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Conserved domains on  [gi|1734339320|ref|NP_001360720|]
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EGF-like domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CE4_CDA_like_1 cd10974
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ...
 1409-1684 3.00e-139

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: 431.76  E-value: 3.00e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1409 PQFVVLTFDDAVNGKTFSDYKKLFENDVlKNPNGCDVKATFFISHEWTNYDAVNWLVQKNMEIASNSISHESLE-NANTN 1487
Cdd:cd10974      1 PQMITLTFDDAINDNNIELYKKIFNGKR-NNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDEnNATYE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1488 RWLNEMDGQRRILAKFGGAPEEEIVGIRSPQLALGGDNQFEMMIGAEFLWDNSMSANPgiHGEPFWPQTMDYQVAWDCNE 1567
Cdd:cd10974     80 DWVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAPP--SNVPLWPYTLDYKMPHECHG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1568 ASCPKSSFPGVWSVPLNQFYGSYMSQIDSFRrssMLRAAVDLNNTVDELEEIITRNFERSYSANRAPYVLSLNADFLQLG 1647
Cdd:cd10974    158 QNCPTRSFPGVWEMVLNELDVRDDPQGDEPL---AMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTK 234

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1734339320 1648 ghNKGMKAVQKFLNRMSAQKDVYIVTIKQLIDWMKRP 1684
Cdd:cd10974    235 --NELLRALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1290-1346 2.46e-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: 51.66  E-value: 2.46e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339320 1290 CAAQHVAIRGICKQKsapafAAPGDTCSMREKCTGGATCFEGMCTCDDHHFAEDGYC 1346
Cdd:pfam01683    1 CPPGQVLVNGQCVPK-----VAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 565-620 2.02e-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: 48.96  E-value: 2.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339320  565 CLSTHVNIEGRCEKVIYPGQVgCRSDLQCHaahSGTHCIDRICVCPEGQRAVDQTC 620
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPGES-CEADEQCP---GGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 911-967 2.56e-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: 48.96  E-value: 2.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339320  911 CPQDKSEIsQGQCVTprklEVVPGASCNANTVCTKGSTCESGLCRCQPGYIAVSGNC 967
Cdd:pfam01683    1 CPPGQVLV-NGQCVP----KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 609-666 3.71e-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: 3.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734339320  609 CPEGQRAVDQTCVSasepvTSPPGGSCSNLRECTGGSVCREGWCICPDPSMIVNrGIC 666
Cdd:pfam01683    1 CPPGQVLVNGQCVP-----KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVN-GRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 956-1020 4.11e-06

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: 45.49  E-value: 4.11e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1734339320  956 CQPGYIAVSGNCVAlpmsttpkmrvIAKPLESCENGETCEGGSNCDydTGICMCPPGQIVFNVQC 1020
Cdd:pfam01683    1 CPPGQVLVNGQCVP-----------KVAPGESCEADEQCPGGSVCV--NGVCQCPPGFTPVNGRC 52
PHA02682 super family cl31817
ORF080 virion core protein; Provisional
 388-493 6.16e-06

ORF080 virion core protein; Provisional


The actual alignment was detected with superfamily member PHA02682:

Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 49.86  E-value: 6.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320  388 QKIVGPGELCDSGETCGKGSICDSVIPVCVCPAQTdlsngecISVPAPTSQPVQVMT--PPPTLPPVQVPIQTLPPQTRp 465
Cdd:PHA02682    74 QRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVT-------CPAPAPACPPATAPTcpPPAVCPAPARPAPACPPSTR- 145

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1734339320  466 pQLPPVqitqPPIQTP-----VQPIFFQTTRPP 493
Cdd:PHA02682   146 -QCPPA----PPLPTPkpapaAKPIFLHNQLPP 173
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1242-1301 9.75e-06

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: 44.34  E-value: 9.75e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1242 CPENYIRQNGQCISKeckhkvAKVGETCKNGEICAGGSICdyDRKRCICAAQHVAIRGIC 1301
Cdd:pfam01683    1 CPPGQVLVNGQCVPK------VAPGESCEADEQCPGGSVC--VNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1215-1253 6.06e-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: 42.03  E-value: 6.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339320 1215 KVAAVGSACRPIDICLGESVCTNGFCHCPENYIRQNGQC 1253
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 322-382 3.70e-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: 40.10  E-value: 3.70e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1734339320  322 CPGDLEAREGECVlpaastisvQKVGIGALCSDLAECDHGSTCVMGRCTCVSPLVQHEGKC 382
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 ...
 718-757 1.79e-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: 38.18  E-value: 1.79e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1734339320  718 KKIVPGGRCGPIDVCVGGSNCIEGFCLCPAGQQPSNsGRC 757
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVN-GRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1009-1083 6.37e-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: 36.64  E-value: 6.37e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339320 1009 CPPGQIVFNVQCMP--PPTQPqittrvttpvkaapvvtpkpihstdCEIDANCGENKICVSGKCKCKPGFVDNSGTC 1083
Cdd:pfam01683    1 CPPGQVLVNGQCVPkvAPGES-------------------------CEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
 
Name Accession Description Interval E-value
CE4_CDA_like_1 cd10974
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ...
 1409-1684 3.00e-139

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: 431.76  E-value: 3.00e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1409 PQFVVLTFDDAVNGKTFSDYKKLFENDVlKNPNGCDVKATFFISHEWTNYDAVNWLVQKNMEIASNSISHESLE-NANTN 1487
Cdd:cd10974      1 PQMITLTFDDAINDNNIELYKKIFNGKR-NNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDEnNATYE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1488 RWLNEMDGQRRILAKFGGAPEEEIVGIRSPQLALGGDNQFEMMIGAEFLWDNSMSANPgiHGEPFWPQTMDYQVAWDCNE 1567
Cdd:cd10974     80 DWVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAPP--SNVPLWPYTLDYKMPHECHG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1568 ASCPKSSFPGVWSVPLNQFYGSYMSQIDSFRrssMLRAAVDLNNTVDELEEIITRNFERSYSANRAPYVLSLNADFLQLG 1647
Cdd:cd10974    158 QNCPTRSFPGVWEMVLNELDVRDDPQGDEPL---AMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTK 234

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1734339320 1648 ghNKGMKAVQKFLNRMSAQKDVYIVTIKQLIDWMKRP 1684
Cdd:cd10974    235 --NELLRALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1290-1346 2.46e-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: 51.66  E-value: 2.46e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339320 1290 CAAQHVAIRGICKQKsapafAAPGDTCSMREKCTGGATCFEGMCTCDDHHFAEDGYC 1346
Cdd:pfam01683    1 CPPGQVLVNGQCVPK-----VAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
 1396-1517 3.42e-08

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: 55.44  E-value: 3.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1396 GRRAPGGLRPDETPQ-FVVLTFDDAVNgktfSDYKKLFenDVLKNpngCDVKATFFISHEW--TNYDAVNWLVQKNMEIA 1472
Cdd:COG0726      5 LDELLPALRWGPLPKkAVALTFDDGPR----EGTPRLL--DLLKK---YGVKATFFVVGSAveRHPELVREIAAAGHEIG 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1734339320 1473 SNSISHESLENANTNRWLNEMDGQRRILAKFGGAPeeeIVGIRSP 1517
Cdd:COG0726     76 NHTYTHPDLTKLSEEEERAEIARAKEALEELTGKR---PRGFRPP 117
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 565-620 2.02e-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: 48.96  E-value: 2.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339320  565 CLSTHVNIEGRCEKVIYPGQVgCRSDLQCHaahSGTHCIDRICVCPEGQRAVDQTC 620
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPGES-CEADEQCP---GGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 911-967 2.56e-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: 48.96  E-value: 2.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339320  911 CPQDKSEIsQGQCVTprklEVVPGASCNANTVCTKGSTCESGLCRCQPGYIAVSGNC 967
Cdd:pfam01683    1 CPPGQVLV-NGQCVP----KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 609-666 3.71e-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: 3.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734339320  609 CPEGQRAVDQTCVSasepvTSPPGGSCSNLRECTGGSVCREGWCICPDPSMIVNrGIC 666
Cdd:pfam01683    1 CPPGQVLVNGQCVP-----KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVN-GRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 956-1020 4.11e-06

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: 45.49  E-value: 4.11e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1734339320  956 CQPGYIAVSGNCVAlpmsttpkmrvIAKPLESCENGETCEGGSNCDydTGICMCPPGQIVFNVQC 1020
Cdd:pfam01683    1 CPPGQVLVNGQCVP-----------KVAPGESCEADEQCPGGSVCV--NGVCQCPPGFTPVNGRC 52
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 388-493 6.16e-06

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 49.86  E-value: 6.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320  388 QKIVGPGELCDSGETCGKGSICDSVIPVCVCPAQTdlsngecISVPAPTSQPVQVMT--PPPTLPPVQVPIQTLPPQTRp 465
Cdd:PHA02682    74 QRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVT-------CPAPAPACPPATAPTcpPPAVCPAPARPAPACPPSTR- 145

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1734339320  466 pQLPPVqitqPPIQTP-----VQPIFFQTTRPP 493
Cdd:PHA02682   146 -QCPPA----PPLPTPkpapaAKPIFLHNQLPP 173
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1242-1301 9.75e-06

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: 44.34  E-value: 9.75e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1242 CPENYIRQNGQCISKeckhkvAKVGETCKNGEICAGGSICdyDRKRCICAAQHVAIRGIC 1301
Cdd:pfam01683    1 CPPGQVLVNGQCVPK------VAPGESCEADEQCPGGSVC--VNGVCQCPPGFTPVNGRC 52
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 1412-1517 4.58e-05

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


Pssm-ID: 426305 [Multi-domain]  Cd Length: 124  Bit Score: 44.53  E-value: 4.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1412 VVLTFDDAVNgktfSDYKKLFenDVLK-NpngcDVKATFFISHEW--TNYDAVNWLVQKNMEIASNSISHESLENANTNR 1488
Cdd:pfam01522    9 VALTFDDGPS----ENTPAIL--DVLKkY----GVKATFFVIGGNveRYPDLVKRMVEAGHEIGNHTWSHPNLTGLSPEE 78

                           90       100
                   ....*....|....*....|....*....
gi 1734339320 1489 WLNEMDGQRRILAKFGGAPeeeIVGIRSP 1517
Cdd:pfam01522   79 IRKEIERAQDALEKATGKR---PRLFRPP 104
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1215-1253 6.06e-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: 42.03  E-value: 6.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339320 1215 KVAAVGSACRPIDICLGESVCTNGFCHCPENYIRQNGQC 1253
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 322-382 3.70e-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: 40.10  E-value: 3.70e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1734339320  322 CPGDLEAREGECVlpaastisvQKVGIGALCSDLAECDHGSTCVMGRCTCVSPLVQHEGKC 382
Cdd:pfam01683    1 CPPGQVLVNGQCV---------PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 374-523 5.37e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 5.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320  374 PLVQHEGKCVLRQQQKIVGPGELCDSGETCGKGSIcdsviPVCVCPAQTDLSNGECISVPAPTSQPVQVMTPPPTLPPVQ 453
Cdd:pfam03154  172 PVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSV-----PPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPH 246

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320  454 VPIQTLPPQTRPPQLPPVQITQPPIQTPVQPIffqttrpPMPTYATTPATTQFIPKQIYTTPPQMPKNSI 523
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPM-------PHSLQTGPSHMQHPVPPQPFPLTPQSSQSQV 309
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 718-757 1.79e-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: 38.18  E-value: 1.79e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1734339320  718 KKIVPGGRCGPIDVCVGGSNCIEGFCLCPAGQQPSNsGRC 757
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVN-GRC 52
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 431-494 1.94e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 40.93  E-value: 1.94e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339320   431 SVPAPTSQPV--QVMTPPPTLPpvqvPIQTLPPQTRPPQLPPvqitqppiQTPVQPIFFQTTRPPM 494
Cdd:smart00818   91 NLPQPAQQPFqpQPLQPPQPQQ----PMQPQPPVHPIPPLPP--------QPPLPPMFPMQPLPPL 144
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1009-1083 6.37e-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: 36.64  E-value: 6.37e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339320 1009 CPPGQIVFNVQCMP--PPTQPqittrvttpvkaapvvtpkpihstdCEIDANCGENKICVSGKCKCKPGFVDNSGTC 1083
Cdd:pfam01683    1 CPPGQVLVNGQCVPkvAPGES-------------------------CEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
 
Name Accession Description Interval E-value
CE4_CDA_like_1 cd10974
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ...
 1409-1684 3.00e-139

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: 431.76  E-value: 3.00e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1409 PQFVVLTFDDAVNGKTFSDYKKLFENDVlKNPNGCDVKATFFISHEWTNYDAVNWLVQKNMEIASNSISHESLE-NANTN 1487
Cdd:cd10974      1 PQMITLTFDDAINDNNIELYKKIFNGKR-NNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDEnNATYE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1488 RWLNEMDGQRRILAKFGGAPEEEIVGIRSPQLALGGDNQFEMMIGAEFLWDNSMSANPgiHGEPFWPQTMDYQVAWDCNE 1567
Cdd:cd10974     80 DWVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAPP--SNVPLWPYTLDYKMPHECHG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1568 ASCPKSSFPGVWSVPLNQFYGSYMSQIDSFRrssMLRAAVDLNNTVDELEEIITRNFERSYSANRAPYVLSLNADFLQLG 1647
Cdd:cd10974    158 QNCPTRSFPGVWEMVLNELDVRDDPQGDEPL---AMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTK 234

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1734339320 1648 ghNKGMKAVQKFLNRMSAQKDVYIVTIKQLIDWMKRP 1684
Cdd:cd10974    235 --NELLRALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
CE4_CDA_like_2 cd10975
Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3. ...
 1409-1684 3.47e-82

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: 271.11  E-value: 3.47e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1409 PQFVVLTFDDAVNGKTFSDYKKLFENdvLKNPNGCDVKATFFISHEWTNYDAVNWLVQKNMEIASNSISHESLE----NA 1484
Cdd:cd10975      1 PQLVTLTFDDAVNTLNYPYYEKLFGN--RKNPNGCPIGATFFVSHEYTDYRLVQELYNDGHEIALHSISHRSPQdywrNA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1485 NTNRWLNEMDGQRRILAKFGGAPEEEIVGIRSPQLALGGDNQFEMMIGAEFLWDNSMSAnPGIHGEPFWPQTMDYQVAWD 1564
Cdd:cd10975     79 SVDEWEREFGGQREILAHFANIPAEDIKGFRAPFLQLGGDATFKALKQLGLTYDSSWPT-QSFTNPPLWPYTLDYGSTQD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1565 CNEASCPKSSFPGVWSVPLNQFYGSymsqiDSFRRSSMlrAAVDLNNTVDELEEIITRNFERSYSANRAPYVLSLNADFL 1644
Cdd:cd10975    158 CVIPPCPTDSYPGFWVVPMVDWQDL-----NGVPCSML--AACPPPGTADEVYDWLLSNFERHYNTNRAPFGLYLHASWF 230

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1734339320 1645 QLGGHNKgmKAVQKFLNRMSAQKDVYIVTIKQLIDWMKRP 1684
Cdd:cd10975    231 EFTPNRL--EGFKKFLDELLSLDDVYLVTISQAIEWMRNP 268
CE4_CDA_like cd10919
Putative catalytic domain of chitin deacetylase-like proteins from insects and similar ...
 1409-1684 1.10e-69

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: 235.72  E-value: 1.10e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1409 PQFVVLTFDDAVN-GKTFSDYKKLFENDvlKNPNGCDVKATFFISHEWTNYDAVNWLVQKNMEIASNSISHESLE-NANT 1486
Cdd:cd10919      1 PQFVLFTFDDAINeLNTDAVIQEIADGT--NNNGGCPIPATFFVSTNYTDCSLVKQLWREGHEIATHTVTHVPDDsNASV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1487 NRWLNEMDGQRRILAKFGGAPEEEIVGIRSPQLAlGGDNQFEMMIGAEFLWDNSMSANPGIHGEPF-WPQTMDYQVAWDC 1565
Cdd:cd10919     79 DEWEEEIAGQREWLNKTCGIPLEKVVGFRAPYLA-YNPNTREVLEENGFLYDSSIPEPYTPSGTNRlWPYTLDYGIPQDC 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1566 NEASC---PKSSFPGVWSVPLnqfygsYMSQIDSFRRSSMLRAAVDLNN-TVDELEEIITRNFERSYSANRAPYVLSLNA 1641
Cdd:cd10919    158 NLVPGscsPTERYPGLWEVPL------YTLQDGNDTTGDSYYCTPDDGPlNGDSFYALLKYNFDRHYNGNRAPFGIYLHA 231

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1734339320 1642 DFLQLGGHNKgMKAVQKFLNRMSAQKDVYIVTIKQLIDWMKRP 1684
Cdd:cd10919    232 AWLSPPYSER-RAALEKFLDYALSKPDVWFVTNSQLLDWMQNP 273
CE4_CDA_like_3 cd10976
Putative catalytic domain of uncharacterized bacterial hypothetical proteins similar to insect ...
 1489-1683 1.18e-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: 1.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1489 WLNEMDGQRRIL----AKFGGAPEE--------EIVGIRSPQLAlGGDNQFEMMIGAEFLWDNSMSANpgihgEPFWPQT 1556
Cdd:cd10976    110 WKREFDQFYRFVenayAINGIEGAPpwpafapnSIKGFRAPCLE-GSKGLQPALKKHGFTYDASSVTQ-----GPYWPQK 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1557 MDyqvawdcneascpkssfpGVWSVPLNQFY--GSYMSQI----DSFRRSSMlraAVDLNNTVDELEEI---ITRN-FER 1626
Cdd:cd10976    184 VD------------------GIWNFPLPLVPegPTSRPVIamdyNLFVRHSG---GVEAPAKAAEFEARmlaTYRNaFDR 242

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1734339320 1627 SYSANRAPyvlslnadfLQLGGH----NKG--MKAVQKFLNRMSAQKDVYIVTIKQLIDWMKR 1683
Cdd:cd10976    243 AYNGNRAP---------LQLGNHfvkwNGGayWNALERFAEEVCTKPEVKCVTYRELVDFLEA 296
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1290-1346 2.46e-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: 51.66  E-value: 2.46e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339320 1290 CAAQHVAIRGICKQKsapafAAPGDTCSMREKCTGGATCFEGMCTCDDHHFAEDGYC 1346
Cdd:pfam01683    1 CPPGQVLVNGQCVPK-----VAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
 1396-1517 3.42e-08

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: 55.44  E-value: 3.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1396 GRRAPGGLRPDETPQ-FVVLTFDDAVNgktfSDYKKLFenDVLKNpngCDVKATFFISHEW--TNYDAVNWLVQKNMEIA 1472
Cdd:COG0726      5 LDELLPALRWGPLPKkAVALTFDDGPR----EGTPRLL--DLLKK---YGVKATFFVVGSAveRHPELVREIAAAGHEIG 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1734339320 1473 SNSISHESLENANTNRWLNEMDGQRRILAKFGGAPeeeIVGIRSP 1517
Cdd:COG0726     76 NHTYTHPDLTKLSEEEERAEIARAKEALEELTGKR---PRGFRPP 117
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 565-620 2.02e-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: 48.96  E-value: 2.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339320  565 CLSTHVNIEGRCEKVIYPGQVgCRSDLQCHaahSGTHCIDRICVCPEGQRAVDQTC 620
Cdd:pfam01683    1 CPPGQVLVNGQCVPKVAPGES-CEADEQCP---GGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 911-967 2.56e-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: 48.96  E-value: 2.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339320  911 CPQDKSEIsQGQCVTprklEVVPGASCNANTVCTKGSTCESGLCRCQPGYIAVSGNC 967
Cdd:pfam01683    1 CPPGQVLV-NGQCVP----KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 609-666 3.71e-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: 3.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734339320  609 CPEGQRAVDQTCVSasepvTSPPGGSCSNLRECTGGSVCREGWCICPDPSMIVNrGIC 666
Cdd:pfam01683    1 CPPGQVLVNGQCVP-----KVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVN-GRC 52
CE4_NodB_like_6s_7s cd10917
Catalytic NodB homology domain of rhizobial NodB-like proteins; This family belongs to the ...
 1412-1507 1.01e-06

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: 50.70  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1412 VVLTFDDAVNGKTFSDYkkLfenDVLKNpNGcdVKATFFISHEW--TNYDAVNWLVQKNMEIASNSISHESLENANTNRW 1489
Cdd:cd10917      3 VALTFDDGPDPEYTPKI--L---DILAE-YG--VKATFFVVGENveKHPDLVRRIVAEGHEIGNHTYSHPDLTKLSPEEI 74

                           90
                   ....*....|....*...
gi 1734339320 1490 LNEMDGQRRILAKFGGAP 1507
Cdd:cd10917     75 RAEIERTQDAIEEATGVR 92
CE4_GLA_like_6s cd10967
Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is ...
 1412-1507 1.68e-06

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: 50.45  E-value: 1.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1412 VVLTFDDAVNgktfSDYK--KLFEndvlKNpngcDVKATFFIS------HEWTNYDAVNWLVQKNMEIASNSISHESLEN 1483
Cdd:cd10967      3 VSLTFDDGYA----QDLRaaPLLA----KY----GLKGTFFVNsgllgrRGYLDLEELRELAAAGHEIGSHTVTHPDLTS 70

