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Conserved domains on  [gi|1078671896|gb|AOW19003|]
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hypothetical protein LPB03_04965 [Polaribacter vadi]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
44-284 4.65e-51

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 181.01  E-value: 4.65e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896  44 FFQKQDLDSIKKWGYNSVRLAMHYNLFTPPieaepiQGENTWLETGFEMVDELLTWCEANEIYLILDMHAAPGGQGqdaa 123
Cdd:COG2730    26 NITEEDIDAIADWGFNTVRLPVSWERLQDP------DNPYTLDEAYLERVDEVVDWAKARGLYVILDLHHAPGYQG---- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 124 isdydsdkpslWESELNKSKTMALWGKLAERYKDKEWIGGYDLLNEVNWPLGDsVLRDLYVRITNEIRTYDSNHILFIEG 203
Cdd:COG2730    96 -----------WYDAATQERFIAFWRQLAERYKDYPNVLGFELLNEPHGATWA-DWNALAQRAIDAIRATNPDRLIIVEG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 204 NWF--ANDFSGLTPPWDSNMVYSFHKYWTYNDTASIQW----------------VLDLRNQHNVPLWMGESG-------E 258
Cdd:COG2730   164 NNWggAHNLRALDPLDDDNLVYSVHFYGPFVFTHQGAWfagptypanlearldnWGDWAADNGVPVFVGEFGaynddpdA 243
                         250       260
                  ....*....|....*....|....*.
gi 1078671896 259 NSNVWYTEAINLFEDNNIGWSWWPWK 284
Cdd:COG2730   244 SRLAWLRDLLDYLEENGIGWTYWSFN 269
CBM6_cellulase-like cd04080
Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including ...
363-520 2.72e-41

Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including GH5 (cellulase); This family includes carbohydrate binding module 6 (CBM6) domains that are appended to several glycoside hydrolase (GH) domains, including GH5 (cellulase) and GH16, as well as to coagulation factor 5/8 carbohydrate-binding domains. CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. The CBM6s are appended to GHs that display a diversity of substrate specificities. For some members of this family information is available about the specific substrates of the appended GH domains. It includes the CBM domains of various enzymes involved in cell wall degradation including, an extracellular beta-1,3-glucanase from Lysobacter enzymogenes encoded by the gluC gene (its catalytic domain belongs to the GH16 family), the tandem CBM domains of Pseudomonas sp. PE2 beta-1,3(4)-glucanase A (its catalytic domain also belongs to GH16), and a family 6 CBM from Cellvibrio mixtus Endoglucanase 5A (CmCBM6) which binds to the beta1,4-beta1,3-mixed linked glucans lichenan, and barley beta-glucan, cello-oligosaccharides, insoluble forms of cellulose, the beta1,3-glucan laminarin, and xylooligosaccharides, and the CBM6 of Fibrobacter succinogenes S85 XynD xylanase, appended to a GH10 domain, and Cellvibrio japonicas Cel5G appended to a GH5 (cellulase) domain. GH5 (cellulase) family includes enzymes with several known activities such as endoglucanase, beta-mannanase, and xylanase, which are involved in the degradation of cellulose and xylans. GH16 family includes enzymes with lichenase, xyloglucan endotransglycosylase (XET), and beta-agarase activities. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. For CmCBM6 it has been shown that these two binding sites have different ligand specificities.


:

Pssm-ID: 271146  Cd Length: 144  Bit Score: 147.76  E-value: 2.72e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 363 IPGVIYLSDYDLGTNGIAYNDIDYANYslstneykawnsGWNYRNDGVDIQTNTDNtnSNGYHIGFTQKNEWLKYTVNVE 442
Cdd:cd04080     1 IPGRIEAEDYDLGGEGVAYHDTTPGNE------------GGYYRNDGVDIETTSDT--GGGYNVGWIDAGEWLEYTVNVP 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078671896 443 ETGFYNFKFRYATEQSGGKPKFFLDEVDFAGDVTLGSTGGWSNFVFQTVSNKYMEAGKHILKILVDGNaSYNMSSIEF 520
Cdd:cd04080    67 EAGTYTVSFRVASPSGGGSLSLEVDGGTVLGTVDVPNTGGWQTWQTVTTTVVLLPAGTHTLRLVFVGG-GFNLNWFEF 143
CBM6_cellulase-like cd04080
Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including ...
635-760 1.39e-34

Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including GH5 (cellulase); This family includes carbohydrate binding module 6 (CBM6) domains that are appended to several glycoside hydrolase (GH) domains, including GH5 (cellulase) and GH16, as well as to coagulation factor 5/8 carbohydrate-binding domains. CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. The CBM6s are appended to GHs that display a diversity of substrate specificities. For some members of this family information is available about the specific substrates of the appended GH domains. It includes the CBM domains of various enzymes involved in cell wall degradation including, an extracellular beta-1,3-glucanase from Lysobacter enzymogenes encoded by the gluC gene (its catalytic domain belongs to the GH16 family), the tandem CBM domains of Pseudomonas sp. PE2 beta-1,3(4)-glucanase A (its catalytic domain also belongs to GH16), and a family 6 CBM from Cellvibrio mixtus Endoglucanase 5A (CmCBM6) which binds to the beta1,4-beta1,3-mixed linked glucans lichenan, and barley beta-glucan, cello-oligosaccharides, insoluble forms of cellulose, the beta1,3-glucan laminarin, and xylooligosaccharides, and the CBM6 of Fibrobacter succinogenes S85 XynD xylanase, appended to a GH10 domain, and Cellvibrio japonicas Cel5G appended to a GH5 (cellulase) domain. GH5 (cellulase) family includes enzymes with several known activities such as endoglucanase, beta-mannanase, and xylanase, which are involved in the degradation of cellulose and xylans. GH16 family includes enzymes with lichenase, xyloglucan endotransglycosylase (XET), and beta-agarase activities. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. For CmCBM6 it has been shown that these two binding sites have different ligand specificities.


:

Pssm-ID: 271146  Cd Length: 144  Bit Score: 128.89  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 635 IPGKIQAEDFST--------------------QQGLETENTTDTGAGQNIGYTDAGDYAEYLIYISESGYYNLNLRTAAE 694
Cdd:cd04080     1 IPGRIEAEDYDLggegvayhdttpgneggyyrNDGVDIETTSDTGGGYNVGWIDAGEWLEYTVNVPEAGTYTVSFRVASP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078671896 695 SSAGKIEFELSHNEVTqsiSTIDLPVTGGWQSWQT-TATQTTLNEGIYTLKMKVLQSGFNMNWFEFE 760
Cdd:cd04080    81 SGGGSLSLEVDGGTVL---GTVDVPNTGGWQTWQTvTTTVVLLPAGTHTLRLVFVGGGFNLNWFEFT 144
Por_Secre_tail TIGR04183
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
777-848 4.43e-15

Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.


