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Conserved domains on  [gi|386768834|ref|NP_001245806|]
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chitin deacetylase-like 5, isoform G [Drosophila melanogaster]

Protein Classification

chitin binding peritrophin-A domain-containing protein; glycoside hydrolase family 18 protein( domain architecture ID 10482850)

chitin binding peritrophin-A domain-containing protein similar to Blomia tropicalis major allergen Blo t 12 and Caenorhabditis elegans chondroitin proteoglycan 1| glycoside hydrolase family 18 protein similar to chitinase, which catalyzes the random endo-hydrolysis of the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins

Graphical summary

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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. ...
 1456-1718 2.15e-149

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: 459.86  E-value: 2.15e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1456 PQIVLLTFDDSVNDLNKQLYTDLFEkGRVNPNGCPITATFYVSHEWTDYSQVQNLYADGHEMASHTVSHSFGEQF----S 1531
Cdd:cd10975     1 PQLVTLTFDDAVNTLNYPYYEKLFG-NRKNPNGCPIGATFFVSHEYTDYRLVQELYNDGHEIALHSISHRSPQDYwrnaS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1532 QKKWTREIAGQREILAAYGGVKMSDVRGMRAPFLSVGGNKMYKMLYDSNFTYDSSMPVYE-NRPPSWPYTLDYKIFHDCM 1610
Cdd:cd10975    80 VDEWEREFGGQREILAHFANIPAEDIKGFRAPFLQLGGDATFKALKQLGLTYDSSWPTQSfTNPPLWPYTLDYGSTQDCV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1611 IPPCPTRSYPGVWQVPMVMWQDLNGGRCSMGDACSNPSDADGVTKMIMKNFERHYTTNRAPFGLFYHAAWFTQ-PHHKEG 1689
Cdd:cd10975   160 IPPCPTDSYPGFWVVPMVDWQDLNGVPCSMLAACPPPGTADEVYDWLLSNFERHYNTNRAPFGLYLHASWFEFtPNRLEG 239

                         250       260
                  ....*....|....*....|....*....
gi 386768834 1690 FIKFLDAINAMQDVWIITNWQALQWVRDP 1718
Cdd:cd10975   240 FKKFLDELLSLDDVYLVTISQAIEWMRNP 268
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 58-106 3.66e-14

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 68.21  E-value: 3.66e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 386768834    58 CPE-EFGYYPHPSDCTQYYVCVFGGALLESCTGGLMYSHDLQTCDWPRNV 106
Cdd:pfam01607    1 CAGkEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNV 50
PTZ00395 super family cl33180
Sec24-related protein; Provisional
 442-537 6.05e-05

Sec24-related protein; Provisional


The actual alignment was detected with superfamily member PTZ00395:

Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 48.15  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834  442 AGYSFGNYN-------PYLTPPNTNPVHNQQPYGNPNYNHLPgYHSYVHQQQQLASAGPFSQKKHKLAY-TGY---NLSL 510
Cdd:PTZ00395  417 PGNSNPGYNnapnsntPYNNPPNSNTPYSNPPNSNPPYSNLP-YSNTPYSNAPLSNAPPSSAKDHHSAYhAAYqhrAANQ 495

                          90       100
                  ....*....|....*....|....*..
gi 386768834  511 PPPPLEDDFRPIAGSYYEAAGAAQTSP 537
Cdd:PTZ00395  496 PAANLPTANQPAANNFHGAAGNSVGNP 522
 
Name Accession Description Interval E-value
CE4_CDA_like_2 cd10975
Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3. ...
 1456-1718 2.15e-149

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: 459.86  E-value: 2.15e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1456 PQIVLLTFDDSVNDLNKQLYTDLFEkGRVNPNGCPITATFYVSHEWTDYSQVQNLYADGHEMASHTVSHSFGEQF----S 1531
Cdd:cd10975     1 PQLVTLTFDDAVNTLNYPYYEKLFG-NRKNPNGCPIGATFFVSHEYTDYRLVQELYNDGHEIALHSISHRSPQDYwrnaS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1532 QKKWTREIAGQREILAAYGGVKMSDVRGMRAPFLSVGGNKMYKMLYDSNFTYDSSMPVYE-NRPPSWPYTLDYKIFHDCM 1610
Cdd:cd10975    80 VDEWEREFGGQREILAHFANIPAEDIKGFRAPFLQLGGDATFKALKQLGLTYDSSWPTQSfTNPPLWPYTLDYGSTQDCV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1611 IPPCPTRSYPGVWQVPMVMWQDLNGGRCSMGDACSNPSDADGVTKMIMKNFERHYTTNRAPFGLFYHAAWFTQ-PHHKEG 1689
Cdd:cd10975   160 IPPCPTDSYPGFWVVPMVDWQDLNGVPCSMLAACPPPGTADEVYDWLLSNFERHYNTNRAPFGLYLHASWFEFtPNRLEG 239

