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Conserved domains on  [gi|1197928511|ref|WP_086845818|]
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beta-L-arabinofuranosidase domain-containing protein [Amycolatopsis kentuckyensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_hydro_127 pfam07944
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, ...
51-553 0e+00

Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.


:

Pssm-ID: 400342 [Multi-domain]  Cd Length: 503  Bit Score: 560.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511  51 AVRLQAGPFLDNMNRQLAYFRFVDADRLLHTFRTNAGLASSAQPCGGWESPGTELRGHSTGHLLSGLAQAYANTGDTAYK 130
Cdd:pfam07944   1 DVRLTDSFFGDRQQTNREYLLPLDPDRLLHTFRKEAGLPSKAIAYGGWEHPGFPFRGHDLGHWLSAVAYMLASTGDPELE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 131 TKGDYLVNALAACQAaapgrgfHTGYLSAFPETFFDRLESGQSVWAP---YYTLHKIMAGLLDQYLLAGNQQALDVLLRK 207
Cdd:pfam07944  81 ARLDRLVDELAEAQQ-------GDGYLGTYPESNFDRNEAGKGVWAPnheLYNLGKLIAGLVDYYQLTGKTQALDVATRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 208 AAWTKTRTDPLSTSQMQAALRTEFGGMPEVLTNLYQVTGDANHLATAQRFDHAQILDPLAANQDRLSGFHANTQIPKII- 286
Cdd:pfam07944 154 ADWLYDVTDVLGDEQGQRVLVPEHGGINEALVELYELTGDKRYLDLAKRFIHNRGLDPLAYGQDELPGRHQNTAIGHAVr 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 287 GAIREYHATGTTRYRDIAVNFWRIVLDHHSYVIGGNSDG-EYFQTPDAIASRLSDstCEVCNTYNMLKLTRQLFFTDPAP 365
Cdd:pfam07944 234 GAADVYEETGDDALLKAAEFFWDNVVTHHMYVTGGNGARhEHFGPPYELPNRLAY--CETCASYNMLKLTRRLFCWTPDA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 366 EYMDYYELALFNQILGEQDPNSshGFVTYYTPLRAGGIKTYaNDYDDFTCDHGTGMESQTKFADSVYFFTGETLYVNLFI 445
Cdd:pfam07944 312 KYADYYERALYNHILAGQSPDG--GMFFYFNPLESGSYRLR-WPWDSFWCCPGNGAETHAKFGDYIYAHSDDGIYVNLYI 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 446 ASVLTWPGRGITVRQDTTFPTSPSTKLTI--GGAGHIALKIRIPKWTTGAVVKVNGVAQG-SPAPGSYFTIDRTWAAGDV 522
Cdd:pfam07944 389 PSTADWKLKGVELEQETDYPWEGKVRLTVntAKKADFTLYLRIPGWAAGATLTVNGKPTVvAPKSDGYLSIEREWKDGDR 468
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1197928511 523 VDVSVPASL----TFPRANDDGGVGAAKYGPIVLA 553
Cdd:pfam07944 469 VELELPMPVrleaAHPLVPDDPNKVAVLRGPLVLA 503
CBM35_galactosidase-like cd04081
Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind ...
618-738 1.42e-43

Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43; This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. 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). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases.


:

Pssm-ID: 271147  Cd Length: 125  Bit Score: 153.22  E-value: 1.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 618 TSYEAEAGTLAGQAAVRSSS-GASGGALVGYVGGGSANYLQFNGVNA-TAGAHPVTIFYASGE--ARSLTVSVNGGAAVS 693
Cdd:cd04081     1 TSYEAEAATLTGSAAAVSCScGCSGGGAVGVGGGGNGGTVTFNNVTAsAAGTYTLTIDYINGDvnDRNATVSVNGGAAQR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1197928511 694 VATPGTGGWDTVGSVQVTLTLAAGANTIRLGNGSGWAPDIDRIVV 738
Cdd:cd04081    81 VAFPPTGGWNTPGSVTVLVDLKAGSNTITFSNSGGWAPDIDRITV 125
DUF4986 super family cl37907
Domain of unknown function; This family around 150 residues locates in the C-terminal of some ...
572-608 2.20e-04

Domain of unknown function; This family around 150 residues locates in the C-terminal of some uncharacterized proteins in various Bacteroides and Bacillus species. The function of this family remains unknown.


