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Conserved domains on  [gi|1099704529|emb|SFD66193|]
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glucosylceramidase [Paenibacillus catalpae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_hydro_30 super family cl23815
Glycosyl hydrolase family 30 TIM-barrel domain;
55-482 4.73e-86

Glycosyl hydrolase family 30 TIM-barrel domain;


The actual alignment was detected with superfamily member COG5520:

Pssm-ID: 329099 [Multi-domain]  Cd Length: 433  Bit Score: 288.72  E-value: 4.73e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529   55 PDVAFETNGAPAELTIDLDENTKYQTIDGFGGslTDSSAYVIsqmdeQAKDALMNKLFSREGDGAGFSYLRLPMGASDFA 134
Cdd:COG5520     21 PFVSGSTEVLAASEDITVNVAAKHQVIRGFGG--MNSSAWAG-----DLSAAQLETLFGNGANQLGFSILRVPIDSNDFS 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  135 TSiytyddmpaGESDPELEHFSIAHDSayiipllqqaleINPDLKIMGTPWSAPGWMKTTDS---SIKGKLKEEYYGAYA 211
Cdd:COG5520     94 LG---------GSADNWYKELSTAKSA------------INPGMIVFASPWSPPASMKTTNNrngGNAGRLKYEKYADYA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  212 QYFVKFIEAYEAAGIPIDAVTLQNEPHFEPgDYPGMRMEPEDQAKFVKDYLGPAFETaeidTKIVVWDHNWSEPQYPIDV 291
Cdd:COG5520    153 DYLNDFVLEMKNNGVNLYALSVQNEPDYAP-TYDWCWWTPQEELRFMRQYLASINAE----MRVIIPESFKDLPNMSDPI 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  292 LNDADAKKYIAGSAFHGYAGNVSAQSLVYDQHP--DKDIYFTESSGGEFSPDFAGNVQWD-FQNLIIGATRNWARTSLKW 368
Cdd:COG5520    228 LNDPKALANMDILGTHLYGGQVSDQPYPLAKQKpaGKDLWMTECYPPESDPNSADREALHvALHIHIGMTEGGFQAYVWW 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  369 NIALDENHGPYVGGCKD---CRGIVTVNSSTDE--VTYNEEFYAFGQASKFVLPGAQRIKSNTFGA-GSIEDVAFVNPDG 442
Cdd:COG5520    308 NIRLDYGGGPNHGGNSKrgyCMAHFSKFVQNGYvrLDATKSPYGNVYVSAYVGPNKVVIVAINKGTyPVNQSFNFQNPDG 387
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1099704529  443 SKVLLALNSSKEPKDF--KVRWGAKSFAYTLPAGAAASFVWN 482
Cdd:COG5520    388 SNVSSWVNSSTLNMAKtsNILAAGGRFNASLPAQSVTTFVWD 429
CBM6_xylanase-like cd04084
Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 ...
498-612 7.90e-31

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: 118.11  E-value: 7.90e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  498 QAEDYSESNGITTAVTTDtgGGKYAGSSSDGSYIAFDHVEFLNGTASVKVRAQAQGDGG-IEFRLDAPDGAYAGGIDLTD 576
Cdd:cd04084      4 EAETYADSSGVKTEATGD--GGVYVGAIDNGDWIAFKNVDFGSGATSFTARVASAGAGGtIEVRLDSPDGPLIGTLEVPN 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1099704529  577 TNG--SWITKAAQVEAVTGKHKLYVVFRGK----VNLNWFQF 612
Cdd:cd04084     82 TGGwqTWTTVSAPVTGVTGVHDLYLVFKGGggdlFNLDWFQF 123
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
1132-1261 6.77e-11

Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only];


:

Pssm-ID: 227779 [Multi-domain]  Cd Length: 329  Bit Score: 65.59  E-value: 6.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529 1132 ATVGVTGVTLDKAELSLNLSnmKTGTLTAAVQPGDAENHNVYWSSSNSSVAAVAG--GVVTAKGVGTAEITVTTEDGGFT 1209
Cdd:COG5492    177 SIVPVTGITVNKTSDTLKVG--DTDTLTATVTPDNATDKTVTWTSSDPSKATVDDntGKITAVAAGTANITATTNDGSKT 254
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1099704529 1210 AKANVTVSSgeTTPTNPTDPNGAGNTTGPvvtkdgtGSTISGFTSKTETDPN 1261
Cdd:COG5492    255 ATCKVTVNK--ATDLTVSYNAHVTNTGWQ-------TDASDKVVAGTSSNSN 297
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
759-967 3.16e-10