                         250       260
                  ....*....|....*....|....*....
gi 386768834 1690 FIKFLDAINAMQDVWIITNWQALQWVRDP 1718
Cdd:cd10975   240 FKKFLDELLSLDDVYLVTISQAIEWMRNP 268
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
 1459-1606 2.59e-15

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: 76.24  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1459 VLLTFDDSVNDLNKQLYtDLFEKgrvnpNGcpITATFYVSHEWTDYS--QVQNLYADGHEMASHTVSHSFGEQFSQKKWT 1536
Cdd:COG0726    22 VALTFDDGPREGTPRLL-DLLKK-----YG--VKATFFVVGSAVERHpeLVREIAAAGHEIGNHTYTHPDLTKLSEEEER 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1537 REIAGQREILAAYGGVKmsdVRGMRAPFLSVgGNKMYKMLYDSNFTYDSSMPVYenrPPSWPYTLDYKIF 1606
Cdd:COG0726    94 AEIARAKEALEELTGKR---PRGFRPPYGRY-SPETLDLLAELGYRYILWDSVD---SDDWPYPSADAIV 156
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 58-106 3.66e-14

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 68.21  E-value: 3.66e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 386768834    58 CPE-EFGYYPHPSDCTQYYVCVFGGALLESCTGGLMYSHDLQTCDWPRNV 106
Cdd:pfam01607    1 CAGkEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNV 50
ChtBD2 smart00494
Chitin-binding domain type 2;
56-103 2.29e-12

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 63.23  E-value: 2.29e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 386768834     56 FDCPE-EFGYYPHPSDCTQYYVCVFGGALLESCTGGLMYSHDLQTCDWP 103
Cdd:smart00494    1 NECPGrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 1459-1566 4.08e-10

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: 59.17  E-value: 4.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834  1459 VLLTFDDSVNDLNKQLYtDLFEKGRVNpngcpitATFYVSHEWTDY--SQVQNLYADGHEMASHTVSHSFGEQFSQKKWT 1536
Cdd:pfam01522    9 VALTFDDGPSENTPAIL-DVLKKYGVK-------ATFFVIGGNVERypDLVKRMVEAGHEIGNHTWSHPNLTGLSPEEIR 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 386768834  1537 REIAGQREILAAYGGVKmsdVRGMRAPFLS 1566
Cdd:pfam01522   81 KEIERAQDALEKATGKR---PRLFRPPYGS 107
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 442-537 6.05e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 48.15  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834  442 AGYSFGNYN-------PYLTPPNTNPVHNQQPYGNPNYNHLPgYHSYVHQQQQLASAGPFSQKKHKLAY-TGY---NLSL 510
Cdd:PTZ00395  417 PGNSNPGYNnapnsntPYNNPPNSNTPYSNPPNSNPPYSNLP-YSNTPYSNAPLSNAPPSSAKDHHSAYhAAYqhrAANQ 495

                          90       100
                  ....*....|....*....|....*..
gi 386768834  511 PPPPLEDDFRPIAGSYYEAAGAAQTSP 537
Cdd:PTZ00395  496 PAANLPTANQPAANNFHGAAGNSVGNP 522
 
Name Accession Description Interval E-value
CE4_CDA_like_2 cd10975
Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3. ...
 1456-1718 2.15e-149