The actual alignment was detected with superfamily member pfam16375:

Pssm-ID: 435310  Cd Length: 82  Bit Score: 40.33  E-value: 2.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1197928511 572 VKQDPANPLRFTGTAST-----GAVTLLPFYATHHQRYTVYW 608
Cdd:pfam16375  41 LKPVAGKPLTFKLDGLVypakyESLTLEPFYRLHDARYMVYW 82
 
Name Accession Description Interval E-value
Glyco_hydro_127 pfam07944
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, ...
51-553 0e+00

Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.


Pssm-ID: 400342 [Multi-domain]  Cd Length: 503  Bit Score: 560.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511  51 AVRLQAGPFLDNMNRQLAYFRFVDADRLLHTFRTNAGLASSAQPCGGWESPGTELRGHSTGHLLSGLAQAYANTGDTAYK 130
Cdd:pfam07944   1 DVRLTDSFFGDRQQTNREYLLPLDPDRLLHTFRKEAGLPSKAIAYGGWEHPGFPFRGHDLGHWLSAVAYMLASTGDPELE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 131 TKGDYLVNALAACQAaapgrgfHTGYLSAFPETFFDRLESGQSVWAP---YYTLHKIMAGLLDQYLLAGNQQALDVLLRK 207
Cdd:pfam07944  81 ARLDRLVDELAEAQQ-------GDGYLGTYPESNFDRNEAGKGVWAPnheLYNLGKLIAGLVDYYQLTGKTQALDVATRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 208 AAWTKTRTDPLSTSQMQAALRTEFGGMPEVLTNLYQVTGDANHLATAQRFDHAQILDPLAANQDRLSGFHANTQIPKII- 286
Cdd:pfam07944 154 ADWLYDVTDVLGDEQGQRVLVPEHGGINEALVELYELTGDKRYLDLAKRFIHNRGLDPLAYGQDELPGRHQNTAIGHAVr 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 287 GAIREYHATGTTRYRDIAVNFWRIVLDHHSYVIGGNSDG-EYFQTPDAIASRLSDstCEVCNTYNMLKLTRQLFFTDPAP 365
Cdd:pfam07944 234 GAADVYEETGDDALLKAAEFFWDNVVTHHMYVTGGNGARhEHFGPPYELPNRLAY--CETCASYNMLKLTRRLFCWTPDA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 366 EYMDYYELALFNQILGEQDPNSshGFVTYYTPLRAGGIKTYaNDYDDFTCDHGTGMESQTKFADSVYFFTGETLYVNLFI 445
Cdd:pfam07944 312 KYADYYERALYNHILAGQSPDG--GMFFYFNPLESGSYRLR-WPWDSFWCCPGNGAETHAKFGDYIYAHSDDGIYVNLYI 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 446 ASVLTWPGRGITVRQDTTFPTSPSTKLTI--GGAGHIALKIRIPKWTTGAVVKVNGVAQG-SPAPGSYFTIDRTWAAGDV 522
Cdd:pfam07944 389 PSTADWKLKGVELEQETDYPWEGKVRLTVntAKKADFTLYLRIPGWAAGATLTVNGKPTVvAPKSDGYLSIEREWKDGDR 468
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1197928511 523 VDVSVPASL----TFPRANDDGGVGAAKYGPIVLA 553
Cdd:pfam07944 469 VELELPMPVrleaAHPLVPDDPNKVAVLRGPLVLA 503
HybA1 COG3533
Beta-L-arabinofuranosidase, GH127 family [Carbohydrate transport and metabolism];
46-609 6.47e-156