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 225936 [Multi-domain]  Cd Length: 343  Bit Score: 63.37  E-value: 3.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  759 FDDVELTPVitkapsaaqgtDAPETPQGVSAELDGGHNIKLAWTSVPGAEGYKIYRSTadsattaggvYPDYRLIGLASG 838
Cdd:COG3401    154 FTGVEATPK-----------AEPKEITNVRVSFDLGNNIELSEDGSEAEDYYRIYASD----------SGNEEYGFIAQT 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  839 EATSYVD--QGLrGSTAYSYRVTAFNTTGESAASVSDIATTAAGSdtaaPAAPASLIAEPGIEQVMLVWEPNAETDFLKY 916
Cdd:COG3401    213 TENSYYDvkEGL-GAVEYYKVTTVDNTGFESDLPNEPTVGETGGR----YEVPTIPGETTEASFIGVAAEQNQLRQAVTY 287
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1099704529  917 NVY-VNGFKRASVDPAPESRYTVTNLKAGTRYTFTVKAVDQAGNESAASNAV 967
Cdd:COG3401    288 TVYrVEDGTPTKFFTITETDGQDNDMLTGVEYRYEVVAVDKAGLSSHPSKEV 339
SLH pfam00395
S-layer homology domain;
1463-1502 9.15e-08

S-layer homology domain;


:

Pssm-ID: 306825  Cd Length: 41  Bit Score: 49.49  E-value: 9.15e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1099704529 1463 FRDTKGHWAEKEINALASSFIVNGVTADQFAPEQQLTRAE 1502
Cdd:pfam00395    1 FKDVKSHWWAEAVQALAELGIISGYPDGTFRPNKPITRAE 40
SLH pfam00395
S-layer homology domain;
1542-1563 5.23e-05

S-layer homology domain;


:

Pssm-ID: 306825  Cd Length: 41  Bit Score: 41.79  E-value: 5.23e-05
                           10        20
                   ....*....|....*....|..
gi 1099704529 1542 GIIQGFTDGTFRPNDKMTRQQM 1563
Cdd:pfam00395   20 GIISGYPDGTFRPNKPITRAEA 41
SLH pfam00395
S-layer homology domain;
1606-1630 9.72e-03

S-layer homology domain;


:

Pssm-ID: 306825  Cd Length: 41  Bit Score: 35.24  E-value: 9.72e-03
                           10        20
                   ....*....|....*....|....*
gi 1099704529 1606 LKSGLIKGTPEGRYYPNKTATRAEA 1630
Cdd:pfam00395   17 AELGIISGYPDGTFRPNKPITRAEA 41
 
Name Accession Description Interval E-value
XynC COG5520
O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis];
55-482 4.73e-86

O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 227807 [Multi-domain]  Cd Length: 433  Bit Score: 288.72  E-value: 4.73e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529   55 PDVAFETNGAPAELTIDLDENTKYQTIDGFGGslTDSSAYVIsqmdeQAKDALMNKLFSREGDGAGFSYLRLPMGASDFA 134
Cdd:COG5520     21 PFVSGSTEVLAASEDITVNVAAKHQVIRGFGG--MNSSAWAG-----DLSAAQLETLFGNGANQLGFSILRVPIDSNDFS 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  135 TSiytyddmpaGESDPELEHFSIAHDSayiipllqqaleINPDLKIMGTPWSAPGWMKTTDS---SIKGKLKEEYYGAYA 211
Cdd:COG5520     94 LG---------GSADNWYKELSTAKSA------------INPGMIVFASPWSPPASMKTTNNrngGNAGRLKYEKYADYA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  212 QYFVKFIEAYEAAGIPIDAVTLQNEPHFEPgDYPGMRMEPEDQAKFVKDYLGPAFETaeidTKIVVWDHNWSEPQYPIDV 291
Cdd:COG5520    153 DYLNDFVLEMKNNGVNLYALSVQNEPDYAP-TYDWCWWTPQEELRFMRQYLASINAE----MRVIIPESFKDLPNMSDPI 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  292 LNDADAKKYIAGSAFHGYAGNVSAQSLVYDQHP--DKDIYFTESSGGEFSPDFAGNVQWD-FQNLIIGATRNWARTSLKW 368
Cdd:COG5520    228 LNDPKALANMDILGTHLYGGQVSDQPYPLAKQKpaGKDLWMTECYPPESDPNSADREALHvALHIHIGMTEGGFQAYVWW 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  369 NIALDENHGPYVGGCKD---CRGIVTVNSSTDE--VTYNEEFYAFGQASKFVLPGAQRIKSNTFGA-GSIEDVAFVNPDG 442
Cdd:COG5520    308 NIRLDYGGGPNHGGNSKrgyCMAHFSKFVQNGYvrLDATKSPYGNVYVSAYVGPNKVVIVAINKGTyPVNQSFNFQNPDG 387
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1099704529  443 SKVLLALNSSKEPKDF--KVRWGAKSFAYTLPAGAAASFVWN 482
Cdd:COG5520    388 SNVSSWVNSSTLNMAKtsNILAAGGRFNASLPAQSVTTFVWD 429
Glyco_hydro_30 pfam02055
Glycosyl hydrolase family 30 TIM-barrel domain;
81-415 1.02e-54

Glycosyl hydrolase family 30 TIM-barrel domain;


