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Conserved domains on  [gi|193210226|ref|NP_741841|]
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Peritrophic membrane chitin binding protein [Caenorhabditis elegans]

Protein Classification

polysaccharide deacetylase family protein( domain architecture ID 79029)

metal-dependent polysaccharide deacetylase family protein, belonging to the carbohydrate esterase 4 (CE4) superfamily, may catalyze the N- or O-deacetylation of a substrate such as acetylated chitin, peptidoglycan, and acetylated xylan

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CE4_SF super family cl15692
Catalytic NodB homology domain of the carbohydrate esterase 4 superfamily; The carbohydrate ...
 55-317 4.58e-142

Catalytic NodB homology domain of the carbohydrate esterase 4 superfamily; The carbohydrate esterase 4 (CE4) superfamily mainly includes chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan, respectively. Members in this superfamily contain a NodB homology domain that adopts a deformed (beta/alpha)8 barrel fold, which encompasses a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad, closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The NodB homology domain of CE4 superfamily is remotely related to the 7-stranded beta/alpha barrel catalytic domain of the superfamily consisting of family 38 glycoside hydrolases (GH38), family 57 heat stable retaining glycoside hydrolases (GH57), lactam utilization protein LamB/YcsF family proteins, and YdjC-family proteins.


The actual alignment was detected with superfamily member cd10974:

Pssm-ID: 472828  Cd Length: 269  Bit Score: 404.03  E-value: 4.58e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226  55 PQMVMLSFDDPITDRIINTLKSLFSGSIRNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLSG-RTQER 133
Cdd:cd10974    1 PQMITLTFDDAINDNNIELYKKIFNGKRNNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDENnATYED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 134 WYKEQKGMRETLAEFSFIDRSHIIGTRAPELKIGGDAQYRMMSENNFTFDNSMLV---SSPYWPQTLDHKLAWECDG-NC 209
Cdd:cd10974   81 WVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAppsNVPLWPYTLDYKMPHECHGqNC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 210 PTQSHKAIWEIPIQNIQANDTRWYKT---LTRAMKPFDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYLPDngAV 286
Cdd:cd10974  161 PTRSFPGVWEMVLNELDVRDDPQGDEplaMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTKNE--LL 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 193210226 287 YALRDFLKFIVQKQDVFVVTGSQIIDYMRNP 317
Cdd:cd10974  239 RALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
 
Name Accession Description Interval E-value
CE4_CDA_like_1 cd10974
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ...
 55-317 4.58e-142

Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding peritrophin-A domain (ChBD) and/or a low-density lipoprotein receptor class A domain (LDLa); Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase 4 (CE4) superfamily. This family includes many CDA-like proteins mainly from insects, which contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. In addition to the CDA-like domain, family members contain two additional domains, a chitin-binding peritrophin-A domain (ChBD) and a low-density lipoprotein receptor class A domain (LDLa), or have the ChBD domain but do not have the LDLa domain.


Pssm-ID: 200596  Cd Length: 269  Bit Score: 404.03  E-value: 4.58e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226  55 PQMVMLSFDDPITDRIINTLKSLFSGSIRNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLSG-RTQER 133
Cdd:cd10974    1 PQMITLTFDDAINDNNIELYKKIFNGKRNNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDENnATYED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 134 WYKEQKGMRETLAEFSFIDRSHIIGTRAPELKIGGDAQYRMMSENNFTFDNSMLV---SSPYWPQTLDHKLAWECDG-NC 209
Cdd:cd10974   81 WVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAppsNVPLWPYTLDYKMPHECHGqNC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 210 PTQSHKAIWEIPIQNIQANDTRWYKT---LTRAMKPFDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYLPDngAV 286
Cdd:cd10974  161 PTRSFPGVWEMVLNELDVRDDPQGDEplaMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTKNE--LL 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 193210226 287 YALRDFLKFIVQKQDVFVVTGSQIIDYMRNP 317
Cdd:cd10974  239 RALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 55-147 4.98e-05

Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyses glucosidic bonds in xylan.


Pssm-ID: 426305 [Multi-domain]  Cd Length: 124  Bit Score: 42.60  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226   55 PQMVMLSFDD---PITDRIINTLKSLfsgsirnpngcAIKGTFFVSHQW--NNYDQSLWLHSTNHEIGVNSITREDLSGR 129
Cdd:pfam01522   6 KKVVALTFDDgpsENTPAILDVLKKY-----------GVKATFFVIGGNveRYPDLVKRMVEAGHEIGNHTWSHPNLTGL 74

                          90
                  ....*....|....*...
gi 193210226  130 TQERWYKEQKGMRETLAE 147
Cdd:pfam01522  75 SPEEIRKEIERAQDALEK 92
 
Name Accession Description Interval E-value
CE4_CDA_like_1 cd10974
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ...
 55-317 4.58e-142

Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding peritrophin-A domain (ChBD) and/or a low-density lipoprotein receptor class A domain (LDLa); Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase 4 (CE4) superfamily. This family includes many CDA-like proteins mainly from insects, which contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. In addition to the CDA-like domain, family members contain two additional domains, a chitin-binding peritrophin-A domain (ChBD) and a low-density lipoprotein receptor class A domain (LDLa), or have the ChBD domain but do not have the LDLa domain.


Pssm-ID: 200596  Cd Length: 269  Bit Score: 404.03  E-value: 4.58e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226  55 PQMVMLSFDDPITDRIINTLKSLFSGSIRNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLSG-RTQER 133
Cdd:cd10974    1 PQMITLTFDDAINDNNIELYKKIFNGKRNNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDENnATYED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 134 WYKEQKGMRETLAEFSFIDRSHIIGTRAPELKIGGDAQYRMMSENNFTFDNSMLV---SSPYWPQTLDHKLAWECDG-NC 209
Cdd:cd10974   81 WVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAppsNVPLWPYTLDYKMPHECHGqNC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 210 PTQSHKAIWEIPIQNIQANDTRWYKT---LTRAMKPFDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYLPDngAV 286
Cdd:cd10974  161 PTRSFPGVWEMVLNELDVRDDPQGDEplaMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTKNE--LL 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 193210226 287 YALRDFLKFIVQKQDVFVVTGSQIIDYMRNP 317
Cdd:cd10974  239 RALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
CE4_CDA_like_2 cd10975
Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3. ...
 55-317 3.88e-72

Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase 4 (CE4) superfamily. This family includes many midgut-specific CDA-like proteins mainly from insects, such as Tribolium castaneum CDAs (TcCDA6-9). These proteins contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. In addition to the CDA-like domain, some family members have an additional chitin-binding peritrophin-A domain (ChBD).


Pssm-ID: 200597  Cd Length: 268  Bit Score: 226.04  E-value: 3.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226  55 PQMVMLSFDDPITDRIINTLKSLFSGSIrNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLS----GRT 130
Cdd:cd10975    1 PQLVTLTFDDAVNTLNYPYYEKLFGNRK-NPNGCPIGATFFVSHEYTDYRLVQELYNDGHEIALHSISHRSPQdywrNAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 131 QERWYKEQKGMRETLAEFSFIDRSHIIGTRAPELKIGGDAQYRMMSENNFTFDNSMLVSS----PYWPQTLDHKLAWECD 206
Cdd:cd10975   80 VDEWEREFGGQREILAHFANIPAEDIKGFRAPFLQLGGDATFKALKQLGLTYDSSWPTQSftnpPLWPYTLDYGSTQDCV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 207 -GNCPTQSHKAIWEIPIQNIQANDTRWYKTLTRAMKPfDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYlPDNgA 285
Cdd:cd10975  160 iPPCPTDSYPGFWVVPMVDWQDLNGVPCSMLAACPPP-GTADEVYDWLLSNFERHYNTNRAPFGLYLHASWFEF-TPN-R 236

                        250       260       270
                 ....*....|....*....|....*....|..
gi 193210226 286 VYALRDFLKFIVQKQDVFVVTGSQIIDYMRNP 317
Cdd:cd10975  237 LEGFKKFLDELLSLDDVYLVTISQAIEWMRNP 268
CE4_CDA_like cd10919
Putative catalytic domain of chitin deacetylase-like proteins from insects and similar ...
 55-317 3.80e-68

Putative catalytic domain of chitin deacetylase-like proteins from insects and similar proteins; Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase family 4 (CE4). This family includes many CDA-like proteins, mainly from insects, which contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. Some family members have an additional chitin binding domain (ChBD), or an additional low-density lipoprotein receptor class A domain (LDLa), or both. Due to the lack of some catalytically relevant residues, several insect CDA-like proteins are devoid of enzymatic activity and may simply bind to chitin and thus influence the mechanical or permeability properties of chitin-containing structures such as the cuticle or the peritrophic membrane. This family also includes many uncharacterized hypothetical proteins from bacteria, exhibiting high sequence similarity to insect CDA-like proteins.


Pssm-ID: 200545 [Multi-domain]  Cd Length: 273  Bit Score: 216.07  E-value: 3.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226  55 PQMVMLSFDDPITDRIINTLKSLFSGSIRNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLSGR-TQER 133
Cdd:cd10919    1 PQFVLFTFDDAINELNTDAVIQEIADGTNNNGGCPIPATFFVSTNYTDCSLVKQLWREGHEIATHTVTHVPDDSNaSVDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 134 WYKEQKGMRETLAEFSFIDRSHIIGTRAPELKiGGDAQYRMMSENNFTFDNSMLV------SSPYWPQTLD----HKLAW 203
Cdd:cd10919   81 WEEEIAGQREWLNKTCGIPLEKVVGFRAPYLA-YNPNTREVLEENGFLYDSSIPEpytpsgTNRLWPYTLDygipQDCNL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 204 ECDGNCPTQSHKAIWEIPIQNIQ-ANDTRWYKTLTRAMKPFDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYlPD 282
Cdd:cd10919  160 VPGSCSPTERYPGLWEVPLYTLQdGNDTTGDSYYCTPDDGPLNGDSFYALLKYNFDRHYNGNRAPFGIYLHAAWLSP-PY 238

