain; |
1288-1329 |
2.47e-08 |
|
S-layer homology domain;
Pssm-ID: 459798 [Multi-domain] Cd Length: 42 Bit Score: 51.05 E-value: 2.47e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 62990090 1288 FGDLAKVPWAKEAIDAMASRGVIKGTGENTFSPAASIKRADF 1329
Cdd:pfam00395 1 FKDVKSVAAWAEAVAALAELGIISGYPDGTFRPNEPITRAEA 42
|
|
| SLH |
pfam00395 |
S-layer homology domain; |
1350-1391 |
4.28e-07 |
|
S-layer homology domain;
Pssm-ID: 459798 [Multi-domain] Cd Length: 42 Bit Score: 47.59 E-value: 4.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 62990090 1350 FSDVPANAYYYNELAVAKQLGIATGFEDNTFKPDSSISRQDM 1391
Cdd:pfam00395 1 FKDVKSVAAWAEAVAALAELGIISGYPDGTFRPNEPITRAEA 42
|
|
| CBM_4_9 |
pfam02018 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
53-165 |
6.86e-07 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
Pssm-ID: 396553 Cd Length: 134 Bit Score: 50.14 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 53 GGASLTQVTGKVFDGNNdgsALYVSNRANTWDAAdFKFADIGLQNGKTYTVTVKGYVDQDATVPSGAQAFLQAVDSNNYG 132
Cdd:pfam02018 21 GGSGKATVDVTSYNGTY---SLKVSGRTATWDGQ-IIDITIRLEKGTTYTVSFWVKASSGPPQTVSVTLQITDASGNYDT 96
|
90 100 110
....*....|....*....|....*....|....
gi 62990090 133 FLASANFAAGTAFTLTKEFTVDTSVST-QLRVQS 165
Cdd:pfam02018 97 VADEKVVLTGEWTKLEGTFTIPKTASTvELYVEL 130
|
|
| CBM_4_9 |
pfam02018 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
208-320 |
1.68e-06 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
Pssm-ID: 396553 Cd Length: 134 Bit Score: 48.98 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 208 GGANLAQVADKVFDGNddgKALYVSNRANTWDAAdFKFADIGLQNGKTYTVTVKGYVDQDATVPSGAQAFLQAVDSNNYG 287
Cdd:pfam02018 21 GGSGKATVDVTSYNGT---YSLKVSGRTATWDGQ-IIDITIRLEKGTTYTVSFWVKASSGPPQTVSVTLQITDASGNYDT 96
|
90 100 110
....*....|....*....|....*....|....
gi 62990090 288 FLASANFAARSAFTLTKEFTVDTSVTT-QLRVQS 320
Cdd:pfam02018 97 VADEKVVLTGEWTKLEGTFTIPKTASTvELYVEL 130
|
|
| SLH |
pfam00395 |
S-layer homology domain; |
1415-1456 |
1.10e-05 |
|
S-layer homology domain;
Pssm-ID: 459798 [Multi-domain] Cd Length: 42 Bit Score: 43.73 E-value: 1.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 62990090 1415 FSDAASVAGYAqDSVAALVKAGVVQGSGSK-LAPNDQLTRAEA 1456
Cdd:pfam00395 1 FKDVKSVAAWA-EAVAALAELGIISGYPDGtFRPNEPITRAEA 42
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_hydro_10 |
pfam00331 |
Glycosyl hydrolase family 10; |
525-855 |
1.24e-116 |
|
Glycosyl hydrolase family 10;
Pssm-ID: 425613 Cd Length: 310 Bit Score: 368.54 E-value: 1.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 525 LKDVYKNDF-LIGNAISAEDLEG--TRLELLKMHHDVVTAGNAMKPDALQPTKGNFTFTAADAMIDKVLAEGMKMHGHVL 601
Cdd:pfam00331 1 LKDAAKAKGkYFGTAVSAGELLGnsQYTAILKAEFNQVTPENEMKWDALEPSRGNFTFANADRIVNFAKQNGMAVRGHTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 602 VWHQQSPAWLNTKKDDNNNtvplgrdeALDNLRTHIQTVMKHFGNKVISWDVVNEAMNDNPSNpadykaSLRQTPWYQAI 681
Cdd:pfam00331 81 VWHSQLPDWVFNINGSKAD--------LLQVLENHITTVVGHYKGKIYAWDVVNEAFDDDGSG------GLRSSVWYQVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 682 GSDYVEQAFLAAREVLDenpswNIKLYYNDYNEDNQN-KATAIYNMVKDINDRYaaahngkLLIDGVGMQGHYNINTN-P 759
Cdd:pfam00331 147 GEDYIEIAFRAAREADP-----DAKLYYNDYNIEEDGaKRDAVYNLVKDLKAKG-------VPIDGIGFQSHLSAGGPsI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 760 DNVKLSLEKFISLGVEVSVSELDVTAGNNYTLPENLAvgQAYLYAQLFKLYKEHADhIARVTFWGMDDNTSWRAE---NN 836
Cdd:pfam00331 215 SNIRAALQRFAALGLEVAITELDIRGPDPSDEEALQA--QAARYKEVFKACLAVPN-CTGITVWGVTDKYSWLSGffpGA 291
|
330
....*....|....*....
