NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1983980463|gb|QRN76671|]
View 

silk gland uncharacterized conserved 2 [Tineola bisselliella]

Protein Classification

CE4_CDA_like_2 domain-containing protein( domain architecture ID 10181088)

CE4_CDA_like_2 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CE4_CDA_like_2 cd10975
Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3. ...
 51-321 5.94e-135

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: 386.29  E-value: 5.94e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  51 PQFVMVTFDDGVNIRNIETYRRVLYGRVNSKGCRAGVTFYVNHQFTSYALVNELYNQGYELSLHSISHQTPQTYWADADF 130
Cdd:cd10975     1 PQLVTLTFDDAVNTLNYPYYEKLFGNRKNPNGCPIGATFFVSHEYTDYRLVQELYNDGHEIALHSISHRSPQDYWRNASV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 131 ETLVKEIADQRPQMAHFANIPEEAIKGVRIPFLQLSGNNSFAAMKEAGLLYDCTWGTVNQIDPGLWPYTLDFRSTQECLT 210
Cdd:cd10975    81 DEWEREFGGQREILAHFANIPAEDIKGFRAPFLQLGGDATFKALKQLGLTYDSSWPTQSFTNPPLWPYTLDYGSTQDCVI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 211 PPCPTASIPGIWVLPMISWIDDSNSPCVMVDACfspPDQDDEDAWFRFIVRNFERHYLGNRAPFGFFIHEWYLTVYPKVE 290
Cdd:cd10975   161 PPCPTDSYPGFWVVPMVDWQDLNGVPCSMLAAC---PPPGTADEVYDWLLSNFERHYNTNRAPFGLYLHASWFEFTPNRL 237

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1983980463 291 RALERFMDMINNMHDVFMVNSHEVIDWVKNP 321
Cdd:cd10975   238 EGFKKFLDELLSLDDVYLVTISQAIEWMRNP 268
 
Name Accession Description Interval E-value
CE4_CDA_like_2 cd10975
Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3. ...
 51-321 5.94e-135

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: 386.29  E-value: 5.94e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  51 PQFVMVTFDDGVNIRNIETYRRVLYGRVNSKGCRAGVTFYVNHQFTSYALVNELYNQGYELSLHSISHQTPQTYWADADF 130
Cdd:cd10975     1 PQLVTLTFDDAVNTLNYPYYEKLFGNRKNPNGCPIGATFFVSHEYTDYRLVQELYNDGHEIALHSISHRSPQDYWRNASV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 131 ETLVKEIADQRPQMAHFANIPEEAIKGVRIPFLQLSGNNSFAAMKEAGLLYDCTWGTVNQIDPGLWPYTLDFRSTQECLT 210
Cdd:cd10975    81 DEWEREFGGQREILAHFANIPAEDIKGFRAPFLQLGGDATFKALKQLGLTYDSSWPTQSFTNPPLWPYTLDYGSTQDCVI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 211 PPCPTASIPGIWVLPMISWIDDSNSPCVMVDACfspPDQDDEDAWFRFIVRNFERHYLGNRAPFGFFIHEWYLTVYPKVE 290
Cdd:cd10975   161 PPCPTDSYPGFWVVPMVDWQDLNGVPCSMLAAC---PPPGTADEVYDWLLSNFERHYNTNRAPFGLYLHASWFEFTPNRL 237

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1983980463 291 RALERFMDMINNMHDVFMVNSHEVIDWVKNP 321
Cdd:cd10975   238 EGFKKFLDELLSLDDVYLVTISQAIEWMRNP 268
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
 37-198 5.03e-07

Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440490 [Multi-domain]  Cd Length: 195  Bit Score: 49.66  E-value: 5.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  37 SSSSIPDGLAARDTPQ-FVMVTFDDGVNirniETYRRVL-----YGrvnskgcrAGVTFYVNHQF--TSYALVNELYNQG 108
Cdd:COG0726     4 SLDELLPALRWGPLPKkAVALTFDDGPR----EGTPRLLdllkkYG--------VKATFFVVGSAveRHPELVREIAAAG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 109 YELSLHSISHQtpqtYWADADFETLVKEIADQRpqmAHFANIPEEAIKGVRIPFLQLSgNNSFAAMKEAGLLYDCTwgtv 188
Cdd:COG0726    72 HEIGNHTYTHP----DLTKLSEEEERAEIARAK---EALEELTGKRPRGFRPPYGRYS-PETLDLLAELGYRYILW---- 139