Pssm-ID: 307945  Cd Length: 348  Bit Score: 195.15  E-value: 1.02e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529   81 IDGFGGSLTDSSAYVISQMDEQAKDALMNKLFSREGdgAGFSYLRLPMGASDFATSIYTYDDMPageSDPELEHFSIA-H 159
Cdd:pfam02055    1 IQGFGSTFSDASGANLKSLPDPAQDLILKQYFSDEG--LNLQFGRVPIASCDFSIRVYTYADTP---DDYQMHNFSLPeE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  160 DSAYIIPLLQQALEINPDLKIMGTPWSAPGWMKTTDS-----SIKGKLKEEYYGAYAQYFVKFIEAYEAAGIPIDAVTLQ 234
Cdd:pfam02055   76 DTQWKIPYIHRAQKYNQRLKLFASPWTAPGWLKTTGAvngkgSLKGQPGDIYHQTYARYFVKFLEEYAKHGIQFWGLSTQ 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  235 NEPhfEPGDYPGMRME-----PEDQAKFVKDYLGPAF--ETAEIDTKIVVWDHNWSE-PQYPIDVLNDADAKKYIAGSAF 306
Cdd:pfam02055  156 NEP--TAGSDKKYKFQslgftAEHQRDFIKRDLGPALanSTHGKNVKLLILDDNRGNlPKWADTVLNDPDAAKYVHGIAV 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  307 HGYAGNVSAQSL--VYDQHPDKDIYFTESSGGEFSPDFAGNV-QWD----FQNLIIGATRNWARTSLKWNIALDENHGP- 378
Cdd:pfam02055  234 HWYQDAEADAHLgeTHRLHPNTFIFGTEASEGSKSKDQSVDYgSWDramdYSSDILDNLNNWVTGWTERNLALDAEGGPs 313
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1099704529  379 YVGGCKDCRgiVTVNSSTDEVTYNEEFYAFGQASKFV 415
Cdd:pfam02055  314 WVSNFVDAP--VIAFPAKAQFYKQPMFYAIAHFSHFI 348
CBM6_xylanase-like cd04084
Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 ...
498-612 7.90e-31

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: 118.11  E-value: 7.90e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  498 QAEDYSESNGITTAVTTDtgGGKYAGSSSDGSYIAFDHVEFLNGTASVKVRAQAQGDGG-IEFRLDAPDGAYAGGIDLTD 576
Cdd:cd04084      4 EAETYADSSGVKTEATGD--GGVYVGAIDNGDWIAFKNVDFGSGATSFTARVASAGAGGtIEVRLDSPDGPLIGTLEVPN 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1099704529  577 TNG--SWITKAAQVEAVTGKHKLYVVFRGK----VNLNWFQF 612
Cdd:cd04084     82 TGGwqTWTTVSAPVTGVTGVHDLYLVFKGGggdlFNLDWFQF 123
CBD_IV smart00606
Cellulose Binding Domain Type IV;
490-612 6.45e-23

Cellulose Binding Domain Type IV;


Pssm-ID: 128869  Cd Length: 129  Bit Score: 95.48  E-value: 6.45e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529   490 SISPYAALQAEDYSESNGITTAVTTDTGGGKYAGSSSDGSYIAFDHVEFLN-GTASVKVRAQAQGDGG-IEFRLDAPDGA 567
Cdd:smart00606    1 GRDPYNAIQAESYDSQSGVQTETTSDAGGGKNVGYIDDGDWIAYKDVDFGSsGAYTFTARVASGNAGGsIELRLDSPTGT 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1099704529   568 YAGGIDLTDTNG--SWITKAAQVEAVTGKHKLYVVFRG--KVNLNWFQF 612
Cdd:smart00606   81 LVGTVDVPSTGGwqTYQTVSATVTLPAGVHDVYLVFKGgnYFNIDWFRF 129
CBM_6 pfam03422
Carbohydrate binding module (family 6);
498-613 2.26e-21

Carbohydrate binding module (family 6);


Pssm-ID: 308816  Cd Length: 125  Bit Score: 90.88  E-value: 2.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  498 QAEDYSESNGITTAVTTDTGGGKYAGSSSDGSYIAFDHVEF-LNGTASVKVRAQAQGDGG-IEFRLDAPDGAYAGGIDLT 575
Cdd:pfam03422    1 QAETYDKQSGVSTEKTTDYGGGVNVGYIDNGDWIAYKDVDFgSGGAYTFTARVASGAGGGsIELRLDSPTGTLIGTVSVP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1099704529  576 DTNG--SWITKAAQVEAVTGKHKLYVVFRGK----VNLNWFQFS 613
Cdd:pfam03422   81 STGGwqTYVTVSANVTLPTGVHDLYLVFTGGggylFNIDWFQFT 124
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
1132-1261 6.77e-11

Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only];