gi 62990090 837 PLLFDKNLQAKPAYYGVID 855
Cdd:pfam00331 292 PLLFDSNYQPKPAYNAVVD 310
|
|
| XynA |
COG3693 |
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]; |
505-855 |
2.32e-116 |
|
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism];
Pssm-ID: 442908 Cd Length: 328 Bit Score: 368.45 E-value: 2.32e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 505 DISFESTGSGPvgiQKDLAPLKDVYKN-DFLIGNAISAEDL-EGTRLELLKMHHDVVTAGNAMKPDALQPTKGNFTFTAA 582
Cdd:COG3693 1 ALALAALDAAA---APGAASLKDLAADkGFLFGTAVNAGQLdDPAYRELLAREFNSVTPENEMKWGSIEPERGEFNFSAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 583 DAMIDKVLAEGMKMHGHVLVWHQQSPAWLNTKKddnnntvpLGRDEALDNLRTHIQTVMKHFGNKVISWDVVNEAMNDNP 662
Cdd:COG3693 78 DAIVAFAKANGMKVRGHTLVWHSQTPDWVFEDA--------LSKEELRARLEEHITTVVGRYKGKIYAWDVVNEAIDDDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 663 snpadykaSLRQTPWYQAIGSDYVEQAFLAAREVLdenpsWNIKLYYNDYN-EDNQNKATAIYNMVKDINDRYAaahngk 741
Cdd:COG3693 150 --------SLRNSPWYQALGPDYIADAFRWAREAD-----PDAKLFYNDYNiEGGPAKRDAYLELVKDLKARGV------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 742 lLIDGVGMQGHYNINT-NPDNVKLSLEKFISLGVEVSVSELDVTAGNNYTLPENLAVGQAYLYAQLFKLYKEHaDHIARV 820
Cdd:COG3693 211 -PIDGVGLQGHLGLDYpSPEEIEAALDRFAALGLPIHITELDVRVLPLPDLTEEDDAAQADRYRDLFDAFLSH-PAVTGV 288
|
330 340 350
....*....|....*....|....*....|....*...
gi 62990090 821 TFWGMDDNTSWRA---ENNPLLFDKNLQAKPAYYGVID 855
Cdd:COG3693 289 TFWGLTDGYSWRPgfrTGYPLLFDEDYQPKPAYDAVLD 326
|
|
| Glyco_10 |
smart00633 |
Glycosyl hydrolase family 10; |
565-853 |
2.97e-100 |
|
Glycosyl hydrolase family 10;
Pssm-ID: 214750 Cd Length: 263 Bit Score: 321.49 E-value: 2.97e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 565 MKPDALQPTKGNFTFTAADAMIDKVLAEGMKMHGHVLVWHQQSPAWLNTKKDDnnntvplGRDEALDNLRTHIQTVMKHF 644
Cdd:smart00633 1 MKWDSTEPSRGQFNFSGADAIVNFAKENGIKVRGHTLVWHSQTPDWVFNLNIS-------GKETLLARLENHIKTVVGRY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 645 GNKVISWDVVNEAMNDNPSNpadykaSLRQTPWYQAIGSDYVEQAFLAAREVLDenpswNIKLYYNDYNEDNQN-KATAI 723
Cdd:smart00633 74 KGKIYAWDVVNEAIHDNGSG------LRRSSVWYQILGEDYIEKAFRYAREADP-----DAKLFYNDYNTEEPNaKRQAI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 724 YNMVKDINDRYAaahngklLIDGVGMQGHYNIN-TNPDNVKLSLEKFISLGVEVSVSELDVTAGNNytlPENLAVGQAYL 802
Cdd:smart00633 143 YELVKKLKAKGV-------PIDGIGLQSHLSLGgPNIAEIRAALDRFASLGLEIWITELDISGPPN---PEENLQAQAAD 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 62990090 803 YAQLFKLYKEHaDHIARVTFWGMDDNTSWRA-ENNPLLFDKNLQAKPAYYGV 853
Cdd:smart00633 213 YEEVFKACLAH-PAVTGVTVWGVTDGYSWLDgFGAPLLFDANYQPKPAYWAI 263
|
|
| CBM9_like_1 |
cd00005 |
DOMON-like type 9 carbohydrate binding module of xylanases; Family 9 carbohydrate-binding ... |
873-1054 |
2.05e-92 |
|
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: 296.45 E-value: 2.05e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 873 AEAQYGTPVIDGTVDSIWSNAQAMPVNRYQMAWQGATGTAKALWDDQNLYVLIQVSDSQLNKANENAWEQDSVEVFLDQN 952
Cdd:cd00005 2 ATAKYGTPVIDGEVDDVWAKAEEITTDKKVSGTDGATATARTLWDEDNLYVLAEVKDPVLNKASANPWEQDSVEIFVDEN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 953 NGKTTFYQNDDGQYRVNFDNETSFSPASIAAGFESQTKKTANSYTVELKIPLTAVTPANQKKLGFDVQINDATDG-ARTS 1031
Cdd:cd00005 82 NAKTSSYEDDDAQYRVNFDNEQSFGGGAIAERFTSATKLTDGGYVVEAAIPLKTITPAAGTVIGFDLQVNDADDGgKRIG 161
|
170 180
....*....|....*....|...
gi 62990090 1032 VAAWNDTTGNGYQDTSVYGELTL 1054
Cdd:cd00005 162 VANWNDPTGNGYQDTSRFGVLLL 184
|
|
| CBM9_1 |
pfam06452 |
Carbohydrate family 9 binding domain-like; CBM9_1 is a C-terminal domain on bacterial xylanase ... |
882-1054 |
2.84e-75 |
|
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: 247.65 E-value: 2.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 882 IDGTVDSIWSNAQAMPVNRYQMAWQ--GATGTAKALWDDQNLYVLIQVSDSQLNKANENAWEQDSVEVFLDQNNGKTTFY 959
Cdd:pfam06452 1 IDGTVDAVWSNAQSLTIFKLWTGTVssDASGTFKALWDDDNLYVLAEVTDDVLNDGSTNPWEDDSVEIFIDENNGKTTEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 960 QNDDGQYRVNFDNETSFSPAS--IAAGFESQTKKTANSYTVELKIPLTAV-TPANQKKLGFDVQIND-ATDGARTSVAAW 1035
Cdd:pfam06452 81 GANDFQYRVNYNNETSFDPGNglIAAGFTSASKVSDGGYIVEAKIPLKTItTPANNKVIGFDVQINDdDDGGTRQGKITW 160
|
170
....*....|....*....
gi 62990090 1036 NDTTGNGYQDTSVYGELTL 1054
Cdd:pfam06452 161 NDPTGNAWQDPSVFGTVTL 179
|
|
| CBM9_like_4 |
cd09619 |
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) ... |
879-1050 |
8.49e-28 |
|
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: 111.76 E-value: 8.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 879 TPVIDGTVDSIWSNAQAMPVNRY---QMAWQGAT---GTAKALWDDQNLYVLIQVSDSQL--NKANENAWEQDSVEVFLD 950
Cdd:cd09619 1 APAIDGTLEAAWYPGSILPLEAKgliDDTGPSATdlsATFAAMWDDTNLYVLVDVTDDTLrnDLDGKDHWRGDAVEIFID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 951 QNNGKTTFYQNDDGQY----RVNFDNETSFSPASIAAGFESQTKKTANSYTVELKIPLTA--VTPANQKKLGFDVQINDA 1024
Cdd:cd09619 81 PDGNKLATYTANDFQLgfrpNDETGQPEGWNHTTPAPGIRVASTPRYGGYTVEAAIPWSTlgITPAANLLLGFDVAINDD 160
|
170 180
....*....|....*....|....*..
gi 62990090 1025 -TDGARTSVAAWNDTTGNGYQDTSVYG 1050
Cdd:cd09619 161 dTGGTRDQQIAWNAKDDQNWSNPSLFG 187
|
|
| CBM_4_9 |
pfam02018 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
361-498 |
9.04e-15 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
Pssm-ID: 396553 Cd Length: 134 Bit Score: 72.48 E-value: 9.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 361 TFEDQTAGGFTGRaGTETLTVTNESNHtaDGSYSLKVEGRTTSWHGPSLRVEKYVDKGYEYKVTAWVKLLSPETsTKLEL 440
Cdd:pfam02018 8 TFEDGGLDGWKAR-GGSGKATVDVTSY--NGTYSLKVSGRTATWDGQIIDITIRLEKGTTYTVSFWVKASSGPP-QTVSV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 62990090 441 ASQvGDGGSANYPTPTTQAWQARrlpaaDGWVQLQGNYRYNSvGGEYLTIYVQSSNAT 498
Cdd:pfam02018 84 TLQ-ITDASGNYDTVADEKVVLT-----GEWTKLEGTFTIPK-TASTVELYVELPDST 134
|
|
| DOMON_like |
cd00241 |
Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of ... |
908-1035 |
1.80e-13 |
|
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: 69.52 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 908 ATGTAKALWDDQNLYVLIQVSDSQLNK--ANENAWEQDSVEVFLDQNNGKTTF--YQNDDGQYRVNFDNETSFSPASIAA 983
Cdd:cd00241 18 LSATVKLAWDGEYLYFLVEVTDDVLRDtaALSLVWDGDGVELFFDPDNDGTDGnaFGYGIDLYGFSVDLADGSGTAADYG 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62990090 984 ------GFESQTKKTANSYTVELKIPLTAVTPANQKK---LGFDVQINDATDGARTSVAAW 1035
Cdd:cd00241 98 teggreGVSSSAKKGGGGYTVEFAIPLAALDGLDPGKgkgYGFAFAINDGSADDRRHPSVF 158
|
|
| CBM9_like_5 |
cd09621 |
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) ... |
905-1054 |
1.06e-12 |
|
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: 68.11 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 905 WQGAT---GTAKALWDDQNLYVLIQVSDSQ--LNKANENAWEQDSVEVFLD---QNNGKTTFY-----QNDDGQYRVNFD 971
Cdd:cd09621 22 WKGPEdlsAKVWLGWDADNLYLAARVTDDRhsQPFTGADIWKGDSIQLALDlpgQKGGADGFWelglaRTDDGGALVWRW 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 972 NETS-FSPASIAAGFESQTKKTANSYTV-ELKIPLTAVTPANQK---KLGFDVQINDATDGARTSVAAWNDTTGNGYqDT 1046
Cdd:cd09621 102 NAPAgFDPAAAAAAIRLETSRDEAKVTVyEAAIPWAELGLTGPAagdGFRFNLLVNDNDGGGREGWIEWAPGIGESK-DP 180
|
....*...
gi 62990090 1047 SVYGELTL 1054
Cdd:cd09621 181 ALFPLVTL 188
|
|
| CBM9_like_3 |
cd09620 |
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) ... |
882-1012 |
2.08e-12 |
|
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: 67.79 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 882 IDGTVD-SIWSNAQAMPVNRYqmAWQGATG----TAKALWDDQNLYVLIQVSDSQLN----KANENAWEQDSVEVFLDqN 952
Cdd:cd09620 1 IDGKLDePAWQAAPWVELFVD--IGGGPPPkpqtRVRLLYDDEYLYLAFEVEDDDIWatytERDDPVWEDDVVEVFID-P 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62990090 953 NGKTTFYQN---------DDGQYRVNFDNETSFSPA-SIAAGFESQT--------KKTANSYTVELKIPLTAVTPANQ 1012
Cdd:cd09620 78 DGDGPNYYEfevnplgtvLDAFIRRPRDGGGDRDNRqPDSAGLESAVsidgtlndSDGDKGWTVELAIPFAALAKAAG 155
|
|
| CBM9_like_2 |
cd09618 |
DOMON-like type 9 carbohydrate binding module; Family 9 carbohydrate-binding modules (CBM9) ... |
878-1036 |
3.01e-09 |
|
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: 58.04 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 878 GTPVIDGTVD-SIWSNAQamPVNRYQMAWQGATGTA------KALWDDQNLYVLIQVSDSQLNKAN-------ENAWEQD 943
Cdd:cd09618 9 GPPVIDGVLDeAVWQQAP--VATDFVQREPNDGGPApertevRVLYDDEALYVAAVCYDPEPDKIRaqllrrdDDGENDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 944 SVEVFLDQNNGKTTFYQ---NDDG-QY--RVNFDNETSFSPASIaagFESQTKKTANSYTVELKIPLTAV--TPANQKKL 1015
Cdd:cd09618 87 RFGVALDTFNDRRNAYQfgvNPAGvQRdaLEFDGNNEDFSWDAV---WESATKITDDGWTAEMAIPFSSLrfPKGSVQTW 163
|
170 180
....*....|....*....|.