                         170
                  ....*....|
gi 1983980463 189 NQIDPGLWPY 198
Cdd:COG0726   140 DSVDSDDWPY 149
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 54-181 1.80e-04

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: 40.68  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  54 VMVTFDDGVNirniETYRRVLygRV-NSKGCRAgvTFYVNhqfTSYA-----LVNELYNQGYELSLHSISHQtpqtYWAD 127
Cdd:pfam01522   9 VALTFDDGPS----ENTPAIL--DVlKKYGVKA--TFFVI---GGNVerypdLVKRMVEAGHEIGNHTWSHP----NLTG 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1983980463 128 ADFETLVKEIadQRPQMAhFANIPEEAIKGVRIPFLQLSgNNSFAAMKEAGLLY 181
Cdd:pfam01522  74 LSPEEIRKEI--ERAQDA-LEKATGKRPRLFRPPYGSYN-DTVLEVAKKLGYTA 123
 
Name Accession Description Interval E-value
CE4_CDA_like_2 cd10975
Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3. ...
 51-321 5.94e-135

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: 386.29  E-value: 5.94e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  51 PQFVMVTFDDGVNIRNIETYRRVLYGRVNSKGCRAGVTFYVNHQFTSYALVNELYNQGYELSLHSISHQTPQTYWADADF 130
Cdd:cd10975     1 PQLVTLTFDDAVNTLNYPYYEKLFGNRKNPNGCPIGATFFVSHEYTDYRLVQELYNDGHEIALHSISHRSPQDYWRNASV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 131 ETLVKEIADQRPQMAHFANIPEEAIKGVRIPFLQLSGNNSFAAMKEAGLLYDCTWGTVNQIDPGLWPYTLDFRSTQECLT 210
Cdd:cd10975    81 DEWEREFGGQREILAHFANIPAEDIKGFRAPFLQLGGDATFKALKQLGLTYDSSWPTQSFTNPPLWPYTLDYGSTQDCVI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 211 PPCPTASIPGIWVLPMISWIDDSNSPCVMVDACfspPDQDDEDAWFRFIVRNFERHYLGNRAPFGFFIHEWYLTVYPKVE 290
Cdd:cd10975   161 PPCPTDSYPGFWVVPMVDWQDLNGVPCSMLAAC---PPPGTADEVYDWLLSNFERHYNTNRAPFGLYLHASWFEFTPNRL 237

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1983980463 291 RALERFMDMINNMHDVFMVNSHEVIDWVKNP 321
Cdd:cd10975   238 EGFKKFLDELLSLDDVYLVTISQAIEWMRNP 268
CE4_CDA_like_1 cd10974
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ...
 51-321 3.51e-83

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: 254.57  E-value: 3.51e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  51 PQFVMVTFDDGVNIRNIETYRRVLYGRV-NSKGCRAGVTFYVNHQFTSYALVNELYNQGYELSLHSISHQTPQTywaDAD 129
Cdd:cd10974     1 PQMITLTFDDAINDNNIELYKKIFNGKRnNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDEN---NAT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 130 FETLVKEIADQRPQMAHFANIPEEAIKGVRIPFLQLSGNNSFAAMKEAGLLYDCTWgTVNQIDPGLWPYTLDFRSTQECL 209
Cdd:cd10974    78 YEDWVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSI-TAPPSNVPLWPYTLDYKMPHECH 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 210 TPPCPTASIPGIWVLPM-------ISWIDdsnSPCVMVDACfspPDQDDEDAWFRFIVRNFERHYLGNRAPFGFFIHEWY 282
Cdd:cd10974   157 GQNCPTRSFPGVWEMVLneldvrdDPQGD---EPLAMDDSC---LNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNW 230

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1983980463 283 LTVYPKVERALERFMDMINNMHDVFMVNSHEVIDWVKNP 321
Cdd:cd10974   231 LKTKNELLRALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
CE4_CDA_like cd10919
Putative catalytic domain of chitin deacetylase-like proteins from insects and similar ...
 51-321 5.29e-64