Beta-L-arabinofuranosidase, GH127 family [Carbohydrate transport and metabolism];


Pssm-ID: 442754 [Multi-domain]  Cd Length: 597  Bit Score: 465.09  E-value: 6.47e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511  46 PFPLGAVRLQAGPFLDNMNRQLAY-----FRFVDADRLLHTFRTNAGLASSaqPCGGWEspgteLRGHSTGHLLSGLAQA 120
Cdd:COG3533     5 PVPLSDVRLTDGFWGERQELNREYtlphqWEQLEPDGLLANFRIAAGLKKG--EYGGWE-----FDDHDVGKWLEAAAYA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 121 YANTGDTAYKTKGDYLVNALAACQAaapgrgfHTGYLSafpeTFFDRlESGQSVWA-----PYYTLHKIMAGLLDQYLLA 195
Cdd:COG3533    78 YARTGDPELEARLDYVIDELAAAQE-------PDGYLG----TYFTI-EGGEKRWVlrlshELYNAGHLIEGAVAHYRAT 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 196 GNQQALDVLLRKAAWTKTRTDPLSTsQMQAALrtEFGGMPEVLTNLYQVTGDANHLATAQRFDH------------AQIL 263
Cdd:COG3533   146 GKRKLLDVAIRLADWIDDTFGPLPD-QLQGML--GHGGIEEALVELYRVTGDKRYLDLAKRFIDrrgrlplrggeyFQDH 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 264 DPLAANQDrLSGfHANTQIPKIIGAIREYHATGTTRYRDIAVNFWRIVLDHHSYVIGGNS---DGEYFQTPDAIASrlSD 340
Cdd:COG3533   223 DPLREQTD-AVG-HAVRAIYLYAGAADVAAETGDEEYLDALERLWDNVVNRKMYITGGNGsrhDGEAFGPDYDLPN--DT 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 341 STCEVCNTYNMLKLTRQLFFTDPAPEYMDYYELALFNQILGEQDPNssHGFVTYYTPLRAGGiKTYANDYDDFTCDHGTG 420
Cdd:COG3533   299 AYAETCASIGMLKLNRRLLLLTGDAKYADVYERALYNHILSGQSLD--GGGFFYFNPLRSGG-YHERQPWFGCACCPGNG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 421 MESQTKFADSVYFFTGETLYVNLFIASVLTWP--GRGITVRQDTTFPTSPSTKLTI--GGAGHIALKIRIPKWTTGAVVK 496
Cdd:COG3533   376 ARTLASLGGYIYATSDDGLYVNLYIGSTLNWKldGKGVKLRQETNYPWDGKVRITVdpAKPGEFTLRLRIPGWAKGATVK 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 497 VNGVAQ-GSPAPGSYFTIDRTWAAGDVVDVSVPASLTF----PRANDDGGVGAAKYGPIVLAGQYGST--NLSAL----- 564
Cdd:COG3533   456 VNGKPVdAEVEPGSYATINRTWKKGDVVELDLPMPVRLveanPRVPDDRGKVAVKRGPLVYCAESGDNggDLDDLrlpdd 535
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1197928511 565 --------PTLQTGTVK-----QDPANPLRFTGT-ASTGAVTLLPFYATHHqRY----TVYWR 609
Cdd:COG3533   536 apleaeyaPDLLGGVVVlkgegLVSGDPLTYRTPgGKPVDLTLIPYYAWAN-RGpgemRVWLP 597
CBM35_galactosidase-like cd04081
Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind ...
618-738 1.42e-43

Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43; This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. 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). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases.


Pssm-ID: 271147  Cd Length: 125  Bit Score: 153.22  E-value: 1.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 618 TSYEAEAGTLAGQAAVRSSS-GASGGALVGYVGGGSANYLQFNGVNA-TAGAHPVTIFYASGE--ARSLTVSVNGGAAVS 693
Cdd:cd04081     1 TSYEAEAATLTGSAAAVSCScGCSGGGAVGVGGGGNGGTVTFNNVTAsAAGTYTLTIDYINGDvnDRNATVSVNGGAAQR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1197928511 694 VATPGTGGWDTVGSVQVTLTLAAGANTIRLGNGSGWAPDIDRIVV 738
Cdd:cd04081    81 VAFPPTGGWNTPGSVTVLVDLKAGSNTITFSNSGGWAPDIDRITV 125
CBD_IV smart00606
Cellulose Binding Domain Type IV;
637-723 1.39e-09

Cellulose Binding Domain Type IV;


Pssm-ID: 128869 [Multi-domain]  Cd Length: 129  Bit Score: 56.57  E-value: 1.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511  637 SGASGGALVGYVGGGSanYLQFNGVN-ATAGAHPVTIFYASGEARS-LTVSVNGGAAVSVAT---PGTGGWDTVGSVQVT 711
Cdd:smart00606  25 SDAGGGKNVGYIDDGD--WIAYKDVDfGSSGAYTFTARVASGNAGGsIELRLDSPTGTLVGTvdvPSTGGWQTYQTVSAT 102
                           90
                   ....*....|..
gi 1197928511  712 LTLAAGANTIRL 723
Cdd:smart00606 103 VTLPAGVHDVYL 114
CBM_35 pfam16990
Carbohydrate binding module (family 35); This is a mannan-specific carbohydrate binding domain, ...
620-729 1.41e-09

Carbohydrate binding module (family 35); This is a mannan-specific carbohydrate binding domain, previously known as the X4 module. Unlike other carbohydrate binding modules, binding to substrate causes a conformational change.


Pssm-ID: 293595  Cd Length: 119  Bit Score: 56.38  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 620 YEAEAGTLAGQAAvrsSSGASGGALVGYVGG--GSANYLQFNGVNATAGAHPVTIFYASG-EARSLTVSVNGGAAVSVAT 696
Cdd:pfam16990   2 YEAEKGTLTGTSV---DTTAPGVSGTGYVGEfqGAGDAVSWNVNVPVAGEYNLNVTHSAPyGSKENTLVVNGTAVATNAF 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1197928511 697 PGTggwDTVG-SVQVTLTLAAGANTIRLGNGSGW 729
Cdd:pfam16990  79 AES---TEVPqTTVITVTLKAGANTIGIDRDWGW 109
DUF4986 pfam16375
Domain of unknown function; This family around 150 residues locates in the C-terminal of some ...
572-608 2.20e-04

Domain of unknown function; This family around 150 residues locates in the C-terminal of some uncharacterized proteins in various Bacteroides and Bacillus species. The function of this family remains unknown.


Pssm-ID: 435310  Cd Length: 82  Bit Score: 40.33  E-value: 2.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1197928511 572 VKQDPANPLRFTGTAST-----GAVTLLPFYATHHQRYTVYW 608
Cdd:pfam16375  41 LKPVAGKPLTFKLDGLVypakyESLTLEPFYRLHDARYMVYW 82
 
Name Accession Description Interval E-value
Glyco_hydro_127 pfam07944
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, ...
51-553 0e+00

Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.