Pssm-ID: 227779 [Multi-domain]  Cd Length: 329  Bit Score: 65.59  E-value: 6.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529 1132 ATVGVTGVTLDKAELSLNLSnmKTGTLTAAVQPGDAENHNVYWSSSNSSVAAVAG--GVVTAKGVGTAEITVTTEDGGFT 1209
Cdd:COG5492    177 SIVPVTGITVNKTSDTLKVG--DTDTLTATVTPDNATDKTVTWTSSDPSKATVDDntGKITAVAAGTANITATTNDGSKT 254
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1099704529 1210 AKANVTVSSgeTTPTNPTDPNGAGNTTGPvvtkdgtGSTISGFTSKTETDPN 1261
Cdd:COG5492    255 ATCKVTVNK--ATDLTVSYNAHVTNTGWQ-------TDASDKVVAGTSSNSN 297
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
759-967 3.16e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 225936 [Multi-domain]  Cd Length: 343  Bit Score: 63.37  E-value: 3.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  759 FDDVELTPVitkapsaaqgtDAPETPQGVSAELDGGHNIKLAWTSVPGAEGYKIYRSTadsattaggvYPDYRLIGLASG 838
Cdd:COG3401    154 FTGVEATPK-----------AEPKEITNVRVSFDLGNNIELSEDGSEAEDYYRIYASD----------SGNEEYGFIAQT 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  839 EATSYVD--QGLrGSTAYSYRVTAFNTTGESAASVSDIATTAAGSdtaaPAAPASLIAEPGIEQVMLVWEPNAETDFLKY 916
Cdd:COG3401    213 TENSYYDvkEGL-GAVEYYKVTTVDNTGFESDLPNEPTVGETGGR----YEVPTIPGETTEASFIGVAAEQNQLRQAVTY 287
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1099704529  917 NVY-VNGFKRASVDPAPESRYTVTNLKAGTRYTFTVKAVDQAGNESAASNAV 967
Cdd:COG3401    288 TVYrVEDGTPTKFFTITETDGQDNDMLTGVEYRYEVVAVDKAGLSSHPSKEV 339
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
781-877 2.43e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.58  E-value: 2.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  781 PETPQGVSAELDGGHNIKLAWTSVPGA----EGYKIYRSTADSattaggvyPDYRLIGLASGEATSYVDQGLRGSTAYSY 856
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpiTGYVVEYREKGS--------GDWKEVEVTPGSETSYTLTGLKPGTEYEF 72
                           90       100
                   ....*....|....*....|.
gi 1099704529  857 RVTAFNTTGESAASVSDIATT 877
Cdd:cd00063     73 RVRAVNGGGESPPSESVTVTT 93
SLH pfam00395
S-layer homology domain;
1463-1502 9.15e-08

S-layer homology domain;


Pssm-ID: 306825  Cd Length: 41  Bit Score: 49.49  E-value: 9.15e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1099704529 1463 FRDTKGHWAEKEINALASSFIVNGVTADQFAPEQQLTRAE 1502
Cdd:pfam00395    1 FKDVKSHWWAEAVQALAELGIISGYPDGTFRPNKPITRAE 40
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
886-958 3.95e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.15  E-value: 3.95e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529   886 PAAPASLIAEP-GIEQVMLVWEPNAETDFLKYNVYVNGFKRASVD-------PAPESRYTVTNLKAGTRYTFTVKAVDQA 957
Cdd:smart00060    1 PSPPSNLRVTDvTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSewkevnvTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                    .
gi 1099704529   958 G 958
Cdd:smart00060   81 G 81
fn3 pfam00041
Fibronectin type III domain;
905-959 3.33e-05

Fibronectin type III domain;


Pssm-ID: 333790  Cd Length: 84  Bit Score: 43.55  E-value: 3.33e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1099704529  905 WEP--NAETDFLKYNVYV-----NGFKRASVDPAPESRYTVTNLKAGTRYTFTVKAVDQAGN 959
Cdd:pfam00041   20 WTPppDGNGPITGYRVEYrpvngGEPWNEITVPGTTTSVTLTGLRPGTEYEVRVQAVNGGGE 81
SLH pfam00395
S-layer homology domain;
1542-1563 5.23e-05

S-layer homology domain;


Pssm-ID: 306825  Cd Length: 41  Bit Score: 41.79  E-value: 5.23e-05
                           10        20
                   ....*....|....*....|..
gi 1099704529 1542 GIIQGFTDGTFRPNDKMTRQQM 1563
Cdd:pfam00395   20 GIISGYPDGTFRPNKPITRAEA 41
Big_2 pfam02368
Bacterial Ig-like domain (group 2); This family consists of bacterial domains with an Ig-like ...
1137-1214 9.12e-04

Bacterial Ig-like domain (group 2); This family consists of bacterial domains with an Ig-like fold. Members of this family are found in bacterial and phage surface proteins such as intimins.