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: 459.86  E-value: 2.15e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1456 PQIVLLTFDDSVNDLNKQLYTDLFEkGRVNPNGCPITATFYVSHEWTDYSQVQNLYADGHEMASHTVSHSFGEQF----S 1531
Cdd:cd10975     1 PQLVTLTFDDAVNTLNYPYYEKLFG-NRKNPNGCPIGATFFVSHEYTDYRLVQELYNDGHEIALHSISHRSPQDYwrnaS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1532 QKKWTREIAGQREILAAYGGVKMSDVRGMRAPFLSVGGNKMYKMLYDSNFTYDSSMPVYE-NRPPSWPYTLDYKIFHDCM 1610
Cdd:cd10975    80 VDEWEREFGGQREILAHFANIPAEDIKGFRAPFLQLGGDATFKALKQLGLTYDSSWPTQSfTNPPLWPYTLDYGSTQDCV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1611 IPPCPTRSYPGVWQVPMVMWQDLNGGRCSMGDACSNPSDADGVTKMIMKNFERHYTTNRAPFGLFYHAAWFTQ-PHHKEG 1689
Cdd:cd10975   160 IPPCPTDSYPGFWVVPMVDWQDLNGVPCSMLAACPPPGTADEVYDWLLSNFERHYNTNRAPFGLYLHASWFEFtPNRLEG 239

                         250       260
                  ....*....|....*....|....*....
gi 386768834 1690 FIKFLDAINAMQDVWIITNWQALQWVRDP 1718
Cdd:cd10975   240 FKKFLDELLSLDDVYLVTISQAIEWMRNP 268
CE4_CDA_like_1 cd10974
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ...
 1456-1718 1.36e-111

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: 355.11  E-value: 1.36e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1456 PQIVLLTFDDSVNDLNKQLYTDLFEKGRVNPNGCPITATFYVSHEWTDYSQVQNLYADGHEMASHTVSHSFGEQF-SQKK 1534
Cdd:cd10974     1 PQMITLTFDDAINDNNIELYKKIFNGKRNNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDENNaTYED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1535 WTREIAGQREILAAYGGVKMSDVRGMRAPFLSVGGNKMYKMLYDSNFTYDSSMPVYENRPPSWPYTLDYKIFHDCMIPPC 1614
Cdd:cd10974    81 WVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAPPSNVPLWPYTLDYKMPHECHGQNC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1615 PTRSYPGVWQVPMVMWQ--DLNGGRCS--MGDACSNPSDADGVTKMIMKNFERHYTTNRAPFGLFYHAAWFTQ-PHHKEG 1689
Cdd:cd10974   161 PTRSFPGVWEMVLNELDvrDDPQGDEPlaMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTkNELLRA 240

                         250       260
                  ....*....|....*....|....*....
gi 386768834 1690 FIKFLDAINAMQDVWIITNWQALQWVRDP 1718
Cdd:cd10974   241 LQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
CE4_CDA_like cd10919
Putative catalytic domain of chitin deacetylase-like proteins from insects and similar ...
 1456-1718 7.17e-111

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: 353.59  E-value: 7.17e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1456 PQIVLLTFDDSVNDLNKQLYTDLFEKGRVNPNGCPITATFYVSHEWTDYSQVQNLYADGHEMASHTVSHSFGEQ-FSQKK 1534
Cdd:cd10919     1 PQFVLFTFDDAINELNTDAVIQEIADGTNNNGGCPIPATFFVSTNYTDCSLVKQLWREGHEIATHTVTHVPDDSnASVDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1535 WTREIAGQREILAAYGGVKMSDVRGMRAPFLsVGGNKMYKMLYDSNFTYDSSMPVY---ENRPPSWPYTLDYKIFHDCMI 1611
Cdd:cd10919    81 WEEEIAGQREWLNKTCGIPLEKVVGFRAPYL-AYNPNTREVLEENGFLYDSSIPEPytpSGTNRLWPYTLDYGIPQDCNL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1612 PPC---PTRSYPGVWQVPMVMWQDLNGGRCS--MGDACSNPSDADGVTKMIMKNFERHYTTNRAPFGLFYHAAWFTQP-- 1684
Cdd:cd10919   160 VPGscsPTERYPGLWEVPLYTLQDGNDTTGDsyYCTPDDGPLNGDSFYALLKYNFDRHYNGNRAPFGIYLHAAWLSPPys 239