Pssm-ID: 400342 [Multi-domain]  Cd Length: 503  Bit Score: 560.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511  51 AVRLQAGPFLDNMNRQLAYFRFVDADRLLHTFRTNAGLASSAQPCGGWESPGTELRGHSTGHLLSGLAQAYANTGDTAYK 130
Cdd:pfam07944   1 DVRLTDSFFGDRQQTNREYLLPLDPDRLLHTFRKEAGLPSKAIAYGGWEHPGFPFRGHDLGHWLSAVAYMLASTGDPELE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 131 TKGDYLVNALAACQAaapgrgfHTGYLSAFPETFFDRLESGQSVWAP---YYTLHKIMAGLLDQYLLAGNQQALDVLLRK 207
Cdd:pfam07944  81 ARLDRLVDELAEAQQ-------GDGYLGTYPESNFDRNEAGKGVWAPnheLYNLGKLIAGLVDYYQLTGKTQALDVATRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 208 AAWTKTRTDPLSTSQMQAALRTEFGGMPEVLTNLYQVTGDANHLATAQRFDHAQILDPLAANQDRLSGFHANTQIPKII- 286
Cdd:pfam07944 154 ADWLYDVTDVLGDEQGQRVLVPEHGGINEALVELYELTGDKRYLDLAKRFIHNRGLDPLAYGQDELPGRHQNTAIGHAVr 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 287 GAIREYHATGTTRYRDIAVNFWRIVLDHHSYVIGGNSDG-EYFQTPDAIASRLSDstCEVCNTYNMLKLTRQLFFTDPAP 365
Cdd:pfam07944 234 GAADVYEETGDDALLKAAEFFWDNVVTHHMYVTGGNGARhEHFGPPYELPNRLAY--CETCASYNMLKLTRRLFCWTPDA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 366 EYMDYYELALFNQILGEQDPNSshGFVTYYTPLRAGGIKTYaNDYDDFTCDHGTGMESQTKFADSVYFFTGETLYVNLFI 445
Cdd:pfam07944 312 KYADYYERALYNHILAGQSPDG--GMFFYFNPLESGSYRLR-WPWDSFWCCPGNGAETHAKFGDYIYAHSDDGIYVNLYI 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 446 ASVLTWPGRGITVRQDTTFPTSPSTKLTI--GGAGHIALKIRIPKWTTGAVVKVNGVAQG-SPAPGSYFTIDRTWAAGDV 522
Cdd:pfam07944 389 PSTADWKLKGVELEQETDYPWEGKVRLTVntAKKADFTLYLRIPGWAAGATLTVNGKPTVvAPKSDGYLSIEREWKDGDR 468
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1197928511 523 VDVSVPASL----TFPRANDDGGVGAAKYGPIVLA 553
Cdd:pfam07944 469 VELELPMPVrleaAHPLVPDDPNKVAVLRGPLVLA 503
HybA1 COG3533
Beta-L-arabinofuranosidase, GH127 family [Carbohydrate transport and metabolism];
46-609 6.47e-156

Beta-L-arabinofuranosidase, GH127 family [Carbohydrate transport and metabolism];