Pssm-ID: 308144 [Multi-domain]  Cd Length: 77  Bit Score: 39.30  E-value: 9.12e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1099704529 1137 TGVTLDKAELSLNLSNmkTGTLTAAVQPGDAENHNVYWSSSNSSVAAVAG-GVVTAKGVGTAEITVTTEDGGFTAKANV 1214
Cdd:pfam02368    1 TSVTVSPTSVTVLVGA--TQQLTVYVTPSNASDKKVTWTSSNGSVATVSQtGLVTGVAAGKATITATSKDGNDKATKTV 77
SLH pfam00395
S-layer homology domain;
1606-1630 9.72e-03

S-layer homology domain;


Pssm-ID: 306825  Cd Length: 41  Bit Score: 35.24  E-value: 9.72e-03
                           10        20
                   ....*....|....*....|....*
gi 1099704529 1606 LKSGLIKGTPEGRYYPNKTATRAEA 1630
Cdd:pfam00395   17 AELGIISGYPDGTFRPNKPITRAEA 41
 
Name Accession Description Interval E-value
XynC COG5520
O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis];
55-482 4.73e-86

O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 227807 [Multi-domain]  Cd Length: 433  Bit Score: 288.72  E-value: 4.73e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529   55 PDVAFETNGAPAELTIDLDENTKYQTIDGFGGslTDSSAYVIsqmdeQAKDALMNKLFSREGDGAGFSYLRLPMGASDFA 134
Cdd:COG5520     21 PFVSGSTEVLAASEDITVNVAAKHQVIRGFGG--MNSSAWAG-----DLSAAQLETLFGNGANQLGFSILRVPIDSNDFS 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  135 TSiytyddmpaGESDPELEHFSIAHDSayiipllqqaleINPDLKIMGTPWSAPGWMKTTDS---SIKGKLKEEYYGAYA 211
Cdd:COG5520     94 LG---------GSADNWYKELSTAKSA------------INPGMIVFASPWSPPASMKTTNNrngGNAGRLKYEKYADYA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  212 QYFVKFIEAYEAAGIPIDAVTLQNEPHFEPgDYPGMRMEPEDQAKFVKDYLGPAFETaeidTKIVVWDHNWSEPQYPIDV 291
Cdd:COG5520    153 DYLNDFVLEMKNNGVNLYALSVQNEPDYAP-TYDWCWWTPQEELRFMRQYLASINAE----MRVIIPESFKDLPNMSDPI 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  292 LNDADAKKYIAGSAFHGYAGNVSAQSLVYDQHP--DKDIYFTESSGGEFSPDFAGNVQWD-FQNLIIGATRNWARTSLKW 368
Cdd:COG5520    228 LNDPKALANMDILGTHLYGGQVSDQPYPLAKQKpaGKDLWMTECYPPESDPNSADREALHvALHIHIGMTEGGFQAYVWW 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  369 NIALDENHGPYVGGCKD---CRGIVTVNSSTDE--VTYNEEFYAFGQASKFVLPGAQRIKSNTFGA-GSIEDVAFVNPDG 442
Cdd:COG5520    308 NIRLDYGGGPNHGGNSKrgyCMAHFSKFVQNGYvrLDATKSPYGNVYVSAYVGPNKVVIVAINKGTyPVNQSFNFQNPDG 387
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1099704529  443 SKVLLALNSSKEPKDF--KVRWGAKSFAYTLPAGAAASFVWN 482
Cdd:COG5520    388 SNVSSWVNSSTLNMAKtsNILAAGGRFNASLPAQSVTTFVWD 429
Glyco_hydro_30 pfam02055
Glycosyl hydrolase family 30 TIM-barrel domain;
81-415 1.02e-54

Glycosyl hydrolase family 30 TIM-barrel domain;


Pssm-ID: 307945  Cd Length: 348  Bit Score: 195.15  E-value: 1.02e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529   81 IDGFGGSLTDSSAYVISQMDEQAKDALMNKLFSREGdgAGFSYLRLPMGASDFATSIYTYDDMPageSDPELEHFSIA-H 159
Cdd:pfam02055    1 IQGFGSTFSDASGANLKSLPDPAQDLILKQYFSDEG--LNLQFGRVPIASCDFSIRVYTYADTP---DDYQMHNFSLPeE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  160 DSAYIIPLLQQALEINPDLKIMGTPWSAPGWMKTTDS-----SIKGKLKEEYYGAYAQYFVKFIEAYEAAGIPIDAVTLQ 234
Cdd:pfam02055   76 DTQWKIPYIHRAQKYNQRLKLFASPWTAPGWLKTTGAvngkgSLKGQPGDIYHQTYARYFVKFLEEYAKHGIQFWGLSTQ 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  235 NEPhfEPGDYPGMRME-----PEDQAKFVKDYLGPAF--ETAEIDTKIVVWDHNWSE-PQYPIDVLNDADAKKYIAGSAF 306
Cdd:pfam02055  156 NEP--TAGSDKKYKFQslgftAEHQRDFIKRDLGPALanSTHGKNVKLLILDDNRGNlPKWADTVLNDPDAAKYVHGIAV 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  307 HGYAGNVSAQSL--VYDQHPDKDIYFTESSGGEFSPDFAGNV-QWD----FQNLIIGATRNWARTSLKWNIALDENHGP- 378
Cdd:pfam02055  234 HWYQDAEADAHLgeTHRLHPNTFIFGTEASEGSKSKDQSVDYgSWDramdYSSDILDNLNNWVTGWTERNLALDAEGGPs 313
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1099704529  379 YVGGCKDCRgiVTVNSSTDEVTYNEEFYAFGQASKFV 415
Cdd:pfam02055  314 WVSNFVDAP--VIAFPAKAQFYKQPMFYAIAHFSHFI 348
CBM6_xylanase-like cd04084
Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 ...
498-612 7.90e-31