:

Pssm-ID: 275036 [Multi-domain]  Cd Length: 72  Bit Score: 70.51  E-value: 4.43e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078671896 777 IFPNPFTDNFNIKLNNQQIIKDLKIMDLNGRLIKNIHPTESNGVyNLSSLKSGVYLLSIETDKGSFQKKLIK 848
Cdd:TIGR04183   1 IYPNPAKGTLIIILLSSSGKVKVEIYDLSGKLVKKTTLNNSNSI-DLSNLSSGVYIVKITTGNGTITKKIIK 71
SWM_repeat super family cl23886
Putative flagellar system-associated repeat; This family appears to be a repeated unit that ...
524-608 1.31e-04

Putative flagellar system-associated repeat; This family appears to be a repeated unit that can occur up to 29 times in these outer membrane proteins. It is putatively associated with a novel flagellar system.


The actual alignment was detected with superfamily member TIGR02059:

Pssm-ID: 420078 [Multi-domain]  Cd Length: 101  Bit Score: 41.80  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 524 TETIPSFNVLSASTNDDEKSLKIVLNQPLN---NQELTNNPFEVTVNNATRTITSAAIDPSNNRlIVIELAKYLFYQDEI 600
Cdd:TIGR02059  13 TAPVLLFGSTSTAVATNGNLLVLTFNEPLAditNHAPTRDQFAVTVNGAPNTVTSVSLGGSNTT-ITLTLAQVVEDGDEV 91

                  ....*...
gi 1078671896 601 KVSYIGNS 608
Cdd:TIGR02059  92 TLSYTKNS 99
 
Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
44-284 4.65e-51

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 181.01  E-value: 4.65e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896  44 FFQKQDLDSIKKWGYNSVRLAMHYNLFTPPieaepiQGENTWLETGFEMVDELLTWCEANEIYLILDMHAAPGGQGqdaa 123
Cdd:COG2730    26 NITEEDIDAIADWGFNTVRLPVSWERLQDP------DNPYTLDEAYLERVDEVVDWAKARGLYVILDLHHAPGYQG---- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 124 isdydsdkpslWESELNKSKTMALWGKLAERYKDKEWIGGYDLLNEVNWPLGDsVLRDLYVRITNEIRTYDSNHILFIEG 203
Cdd:COG2730    96 -----------WYDAATQERFIAFWRQLAERYKDYPNVLGFELLNEPHGATWA-DWNALAQRAIDAIRATNPDRLIIVEG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 204 NWF--ANDFSGLTPPWDSNMVYSFHKYWTYNDTASIQW----------------VLDLRNQHNVPLWMGESG-------E 258
Cdd:COG2730   164 NNWggAHNLRALDPLDDDNLVYSVHFYGPFVFTHQGAWfagptypanlearldnWGDWAADNGVPVFVGEFGaynddpdA 243
                         250       260
                  ....*....|....*....|....*.
gi 1078671896 259 NSNVWYTEAINLFEDNNIGWSWWPWK 284
Cdd:COG2730   244 SRLAWLRDLLDYLEENGIGWTYWSFN 269
CBM6_cellulase-like cd04080
Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including ...
363-520 2.72e-41

Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including GH5 (cellulase); This family includes carbohydrate binding module 6 (CBM6) domains that are appended to several glycoside hydrolase (GH) domains, including GH5 (cellulase) and GH16, as well as to coagulation factor 5/8 carbohydrate-binding domains. CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. The CBM6s are appended to GHs that display a diversity of substrate specificities. For some members of this family information is available about the specific substrates of the appended GH domains. It includes the CBM domains of various enzymes involved in cell wall degradation including, an extracellular beta-1,3-glucanase from Lysobacter enzymogenes encoded by the gluC gene (its catalytic domain belongs to the GH16 family), the tandem CBM domains of Pseudomonas sp. PE2 beta-1,3(4)-glucanase A (its catalytic domain also belongs to GH16), and a family 6 CBM from Cellvibrio mixtus Endoglucanase 5A (CmCBM6) which binds to the beta1,4-beta1,3-mixed linked glucans lichenan, and barley beta-glucan, cello-oligosaccharides, insoluble forms of cellulose, the beta1,3-glucan laminarin, and xylooligosaccharides, and the CBM6 of Fibrobacter succinogenes S85 XynD xylanase, appended to a GH10 domain, and Cellvibrio japonicas Cel5G appended to a GH5 (cellulase) domain. GH5 (cellulase) family includes enzymes with several known activities such as endoglucanase, beta-mannanase, and xylanase, which are involved in the degradation of cellulose and xylans. GH16 family includes enzymes with lichenase, xyloglucan endotransglycosylase (XET), and beta-agarase activities. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. For CmCBM6 it has been shown that these two binding sites have different ligand specificities.


Pssm-ID: 271146  Cd Length: 144  Bit Score: 147.76  E-value: 2.72e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 363 IPGVIYLSDYDLGTNGIAYNDIDYANYslstneykawnsGWNYRNDGVDIQTNTDNtnSNGYHIGFTQKNEWLKYTVNVE 442
Cdd:cd04080     1 IPGRIEAEDYDLGGEGVAYHDTTPGNE------------GGYYRNDGVDIETTSDT--GGGYNVGWIDAGEWLEYTVNVP 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078671896 443 ETGFYNFKFRYATEQSGGKPKFFLDEVDFAGDVTLGSTGGWSNFVFQTVSNKYMEAGKHILKILVDGNaSYNMSSIEF 520
Cdd:cd04080    67 EAGTYTVSFRVASPSGGGSLSLEVDGGTVLGTVDVPNTGGWQTWQTVTTTVVLLPAGTHTLRLVFVGG-GFNLNWFEF 143
CBM6_cellulase-like cd04080
Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including ...
635-760 1.39e-34

Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including GH5 (cellulase); This family includes carbohydrate binding module 6 (CBM6) domains that are appended to several glycoside hydrolase (GH) domains, including GH5 (cellulase) and GH16, as well as to coagulation factor 5/8 carbohydrate-binding domains. CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. The CBM6s are appended to GHs that display a diversity of substrate specificities. For some members of this family information is available about the specific substrates of the appended GH domains. It includes the CBM domains of various enzymes involved in cell wall degradation including, an extracellular beta-1,3-glucanase from Lysobacter enzymogenes encoded by the gluC gene (its catalytic domain belongs to the GH16 family), the tandem CBM domains of Pseudomonas sp. PE2 beta-1,3(4)-glucanase A (its catalytic domain also belongs to GH16), and a family 6 CBM from Cellvibrio mixtus Endoglucanase 5A (CmCBM6) which binds to the beta1,4-beta1,3-mixed linked glucans lichenan, and barley beta-glucan, cello-oligosaccharides, insoluble forms of cellulose, the beta1,3-glucan laminarin, and xylooligosaccharides, and the CBM6 of Fibrobacter succinogenes S85 XynD xylanase, appended to a GH10 domain, and Cellvibrio japonicas Cel5G appended to a GH5 (cellulase) domain. GH5 (cellulase) family includes enzymes with several known activities such as endoglucanase, beta-mannanase, and xylanase, which are involved in the degradation of cellulose and xylans. GH16 family includes enzymes with lichenase, xyloglucan endotransglycosylase (XET), and beta-agarase activities. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. For CmCBM6 it has been shown that these two binding sites have different ligand specificities.