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 193210226 283 NGAVYALRDFLKFIVQKQDVFVVTGSQIIDYMRNP 317
Cdd:cd10919  239 SERRAALEKFLDYALSKPDVWFVTNSQLLDWMQNP 273
CE4_CDA_like_3 cd10976
Putative catalytic domain of uncharacterized bacterial hypothetical proteins similar to insect ...
 107-314 1.26e-11

Putative catalytic domain of uncharacterized bacterial hypothetical proteins similar to insect chitin deacetylase-like proteins; The family includes many uncharacterized bacterial hypothetical proteins that show high sequence similarity to insect chitin deacetylase-like proteins. Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues.


Pssm-ID: 200598 [Multi-domain]  Cd Length: 299  Bit Score: 64.69  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 107 LWL-HSTNHEIGVNSITREDLSGR----TQERWYKEQKGMRETLAE------------FSFIDRSHIIGTRAPELKiGGD 169
Cdd:cd10976   78 LNAaYREGHEIGSHANGHFDGKGGggrwSVADWKREFDQFYRFVENayaingiegappWPAFAPNSIKGFRAPCLE-GSK 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 170 AQYRMMSENNFTFDNSMLVSSPYWPQTLDhklawecdgncptqshkAIWEIPIQNIQANDTR----------WYKTLTRA 239
Cdd:cd10976  157 GLQPALKKHGFTYDASSVTQGPYWPQKVD-----------------GIWNFPLPLVPEGPTSrpviamdynlFVRHSGGV 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226 240 MKPFDS--RDSVTKMLQRN-FMNHYKTNRAPfiLTLDTEFLTYlpdNGAVY--ALRDFLKFIVQKQDVFVVTGSQIIDYM 314
Cdd:cd10976  220 EAPAKAaeFEARMLATYRNaFDRAYNGNRAP--LQLGNHFVKW---NGGAYwnALERFAEEVCTKPEVKCVTYRELVDFL 294
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 55-147 4.98e-05

Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyses glucosidic bonds in xylan.


Pssm-ID: 426305 [Multi-domain]  Cd Length: 124  Bit Score: 42.60  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226   55 PQMVMLSFDD---PITDRIINTLKSLfsgsirnpngcAIKGTFFVSHQW--NNYDQSLWLHSTNHEIGVNSITREDLSGR 129
Cdd:pfam01522   6 KKVVALTFDDgpsENTPAILDVLKKY-----------GVKATFFVIGGNveRYPDLVKRMVEAGHEIGNHTWSHPNLTGL 74

                          90
                  ....*....|....*...
gi 193210226  130 TQERWYKEQKGMRETLAE 147
Cdd:pfam01522  75 SPEEIRKEIERAQDALEK 92
CE4_NodB_like_6s_7s cd10917
Catalytic NodB homology domain of rhizobial NodB-like proteins; This family belongs to the ...
 58-137 2.18e-04

Catalytic NodB homology domain of rhizobial NodB-like proteins; This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.


Pssm-ID: 213022 [Multi-domain]  Cd Length: 171  Bit Score: 41.45  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226  58 VMLSFDD----PITDRIINTLKSlfsgsirnpNGcaIKGTFFVSHQW--NNYDQSLWLHSTNHEIGVNSITREDLSGRTQ 131
Cdd:cd10917    3 VALTFDDgpdpEYTPKILDILAE---------YG--VKATFFVVGENveKHPDLVRRIVAEGHEIGNHTYSHPDLTKLSP 71


                 ....*.
gi 193210226 132 ERWYKE 137
Cdd:cd10917   72 EEIRAE 77
CE4_GLA_like_6s cd10967
Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is ...
 57-147 3.44e-04

Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is represented by the extracellular polysaccharide-degrading enzyme, gellan lyase (gellanase, EC 4.2.2.-), from Bacillus sp. The enzyme acts on gellan exolytically and releases a tetrasaccharide of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the nonreducing terminus. The family also includes many uncharacterized prokaryotic polysaccharide deacetylases, which show high sequence similarity to Bacillus sp. gellan lyase. Although their biological functions remain unknown, all members of the family contain a conserved domain with a 6-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 200589 [Multi-domain]  Cd Length: 202  Bit Score: 41.21  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210226  57 MVMLSFDD-PITD-RIINTLKSlfsgsirnpNGcaIKGTFFVSHQWNNYDQSL------WLHSTNHEIGVNSITREDLSG 128
Cdd:cd10967    2 AVSLTFDDgYAQDlRAAPLLAK---------YG--LKGTFFVNSGLLGRRGYLdleelrELAAAGHEIGSHTVTHPDLTS 70

                         90
                 ....*....|....*....
gi 193210226 129 RTQERWYKEQKGMRETLAE 147
Cdd:cd10967   71 LPPAELRREIAESRAALEE 89
 
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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