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: 118.11  E-value: 7.90e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  498 QAEDYSESNGITTAVTTDtgGGKYAGSSSDGSYIAFDHVEFLNGTASVKVRAQAQGDGG-IEFRLDAPDGAYAGGIDLTD 576
Cdd:cd04084      4 EAETYADSSGVKTEATGD--GGVYVGAIDNGDWIAFKNVDFGSGATSFTARVASAGAGGtIEVRLDSPDGPLIGTLEVPN 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1099704529  577 TNG--SWITKAAQVEAVTGKHKLYVVFRGK----VNLNWFQF 612
Cdd:cd04084     82 TGGwqTWTTVSAPVTGVTGVHDLYLVFKGGggdlFNLDWFQF 123
CBD_IV smart00606
Cellulose Binding Domain Type IV;
490-612 6.45e-23

Cellulose Binding Domain Type IV;


Pssm-ID: 128869  Cd Length: 129  Bit Score: 95.48  E-value: 6.45e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529   490 SISPYAALQAEDYSESNGITTAVTTDTGGGKYAGSSSDGSYIAFDHVEFLN-GTASVKVRAQAQGDGG-IEFRLDAPDGA 567
Cdd:smart00606    1 GRDPYNAIQAESYDSQSGVQTETTSDAGGGKNVGYIDDGDWIAYKDVDFGSsGAYTFTARVASGNAGGsIELRLDSPTGT 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1099704529   568 YAGGIDLTDTNG--SWITKAAQVEAVTGKHKLYVVFRG--KVNLNWFQF 612
Cdd:smart00606   81 LVGTVDVPSTGGwqTYQTVSATVTLPAGVHDVYLVFKGgnYFNIDWFRF 129
CBM_6 pfam03422
Carbohydrate binding module (family 6);
498-613 2.26e-21

Carbohydrate binding module (family 6);


Pssm-ID: 308816  Cd Length: 125  Bit Score: 90.88  E-value: 2.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  498 QAEDYSESNGITTAVTTDTGGGKYAGSSSDGSYIAFDHVEF-LNGTASVKVRAQAQGDGG-IEFRLDAPDGAYAGGIDLT 575
Cdd:pfam03422    1 QAETYDKQSGVSTEKTTDYGGGVNVGYIDNGDWIAYKDVDFgSGGAYTFTARVASGAGGGsIELRLDSPTGTLIGTVSVP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1099704529  576 DTNG--SWITKAAQVEAVTGKHKLYVVFRGK----VNLNWFQFS 613
Cdd:pfam03422   81 STGGwqTYVTVSANVTLPTGVHDLYLVFTGGggylFNIDWFQFT 124
Glyco_hydro_30C pfam17189
Glycosyl hydrolase family 30 beta sandwich domain;
418-479 2.81e-17

Glycosyl hydrolase family 30 beta sandwich domain;


Pssm-ID: 339927  Cd Length: 63  Bit Score: 77.21  E-value: 2.81e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1099704529  418 GAQRIKSNTFGAGSIEDVAFVNPDGSKVLLALNSSKEPKDFKVRWGAKS-FAYTLPAGAAASF 479
Cdd:pfam17189    1 GAVRIGSSSSGSNGLEAVAFLNPDGSIVLVVLNRSDSDVPFTVKDGGGSvFSLTLPARSIATF 63
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
1132-1261 6.77e-11

Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only];