Pssm-ID: 271146  Cd Length: 144  Bit Score: 128.89  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 635 IPGKIQAEDFST--------------------QQGLETENTTDTGAGQNIGYTDAGDYAEYLIYISESGYYNLNLRTAAE 694
Cdd:cd04080     1 IPGRIEAEDYDLggegvayhdttpgneggyyrNDGVDIETTSDTGGGYNVGWIDAGEWLEYTVNVPEAGTYTVSFRVASP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078671896 695 SSAGKIEFELSHNEVTqsiSTIDLPVTGGWQSWQT-TATQTTLNEGIYTLKMKVLQSGFNMNWFEFE 760
Cdd:cd04080    81 SGGGSLSLEVDGGTVL---GTVDVPNTGGWQTWQTvTTTVVLLPAGTHTLRLVFVGGGFNLNWFEFT 144
CBD_IV smart00606
Cellulose Binding Domain Type IV;
635-759 1.29e-25

Cellulose Binding Domain Type IV;


Pssm-ID: 128869 [Multi-domain]  Cd Length: 129  Bit Score: 102.80  E-value: 1.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896  635 IPGKIQAEDFSTQQGLETENTTDTGAGQNIGYTDAGDYAEYL-IYISESGYYNLNLRTAAESSAGKIEFELshNEVT-QS 712
Cdd:smart00606   4 PYNAIQAESYDSQSGVQTETTSDAGGGKNVGYIDDGDWIAYKdVDFGSSGAYTFTARVASGNAGGSIELRL--DSPTgTL 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1078671896  713 ISTIDLPVTGGWQSWQTTATQTTLNEGIYTL-KMKVLQSGFNMNWFEF 759
Cdd:smart00606  82 VGTVDVPSTGGWQTYQTVSATVTLPAGVHDVyLVFKGGNYFNIDWFRF 129
Cellulase pfam00150
Cellulase (glycosyl hydrolase family 5);
35-283 7.25e-24

Cellulase (glycosyl hydrolase family 5);


Pssm-ID: 395098 [Multi-domain]  Cd Length: 272  Bit Score: 102.07  E-value: 7.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896  35 TFYSNWRKNFF-QKQDLDSIKKWGYNSVRLAMHYNLFTPPieaepiQGENTWLETGFEMVDELLTWCEANEIYLILDMHA 113
Cdd:pfam00150  14 THGGQWGNPYVtTKAMIDLVKDWGFNVVRLPVSWGGYVPN------NPDYLIDENWLNRVDEVVDYAIDNGMYVIIDWHH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 114 APGGQGqdAAISDYDSDkpslweselnKSKTMALWGKLAERYKDKEWIgGYDLLNE------VNWplgDSVLRDLYVRIT 187
Cdd:pfam00150  88 DGGWPG--DPNGNIDTA----------KAFFKKIWTQIATRYGNNPNV-IFELMNEphgndqATW---ADDVKDYAQEAI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 188 NEIRTYDSNHILFIEGNWFA--NDFSGLTPPWD-SNMVYSFHKYWTYN---------DTASIQWVLDLRNQ----HNVPL 251
Cdd:pfam00150 152 DAIRAAGPNNLIIVGGNSWSqnPDGAALNDPNDdDNLIYSVHFYAPSDfsgtwfdceDPTNLAQRLRAAANwaldNGIPV 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1078671896 252 WMGESG--ENSNVWYTEA---INLFEDNNIGWSWWPW 283
Cdd:pfam00150 232 FIGEFGggNADGPCRDEAekwLDYLKENGISWTGWSN 268
CBM_6 pfam03422
Carbohydrate binding module (family 6);
640-760 7.88e-23

Carbohydrate binding module (family 6);


Pssm-ID: 397476  Cd Length: 125  Bit Score: 94.73  E-value: 7.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 640 QAEDFSTQQGLETENTTDTGAGQNIGYTDAGDYAEY-LIYISESGYYNLNLRTAAESSAGKIEFELSHNEVTQsISTIDL 718
Cdd:pfam03422   1 QAETYDKQSGVSTEKTTDYGGGVNVGYIDNGDWIAYkDVDFGSGGAYTFTARVASGAGGGSIELRLDSPTGTL-IGTVSV 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1078671896 719 PVTGGWQSWQTTATQTTLNEGIYTLKMKVLQSG---FNMNWFEFE 760
Cdd:pfam03422  80 PSTGGWQTYVTVSANVTLPTGVHDLYLVFTGGGgylFNIDWFQFT 124
Por_Secre_tail TIGR04183
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
777-848 4.43e-15

Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.


Pssm-ID: 275036 [Multi-domain]  Cd Length: 72  Bit Score: 70.51  E-value: 4.43e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078671896 777 IFPNPFTDNFNIKLNNQQIIKDLKIMDLNGRLIKNIHPTESNGVyNLSSLKSGVYLLSIETDKGSFQKKLIK 848
Cdd:TIGR04183   1 IYPNPAKGTLIIILLSSSGKVKVEIYDLSGKLVKKTTLNNSNSI-DLSNLSSGVYIVKITTGNGTITKKIIK 71
Por_Secre_tail pfam18962
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
777-847 2.20e-14

Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.


Pssm-ID: 436869 [Multi-domain]  Cd Length: 75  Bit Score: 68.79  E-value: 2.20e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078671896 777 IFPNPFTDNFNIKLNNQQIIK-DLKIMDLNGRLIKNIHPTESNGVY--NLSSLKSGVYLLSIETDKGSFQKKLI 847
Cdd:pfam18962   1 IYPNPAKDVLNISLKNSNSSNlNISIYDILGKLVKSNSKTNGNNTKtiDVSNLSSGIYFVKINSGNGSTTKKLI 74
CBD_IV smart00606
Cellulose Binding Domain Type IV;
404-520 2.15e-13

Cellulose Binding Domain Type IV;


Pssm-ID: 128869 [Multi-domain]  Cd Length: 129  Bit Score: 67.74  E-value: 2.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896  404 NYRNDGvDIQTNTDNTNSNGYHIGFTQKNEWLKYT-VNVEETGFYNFKFRYATEQSGGKPKFFLDEVDFA--GDVTLGST 480
Cdd:smart00606  12 SYDSQS-GVQTETTSDAGGGKNVGYIDDGDWIAYKdVDFGSSGAYTFTARVASGNAGGSIELRLDSPTGTlvGTVDVPST 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1078671896  481 GGWSNF--VFQTVSNkymEAGKHILKILVDGNASYNMSSIEF 520
Cdd:smart00606  91 GGWQTYqtVSATVTL---PAGVHDVYLVFKGGNYFNIDWFRF 129
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
763-848 1.56e-12

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 71.61  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 763 SSLSTEDVIKNGVKIFPNPFTDNFNIKLNNQQIIK-DLKIMDLNGRLI--KNIHPTESNGVyNLSSLKSGVYLLSIETDK 839
Cdd:NF038113  780 TSLATNEFGANKFIIYPNPAKGEIFISFSNKDSGEvKVKVYDINGRLVlsDKVELTNTKTI-NTSGLQSGIYIVKIEGGS 858

                  ....*....
gi 1078671896 840 GSFQKKLIK 848
Cdd:NF038113  859 KSYTEKLIV 867
CBM_6 pfam03422
Carbohydrate binding module (family 6);
407-520 3.22e-12