                         250       260       270
                  ....*....|....*....|....*....|....
gi 386768834 1685 HHKEGFIKFLDAINAMQDVWIITNWQALQWVRDP 1718
Cdd:cd10919   240 ERRAALEKFLDYALSKPDVWFVTNSQLLDWMQNP 273
CE4_SF cd10585
Catalytic NodB homology domain of the carbohydrate esterase 4 superfamily; The carbohydrate ...
 1458-1589 7.91e-20

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: 87.50  E-value: 7.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1458 IVLLTFDDSVNDLNKQLYTDLFEKGRvnpNGCPITATFYVSHEW----------TDYSQVQNLYADGHEMASHTVSHSFG 1527
Cdd:cd10585     1 LVLLTLDDDPAFEGSPAALQRLLDLL---EGYGIPATLFVIPGNanpdklmkspLNWDLLRELLAYGHEIGLHGYTHPDL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386768834 1528 E--QFSQKKWTREIAGQREILAAYGGVkmsDVRGMRAPFLSVG-GNKMYKMLYDsnFTYDSSMPV 1589
Cdd:cd10585    78 AygNLSPEEVLEDLLRARRILEEAGGQ---PPKGFRAPGGNLSeTVKALKELGD--IQYDSDLAF 137
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
 1459-1606 2.59e-15

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: 76.24  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1459 VLLTFDDSVNDLNKQLYtDLFEKgrvnpNGcpITATFYVSHEWTDYS--QVQNLYADGHEMASHTVSHSFGEQFSQKKWT 1536
Cdd:COG0726    22 VALTFDDGPREGTPRLL-DLLKK-----YG--VKATFFVVGSAVERHpeLVREIAAAGHEIGNHTYTHPDLTKLSEEEER 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1537 REIAGQREILAAYGGVKmsdVRGMRAPFLSVgGNKMYKMLYDSNFTYDSSMPVYenrPPSWPYTLDYKIF 1606
Cdd:COG0726    94 AEIARAKEALEELTGKR---PRGFRPPYGRY-SPETLDLLAELGYRYILWDSVD---SDDWPYPSADAIV 156
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 58-106 3.66e-14

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 68.21  E-value: 3.66e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 386768834    58 CPE-EFGYYPHPSDCTQYYVCVFGGALLESCTGGLMYSHDLQTCDWPRNV 106
Cdd:pfam01607    1 CAGkEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNV 50
CE4_CDA_like_3 cd10976
Putative catalytic domain of uncharacterized bacterial hypothetical proteins similar to insect ...
 1511-1680 1.81e-12

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: 70.08  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1511 YADGHEMASHTVSH----SFGEQFSQKKWTREIAGQREILA-AYGGVKMSD-----------VRGMRAPFLSVGGNkMYK 1574
Cdd:cd10976    82 YREGHEIGSHANGHfdgkGGGGRWSVADWKREFDQFYRFVEnAYAINGIEGappwpafapnsIKGFRAPCLEGSKG-LQP 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1575 MLYDSNFTYDSSMPvyeNRPPSWPYTLDyKIFHDCM--IPPCPTRSypgvwqvpMVMWQDLN-GGRCSMGdaCSNPSDAD 1651
Cdd:cd10976   161 ALKKHGFTYDASSV---TQGPYWPQKVD-GIWNFPLplVPEGPTSR--------PVIAMDYNlFVRHSGG--VEAPAKAA 226

                         170       180       190
                  ....*....|....*....|....*....|....
gi 386768834 1652 ---GVTKMIMKN-FERHYTTNRAPFGLFYH-AAW 1680
Cdd:cd10976   227 efeARMLATYRNaFDRAYNGNRAPLQLGNHfVKW 260
ChtBD2 smart00494
Chitin-binding domain type 2;
56-103 2.29e-12

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 63.23  E-value: 2.29e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 386768834     56 FDCPE-EFGYYPHPSDCTQYYVCVFGGALLESCTGGLMYSHDLQTCDWP 103
Cdd:smart00494    1 NECPGrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
CE4_GLA_like_6s cd10967
Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is ...
 1459-1564 3.26e-12