Pssm-ID: 442754 [Multi-domain]  Cd Length: 597  Bit Score: 465.09  E-value: 6.47e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511  46 PFPLGAVRLQAGPFLDNMNRQLAY-----FRFVDADRLLHTFRTNAGLASSaqPCGGWEspgteLRGHSTGHLLSGLAQA 120
Cdd:COG3533     5 PVPLSDVRLTDGFWGERQELNREYtlphqWEQLEPDGLLANFRIAAGLKKG--EYGGWE-----FDDHDVGKWLEAAAYA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 121 YANTGDTAYKTKGDYLVNALAACQAaapgrgfHTGYLSafpeTFFDRlESGQSVWA-----PYYTLHKIMAGLLDQYLLA 195
Cdd:COG3533    78 YARTGDPELEARLDYVIDELAAAQE-------PDGYLG----TYFTI-EGGEKRWVlrlshELYNAGHLIEGAVAHYRAT 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 196 GNQQALDVLLRKAAWTKTRTDPLSTsQMQAALrtEFGGMPEVLTNLYQVTGDANHLATAQRFDH------------AQIL 263
Cdd:COG3533   146 GKRKLLDVAIRLADWIDDTFGPLPD-QLQGML--GHGGIEEALVELYRVTGDKRYLDLAKRFIDrrgrlplrggeyFQDH 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 264 DPLAANQDrLSGfHANTQIPKIIGAIREYHATGTTRYRDIAVNFWRIVLDHHSYVIGGNS---DGEYFQTPDAIASrlSD 340
Cdd:COG3533   223 DPLREQTD-AVG-HAVRAIYLYAGAADVAAETGDEEYLDALERLWDNVVNRKMYITGGNGsrhDGEAFGPDYDLPN--DT 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 341 STCEVCNTYNMLKLTRQLFFTDPAPEYMDYYELALFNQILGEQDPNssHGFVTYYTPLRAGGiKTYANDYDDFTCDHGTG 420
Cdd:COG3533   299 AYAETCASIGMLKLNRRLLLLTGDAKYADVYERALYNHILSGQSLD--GGGFFYFNPLRSGG-YHERQPWFGCACCPGNG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 421 MESQTKFADSVYFFTGETLYVNLFIASVLTWP--GRGITVRQDTTFPTSPSTKLTI--GGAGHIALKIRIPKWTTGAVVK 496
Cdd:COG3533   376 ARTLASLGGYIYATSDDGLYVNLYIGSTLNWKldGKGVKLRQETNYPWDGKVRITVdpAKPGEFTLRLRIPGWAKGATVK 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 497 VNGVAQ-GSPAPGSYFTIDRTWAAGDVVDVSVPASLTF----PRANDDGGVGAAKYGPIVLAGQYGST--NLSAL----- 564
Cdd:COG3533   456 VNGKPVdAEVEPGSYATINRTWKKGDVVELDLPMPVRLveanPRVPDDRGKVAVKRGPLVYCAESGDNggDLDDLrlpdd 535
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1197928511 565 --------PTLQTGTVK-----QDPANPLRFTGT-ASTGAVTLLPFYATHHqRY----TVYWR 609
Cdd:COG3533   536 apleaeyaPDLLGGVVVlkgegLVSGDPLTYRTPgGKPVDLTLIPYYAWAN-RGpgemRVWLP 597
CBM35_galactosidase-like cd04081
Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind ...
618-738 1.42e-43

Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43; This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. 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). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases.


Pssm-ID: 271147  Cd Length: 125  Bit Score: 153.22  E-value: 1.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 618 TSYEAEAGTLAGQAAVRSSS-GASGGALVGYVGGGSANYLQFNGVNA-TAGAHPVTIFYASGE--ARSLTVSVNGGAAVS 693
Cdd:cd04081     1 TSYEAEAATLTGSAAAVSCScGCSGGGAVGVGGGGNGGTVTFNNVTAsAAGTYTLTIDYINGDvnDRNATVSVNGGAAQR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1197928511 694 VATPGTGGWDTVGSVQVTLTLAAGANTIRLGNGSGWAPDIDRIVV 738
Cdd:cd04081    81 VAFPPTGGWNTPGSVTVLVDLKAGSNTITFSNSGGWAPDIDRITV 125
CBM35_Lmo2446-like cd04083
Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446; This family includes ...
618-738 3.02e-19

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: 84.23  E-value: 3.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 618 TSYEAEAGTLAGQAAVRSS-SGASGgalVGYVGGGSANY--LQFNgVNA-TAGAHPVTIFYA--SGEARSLTVSVNGGAA 691
Cdd:cd04083     1 TRYEAENAALSGGAVVNTDhAGYSG---TGFVDGFATAGasVTFT-VNVpAAGTYTLTLRYAngTGSAKTLSLYVNGTKV 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1197928511 692 VSVATPGTGGWDTVGSVQVTLTLAAGANTIRLGNGSGWAPD--IDRIVV 738
Cdd:cd04083    77 KQVSLPSTGSWDTWGTATETVTLRAGTNTIELRYDAGDSGNvnLDNITV 125
CBM35_mannanase-like cd04086
Carbohydrate Binding Module 35 (CBM35); appended to several carbohydrate binding enzymes, ...
620-738 1.36e-16