Carbohydrate binding module (family 6);


Pssm-ID: 397476  Cd Length: 125  Bit Score: 64.30  E-value: 3.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 407 NDGVDIQTNTDNTNSNGYHIGFTQKNEWLKYT-VNVEETGFYNFKFRYATEQSGGKPKFFLDEVDFA--GDVTLGSTGGW 483
Cdd:pfam03422   6 DKQSGVSTEKTTDYGGGVNVGYIDNGDWIAYKdVDFGSGGAYTFTARVASGAGGGSIELRLDSPTGTliGTVSVPSTGGW 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1078671896 484 SNFVfqTVSNK-YMEAGKHILKILVDGNASY--NMSSIEF 520
Cdd:pfam03422  86 QTYV--TVSANvTLPTGVHDLYLVFTGGGGYlfNIDWFQF 123
swm_rep_I TIGR02059
cyanobacterial long protein repeat; This domain appears in 29 copies in a large (>10000 amino ...
524-608 1.31e-04

cyanobacterial long protein repeat; This domain appears in 29 copies in a large (>10000 amino protein in Synechococcus sp. WH8102 associated with a novel flagellar system, as one of three different repeats. Similar domains are found in two different large (<3500) proteins of Synechocystis PCC6803.


Pssm-ID: 131114 [Multi-domain]  Cd Length: 101  Bit Score: 41.80  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 524 TETIPSFNVLSASTNDDEKSLKIVLNQPLN---NQELTNNPFEVTVNNATRTITSAAIDPSNNRlIVIELAKYLFYQDEI 600
Cdd:TIGR02059  13 TAPVLLFGSTSTAVATNGNLLVLTFNEPLAditNHAPTRDQFAVTVNGAPNTVTSVSLGGSNTT-ITLTLAQVVEDGDEV 91

                  ....*...
gi 1078671896 601 KVSYIGNS 608
Cdd:TIGR02059  92 TLSYTKNS 99
 
Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
44-284 4.65e-51

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 181.01  E-value: 4.65e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896  44 FFQKQDLDSIKKWGYNSVRLAMHYNLFTPPieaepiQGENTWLETGFEMVDELLTWCEANEIYLILDMHAAPGGQGqdaa 123
Cdd:COG2730    26 NITEEDIDAIADWGFNTVRLPVSWERLQDP------DNPYTLDEAYLERVDEVVDWAKARGLYVILDLHHAPGYQG---- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 124 isdydsdkpslWESELNKSKTMALWGKLAERYKDKEWIGGYDLLNEVNWPLGDsVLRDLYVRITNEIRTYDSNHILFIEG 203
Cdd:COG2730    96 -----------WYDAATQERFIAFWRQLAERYKDYPNVLGFELLNEPHGATWA-DWNALAQRAIDAIRATNPDRLIIVEG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 204 NWF--ANDFSGLTPPWDSNMVYSFHKYWTYNDTASIQW----------------VLDLRNQHNVPLWMGESG-------E 258
Cdd:COG2730   164 NNWggAHNLRALDPLDDDNLVYSVHFYGPFVFTHQGAWfagptypanlearldnWGDWAADNGVPVFVGEFGaynddpdA 243
                         250       260
                  ....*....|....*....|....*.
gi 1078671896 259 NSNVWYTEAINLFEDNNIGWSWWPWK 284
Cdd:COG2730   244 SRLAWLRDLLDYLEENGIGWTYWSFN 269
CBM6_cellulase-like cd04080
Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including ...
363-520 2.72e-41

Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including GH5 (cellulase); This family includes carbohydrate binding module 6 (CBM6) domains that are appended to several glycoside hydrolase (GH) domains, including GH5 (cellulase) and GH16, as well as to coagulation factor 5/8 carbohydrate-binding domains. CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. The CBM6s are appended to GHs that display a diversity of substrate specificities. For some members of this family information is available about the specific substrates of the appended GH domains. It includes the CBM domains of various enzymes involved in cell wall degradation including, an extracellular beta-1,3-glucanase from Lysobacter enzymogenes encoded by the gluC gene (its catalytic domain belongs to the GH16 family), the tandem CBM domains of Pseudomonas sp. PE2 beta-1,3(4)-glucanase A (its catalytic domain also belongs to GH16), and a family 6 CBM from Cellvibrio mixtus Endoglucanase 5A (CmCBM6) which binds to the beta1,4-beta1,3-mixed linked glucans lichenan, and barley beta-glucan, cello-oligosaccharides, insoluble forms of cellulose, the beta1,3-glucan laminarin, and xylooligosaccharides, and the CBM6 of Fibrobacter succinogenes S85 XynD xylanase, appended to a GH10 domain, and Cellvibrio japonicas Cel5G appended to a GH5 (cellulase) domain. GH5 (cellulase) family includes enzymes with several known activities such as endoglucanase, beta-mannanase, and xylanase, which are involved in the degradation of cellulose and xylans. GH16 family includes enzymes with lichenase, xyloglucan endotransglycosylase (XET), and beta-agarase activities. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. For CmCBM6 it has been shown that these two binding sites have different ligand specificities.


Pssm-ID: 271146  Cd Length: 144  Bit Score: 147.76  E-value: 2.72e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 363 IPGVIYLSDYDLGTNGIAYNDIDYANYslstneykawnsGWNYRNDGVDIQTNTDNtnSNGYHIGFTQKNEWLKYTVNVE 442
Cdd:cd04080     1 IPGRIEAEDYDLGGEGVAYHDTTPGNE------------GGYYRNDGVDIETTSDT--GGGYNVGWIDAGEWLEYTVNVP 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078671896 443 ETGFYNFKFRYATEQSGGKPKFFLDEVDFAGDVTLGSTGGWSNFVFQTVSNKYMEAGKHILKILVDGNaSYNMSSIEF 520
Cdd:cd04080    67 EAGTYTVSFRVASPSGGGSLSLEVDGGTVLGTVDVPNTGGWQTWQTVTTTVVLLPAGTHTLRLVFVGG-GFNLNWFEF 143
CBM6_cellulase-like cd04080
Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including ...
635-760 1.39e-34

Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including GH5 (cellulase); This family includes carbohydrate binding module 6 (CBM6) domains that are appended to several glycoside hydrolase (GH) domains, including GH5 (cellulase) and GH16, as well as to coagulation factor 5/8 carbohydrate-binding domains. CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. The CBM6s are appended to GHs that display a diversity of substrate specificities. For some members of this family information is available about the specific substrates of the appended GH domains. It includes the CBM domains of various enzymes involved in cell wall degradation including, an extracellular beta-1,3-glucanase from Lysobacter enzymogenes encoded by the gluC gene (its catalytic domain belongs to the GH16 family), the tandem CBM domains of Pseudomonas sp. PE2 beta-1,3(4)-glucanase A (its catalytic domain also belongs to GH16), and a family 6 CBM from Cellvibrio mixtus Endoglucanase 5A (CmCBM6) which binds to the beta1,4-beta1,3-mixed linked glucans lichenan, and barley beta-glucan, cello-oligosaccharides, insoluble forms of cellulose, the beta1,3-glucan laminarin, and xylooligosaccharides, and the CBM6 of Fibrobacter succinogenes S85 XynD xylanase, appended to a GH10 domain, and Cellvibrio japonicas Cel5G appended to a GH5 (cellulase) domain. GH5 (cellulase) family includes enzymes with several known activities such as endoglucanase, beta-mannanase, and xylanase, which are involved in the degradation of cellulose and xylans. GH16 family includes enzymes with lichenase, xyloglucan endotransglycosylase (XET), and beta-agarase activities. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. For CmCBM6 it has been shown that these two binding sites have different ligand specificities.