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: 67.40  E-value: 3.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1459 VLLTFDDSVNDLNKqlYTDLFEKgrvnpNGCPitATFYVS------HEWTDYSQVQNLYADGHEMASHTVSHSFGEQFSQ 1532
Cdd:cd10967     3 VSLTFDDGYAQDLR--AAPLLAK-----YGLK--GTFFVNsgllgrRGYLDLEELRELAAAGHEIGSHTVTHPDLTSLPP 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 386768834 1533 KKWTREIAGQREILAAYGGVKmsdVRGMRAPF 1564
Cdd:cd10967    74 AELRREIAESRAALEEIGGFP---VTSFAYPF 102
CE4_PuuE_HpPgdA_like_2 cd10941
Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar ...
 1491-1626 2.59e-10

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: 63.08  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1491 ITATFYVSHEWTD-YSQ-VQNLYADGHEMASHTVSHSFGEQFSQKKWTREIAGQREILAAYGGVKmsdVRGMRAPFLSVG 1568
Cdd:cd10941    46 VKATFFVLGEVAErYPDlIRRIAEAGHEIASHGYAHERVDRLTPEEFREDLRRSKKILEDITGQK---VVGFRAPNFSIT 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386768834 1569 GnKMYKMLYDSNFTYDSSMPVYENRPPSWPYTLDYKifhdcmiPPCPTRSYPGVWQVP 1626
Cdd:cd10941   123 P-WALDILAEAGYLYDSSVFPTKRPGYGGPLAPKSE-------PLPPIRAKGGILEFP 172
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 1459-1566 4.08e-10

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: 59.17  E-value: 4.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834  1459 VLLTFDDSVNDLNKQLYtDLFEKGRVNpngcpitATFYVSHEWTDY--SQVQNLYADGHEMASHTVSHSFGEQFSQKKWT 1536
Cdd:pfam01522    9 VALTFDDGPSENTPAIL-DVLKKYGVK-------ATFFVIGGNVERypDLVKRMVEAGHEIGNHTWSHPNLTGLSPEEIR 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 386768834  1537 REIAGQREILAAYGGVKmsdVRGMRAPFLS 1566
Cdd:pfam01522   81 KEIERAQDALEKATGKR---PRLFRPPYGS 107
CE4_NodB_like_6s_7s cd10917
Catalytic NodB homology domain of rhizobial NodB-like proteins; This family belongs to the ...
 1459-1567 1.46e-07

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: 53.01  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1459 VLLTFDDSVNDLNKQLYTDLFEKgrvnpNGcpITATFYVSHEWTDYSQ--VQNLYADGHEMASHTVSHSFGEQFSQKKWT 1536
Cdd:cd10917     3 VALTFDDGPDPEYTPKILDILAE-----YG--VKATFFVVGENVEKHPdlVRRIVAEGHEIGNHTYSHPDLTKLSPEEIR 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 386768834 1537 REIAGQREILAAYGGVKmsdVRGMRAPFLSV 1567
Cdd:cd10917    76 AEIERTQDAIEEATGVR---PRLFRPPYGAY 103
CE4_CtAXE_like cd10954
Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its ...
 1458-1574 1.83e-07

Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs; This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan, as a consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases.


Pssm-ID: 200578 [Multi-domain]  Cd Length: 180  Bit Score: 52.97  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1458 IVLLTFDDSVNDLNKQLYTDLFEKGRVnpngcpiTATFYV------SHEwtdySQVQNLYADGHEMASHTVSHSFGEQFS 1531
Cdd:cd10954     2 MVALTFDDGPNAKYTPRLLDVLEKYNV-------RATFFLvgqnvnGNK----EIVKRMVEMGCEIGNHSYTHPDLTKLS 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 386768834 1532 QKKWTREIAGQREILAAYGGvkmSDVRGMRAPFLSVGGNkMYK 1574
Cdd:cd10954    71 PSEIKKEIEKTNEAIKKITG---KRPKLFRPPYGAVNDT-VKK 109
CE4_ClCDA_like cd10951
Catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase and similar ...
 1454-1596 5.69e-07

Catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase and similar proteins; This family is represented by the chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41) from Colletotrichum lindemuthianum (also known as Glomerella lindemuthiana), which is a member of the carbohydrate esterase 4 (CE4) superfamily. ClCDA catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. It consists of a single catalytic domain similar to the deformed (alpha/beta)8 barrel fold adopted by other CE4 esterases, 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. It possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity. Unlike its bacterial homologs, ClCDA contains two intramolecular disulfide bonds that may add stability to this secreted protein. The family also includes many uncharacterized deacetylases and hypothetical proteins mainly from eukaryotes, which show high sequence similarity to ClCDA.