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: 76.49  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 620 YEAEAGTLAGQAAVRSSSGASGGalvGYVGGGSAN--YLQFNGVNATAGAHPVTIFYAS-GEARSLTVSVNGGAAVSVAT 696
Cdd:cd04086     3 YEAEDGTLTGVTVATSRSGYSGT---GYVTGFDDDgdSLTFTVNVPEAGLYDLVIRYAApYGDKENNLYVNGTSVGEISF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1197928511 697 PGTGGWDTVGSVQVTLTlaAGANTIRLGNGSGWApDIDRIVV 738
Cdd:cd04086    80 PATTKFTEVSAGKVLLN--AGENTITIENSWGWY-DIDYITV 118
CBM6-CBM35-CBM36_like cd02795
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module ...
619-738 1.34e-14

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: 70.68  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 619 SYEAEAGTLAGQAAVRSSSGASGGALVGYvGGGSANYLQFNGVNATAGAHPVTIFYASG---EARSLTVSVNGGAAVSVA 695
Cdd:cd02795     1 RIEAEDATLTGGTAVSTAAGASGGGYVIG-FSSGGDSVTFTVTVPKAGTYRLAVRYASPngnGSRSVSLDGNGKLVGTIT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1197928511 696 TPGTGGWDTVGSVQVTLTLA-AGANTIRL-GNGSGWAPDIDRIVV 738
Cdd:cd02795    80 VPSTGGWDTWGTASVSVNLPdAGGHTLKIvGTGDNGGANIDYVVV 124
CBM35_pectate_lyase-like cd04082
Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes ...
618-738 1.62e-14

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: 70.67  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 618 TSYEAEAGTLaGQAAVRSSSGasggalvGYVGGGSANYLQFNG------VNA-TAGAHPVTIFYASG--EARSLTVSVNG 688
Cdd:cd04082     1 LTYQAEDASV-DQGVIESNHA-------GYTGSGFVNTDNAVGsyiewtVNApTAGTYTLTFRYANGstSNRPADISVNG 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1197928511 689 GAAV-SVATPGTGGWDTVGSVQVTLTLAAGANTIRL-GNGSGWAPDIDRIVV 738
Cdd:cd04082    73 NTVAaTLSFPSTGAWTTWATSSVTVPLNAGTNTIRLtATTAEGLPNIDYLTV 124
CBD_IV smart00606
Cellulose Binding Domain Type IV;
637-723 1.39e-09

Cellulose Binding Domain Type IV;


Pssm-ID: 128869 [Multi-domain]  Cd Length: 129  Bit Score: 56.57  E-value: 1.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511  637 SGASGGALVGYVGGGSanYLQFNGVN-ATAGAHPVTIFYASGEARS-LTVSVNGGAAVSVAT---PGTGGWDTVGSVQVT 711
Cdd:smart00606  25 SDAGGGKNVGYIDDGD--WIAYKDVDfGSSGAYTFTARVASGNAGGsIELRLDSPTGTLVGTvdvPSTGGWQTYQTVSAT 102
                           90
                   ....*....|..
gi 1197928511  712 LTLAAGANTIRL 723
Cdd:smart00606 103 VTLPAGVHDVYL 114
CBM_35 pfam16990
Carbohydrate binding module (family 35); This is a mannan-specific carbohydrate binding domain, ...
620-729 1.41e-09

Carbohydrate binding module (family 35); This is a mannan-specific carbohydrate binding domain, previously known as the X4 module. Unlike other carbohydrate binding modules, binding to substrate causes a conformational change.


Pssm-ID: 293595  Cd Length: 119  Bit Score: 56.38  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 620 YEAEAGTLAGQAAvrsSSGASGGALVGYVGG--GSANYLQFNGVNATAGAHPVTIFYASG-EARSLTVSVNGGAAVSVAT 696
Cdd:pfam16990   2 YEAEKGTLTGTSV---DTTAPGVSGTGYVGEfqGAGDAVSWNVNVPVAGEYNLNVTHSAPyGSKENTLVVNGTAVATNAF 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1197928511 697 PGTggwDTVG-SVQVTLTLAAGANTIRLGNGSGW 729
Cdd:pfam16990  79 AES---TEVPqTTVITVTLKAGANTIGIDRDWGW 109
CBM6_cellulase-like cd04080
Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including ...
633-736 2.65e-09