Pssm-ID: 271146  Cd Length: 144  Bit Score: 128.89  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 635 IPGKIQAEDFST--------------------QQGLETENTTDTGAGQNIGYTDAGDYAEYLIYISESGYYNLNLRTAAE 694
Cdd:cd04080     1 IPGRIEAEDYDLggegvayhdttpgneggyyrNDGVDIETTSDTGGGYNVGWIDAGEWLEYTVNVPEAGTYTVSFRVASP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078671896 695 SSAGKIEFELSHNEVTqsiSTIDLPVTGGWQSWQT-TATQTTLNEGIYTLKMKVLQSGFNMNWFEFE 760
Cdd:cd04080    81 SGGGSLSLEVDGGTVL---GTVDVPNTGGWQTWQTvTTTVVLLPAGTHTLRLVFVGGGFNLNWFEFT 144
CBD_IV smart00606
Cellulose Binding Domain Type IV;
635-759 1.29e-25

Cellulose Binding Domain Type IV;


Pssm-ID: 128869 [Multi-domain]  Cd Length: 129  Bit Score: 102.80  E-value: 1.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896  635 IPGKIQAEDFSTQQGLETENTTDTGAGQNIGYTDAGDYAEYL-IYISESGYYNLNLRTAAESSAGKIEFELshNEVT-QS 712
Cdd:smart00606   4 PYNAIQAESYDSQSGVQTETTSDAGGGKNVGYIDDGDWIAYKdVDFGSSGAYTFTARVASGNAGGSIELRL--DSPTgTL 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1078671896  713 ISTIDLPVTGGWQSWQTTATQTTLNEGIYTL-KMKVLQSGFNMNWFEF 759
Cdd:smart00606  82 VGTVDVPSTGGWQTYQTVSATVTLPAGVHDVyLVFKGGNYFNIDWFRF 129
Cellulase pfam00150
Cellulase (glycosyl hydrolase family 5);
35-283 7.25e-24

Cellulase (glycosyl hydrolase family 5);


Pssm-ID: 395098 [Multi-domain]  Cd Length: 272  Bit Score: 102.07  E-value: 7.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896  35 TFYSNWRKNFF-QKQDLDSIKKWGYNSVRLAMHYNLFTPPieaepiQGENTWLETGFEMVDELLTWCEANEIYLILDMHA 113
Cdd:pfam00150  14 THGGQWGNPYVtTKAMIDLVKDWGFNVVRLPVSWGGYVPN------NPDYLIDENWLNRVDEVVDYAIDNGMYVIIDWHH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 114 APGGQGqdAAISDYDSDkpslweselnKSKTMALWGKLAERYKDKEWIgGYDLLNE------VNWplgDSVLRDLYVRIT 187
Cdd:pfam00150  88 DGGWPG--DPNGNIDTA----------KAFFKKIWTQIATRYGNNPNV-IFELMNEphgndqATW---ADDVKDYAQEAI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 188 NEIRTYDSNHILFIEGNWFA--NDFSGLTPPWD-SNMVYSFHKYWTYN---------DTASIQWVLDLRNQ----HNVPL 251
Cdd:pfam00150 152 DAIRAAGPNNLIIVGGNSWSqnPDGAALNDPNDdDNLIYSVHFYAPSDfsgtwfdceDPTNLAQRLRAAANwaldNGIPV 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1078671896 252 WMGESG--ENSNVWYTEA---INLFEDNNIGWSWWPW 283
Cdd:pfam00150 232 FIGEFGggNADGPCRDEAekwLDYLKENGISWTGWSN 268
CBM_6 pfam03422
Carbohydrate binding module (family 6);
640-760 7.88e-23

Carbohydrate binding module (family 6);


Pssm-ID: 397476  Cd Length: 125  Bit Score: 94.73  E-value: 7.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 640 QAEDFSTQQGLETENTTDTGAGQNIGYTDAGDYAEY-LIYISESGYYNLNLRTAAESSAGKIEFELSHNEVTQsISTIDL 718
Cdd:pfam03422   1 QAETYDKQSGVSTEKTTDYGGGVNVGYIDNGDWIAYkDVDFGSGGAYTFTARVASGAGGGSIELRLDSPTGTL-IGTVSV 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1078671896 719 PVTGGWQSWQTTATQTTLNEGIYTLKMKVLQSG---FNMNWFEFE 760
Cdd:pfam03422  80 PSTGGWQTYVTVSANVTLPTGVHDLYLVFTGGGgylFNIDWFQFT 124
Por_Secre_tail TIGR04183
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
777-848 4.43e-15

Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.


Pssm-ID: 275036 [Multi-domain]  Cd Length: 72  Bit Score: 70.51  E-value: 4.43e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078671896 777 IFPNPFTDNFNIKLNNQQIIKDLKIMDLNGRLIKNIHPTESNGVyNLSSLKSGVYLLSIETDKGSFQKKLIK 848
Cdd:TIGR04183   1 IYPNPAKGTLIIILLSSSGKVKVEIYDLSGKLVKKTTLNNSNSI-DLSNLSSGVYIVKITTGNGTITKKIIK 71
Por_Secre_tail pfam18962
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
777-847 2.20e-14

Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.


Pssm-ID: 436869 [Multi-domain]  Cd Length: 75  Bit Score: 68.79  E-value: 2.20e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078671896 777 IFPNPFTDNFNIKLNNQQIIK-DLKIMDLNGRLIKNIHPTESNGVY--NLSSLKSGVYLLSIETDKGSFQKKLI 847
Cdd:pfam18962   1 IYPNPAKDVLNISLKNSNSSNlNISIYDILGKLVKSNSKTNGNNTKtiDVSNLSSGIYFVKINSGNGSTTKKLI 74
CBM6_xylanase-like cd04084
Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 ...
638-759 3.56e-14

Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 and GH43 xylanase domains; This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family domains, including GH3, GH11, and GH43 domains. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB6s belonging to this family are Microbispora bispora GghA, a 1,4-beta-D-glucan glucohydrolase (GH3); Clostridium thermocellum xylanase U (GH11), and Penicillium purpurogenum ABF3, a bifunctional alpha-L-arabinofuranosidase/xylobiohydrolase (GH43). GH3 comprises enzymes with activities including beta-glucosidase (hydrolyzes beta-galactosidase) and beta-xylosidase (hydrolyzes 1,4-beta-D-xylosidase). GH11 family comprises enzymes with xylanase (endo-1,4-beta-xylanase) activity which catalyze the hydrolysis of beta-1,4 bonds of xylan, the major component of hemicelluloses, to generate xylooligosaccharides and xylose. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold.