Pssm-ID: 200575 [Multi-domain]  Cd Length: 197  Bit Score: 51.89  E-value: 5.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1454 SIPQIVLLTFDDSVNDLNKQLYTDLFEKGrvnpngcpITATFYVS-----HEWTDY-SQVQNLYADGHEMASHTVSHSF- 1526
Cdd:cd10951     5 TVPGTVALTFDDGPSTYTPQLLDLLKEAG--------AKATFFVNgnnfnGCIYDYaDVLRRMYNEGHQIASHTWSHPDl 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1527 ----GEQFSQKKWTREIAGQReILaaygGVKMsdvRGMRAPFLSVGGN------KM-YKMLYDSNFTYDSSMPVYENRPP 1595
Cdd:cd10951    77 tklsAAQIRDEMTKLEDALRK-IL----GVKP---TYMRPPYGECNDEvlavlgELgYHVVTWNLDTGDYNNNSPGSVEE 148


                  .
gi 386768834 1596 S 1596
Cdd:cd10951   149 S 149
CE4_NodB_like_5s_6s cd10918
Putative catalytic NodB homology domain of PgaB, IcaB, and similar proteins which consist of a ...
 1459-1553 6.75e-07

Putative catalytic NodB homology domain of PgaB, IcaB, and similar proteins which consist of a deformed (beta/alpha)8 barrel fold with 5- or 6-strands; 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 bacterial poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB, hemin storage system HmsF protein in gram-negative species, intercellular adhesion proteins IcaB, and many uncharacterized prokaryotic polysaccharide deacetylases. It also includes a putative polysaccharide deacetylase YxkH encoded by the Bacillus subtilis yxkH gene, which is one of six polysaccharide deacetylase gene homologs present in the Bacillus subtilis genome. Sequence comparison shows all family members contain a conserved domain similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, which consists of a deformed (beta/alpha)8 barrel fold with 6 or 7 strands. However, in this family, most proteins have 5 strands and some have 6 strands. Moreover, long insertions are found in many family members, whose function remains unknown.


Pssm-ID: 213023 [Multi-domain]  Cd Length: 157  Bit Score: 50.67  E-value: 6.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1459 VLLTFDDSVNDLNKQLYtDLFEKgrvnpNGCPitATFYVShewTDY--------------------SQVQNLYADGHEMA 1518
Cdd:cd10918     2 VVLTFDDGYRDNYTYAL-PILKK-----YGLP--ATFFVI---TGYigggnpwwapapprppyltwDQLRELAASGVEIG 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 386768834 1519 SHTVSHSFGEQFSQKKWTREIAGQREILAAYGGVK 1553
Cdd:cd10918    71 SHTHTHPDLTTLSDEELRRELAESKERLEEELGKP 105
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 442-537 6.05e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 48.15  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834  442 AGYSFGNYN-------PYLTPPNTNPVHNQQPYGNPNYNHLPgYHSYVHQQQQLASAGPFSQKKHKLAY-TGY---NLSL 510
Cdd:PTZ00395  417 PGNSNPGYNnapnsntPYNNPPNSNTPYSNPPNSNPPYSNLP-YSNTPYSNAPLSNAPPSSAKDHHSAYhAAYqhrAANQ 495

                          90       100
                  ....*....|....*....|....*..
gi 386768834  511 PPPPLEDDFRPIAGSYYEAAGAAQTSP 537
Cdd:PTZ00395  496 PAANLPTANQPAANNFHGAAGNSVGNP 522
CE4_HpPgdA_like cd10938
Catalytic domain of Helicobacter pylori peptidoglycan deacetylase (HpPgdA) and similar ...
 1491-1587 2.36e-04

Catalytic domain of Helicobacter pylori peptidoglycan deacetylase (HpPgdA) and similar proteins; This family is represented by a peptidoglycan deacetylase (HP0310, HpPgdA) from the gram-negative pathogen Helicobacter pylori. 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. It functions as a homotetramer. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase (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, HpPgdA does not exhibit a solvent-accessible polysaccharide binding groove, suggesting that the enzyme binds a small molecule at the active site.


