Conserved Protein Domain Family
CBM35_galactosidase-like

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cd04081: CBM35_galactosidase-like 
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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.
Statistics
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PSSM-Id: 271147
View PSSM: cd04081
Aligned: 56 rows
Threshold Bit Score: 74.6392
Threshold Setting Gi: 156058748
Created: 11-Aug-2005
Updated: 2-Mar-2014
Structure
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Program:
Drawing:
Aligned Rows:
 
Ca binding site
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1: Ca binding site [ion binding site], 3 residue positions
Conserved feature residue pattern:[EQ] E [Dn]Click to see conserved feature residue pattern help
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1            # #                                                                          
2WZ8_A          9 NVYEAEdpantlggaavrqrdnaasggqyvgwigngsnNYLQFNNVYVPqAGTYRMVVQFANAEvfgqhsynnnvvDRYC 88
gi 299799979  816 FMREAEdsandigdagvtscs---pcsggqkvrnigpgAAVTFPGVTVPaAGPYTLYLDFTVNG------------DRSY 880
gi 256396329  460 TTIEAEaagntiagaakiatcaacsgghkvgyigkgaaNAVTINGITESaAGTHTLTISYLVSG------------TRSF 527
gi 297160754  725 ASYEAEsgtlggvaattssey--asggayvgslgagaaNNLKLTVQAPS-AGRYMLIVHYANNQradghqyntniiSRTA 801
gi 297153828  742 KAYEAEggaptgaakvtdaytf-asggkavtgigagkaNALTVDVVAER-SGRHALTIRYSNAEqapathynpdpiARHA 819
gi 257067399 1026 TELQAEdaelsgdtqiterslaegghavediggdpgndSAVTFSVDAES-AGRHAVVVRFSNPEqapashynpnpmARNA 1104
gi 290955048 1054 RTYEGKsaelagsaalaplslatdgtaitgiggapgngNTATFTVTADE-AGTHALRIRYSNPEqspathynpdplARHA 1132
gi 290955042  743 VTYQAEagtltgtaevsnsyd--qatggvvtgigngtaNSLTLDVDAPS-AGTYAMTMRYANAEelpsnhynpdlyAEHA 819
gi 288541510  620 LPLEAEarenrltgaarfvecgacsgarrvvglggglsNSVTYRDVRAPeDGDYRLQLNHTAAA------------TSSL 687
gi 255035636   25 QSFEAEsgtlaggadmqdca-----scsgqkmvgnlggGAVTVPVNVAA-AGNYRLTLFYATGD------------QRTI 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                #    
2WZ8_A         89 SISVNGg--pEKGHYFFNTRgwntYRTDIIDVYLNAGNNTIRFYNgtsgsyAPNIDKIAI 146
gi 299799979  881 FVSVNGgapaEVKVSGVGNNt---PYTTSVPVTLTAGANTIRIGNdg--agAPDLDRISL 935
gi 256396329  528 SISVNGg---PDIVEQLTGTsfatPATTSVAVQLAAGTNTIKFDNdt--ayAPDLDAITV 582
gi 297160754  802 DIAVGSg--aAQRVTFKNTWtwndYWSVGVPVDLAKGANTLTFSNas--syAPNIDRVQL 857
gi 297153828  820 DLSVGGg--pARRILFPTTFhfnnFWDLTVPATLKKGTNRLTFTAd----eLPDFNGDTY 873
gi 257067399 1105 LISVNGg--ePDSMLFVPTFhannFWERTVYVDLEEGENTIRIGAe----eLTNFSGDGH 1158
gi 290955048 1133 DIAVNGg--eSKRVTFPHTFhqnnFWELTVPVQLKKGQNTITFRSe----eLPNFDGTTY 1186
gi 290955042  820 DVGVNGg--dATRVDFAGTLhwnqFADYTAHVTLKKGANKVKFTSs----qLYDWDGTTV 873
gi 288541510  688 SVSVNGa--aPVEVPVVKGSpe-vPESTAVSVPLKAGANTVRIFSta--arGPGLDRIAV 742
gi 255035636   87 NITPNAg--gFVAVTCPASGgwseVASIGVNVSLNAGSNSIKLDNvy--gyGPNVDRFTL 142

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