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: 205.29  E-value: 5.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  51 PQFVMVTFDDGVNIRNIETY-RRVLYGRVNSKGCRAGVTFYVNHQFTSYALVNELYNQGYELSLHSISHQTPQTYWadaD 129
Cdd:cd10919     1 PQFVLFTFDDAINELNTDAViQEIADGTNNNGGCPIPATFFVSTNYTDCSLVKQLWREGHEIATHTVTHVPDDSNA---S 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 130 FETLVKEIADQRPQMAHFANIPEEAIKGVRIPFLQlSGNNSFAAMKEAGLLYDCTwGTVNQIDPG---LWPYTLDFRSTQ 206
Cdd:cd10919    78 VDEWEEEIAGQREWLNKTCGIPLEKVVGFRAPYLA-YNPNTREVLEENGFLYDSS-IPEPYTPSGtnrLWPYTLDYGIPQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 207 ECLTPPCPTASI---PGIWVLPMISWIDDSNSPCVMvDACFSPPDQDDEDAWFRFIVRNFERHYLGNRAPFGFFIH-EWY 282
Cdd:cd10919   156 DCNLVPGSCSPTeryPGLWEVPLYTLQDGNDTTGDS-YYCTPDDGPLNGDSFYALLKYNFDRHYNGNRAPFGIYLHaAWL 234

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1983980463 283 LTVYPKVERALERFMDMINNMHDVFMVNSHEVIDWVKNP 321
Cdd:cd10919   235 SPPYSERRAALEKFLDYALSKPDVWFVTNSQLLDWMQNP 273
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
 37-198 5.03e-07

Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440490 [Multi-domain]  Cd Length: 195  Bit Score: 49.66  E-value: 5.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  37 SSSSIPDGLAARDTPQ-FVMVTFDDGVNirniETYRRVL-----YGrvnskgcrAGVTFYVNHQF--TSYALVNELYNQG 108
Cdd:COG0726     4 SLDELLPALRWGPLPKkAVALTFDDGPR----EGTPRLLdllkkYG--------VKATFFVVGSAveRHPELVREIAAAG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 109 YELSLHSISHQtpqtYWADADFETLVKEIADQRpqmAHFANIPEEAIKGVRIPFLQLSgNNSFAAMKEAGLLYDCTwgtv 188
Cdd:COG0726    72 HEIGNHTYTHP----DLTKLSEEEERAEIARAK---EALEELTGKRPRGFRPPYGRYS-PETLDLLAELGYRYILW---- 139

                         170
                  ....*....|
gi 1983980463 189 NQIDPGLWPY 198
Cdd:COG0726   140 DSVDSDDWPY 149
CE4_CDA_like_3 cd10976
Putative catalytic domain of uncharacterized bacterial hypothetical proteins similar to insect ...
 51-317 2.89e-06

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: 48.51  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  51 PQFVMVTFD---------------DGVNIRNieTY-----------RRVLYGRVNSKGCRAGVTFYVNHQ--FTSYALVN 102
Cdd:cd10976     2 PQFVVFSFDgagdnqlwsrsravaKQTNARF--TYflsgvylltteNRTLYTPPGQKAGRSNIGFAGSRQevADRLRQLN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 103 ELYNQGYELSLHSISH---QTPQTYWADADFE---TLVKEIADQRPQMAHFANIPE------EAIKGVRIPFLQlSGNNS 170
Cdd:cd10976    80 AAYREGHEIGSHANGHfdgKGGGGRWSVADWKrefDQFYRFVENAYAINGIEGAPPwpafapNSIKGFRAPCLE-GSKGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 171 FAAMKEAGLLYDCTwgTVNQIdPGlWPYTLDfrstqecltppcptasipGIWVLPMIS---------WID-DSNSpCVMV 240
Cdd:cd10976   159 QPALKKHGFTYDAS--SVTQG-PY-WPQKVD------------------GIWNFPLPLvpegptsrpVIAmDYNL-FVRH 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 241 DACFSPPDQDDEdawFRFIVRN-----FERHYLGNRAPF--GFFIHEWYLTVYpkvERALERFMDMINNMHDVFMVNSHE 313
Cdd:cd10976   216 SGGVEAPAKAAE---FEARMLAtyrnaFDRAYNGNRAPLqlGNHFVKWNGGAY---WNALERFAEEVCTKPEVKCVTYRE 289


                  ....
gi 1983980463 314 VIDW 317
Cdd:cd10976   290 LVDF 293
CE4_PuuE_HpPgdA_like_2 cd10941
Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar ...
 99-296 6.67e-06

Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar to bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA); This family contains many uncharacterized prokaryotic polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as homotetramers. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCA-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, PuuE allantoinase and HpPgdA do not exhibit a solvent-accessible polysaccharide binding groove and might only bind a small molecule at the active site.