gi 62990090 1016 GFDVQINDATDGARTSvaaWN 1036
Cdd:cd09618 164 GINFYRNIPRTNERSS---WP 181
|
|
| SLH |
pfam00395 |
S-layer homology domain; |
1288-1329 |
2.47e-08 |
|
S-layer homology domain;
Pssm-ID: 459798 [Multi-domain] Cd Length: 42 Bit Score: 51.05 E-value: 2.47e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 62990090 1288 FGDLAKVPWAKEAIDAMASRGVIKGTGENTFSPAASIKRADF 1329
Cdd:pfam00395 1 FKDVKSVAAWAEAVAALAELGIISGYPDGTFRPNEPITRAEA 42
|
|
| SLH |
pfam00395 |
S-layer homology domain; |
1350-1391 |
4.28e-07 |
|
S-layer homology domain;
Pssm-ID: 459798 [Multi-domain] Cd Length: 42 Bit Score: 47.59 E-value: 4.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 62990090 1350 FSDVPANAYYYNELAVAKQLGIATGFEDNTFKPDSSISRQDM 1391
Cdd:pfam00395 1 FKDVKSVAAWAEAVAALAELGIISGYPDGTFRPNEPITRAEA 42
|
|
| CBM_4_9 |
pfam02018 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
53-165 |
6.86e-07 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
Pssm-ID: 396553 Cd Length: 134 Bit Score: 50.14 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 53 GGASLTQVTGKVFDGNNdgsALYVSNRANTWDAAdFKFADIGLQNGKTYTVTVKGYVDQDATVPSGAQAFLQAVDSNNYG 132
Cdd:pfam02018 21 GGSGKATVDVTSYNGTY---SLKVSGRTATWDGQ-IIDITIRLEKGTTYTVSFWVKASSGPPQTVSVTLQITDASGNYDT 96
|
90 100 110
....*....|....*....|....*....|....
gi 62990090 133 FLASANFAAGTAFTLTKEFTVDTSVST-QLRVQS 165
Cdd:pfam02018 97 VADEKVVLTGEWTKLEGTFTIPKTASTvELYVEL 130
|
|
| CBM_4_9 |
pfam02018 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
208-320 |
1.68e-06 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
Pssm-ID: 396553 Cd Length: 134 Bit Score: 48.98 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 208 GGANLAQVADKVFDGNddgKALYVSNRANTWDAAdFKFADIGLQNGKTYTVTVKGYVDQDATVPSGAQAFLQAVDSNNYG 287
Cdd:pfam02018 21 GGSGKATVDVTSYNGT---YSLKVSGRTATWDGQ-IIDITIRLEKGTTYTVSFWVKASSGPPQTVSVTLQITDASGNYDT 96
|
90 100 110
....*....|....*....|....*....|....
gi 62990090 288 FLASANFAARSAFTLTKEFTVDTSVTT-QLRVQS 320
Cdd:pfam02018 97 VADEKVVLTGEWTKLEGTFTIPKTASTvELYVEL 130
|
|
| SLH |
pfam00395 |
S-layer homology domain; |
1415-1456 |
1.10e-05 |
|
S-layer homology domain;
Pssm-ID: 459798 [Multi-domain] Cd Length: 42 Bit Score: 43.73 E-value: 1.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 62990090 1415 FSDAASVAGYAqDSVAALVKAGVVQGSGSK-LAPNDQLTRAEA 1456
Cdd:pfam00395 1 FKDVKSVAAWA-EAVAALAELGIISGYPDGtFRPNEPITRAEA 42
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| CBM9_like_HisKa |
cd09622 |
DOMON-like type 9 carbohydrate binding module at the N-terminus of bacterial sensor histidine ... |
877-1019 |
1.41e-05 |
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DOMON-like type 9 carbohydrate binding module at the N-terminus of bacterial sensor histidine kinases; 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 family are located at the N-terminus of bacterial sensor histidine kinases and may constitute or contribute to the ligand-binding moiety.
Pssm-ID: 187680 Cd Length: 265 Bit Score: 48.54 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62990090 877 YGTPVIDGTVDSiWSNAQampvNRYQ-MAWQGATGTAKALW----DDQNLYVLIQVSDSQLNKANENAWEQDSVE----V 947
Cdd:cd09622 61 AGAILLDGYADD-WPGYD----SAFQlEGEAGQASSLAFKHragkYDRYLYLLFQVSDNTVIYRFNPSLPEDAHDhlllQ 135
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62990090 948 FLDQNNGKTTFYQNDDGQYRVNFDNET--SFSPASIAAGFESQTkktANSYTVELKIPLTAVTpanqKKLGFDV 1019
Cdd:cd09622 136 TEDPNGQRQRYLIATSAPGWVNAFRLTrnAGAPEYRIQGHWQET---ADGYQLELRLPLSLVG----SRLGFAL 202
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