Pssm-ID: 227779 [Multi-domain]  Cd Length: 329  Bit Score: 65.59  E-value: 6.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529 1132 ATVGVTGVTLDKAELSLNLSnmKTGTLTAAVQPGDAENHNVYWSSSNSSVAAVAG--GVVTAKGVGTAEITVTTEDGGFT 1209
Cdd:COG5492    177 SIVPVTGITVNKTSDTLKVG--DTDTLTATVTPDNATDKTVTWTSSDPSKATVDDntGKITAVAAGTANITATTNDGSKT 254
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1099704529 1210 AKANVTVSSgeTTPTNPTDPNGAGNTTGPvvtkdgtGSTISGFTSKTETDPN 1261
Cdd:COG5492    255 ATCKVTVNK--ATDLTVSYNAHVTNTGWQ-------TDASDKVVAGTSSNSN 297
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
759-967 3.16e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 225936 [Multi-domain]  Cd Length: 343  Bit Score: 63.37  E-value: 3.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  759 FDDVELTPVitkapsaaqgtDAPETPQGVSAELDGGHNIKLAWTSVPGAEGYKIYRSTadsattaggvYPDYRLIGLASG 838
Cdd:COG3401    154 FTGVEATPK-----------AEPKEITNVRVSFDLGNNIELSEDGSEAEDYYRIYASD----------SGNEEYGFIAQT 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  839 EATSYVD--QGLrGSTAYSYRVTAFNTTGESAASVSDIATTAAGSdtaaPAAPASLIAEPGIEQVMLVWEPNAETDFLKY 916
Cdd:COG3401    213 TENSYYDvkEGL-GAVEYYKVTTVDNTGFESDLPNEPTVGETGGR----YEVPTIPGETTEASFIGVAAEQNQLRQAVTY 287
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1099704529  917 NVY-VNGFKRASVDPAPESRYTVTNLKAGTRYTFTVKAVDQAGNESAASNAV 967
Cdd:COG3401    288 TVYrVEDGTPTKFFTITETDGQDNDMLTGVEYRYEVVAVDKAGLSSHPSKEV 339
Glyco_hydr_30_2 pfam14587
O-Glycosyl hydrolase family 30;
69-277 4.67e-10

O-Glycosyl hydrolase family 30;


Pssm-ID: 317042  Cd Length: 367  Bit Score: 63.24  E-value: 4.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529   69 TIDLDENTKYQTIDGFGGSLTDSSAYVISQMDEQAKDALMNKLFSREGD------GAGFSYLRLPMGASdfatsiyTYDD 142
Cdd:pfam14587    3 KIRIDLQTEYQTIHSFGASDCWSCQFVGKWWPLEKKNKIADLLFSKETDsngnpkGIGLSLWRFNIGAG-------SYEQ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  143 MPAGESDPEL---EHFsIAHDSAYIIP-------LLQQALEINPDlKIMGTPWSAPGWMKTTDSSIKGK-----LKEEYY 207
Cdd:pfam14587   76 GDASGITDEWrreECF-LNADGTYDWTkqagqqwFLKAARRRGVN-YFLGFTNSAPVQMTRNGKAFSTGglelnLKADKM 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1099704529  208 GAYAQYFVKFIEAYEAAGIPIDAVTLQNEPHFEPGDYPGMRMEP---EDQAKFVKDyLGPAFETAEIDTKIVV 277
Cdd:pfam14587  154 DDFADFLVKVADHFREKGFKFDYLSPVNEPQWDWGPGGSQEGTPatnADIAAIVRK-LSAKLSEKQLKTKIVL 225
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
781-877 2.43e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.58  E-value: 2.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  781 PETPQGVSAELDGGHNIKLAWTSVPGA----EGYKIYRSTADSattaggvyPDYRLIGLASGEATSYVDQGLRGSTAYSY 856
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpiTGYVVEYREKGS--------GDWKEVEVTPGSETSYTLTGLKPGTEYEF 72
                           90       100
                   ....*....|....*....|.
gi 1099704529  857 RVTAFNTTGESAASVSDIATT 877
Cdd:cd00063     73 RVRAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
886-970 9.07e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.04  E-value: 9.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  886 PAAPASLIAEP-GIEQVMLVWEPNAET--DFLKYNVYV-----NGFKRASVDPAPESRYTVTNLKAGTRYTFTVKAVDQA 957
Cdd:cd00063      1 PSPPTNLRVTDvTSTSVTLSWTPPEDDggPITGYVVEYrekgsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                           90
                   ....*....|...
gi 1099704529  958 GnESAASNAVTET 970
Cdd:cd00063     81 G-ESPPSESVTVT 92
SLH pfam00395
S-layer homology domain;
1463-1502 9.15e-08

S-layer homology domain;


Pssm-ID: 306825  Cd Length: 41  Bit Score: 49.49  E-value: 9.15e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1099704529 1463 FRDTKGHWAEKEINALASSFIVNGVTADQFAPEQQLTRAE 1502
Cdd:pfam00395    1 FKDVKSHWWAEAVQALAELGIISGYPDGTFRPNKPITRAE 40
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
886-958 3.95e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.15  E-value: 3.95e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529   886 PAAPASLIAEP-GIEQVMLVWEPNAETDFLKYNVYVNGFKRASVD-------PAPESRYTVTNLKAGTRYTFTVKAVDQA 957
Cdd:smart00060    1 PSPPSNLRVTDvTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSewkevnvTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                    .
gi 1099704529   958 G 958
Cdd:smart00060   81 G 81
CBM6_cellulase-like cd04080
Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including ...
497-613 1.36e-05