Pssm-ID: 200566 [Multi-domain]  Cd Length: 258  Bit Score: 46.90  E-value: 6.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  99 ALVNELYNQGYELSLHSISHQTPQTYWADADFETLVKEIadqrpqmAHFANIPEEAIKGVRIPFLQLSGnNSFAAMKEAG 178
Cdd:cd10941    62 DLIRRIAEAGHEIASHGYAHERVDRLTPEEFREDLRRSK-------KILEDITGQKVVGFRAPNFSITP-WALDILAEAG 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463 179 LLYDCTwgtvnqidpgLWPYTLDFR--STQECLTPPCPTASIPGIWVLPMiswiddSNSPCVMVDACFSPpdqddeDAWF 256
Cdd:cd10941   134 YLYDSS----------VFPTKRPGYggPLAPKSEPLPPIRAKGGILEFPV------SVTKLPGLRLPLAG------GGYF 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1983980463 257 RF----IVRNFERHYLGNRAPFGFFIHEW---------------YLTVYPKVERALERF 296
Cdd:cd10941   192 RLlpyrLIKALIKRSLRRGGPLVLYFHPWefdpeqpvpglpllrRFRTYVGLGKAEEKL 250
CE4_SF cd10585
Catalytic NodB homology domain of the carbohydrate esterase 4 superfamily; The carbohydrate ...
 54-189 1.15e-05

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.


Pssm-ID: 213020 [Multi-domain]  Cd Length: 142  Bit Score: 44.75  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  54 VMVTFDDGVNIRNIetYRRVLYGRVNSKGCRAGVTFYVNHQF----------TSYALVNELYNQGYELSLHSISHQTPQT 123
Cdd:cd10585     2 VLLTLDDDPAFEGS--PAALQRLLDLLEGYGIPATLFVIPGNanpdklmkspLNWDLLRELLAYGHEIGLHGYTHPDLAY 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983980463 124 YWADADFETlvKEIADQRpqmAHFANIPEEAIKGVRIPFLQLsgNNSFAAMKEAGLLYDCTWGTVN 189
Cdd:cd10585    80 GNLSPEEVL--EDLLRAR---RILEEAGGQPPKGFRAPGGNL--SETVKALKELGDIQYDSDLAFV 138
CE4_GLA_like_6s cd10967
Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is ...
 54-141 1.42e-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: 42.37  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  54 VMVTFDDGVNirNIETYRRVLygrvNSKGCRAgvTFYVN------HQFTSYALVNELYNQGYELSLHSISHQTPQTYwad 127
Cdd:cd10967     3 VSLTFDDGYA--QDLRAAPLL----AKYGLKG--TFFVNsgllgrRGYLDLEELRELAAAGHEIGSHTVTHPDLTSL--- 71

                          90
                  ....*....|....
gi 1983980463 128 aDFETLVKEIADQR 141
Cdd:cd10967    72 -PPAELRREIAESR 84
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 54-181 1.80e-04

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: 40.68  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980463  54 VMVTFDDGVNirniETYRRVLygRV-NSKGCRAgvTFYVNhqfTSYA-----LVNELYNQGYELSLHSISHQtpqtYWAD 127
Cdd:pfam01522   9 VALTFDDGPS----ENTPAIL--DVlKKYGVKA--TFFVI---GGNVerypdLVKRMVEAGHEIGNHTWSHP----NLTG 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1983980463 128 ADFETLVKEIadQRPQMAhFANIPEEAIKGVRIPFLQLSgNNSFAAMKEAGLLY 181
Cdd:pfam01522  74 LSPEEIRKEI--ERAQDA-LEKATGKRPRLFRPPYGSYN-DTVLEVAKKLGYTA 123
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH