NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1734339820|ref|NP_001360643|]
View 

EGF-like domain-containing protein [Caenorhabditis elegans]

Protein Classification

EB and CE4_SF domain-containing protein( domain architecture ID 10483738)

EB and CE4_SF 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_SF super family cl15692
Catalytic NodB homology domain of the carbohydrate esterase 4 superfamily; The carbohydrate ...
 1458-1720 2.68e-136

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: 424.06  E-value: 2.68e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1458 PQMVMLSFDDPITDRIINTLKSLFSGSIRNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLSG-RTQER 1536
Cdd:cd10974      1 PQMITLTFDDAINDNNIELYKKIFNGKRNNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDENnATYED 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1537 WYKEQKGMRETLAEFSFIDRSHIIGTRAPELKIGGDAQYRMMSENNFTFDNSMLV---SSPYWPQTLDHKLAWECDG-NC 1612
Cdd:cd10974     81 WVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAppsNVPLWPYTLDYKMPHECHGqNC 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1613 PTQSHKAIWEIPIQNIQANDTRWYKT---LTRAMKPFDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYLPDngAV 1689
Cdd:cd10974    161 PTRSFPGVWEMVLNELDVRDDPQGDEplaMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTKNE--LL 238

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1734339820 1690 YALRDFLKFIVQKQDVFVVTGSQIIDYMRNP 1720
Cdd:cd10974    239 RALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 476-527 1.03e-10

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 58.59  E-value: 1.03e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1734339820  476 CPSGIVEVAGRCVKQVSIGQPCVANAQCNFGSFCQSGTCQCPPGFYVQDEQC 527
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 984-1036 1.38e-09

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 55.12  E-value: 1.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1734339820  984 CPEGLFSVNGKCRSYVQLGQTCTSDDRCAErNAQCQENYCTCRTGYTNINGQC 1036
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPGESCEADEQCPG-GSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 690-739 6.20e-08

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 50.50  E-value: 6.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1734339820  690 QMVIGGECRErlKAHPGYGCTMGEMCVGNSVCVNGKCACVDGKVEINKIC 739
Cdd:pfam01683    5 QVLVNGQCVP--KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1137-1195 3.31e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 48.58  E-value: 3.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1734339820 1137 CPETFFESDGACVKnvakikvVVPPLSSCLGGEECSGNSECVHGICFCKEEFTLFEGKC 1195
Cdd:pfam01683    1 CPPGQVLVNGQCVP-------KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 857-910 4.03e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 48.19  E-value: 4.03e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734339820  857 CVNNMMIRDKMCVqrRKVNIGNSCNNEDQCLGNSTCMDNNCQCGIGFVASMDVC 910
Cdd:pfam01683    1 CPPGQVLVNGQCV--PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 516-568 4.11e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 48.19  E-value: 4.11e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1734339820  516 CPPGFYVQDEQCQAiESEPNESCQNNEKCTKGSVCYNGKCSCPRNHELINGHC 568
Cdd:pfam01683    1 CPPGQVLVNGQCVP-KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 400-456 7.48e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 47.42  E-value: 7.48e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339820  400 CPNNQVYsgVTGECLPEKQPGQDCIYSSQCQasfGGLVCDKNTCRCPNGLVFDGLKC 456
Cdd:pfam01683    1 CPPGQVL--VNGQCVPKVAPGESCEADEQCP---GGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 274-330 1.45e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 43.95  E-value: 1.45e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339820  274 CPAGQTYIReaGVCMTVQQPGEPCQYSQQCSalePGAYCLKMRCECVYGMKKSSNGC 330
Cdd:pfam01683    1 CPPGQVLVN--GQCVPKVAPGESCEADEQCP---GGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 815-868 3.47e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 42.80  E-value: 3.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734339820  815 CPPRMSAIDKKCVhqQTAAPGEPCSEKVACSPFSVCENNVCKCVNNMMIRDKMC 868
Cdd:pfam01683    1 CPPGQVLVNGQCV--PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 899-952 4.90e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 42.41  E-value: 4.90e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734339820  899 CGIGFVASMDVCVlrKTVTPGYLCNPEDICTGQSVCIKGVCQCQPDYKQMHNIC 952
Cdd:pfam01683    1 CPPGQVLVNGQCV--PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 772-826 4.95e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 42.41  E-value: 4.95e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1734339820  772 CRRGENSINGICkgFTFVYPGDLCTdITSRCTGGSYCARGRCECPPRMSAIDKKC 826
Cdd:pfam01683    1 CPPGQVLVNGQC--VPKVAPGESCE-ADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 614-652 9.01e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 41.64  E-value: 9.01e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339820  614 TVPIGSACVrIGVTCDGGSVCVAGICVCPLGKTPRNGVC 652
Cdd:pfam01683   15 KVAPGESCE-ADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1287-1326 4.57e-04

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 39.72  E-value: 4.57e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1734339820 1287 WRLSKPGHMCDNKTHCTNCSVCVNGFCRCPEGLVHYGDKC 1326
Cdd:pfam01683   13 VPKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 728-783 1.34e-03

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 38.56  E-value: 1.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339820  728 CVDGKVEINKICIDQVSakPGDTCGKGIICEGGSYCntDSGKCACRRGENSINGIC 783
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVA--PGESCEADEQCPGGSVC--VNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1315-1357 6.66e-03

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 36.25  E-value: 6.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1734339820 1315 CPEGLVHYGDKCVSEIDA-TKCLASNQCPSGAQCVKGECRCKPG 1357
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPgESCEADEQCPGGSVCVNGVCQCPPG 44
 
Name Accession Description Interval E-value
CE4_CDA_like_1 cd10974
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ...
 1458-1720 2.68e-136

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: 424.06  E-value: 2.68e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1458 PQMVMLSFDDPITDRIINTLKSLFSGSIRNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLSG-RTQER 1536
Cdd:cd10974      1 PQMITLTFDDAINDNNIELYKKIFNGKRNNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDENnATYED 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1537 WYKEQKGMRETLAEFSFIDRSHIIGTRAPELKIGGDAQYRMMSENNFTFDNSMLV---SSPYWPQTLDHKLAWECDG-NC 1612
Cdd:cd10974     81 WVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAppsNVPLWPYTLDYKMPHECHGqNC 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1613 PTQSHKAIWEIPIQNIQANDTRWYKT---LTRAMKPFDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYLPDngAV 1689
Cdd:cd10974    161 PTRSFPGVWEMVLNELDVRDDPQGDEplaMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTKNE--LL 238

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1734339820 1690 YALRDFLKFIVQKQDVFVVTGSQIIDYMRNP 1720
Cdd:cd10974    239 RALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 476-527 1.03e-10

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 58.59  E-value: 1.03e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1734339820  476 CPSGIVEVAGRCVKQVSIGQPCVANAQCNFGSFCQSGTCQCPPGFYVQDEQC 527
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 984-1036 1.38e-09

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 55.12  E-value: 1.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1734339820  984 CPEGLFSVNGKCRSYVQLGQTCTSDDRCAErNAQCQENYCTCRTGYTNINGQC 1036
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPGESCEADEQCPG-GSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 690-739 6.20e-08

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 50.50  E-value: 6.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1734339820  690 QMVIGGECRErlKAHPGYGCTMGEMCVGNSVCVNGKCACVDGKVEINKIC 739
Cdd:pfam01683    5 QVLVNGQCVP--KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1137-1195 3.31e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 48.58  E-value: 3.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1734339820 1137 CPETFFESDGACVKnvakikvVVPPLSSCLGGEECSGNSECVHGICFCKEEFTLFEGKC 1195
Cdd:pfam01683    1 CPPGQVLVNGQCVP-------KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 857-910 4.03e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 48.19  E-value: 4.03e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734339820  857 CVNNMMIRDKMCVqrRKVNIGNSCNNEDQCLGNSTCMDNNCQCGIGFVASMDVC 910
Cdd:pfam01683    1 CPPGQVLVNGQCV--PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 516-568 4.11e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 48.19  E-value: 4.11e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1734339820  516 CPPGFYVQDEQCQAiESEPNESCQNNEKCTKGSVCYNGKCSCPRNHELINGHC 568
Cdd:pfam01683    1 CPPGQVLVNGQCVP-KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 400-456 7.48e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 47.42  E-value: 7.48e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339820  400 CPNNQVYsgVTGECLPEKQPGQDCIYSSQCQasfGGLVCDKNTCRCPNGLVFDGLKC 456
Cdd:pfam01683    1 CPPGQVL--VNGQCVPKVAPGESCEADEQCP---GGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 274-330 1.45e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 43.95  E-value: 1.45e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339820  274 CPAGQTYIReaGVCMTVQQPGEPCQYSQQCSalePGAYCLKMRCECVYGMKKSSNGC 330
Cdd:pfam01683    1 CPPGQVLVN--GQCVPKVAPGESCEADEQCP---GGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 815-868 3.47e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 42.80  E-value: 3.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734339820  815 CPPRMSAIDKKCVhqQTAAPGEPCSEKVACSPFSVCENNVCKCVNNMMIRDKMC 868
Cdd:pfam01683    1 CPPGQVLVNGQCV--PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 899-952 4.90e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 42.41  E-value: 4.90e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734339820  899 CGIGFVASMDVCVlrKTVTPGYLCNPEDICTGQSVCIKGVCQCQPDYKQMHNIC 952
Cdd:pfam01683    1 CPPGQVLVNGQCV--PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 772-826 4.95e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 42.41  E-value: 4.95e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1734339820  772 CRRGENSINGICkgFTFVYPGDLCTdITSRCTGGSYCARGRCECPPRMSAIDKKC 826
Cdd:pfam01683    1 CPPGQVLVNGQC--VPKVAPGESCE-ADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 614-652 9.01e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 41.64  E-value: 9.01e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339820  614 TVPIGSACVrIGVTCDGGSVCVAGICVCPLGKTPRNGVC 652
Cdd:pfam01683   15 KVAPGESCE-ADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 1458-1550 2.61e-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: 42.60  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1458 PQMVMLSFDD---PITDRIINTLKSLfsgsirnpngcAIKGTFFVSHQW--NNYDQSLWLHSTNHEIGVNSITREDLSGR 1532
Cdd:pfam01522    6 KKVVALTFDDgpsENTPAILDVLKKY-----------GVKATFFVIGGNveRYPDLVKRMVEAGHEIGNHTWSHPNLTGL 74

                           90
                   ....*....|....*...
gi 1734339820 1533 TQERWYKEQKGMRETLAE 1550
Cdd:pfam01522   75 SPEEIRKEIERAQDALEK 92
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1287-1326 4.57e-04

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 39.72  E-value: 4.57e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1734339820 1287 WRLSKPGHMCDNKTHCTNCSVCVNGFCRCPEGLVHYGDKC 1326
Cdd:pfam01683   13 VPKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 728-783 1.34e-03

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 38.56  E-value: 1.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339820  728 CVDGKVEINKICIDQVSakPGDTCGKGIICEGGSYCntDSGKCACRRGENSINGIC 783
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVA--PGESCEADEQCPGGSVC--VNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1315-1357 6.66e-03

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 36.25  E-value: 6.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1734339820 1315 CPEGLVHYGDKCVSEIDA-TKCLASNQCPSGAQCVKGECRCKPG 1357
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPgESCEADEQCPGGSVCVNGVCQCPPG 44
 
Name Accession Description Interval E-value
CE4_CDA_like_1 cd10974
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ...
 1458-1720 2.68e-136

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: 424.06  E-value: 2.68e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1458 PQMVMLSFDDPITDRIINTLKSLFSGSIRNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLSG-RTQER 1536
Cdd:cd10974      1 PQMITLTFDDAINDNNIELYKKIFNGKRNNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDENnATYED 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1537 WYKEQKGMRETLAEFSFIDRSHIIGTRAPELKIGGDAQYRMMSENNFTFDNSMLV---SSPYWPQTLDHKLAWECDG-NC 1612
Cdd:cd10974     81 WVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAppsNVPLWPYTLDYKMPHECHGqNC 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1613 PTQSHKAIWEIPIQNIQANDTRWYKT---LTRAMKPFDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYLPDngAV 1689
Cdd:cd10974    161 PTRSFPGVWEMVLNELDVRDDPQGDEplaMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTKNE--LL 238

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1734339820 1690 YALRDFLKFIVQKQDVFVVTGSQIIDYMRNP 1720
Cdd:cd10974    239 RALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
CE4_CDA_like_2 cd10975
Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3. ...
 1458-1720 5.54e-70

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: 236.06  E-value: 5.54e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1458 PQMVMLSFDDPITDRIINTLKSLFSGSIrNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLS----GRT 1533
Cdd:cd10975      1 PQLVTLTFDDAVNTLNYPYYEKLFGNRK-NPNGCPIGATFFVSHEYTDYRLVQELYNDGHEIALHSISHRSPQdywrNAS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1534 QERWYKEQKGMRETLAEFSFIDRSHIIGTRAPELKIGGDAQYRMMSENNFTFDNSMLVSS----PYWPQTLDHKLAWECD 1609
Cdd:cd10975     80 VDEWEREFGGQREILAHFANIPAEDIKGFRAPFLQLGGDATFKALKQLGLTYDSSWPTQSftnpPLWPYTLDYGSTQDCV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1610 -GNCPTQSHKAIWEIPIQNIQANDTRWYKTLTRAMKPfDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYlPDNgA 1688
Cdd:cd10975    160 iPPCPTDSYPGFWVVPMVDWQDLNGVPCSMLAACPPP-GTADEVYDWLLSNFERHYNTNRAPFGLYLHASWFEF-TPN-R 236

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1734339820 1689 VYALRDFLKFIVQKQDVFVVTGSQIIDYMRNP 1720
Cdd:cd10975    237 LEGFKKFLDELLSLDDVYLVTISQAIEWMRNP 268
CE4_CDA_like cd10919
Putative catalytic domain of chitin deacetylase-like proteins from insects and similar ...
 1458-1720 2.97e-66

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: 225.70  E-value: 2.97e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1458 PQMVMLSFDDPITDRIINTLKSLFSGSIRNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLSGR-TQER 1536
Cdd:cd10919      1 PQFVLFTFDDAINELNTDAVIQEIADGTNNNGGCPIPATFFVSTNYTDCSLVKQLWREGHEIATHTVTHVPDDSNaSVDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1537 WYKEQKGMRETLAEFSFIDRSHIIGTRAPELKiGGDAQYRMMSENNFTFDNSMLV------SSPYWPQTLD----HKLAW 1606
Cdd:cd10919     81 WEEEIAGQREWLNKTCGIPLEKVVGFRAPYLA-YNPNTREVLEENGFLYDSSIPEpytpsgTNRLWPYTLDygipQDCNL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1607 ECDGNCPTQSHKAIWEIPIQNIQ-ANDTRWYKTLTRAMKPFDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYlPD 1685
Cdd:cd10919    160 VPGSCSPTERYPGLWEVPLYTLQdGNDTTGDSYYCTPDDGPLNGDSFYALLKYNFDRHYNGNRAPFGIYLHAAWLSP-PY 238