Pssm-ID: 271150  Cd Length: 123  Bit Score: 69.58  E-value: 3.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 638 KIQAEDFSTQQGLETENTTDTGagQNIGYTDAGDYAeyliyisesGYYNLNL---------RTAAESSAGKIEFELshNE 708
Cdd:cd04084     2 RVEAETYADSSGVKTEATGDGG--VYVGAIDNGDWI---------AFKNVDFgsgatsftaRVASAGAGGTIEVRL--DS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1078671896 709 VT-QSISTIDLPVTGGWQSWQTTATQTTLNEGIYTLKMkVLQSG----FNMNWFEF 759
Cdd:cd04084    69 PDgPLIGTLEVPNTGGWQTWTTVSAPVTGVTGVHDLYL-VFKGGggdlFNLDWFQF 123
CBM6_agarase-like cd04079
Carbohydrate Binding Module 6 (CBM6); appended mainly to glycoside hydrolase (GH) family 16 ...
638-760 4.30e-14

Carbohydrate Binding Module 6 (CBM6); appended mainly to glycoside hydrolase (GH) family 16 alpha- and beta agarases; This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family 16 agarases. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the activity of alpha- and beta-agarase catalytic modules which are involved in the hydrolysis of 1,4-beta-D-galactosidic linkages. These CBM6s bind specifically to the non-reducing end of agarose chains, recognizing only the first repeat of the disaccharide, and directing the appended catalytic modules to areas of the plant cell wall attacked by beta-agarases. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. This family includes three tandem CBM6s from the Saccharophagus degradans agarase Aga86E, and three tandem CBM6s from Vibrio sp. strain PO-303 AgaA; in both these proteins these are appended to a GH16 domain. Vibrio AgaA also contains a Big-2-like protein-protein interaction domain. This family also includes two tandem CBM6s from an endo-type beta-agarase from a deep-sea Microbulbifer-like isolate, which are appended to a GH16 domain, and two of three CBM6s of Alteromonas agarilytica AgaA alpha-agarase, which are appended to a GH96 domain.


Pssm-ID: 271145  Cd Length: 134  Bit Score: 69.98  E-value: 4.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 638 KIQAEDFSTQQG-----LETENTTDTGAGQNIGYTDAGDYAEYLIYISESGYYNLNLRTAAESSAGKIEFELSHNEVtqs 712
Cdd:cd04079     5 VIEAESFTATGGtfddgPDGVSGYSVNGGTAINYVNTGDYADYTVNVPEAGTYSVEYLIGTPVSGAAIELLVDGNSV--- 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1078671896 713 iSTIDLPVTGGWQSWQTTATQTTLNEGIYTLKMKVLQSG-----FNMNWFEFE 760
Cdd:cd04079    82 -ATTAVPNTGGWDNFQALTLASTVNLTAGTHTIRLTAAGsndwqWNLDKFTLT 133
CBD_IV smart00606
Cellulose Binding Domain Type IV;
404-520 2.15e-13

Cellulose Binding Domain Type IV;


Pssm-ID: 128869 [Multi-domain]  Cd Length: 129  Bit Score: 67.74  E-value: 2.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896  404 NYRNDGvDIQTNTDNTNSNGYHIGFTQKNEWLKYT-VNVEETGFYNFKFRYATEQSGGKPKFFLDEVDFA--GDVTLGST 480
Cdd:smart00606  12 SYDSQS-GVQTETTSDAGGGKNVGYIDDGDWIAYKdVDFGSSGAYTFTARVASGNAGGSIELRLDSPTGTlvGTVDVPST 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1078671896  481 GGWSNF--VFQTVSNkymEAGKHILKILVDGNASYNMSSIEF 520
Cdd:smart00606  91 GGWQTYqtVSATVTL---PAGVHDVYLVFKGGNYFNIDWFRF 129
CBM6-CBM35-CBM36_like cd02795
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module ...
638-759 1.15e-12

Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality.


Pssm-ID: 271143  Cd Length: 124  Bit Score: 65.67  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 638 KIQAED-FSTQQGLETENTTDTGAGQNIGYTDAGDYAEYLIYISESGYYNLNLRTAAESSAGKIEFELSHNevTQSISTI 716
Cdd:cd02795     1 RIEAEDaTLTGGTAVSTAAGASGGGYVIGFSSGGDSVTFTVTVPKAGTYRLAVRYASPNGNGSRSVSLDGN--GKLVGTI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1078671896 717 DLPVTGGWQSWQTTATQTTLN-EGIYTLKMKVLQSGFNMN--WFEF 759
Cdd:cd02795    79 TVPSTGGWDTWGTASVSVNLPdAGGHTLKIVGTGDNGGANidYVVV 124
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
763-848 1.56e-12

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 71.61  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 763 SSLSTEDVIKNGVKIFPNPFTDNFNIKLNNQQIIK-DLKIMDLNGRLI--KNIHPTESNGVyNLSSLKSGVYLLSIETDK 839
Cdd:NF038113  780 TSLATNEFGANKFIIYPNPAKGEIFISFSNKDSGEvKVKVYDINGRLVlsDKVELTNTKTI-NTSGLQSGIYIVKIEGGS 858

                  ....*....
gi 1078671896 840 GSFQKKLIK 848
Cdd:NF038113  859 KSYTEKLIV 867
CBM_6 pfam03422
Carbohydrate binding module (family 6);
407-520 3.22e-12

Carbohydrate binding module (family 6);


Pssm-ID: 397476  Cd Length: 125  Bit Score: 64.30  E-value: 3.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 407 NDGVDIQTNTDNTNSNGYHIGFTQKNEWLKYT-VNVEETGFYNFKFRYATEQSGGKPKFFLDEVDFA--GDVTLGSTGGW 483
Cdd:pfam03422   6 DKQSGVSTEKTTDYGGGVNVGYIDNGDWIAYKdVDFGSGGAYTFTARVASGAGGGSIELRLDSPTGTliGTVSVPSTGGW 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1078671896 484 SNFVfqTVSNK-YMEAGKHILKILVDGNASY--NMSSIEF 520
Cdd:pfam03422  86 QTYV--TVSANvTLPTGVHDLYLVFTGGGGYlfNIDWFQF 123
CBM6_agarase-like cd04079
Carbohydrate Binding Module 6 (CBM6); appended mainly to glycoside hydrolase (GH) family 16 ...
407-522 6.15e-11

Carbohydrate Binding Module 6 (CBM6); appended mainly to glycoside hydrolase (GH) family 16 alpha- and beta agarases; This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family 16 agarases. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the activity of alpha- and beta-agarase catalytic modules which are involved in the hydrolysis of 1,4-beta-D-galactosidic linkages. These CBM6s bind specifically to the non-reducing end of agarose chains, recognizing only the first repeat of the disaccharide, and directing the appended catalytic modules to areas of the plant cell wall attacked by beta-agarases. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. This family includes three tandem CBM6s from the Saccharophagus degradans agarase Aga86E, and three tandem CBM6s from Vibrio sp. strain PO-303 AgaA; in both these proteins these are appended to a GH16 domain. Vibrio AgaA also contains a Big-2-like protein-protein interaction domain. This family also includes two tandem CBM6s from an endo-type beta-agarase from a deep-sea Microbulbifer-like isolate, which are appended to a GH16 domain, and two of three CBM6s of Alteromonas agarilytica AgaA alpha-agarase, which are appended to a GH96 domain.