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: 46.45  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  497 LQAEDYSE--------------------SNGITTAVTTDTGGGKYAGSSSDGSYIAFD-HVEfLNGTASVKVR-AQAQGD 554
Cdd:cd04080      5 IEAEDYDLggegvayhdttpgneggyyrNDGVDIETTSDTGGGYNVGWIDAGEWLEYTvNVP-EAGTYTVSFRvASPSGG 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1099704529  555 GGIEFRLDapDGAYAGGIDLTDTNG--SWITKAAQVEAVT-GKHKLYVVFR-GKVNLNWFQFS 613
Cdd:cd04080     84 GSLSLEVD--GGTVLGTVDVPNTGGwqTWQTVTTTVVLLPaGTHTLRLVFVgGGFNLNWFEFT 144
fn3 pfam00041
Fibronectin type III domain;
905-959 3.33e-05

Fibronectin type III domain;


Pssm-ID: 333790  Cd Length: 84  Bit Score: 43.55  E-value: 3.33e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1099704529  905 WEP--NAETDFLKYNVYV-----NGFKRASVDPAPESRYTVTNLKAGTRYTFTVKAVDQAGN 959
Cdd:pfam00041   20 WTPppDGNGPITGYRVEYrpvngGEPWNEITVPGTTTSVTLTGLRPGTEYEVRVQAVNGGGE 81
SLH pfam00395
S-layer homology domain;
1542-1563 5.23e-05

S-layer homology domain;


Pssm-ID: 306825  Cd Length: 41  Bit Score: 41.79  E-value: 5.23e-05
                           10        20
                   ....*....|....*....|..
gi 1099704529 1542 GIIQGFTDGTFRPNDKMTRQQM 1563
Cdd:pfam00395   20 GIISGYPDGTFRPNKPITRAEA 41
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
781-867 6.65e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 42.60  E-value: 6.65e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529   781 PETPQGVSAELDGGHNIKLAWTSV--PGAEGYKIYRSTADSATTAGGVYPDyrliglASGEATSYVDQGLRGSTAYSYRV 858
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVN------VTPSSTSYTLTGLKPGTEYEFRV 74

                    ....*....
gi 1099704529   859 TAFNTTGES 867
Cdd:smart00060   75 RAVNGAGEG 83
Big_2 pfam02368
Bacterial Ig-like domain (group 2); This family consists of bacterial domains with an Ig-like ...
1137-1214 9.12e-04

Bacterial Ig-like domain (group 2); This family consists of bacterial domains with an Ig-like fold. Members of this family are found in bacterial and phage surface proteins such as intimins.


Pssm-ID: 308144 [Multi-domain]  Cd Length: 77  Bit Score: 39.30  E-value: 9.12e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1099704529 1137 TGVTLDKAELSLNLSNmkTGTLTAAVQPGDAENHNVYWSSSNSSVAAVAG-GVVTAKGVGTAEITVTTEDGGFTAKANV 1214
Cdd:pfam02368    1 TSVTVSPTSVTVLVGA--TQQLTVYVTPSNASDKKVTWTSSNGSVATVSQtGLVTGVAAGKATITATSKDGNDKATKTV 77
DUF4998 pfam16389
Domain of unknown function; This family around 200 residues locates in the N-terminal of some ...
886-966 2.83e-03

Domain of unknown function; This family around 200 residues locates in the N-terminal of some uncharacterized proteins in various Bacteroides and Parabacteroides species. The function of this family remains unknown.


Pssm-ID: 318580  Cd Length: 198  Bit Score: 40.72  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  886 PAAPASLIAEPGIEQVMLVWEPNAETDFLKYNVYVNGFKRASVDPAPESRYTVT------NLKAGTrYTFTVKAVDQAGN 959
Cdd:pfam16389   20 PGKVDSLKAFSGYNRVKLTWLLVSDPKITKARIFWNNGKDSLEVPVARTAGVDTisviidNLPEGS-YTFSIVTYDDEGN 98

                   ....*..
gi 1099704529  960 ESAASNA 966
Cdd:pfam16389   99 KSLPSEV 105
CBM6-CBM35-CBM36_like cd02795
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module ...
497-612 3.15e-03

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: 39.09  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099704529  497 LQAEDYSESNGITTAVTTDTGGGKYAGS-SSDGSYIAFDHVEFLNGTASVKVR-AQAQGDGGIEFRLDApDGAYAGGIDL 574
Cdd:cd02795      2 IEAEDATLTGGTAVSTAAGASGGGYVIGfSSGGDSVTFTVTVPKAGTYRLAVRyASPNGNGSRSVSLDG-NGKLVGTITV 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1099704529  575 TDTNG--SWITKAAQVE-AVTGKHKLYVVFRGK---VNLNWFQF 612
Cdd:cd02795     81 PSTGGwdTWGTASVSVNlPDAGGHTLKIVGTGDnggANIDYVVV 124
SLH pfam00395
S-layer homology domain;
1606-1630 9.72e-03

S-layer homology domain;


Pssm-ID: 306825  Cd Length: 41  Bit Score: 35.24  E-value: 9.72e-03
                           10        20
                   ....*....|....*....|....*
gi 1099704529 1606 LKSGLIKGTPEGRYYPNKTATRAEA 1630
Cdd:pfam00395   17 AELGIISGYPDGTFRPNKPITRAEA 41
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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