Pssm-ID: 200563 [Multi-domain]  Cd Length: 258  Bit Score: 44.86  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1491 ITATFYVS----HEWTDysQVQNLYADGHEMASHTVSHSFGEQFSQKKWTREIAGQREILAAYGGVKmsdVRGMRAPF-- 1564
Cdd:cd10938    51 VKATFFVPghtaETFPE--AVEAILAAGHEIGHHGYLHENPTGLTPEEERELLERGLELLEKLTGKR---PVGYRSPSwe 125

                          90       100
                  ....*....|....*....|...
gi 386768834 1565 LSVGGNkmyKMLYDSNFTYDSSM 1587
Cdd:cd10938   126 FSPNTL---DLLLEHGFLYDSSL 145
CE4_DAC_u1_6s cd10970
Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide ...
 1458-1608 8.02e-04

Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide deacetylases which consist of a 6-stranded beta/alpha barrel; This family contains uncharacterized prokaryotic polysaccharide deacetylases. 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: 213027 [Multi-domain]  Cd Length: 194  Bit Score: 42.69  E-value: 8.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1458 IVLLTFDDSvndlNKQLYTDLF----EKGrvnpngcpITATFYVSHEW---TDY---SQVQNLYADGHEMASHTVSH-SF 1526
Cdd:cd10970     2 KVSLTFDDG----YESQYTTAFpilqEYG--------IPATAAVIPDSigsSGRltlDQLRELQDAGWEIASHTLTHtDL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1527 GEqFSQKKWTREIAGQREILAAYGGVKmsDVRGMRAPFLSVGGNKMYKM--LYDSNFTYDSSmpvYENRPPSWPYTLDYK 1604
Cdd:cd10970    70 TE-LSADEQRAELTESKRWLEDNGFGD--GADHFAYPYGRYDDEVLELVreYYDLGRSGGGG---PNGRPPLDPYRLRRV 143


                  ....
gi 386768834 1605 IFHD 1608
Cdd:cd10970   144 TGEA 147
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 442-548 1.22e-03

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 43.91  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834  442 AGYSFGNYN--PYLTPPNTNPVHNQQPYGNPNYNHLPgyHSYVHQQQQLASAGPFSQKKH-KLAYTGYNLSLPPPPLEDD 518
Cdd:PTZ00395  402 AAQSNAGFSnaGYSNPGNSNPGYNNAPNSNTPYNNPP--NSNTPYSNPPNSNPPYSNLPYsNTPYSNAPLSNAPPSSAKD 479

                          90       100       110
                  ....*....|....*....|....*....|
gi 386768834  519 FRPIAGSYYEAAGAAQTSPRSPNSKQHHSN 548
Cdd:PTZ00395  480 HHSAYHAAYQHRAANQPAANLPTANQPAAN 509
CE4_DAC_u3_5s cd10972
Putative catalytic NodB homology domain of uncharacterized bacterial polysaccharide ...
 1459-1603 2.41e-03

Putative catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases which consist of a 5-stranded beta/alpha barrel; This family contains uncharacterized bacterial polysaccharide deacetylases. Although their biological functions remain unknown, all members of the family are predicted to contain a conserved domain with a 5-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: 200594 [Multi-domain]  Cd Length: 216  Bit Score: 41.55  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1459 VLLTFDDSVNdlNKQLYTDLFEKGRVNPN--------------GCPITATFYVSHEWTDYSQ-------VQNLYADGHEM 1517
Cdd:cd10972     7 VVLTFDDGSP--GQFRYIEKNGQLVIDPDtavgiledfkeehpDFPPTGTFYVNPGPFGFGQpeyaeqkLRWLVELGYEI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768834 1518 ASHTVSHSFGEQFSQKKWTREIA-GQREILAAYGGVKmsdVRGMRAPF-LSVGGNK--MYKMLYDSN-FTYDSSMPVYEN 1592
Cdd:cd10972    85 GNHTYTHVNLNKLDAEEIQEELArVNKMIEEAIPGYE---VESLALPFgMKPKENRalVLSGEYEGVsYKHQAVLLVGAE 161

                         170
                  ....*....|.
gi 386768834 1593 RPPSwPYTLDY 1603
Cdd:cd10972   162 PAPS-PYSKDF 171
 
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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