Pssm-ID: 271145  Cd Length: 134  Bit Score: 60.73  E-value: 6.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 407 NDGVDIQTNTDNTNsngyhIGFTQKNEWLKYTVNVEETGFYNFKFRYATEQSGGKPKFFLDEVDFAGDvTLGSTGGWSNF 486
Cdd:cd04079    22 PDGVSGYSVNGGTA-----INYVNTGDYADYTVNVPEAGTYSVEYLIGTPVSGAAIELLVDGNSVATT-AVPNTGGWDNF 95
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1078671896 487 V-FQTVSNKYMEAGKHILKILVDGNASY--NMSSIEFLK 522
Cdd:cd04079    96 QaLTLASTVNLTAGTHTIRLTAAGSNDWqwNLDKFTLTK 134
CBM35_pectate_lyase-like cd04082
Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes ...
639-745 3.22e-10

Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans; This family includes carbohydrate binding module family 35 (CBM35) domains that are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. Included in this family are CBM35s of pectate lyases, including pectate lyase 10A from Cellvibrio japonicas, these enzymes release delta-4,5-anhydrogalaturonic acid (delta4,5-GalA) from pectin, thus identifying a signature molecule for plant cell wall degradation. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. Some CBM35s bind their ligands in a calcium-dependent manner, especially those binding uronic acids.


Pssm-ID: 271148  Cd Length: 124  Bit Score: 58.34  E-value: 3.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 639 IQAEDFSTQQG-LETENTTDTGAGqnigYTD----AGDYAEYLIYISESGYYNLNLRTAAESSA---GKIEfelshneV- 709
Cdd:cd04082     3 YQAEDASVDQGvIESNHAGYTGSG----FVNtdnaVGSYIEWTVNAPTAGTYTLTFRYANGSTSnrpADIS-------Vn 71
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1078671896 710 -TQSISTIDLPVTGGWQSWQTTATQTTLNEGIYTLKM 745
Cdd:cd04082    72 gNTVAATLSFPSTGAWTTWATSSVTVPLNAGTNTIRL 108
DUF5010_C pfam18099
DUF5010 C-terminal domain; This domain is found at the end of a family of putative glycosyl ...
406-514 1.01e-09

DUF5010 C-terminal domain; This domain is found at the end of a family of putative glycosyl hydrolases pfam16402. This domain is likely to function as a carbohydrate binding domain due to its similarity with pfam03422.


Pssm-ID: 407934  Cd Length: 112  Bit Score: 56.75  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 406 RNDGVDIQTNTDnTNSnGYHIGFTQKNEWLKYTVNVEETGFYNFKFRYATEQSGGKPKFFLDEVDFAgDVTLGSTGGWSN 485
Cdd:pfam18099   1 RSGNIDIQPTPD-TGG-GWNVTSTAAGEWLEWKEIPLQAGTVTFKVRYATPTEGAKMRFVVDGVAGP-TVTLPATGGWQN 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1078671896 486 FVFQTVSNKYMEAGK-HILKI-LVDGNASYN 514
Cdd:pfam18099  78 WVTVDAGTFTIDAGTyHTVRLeFVAGGIDLN 108
DUF5010_C pfam18099
DUF5010 C-terminal domain; This domain is found at the end of a family of putative glycosyl ...
650-757 1.27e-09

DUF5010 C-terminal domain; This domain is found at the end of a family of putative glycosyl hydrolases pfam16402. This domain is likely to function as a carbohydrate binding domain due to its similarity with pfam03422.


Pssm-ID: 407934  Cd Length: 112  Bit Score: 56.37  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 650 LETENTTDTGAGQNIGYTDAGDYAEYLIYISESGYYNLNLRTAAESSAGKIEFELShnevTQSISTIDLPVTGGWQSWQT 729
Cdd:pfam18099   5 IDIQPTPDTGGGWNVTSTAAGEWLEWKEIPLQAGTVTFKVRYATPTEGAKMRFVVD----GVAGPTVTLPATGGWQNWVT 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1078671896 730 -TATQTTLNEGIY-TLKMKVLQSGFNMNWF 757
Cdd:pfam18099  81 vDAGTFTIDAGTYhTVRLEFVAGGIDLNYW 110
COG3934 COG3934
Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism];
49-283 3.98e-07

Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism];


Pssm-ID: 443135 [Multi-domain]  Cd Length: 331  Bit Score: 53.05  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896  49 DLDSIKKWGYNSVRLamhyNLFTPPIEAEPiqgeNTWLETGFEMVDELLTWCEANEIYLILDM--HAAPGGQGQ------ 120
Cdd:COG3934    34 ELDDLAALGLDVVRV----FLLWEDFQPNP----GLINEEALERLDYFLDAAAERGLKVVLTLfnNWWSGHMSGynwlps 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 121 ---DAAISDYDSDKPSlweselnKSKTMALWGKLAERYKDKEWIGGYDLLNEVNwPLGDSVLRDLYV----RITNEIRTY 193
Cdd:COG3934   106 wvgGWHRRNFYTDPEA-------VEAQKAYVRTLANRYKDDPAILGWELGNEPR-NFGDPASPEAALawlrEMAAAIKSL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 194 DSNHILFIeGNWFANDFSGLTPPWDSNM-----VYSFH---KYW-TYNDTASIQW---VLDLRNQHNVPLWMGE------ 255
Cdd:COG3934   178 DPNHLVSS-GDEGDYWEVDDHPFVPAHAaplidYLTVHlypFNWgWVDRPRSTDKaayLIELARALGKPVVLEEfgaprd 256
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1078671896 256 ----SGENSNVWYTEAINLFEDNN--IGWSWWPW 283
Cdd:COG3934   257 spqaSEEDRAEFYRTVLEAALTLAgaAGANWWCF 290
CBM35_mannanase-like cd04086
Carbohydrate Binding Module 35 (CBM35); appended to several carbohydrate binding enzymes, ...
409-505 7.61e-07

Carbohydrate Binding Module 35 (CBM35); appended to several carbohydrate binding enzymes, including several glycoside hydrolase (GH) family 26 mannanase domains; This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes, including periplasmic component of ABC-type sugar transport system involved in carbohydrate transport and metabolism, and several glycoside hydrolase (GH) domains, including GH26. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB35s belonging to this family are mannanase A from Clostridium thermocellum (GH26), Man26B from Paenibacillus sp. BME-14 (GH26), and the multifunctional Cel44C-Man26A from Paenibacillus polymyxa GS01 (which has two GH domains, GH44 and GH26). GH26 mainly includes mannan endo-1,4-beta-mannosidase which hydrolyzes 1,4-beta-D-linkages in mannans, galacto-mannans, glucomannans, and galactoglucomannans, but displays little activity towards other plant cell wall polysaccharides. A few proteins belonging to this family have additional CBM3 domains; these CBM3s are not found in the CBM6-CBM35-CBM36_like superfamily.