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1734339820 1686 NGAVYALRDFLKFIVQKQDVFVVTGSQIIDYMRNP 1720
Cdd:cd10919    239 SERRAALEKFLDYALSKPDVWFVTNSQLLDWMQNP 273
CE4_CDA_like_3 cd10976
Putative catalytic domain of uncharacterized bacterial hypothetical proteins similar to insect ...
 1510-1717 1.00e-10

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: 1.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1510 LWL-HSTNHEIGVNSITREDLSGR----TQERWYKEQKGMRETLAE------------FSFIDRSHIIGTRAPELKiGGD 1572
Cdd:cd10976     78 LNAaYREGHEIGSHANGHFDGKGGggrwSVADWKREFDQFYRFVENayaingiegappWPAFAPNSIKGFRAPCLE-GSK 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1573 AQYRMMSENNFTFDNSMLVSSPYWPQTLDhklawecdgncptqshkAIWEIPIQNIQANDTR----------WYKTLTRA 1642
Cdd:cd10976    157 GLQPALKKHGFTYDASSVTQGPYWPQKVD-----------------GIWNFPLPLVPEGPTSrpviamdynlFVRHSGGV 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1643 MKPFDS--RDSVTKMLQRN-FMNHYKTNRAPfiLTLDTEFLTYlpdNGAVY--ALRDFLKFIVQKQDVFVVTGSQIIDYM 1717
Cdd:cd10976    220 EAPAKAaeFEARMLATYRNaFDRAYNGNRAP--LQLGNHFVKW---NGGAYwnALERFAEEVCTKPEVKCVTYRELVDFL 294
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 476-527 1.03e-10

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 58.59  E-value: 1.03e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1734339820  476 CPSGIVEVAGRCVKQVSIGQPCVANAQCNFGSFCQSGTCQCPPGFYVQDEQC 527
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 984-1036 1.38e-09

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 55.12  E-value: 1.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1734339820  984 CPEGLFSVNGKCRSYVQLGQTCTSDDRCAErNAQCQENYCTCRTGYTNINGQC 1036
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPGESCEADEQCPG-GSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 690-739 6.20e-08

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 50.50  E-value: 6.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1734339820  690 QMVIGGECRErlKAHPGYGCTMGEMCVGNSVCVNGKCACVDGKVEINKIC 739
Cdd:pfam01683    5 QVLVNGQCVP--KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1137-1195 3.31e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 48.58  E-value: 3.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1734339820 1137 CPETFFESDGACVKnvakikvVVPPLSSCLGGEECSGNSECVHGICFCKEEFTLFEGKC 1195
Cdd:pfam01683    1 CPPGQVLVNGQCVP-------KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 857-910 4.03e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 48.19  E-value: 4.03e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734339820  857 CVNNMMIRDKMCVqrRKVNIGNSCNNEDQCLGNSTCMDNNCQCGIGFVASMDVC 910
Cdd:pfam01683    1 CPPGQVLVNGQCV--PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 516-568 4.11e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 48.19  E-value: 4.11e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1734339820  516 CPPGFYVQDEQCQAiESEPNESCQNNEKCTKGSVCYNGKCSCPRNHELINGHC 568
Cdd:pfam01683    1 CPPGQVLVNGQCVP-KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 400-456 7.48e-07

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 47.42  E-value: 7.48e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339820  400 CPNNQVYsgVTGECLPEKQPGQDCIYSSQCQasfGGLVCDKNTCRCPNGLVFDGLKC 456
Cdd:pfam01683    1 CPPGQVL--VNGQCVPKVAPGESCEADEQCP---GGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 274-330 1.45e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 43.95  E-value: 1.45e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339820  274 CPAGQTYIReaGVCMTVQQPGEPCQYSQQCSalePGAYCLKMRCECVYGMKKSSNGC 330
Cdd:pfam01683    1 CPPGQVLVN--GQCVPKVAPGESCEADEQCP---GGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 815-868 3.47e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 42.80  E-value: 3.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734339820  815 CPPRMSAIDKKCVhqQTAAPGEPCSEKVACSPFSVCENNVCKCVNNMMIRDKMC 868
Cdd:pfam01683    1 CPPGQVLVNGQCV--PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 899-952 4.90e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 42.41  E-value: 4.90e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734339820  899 CGIGFVASMDVCVlrKTVTPGYLCNPEDICTGQSVCIKGVCQCQPDYKQMHNIC 952
Cdd:pfam01683    1 CPPGQVLVNGQCV--PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 772-826 4.95e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 42.41  E-value: 4.95e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1734339820  772 CRRGENSINGICkgFTFVYPGDLCTdITSRCTGGSYCARGRCECPPRMSAIDKKC 826
Cdd:pfam01683    1 CPPGQVLVNGQC--VPKVAPGESCE-ADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 614-652 9.01e-05

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 41.64  E-value: 9.01e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339820  614 TVPIGSACVrIGVTCDGGSVCVAGICVCPLGKTPRNGVC 652
Cdd:pfam01683   15 KVAPGESCE-ADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 1458-1550 2.61e-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: 42.60  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1458 PQMVMLSFDD---PITDRIINTLKSLfsgsirnpngcAIKGTFFVSHQW--NNYDQSLWLHSTNHEIGVNSITREDLSGR 1532
Cdd:pfam01522    6 KKVVALTFDDgpsENTPAILDVLKKY-----------GVKATFFVIGGNveRYPDLVKRMVEAGHEIGNHTWSHPNLTGL 74

                           90
                   ....*....|....*...
gi 1734339820 1533 TQERWYKEQKGMRETLAE 1550
Cdd:pfam01522   75 SPEEIRKEIERAQDALEK 92
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1287-1326 4.57e-04

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 39.72  E-value: 4.57e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1734339820 1287 WRLSKPGHMCDNKTHCTNCSVCVNGFCRCPEGLVHYGDKC 1326
Cdd:pfam01683   13 VPKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
CE4_NodB_like_6s_7s cd10917
Catalytic NodB homology domain of rhizobial NodB-like proteins; This family belongs to the ...
 1461-1540 1.30e-03

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: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1461 VMLSFDD----PITDRIINTLKSlfsgsirnpNGcaIKGTFFVSHQW--NNYDQSLWLHSTNHEIGVNSITREDLSGRTQ 1534
Cdd:cd10917      3 VALTFDDgpdpEYTPKILDILAE---------YG--VKATFFVVGENveKHPDLVRRIVAEGHEIGNHTYSHPDLTKLSP 71


                   ....*.
gi 1734339820 1535 ERWYKE 1540
Cdd:cd10917     72 EEIRAE 77
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 728-783 1.34e-03

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 38.56  E-value: 1.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339820  728 CVDGKVEINKICIDQVSakPGDTCGKGIICEGGSYCntDSGKCACRRGENSINGIC 783
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVA--PGESCEADEQCPGGSVC--VNGVCQCPPGFTPVNGRC 52
CE4_GLA_like_6s cd10967
Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is ...
 1460-1550 2.15e-03

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: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339820 1460 MVMLSFDD-PITD-RIINTLKSlfsgsirnpNGcaIKGTFFVSHQWNNYDQSL------WLHSTNHEIGVNSITREDLSG 1531
Cdd:cd10967      2 AVSLTFDDgYAQDlRAAPLLAK---------YG--LKGTFFVNSGLLGRRGYLdleelrELAAAGHEIGSHTVTHPDLTS 70

                           90
                   ....*....|....*....
gi 1734339820 1532 RTQERWYKEQKGMRETLAE 1550
Cdd:cd10967     71 LPPAELRREIAESRAALEE 89
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1315-1357 6.66e-03

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 36.25  E-value: 6.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1734339820 1315 CPEGLVHYGDKCVSEIDA-TKCLASNQCPSGAQCVKGECRCKPG 1357
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPgESCEADEQCPGGSVCVNGVCQCPPG 44
 
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