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: 56.08  E-value: 2.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 633 VRSSSGASGGALVGYVGGGSanYLQFNgVN-ATAGAHPVTIFYASGEA-RSLTVSVNGGAAV-SVATPGTGGWDTVGSVQ 709
Cdd:cd04080    38 IETTSDTGGGYNVGWIDAGE--WLEYT-VNvPEAGTYTVSFRVASPSGgGSLSLEVDGGTVLgTVDVPNTGGWQTWQTVT 114
                          90       100
                  ....*....|....*....|....*....
gi 1197928511 710 VTLTL-AAGANTIRLG-NGSGWapDIDRI 736
Cdd:cd04080   115 TTVVLlPAGTHTLRLVfVGGGF--NLNWF 141
CBM6_agarase-like cd04079
Carbohydrate Binding Module 6 (CBM6); appended mainly to glycoside hydrolase (GH) family 16 ...
638-737 2.00e-06

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: 47.64  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 638 GASGGALVGYVGGGsaNYLQFNGVNATAGAHPVTIFYASGEARS-LTVSVNGGAAVSVATPGTGGWDTVGSVQV--TLTL 714
Cdd:cd04079    29 SVNGGTAINYVNTG--DYADYTVNVPEAGTYSVEYLIGTPVSGAaIELLVDGNSVATTAVPNTGGWDNFQALTLasTVNL 106
                          90       100
                  ....*....|....*....|....*
gi 1197928511 715 AAGANTIRL-GNGS-GWAPDIDRIV 737
Cdd:cd04079   107 TAGTHTIRLtAAGSnDWQWNLDKFT 131
CBM_6 pfam03422
Carbohydrate binding module (family 6);
621-723 5.87e-06

Carbohydrate binding module (family 6);


Pssm-ID: 397476  Cd Length: 125  Bit Score: 46.19  E-value: 5.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 621 EAEAGTLAGQAAVRSSSGASGGALVGYVGGGSanYLQFNGVN-ATAGAHPVTIFYASG-EARSLTVSVNGGAAVSVAT-- 696
Cdd:pfam03422   1 QAETYDKQSGVSTEKTTDYGGGVNVGYIDNGD--WIAYKDVDfGSGGAYTFTARVASGaGGGSIELRLDSPTGTLIGTvs 78
                          90       100
                  ....*....|....*....|....*...
gi 1197928511 697 -PGTGGWDTVGSVQVTLTLAAGANTIRL 723
Cdd:pfam03422  79 vPSTGGWQTYVTVSANVTLPTGVHDLYL 106
CBM6_xylanase-like cd04084
Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 ...
623-721 2.44e-05

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: 44.16  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197928511 623 EAGTLAGQAAVRSSSGASGGALVGYVGGGSanYLQFNGVNATAGAHPVTIFYASGEAR-SLTV---SVNGGAAVSVATPG 698
Cdd:cd04084     4 EAETYADSSGVKTEATGDGGVYVGAIDNGD--WIAFKNVDFGSGATSFTARVASAGAGgTIEVrldSPDGPLIGTLEVPN 81
                          90       100
                  ....*....|....*....|...
gi 1197928511 699 TGGWDTVGSVQVTLTLAAGANTI 721
Cdd:cd04084    82 TGGWQTWTTVSAPVTGVTGVHDL 104
DUF4986 pfam16375
Domain of unknown function; This family around 150 residues locates in the C-terminal of some ...
572-608 2.20e-04

Domain of unknown function; This family around 150 residues locates in the C-terminal of some uncharacterized proteins in various Bacteroides and Bacillus species. The function of this family remains unknown.


Pssm-ID: 435310  Cd Length: 82  Bit Score: 40.33  E-value: 2.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1197928511 572 VKQDPANPLRFTGTAST-----GAVTLLPFYATHHQRYTVYW 608
Cdd:pfam16375  41 LKPVAGKPLTFKLDGLVypakyESLTLEPFYRLHDARYMVYW 82
 
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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