Pssm-ID: 271152  Cd Length: 119  Bit Score: 48.75  E-value: 7.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 409 GVDIQTNTDNTNSNGYHIGFTQKNEWLKYTVNVEETGFYNFKFRYATEQSGGKPKFFLDEVdFAGDVTLGSTGGWSNFVF 488
Cdd:cd04086    12 GVTVATSRSGYSGTGYVTGFDDDGDSLTFTVNVPEAGLYDLVIRYAAPYGDKENNLYVNGT-SVGEISFPATTKFTEVSA 90
                          90
                  ....*....|....*..
gi 1078671896 489 QTVsnkYMEAGKHILKI 505
Cdd:cd04086    91 GKV---LLNAGENTITI 104
CBM35_Lmo2446-like cd04083
Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446; This family includes ...
640-746 7.75e-06

Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446; This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases.


Pssm-ID: 271149  Cd Length: 125  Bit Score: 46.09  E-value: 7.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 640 QAEDFSTQQGL--ETENTTDTGAGQNIGYTDAGDYAEYLIYISESGYYNLNLRTAAESSAGKiefelshnevTQSIS--- 714
Cdd:cd04083     4 EAENAALSGGAvvNTDHAGYSGTGFVDGFATAGASVTFTVNVPAAGTYTLTLRYANGTGSAK----------TLSLYvng 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1078671896 715 ----TIDLPVTGGWQSWQTTATQTTLNEGIYTLKMK 746
Cdd:cd04083    74 tkvkQVSLPSTGSWDTWGTATETVTLRAGTNTIELR 109
CBM6-CBM35-CBM36_like cd02795
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module ...
423-510 1.28e-05

Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality.


Pssm-ID: 271143  Cd Length: 124  Bit Score: 45.26  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 423 GYHIGFTQKNEWLKYTVNVEETGFYNFKFRYATEQSGGKPKFFLDEVDF-AGDVTLGSTGGWSNFVFQTVSNKYMEAGKH 501
Cdd:cd02795    25 GYVIGFSSGGDSVTFTVTVPKAGTYRLAVRYASPNGNGSRSVSLDGNGKlVGTITVPSTGGWDTWGTASVSVNLPDAGGH 104

                  ....*....
gi 1078671896 502 ILKILVDGN 510
Cdd:cd02795   105 TLKIVGTGD 113
swm_rep_I TIGR02059
cyanobacterial long protein repeat; This domain appears in 29 copies in a large (>10000 amino ...
524-608 1.31e-04

cyanobacterial long protein repeat; This domain appears in 29 copies in a large (>10000 amino protein in Synechococcus sp. WH8102 associated with a novel flagellar system, as one of three different repeats. Similar domains are found in two different large (<3500) proteins of Synechocystis PCC6803.


Pssm-ID: 131114 [Multi-domain]  Cd Length: 101  Bit Score: 41.80  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 524 TETIPSFNVLSASTNDDEKSLKIVLNQPLN---NQELTNNPFEVTVNNATRTITSAAIDPSNNRlIVIELAKYLFYQDEI 600
Cdd:TIGR02059  13 TAPVLLFGSTSTAVATNGNLLVLTFNEPLAditNHAPTRDQFAVTVNGAPNTVTSVSLGGSNTT-ITLTLAQVVEDGDEV 91

                  ....*...
gi 1078671896 601 KVSYIGNS 608
Cdd:TIGR02059  92 TLSYTKNS 99
CBM35_pectate_lyase-like cd04082
Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes ...
415-505 3.08e-04

Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans; This family includes carbohydrate binding module family 35 (CBM35) domains that are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. Included in this family are CBM35s of pectate lyases, including pectate lyase 10A from Cellvibrio japonicas, these enzymes release delta-4,5-anhydrogalaturonic acid (delta4,5-GalA) from pectin, thus identifying a signature molecule for plant cell wall degradation. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. Some CBM35s bind their ligands in a calcium-dependent manner, especially those binding uronic acids.


Pssm-ID: 271148  Cd Length: 124  Bit Score: 41.39  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 415 NTDNTNsnGYHIgftqknEWlkyTVNVEETGFYNFKFRYATEQSGGKP-KFFLDEVDFAGDVTLGSTGGWSNFVFQTVsN 493
Cdd:cd04082    29 NTDNAV--GSYI------EW---TVNAPTAGTYTLTFRYANGSTSNRPaDISVNGNTVAATLSFPSTGAWTTWATSSV-T 96
                          90
                  ....*....|..
gi 1078671896 494 KYMEAGKHILKI 505
Cdd:cd04082    97 VPLNAGTNTIRL 108
CBM6_xylanase-like cd04084
Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 ...
416-520 3.27e-03

Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 and GH43 xylanase domains; This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family domains, including GH3, GH11, and GH43 domains. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB6s belonging to this family are Microbispora bispora GghA, a 1,4-beta-D-glucan glucohydrolase (GH3); Clostridium thermocellum xylanase U (GH11), and Penicillium purpurogenum ABF3, a bifunctional alpha-L-arabinofuranosidase/xylobiohydrolase (GH43). GH3 comprises enzymes with activities including beta-glucosidase (hydrolyzes beta-galactosidase) and beta-xylosidase (hydrolyzes 1,4-beta-D-xylosidase). GH11 family comprises enzymes with xylanase (endo-1,4-beta-xylanase) activity which catalyze the hydrolysis of beta-1,4 bonds of xylan, the major component of hemicelluloses, to generate xylooligosaccharides and xylose. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold.


Pssm-ID: 271150  Cd Length: 123  Bit Score: 38.38  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 416 TDNTNSNGYHIGFTQKNEWLKYTvNVE-ETGFYNFKFRYATEQSGGKPKFFLDEVD--FAGDVTLGSTGGWSNFVFQTVS 492
Cdd:cd04084    16 TEATGDGGVYVGAIDNGDWIAFK-NVDfGSGATSFTARVASAGAGGTIEVRLDSPDgpLIGTLEVPNTGGWQTWTTVSAP 94
                          90       100       110
                  ....*....|....*....|....*....|
gi 1078671896 493 NKYMeAGKHILKILVDGNASY--NMSSIEF 520
Cdd:cd04084    95 VTGV-TGVHDLYLVFKGGGGDlfNLDWFQF 123
CBM35_Lmo2446-like cd04083
Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446; This family includes ...
414-512 7.68e-03

Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446; This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases.


Pssm-ID: 271149  Cd Length: 125  Bit Score: 37.23  E-value: 7.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078671896 414 TNTDNTN--SNGYHIGFTQKNEWLKYTVNVEETGFYNFKFRYATeqSGGKPKFFLDEVD--FAGDVTLGSTGGWSNF--V 487
Cdd:cd04083    16 VNTDHAGysGTGFVDGFATAGASVTFTVNVPAAGTYTLTLRYAN--GTGSAKTLSLYVNgtKVKQVSLPSTGSWDTWgtA 93
                          90       100
                  ....*....|....*....|....*
gi 1078671896 488 FQTVsnkYMEAGKHILKILVDGNAS 512
Cdd:cd04083    94 TETV---TLRAGTNTIELRYDAGDS 115
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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