                           90       100
                   ....*....|....*....|....
gi 1734339320 1484 ANTNRWLNEMDGQRRILAKFGGAP 1507
Cdd:cd10967     71 LPPAELRREIAESRAALEEIGGFP 94
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 956-1020 4.11e-06

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: 45.49  E-value: 4.11e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1734339320  956 CQPGYIAVSGNCVAlpmsttpkmrvIAKPLESCENGETCEGGSNCDydTGICMCPPGQIVFNVQC 1020
Cdd:pfam01683    1 CPPGQVLVNGQCVP-----------KVAPGESCEADEQCPGGSVCV--NGVCQCPPGFTPVNGRC 52
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 388-493 6.16e-06

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 49.86  E-value: 6.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320  388 QKIVGPGELCDSGETCGKGSICDSVIPVCVCPAQTdlsngecISVPAPTSQPVQVMT--PPPTLPPVQVPIQTLPPQTRp 465
Cdd:PHA02682    74 QRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVT-------CPAPAPACPPATAPTcpPPAVCPAPARPAPACPPSTR- 145

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1734339320  466 pQLPPVqitqPPIQTP-----VQPIFFQTTRPP 493
Cdd:PHA02682   146 -QCPPA----PPLPTPkpapaAKPIFLHNQLPP 173
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1242-1301 9.75e-06

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: 44.34  E-value: 9.75e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1242 CPENYIRQNGQCISKeckhkvAKVGETCKNGEICAGGSICdyDRKRCICAAQHVAIRGIC 1301
Cdd:pfam01683    1 CPPGQVLVNGQCVPK------VAPGESCEADEQCPGGSVC--VNGVCQCPPGFTPVNGRC 52
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 1412-1517 4.58e-05

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


Pssm-ID: 426305 [Multi-domain]  Cd Length: 124  Bit Score: 44.53  E-value: 4.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1412 VVLTFDDAVNgktfSDYKKLFenDVLK-NpngcDVKATFFISHEW--TNYDAVNWLVQKNMEIASNSISHESLENANTNR 1488
Cdd:pfam01522    9 VALTFDDGPS----ENTPAIL--DVLKkY----GVKATFFVIGGNveRYPDLVKRMVEAGHEIGNHTWSHPNLTGLSPEE 78

                           90       100
                   ....*....|....*....|....*....
gi 1734339320 1489 WLNEMDGQRRILAKFGGAPeeeIVGIRSP 1517
Cdd:pfam01522   79 IRKEIERAQDALEKATGKR---PRLFRPP 104
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1215-1253 6.06e-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: 42.03  E-value: 6.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339320 1215 KVAAVGSACRPIDICLGESVCTNGFCHCPENYIRQNGQC 1253
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 322-382 3.70e-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: 40.10  E-value: 3.70e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1734339320  322 CPGDLEAREGECVlpaastisvQKVGIGALCSDLAECDHGSTCVMGRCTCVSPLVQHEGKC 382
Cdd:pfam01683    1 CPPGQVLVNGQCV---------PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 374-523 5.37e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 5.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320  374 PLVQHEGKCVLRQQQKIVGPGELCDSGETCGKGSIcdsviPVCVCPAQTDLSNGECISVPAPTSQPVQVMTPPPTLPPVQ 453
Cdd:pfam03154  172 PVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSV-----PPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPH 246

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320  454 VPIQTLPPQTRPPQLPPVQITQPPIQTPVQPIffqttrpPMPTYATTPATTQFIPKQIYTTPPQMPKNSI 523
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPM-------PHSLQTGPSHMQHPVPPQPFPLTPQSSQSQV 309
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 718-757 1.79e-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: 38.18  E-value: 1.79e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1734339320  718 KKIVPGGRCGPIDVCVGGSNCIEGFCLCPAGQQPSNsGRC 757
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVN-GRC 52
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 431-494 1.94e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 40.93  E-value: 1.94e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339320   431 SVPAPTSQPV--QVMTPPPTLPpvqvPIQTLPPQTRPPQLPPvqitqppiQTPVQPIFFQTTRPPM 494
Cdd:smart00818   91 NLPQPAQQPFqpQPLQPPQPQQ----PMQPQPPVHPIPPLPP--------QPPLPPMFPMQPLPPL 144
CE4_NodB_like_5s_6s cd10918
Putative catalytic NodB homology domain of PgaB, IcaB, and similar proteins which consist of a ...
 1412-1507 2.16e-03

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: 40.66  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339320 1412 VVLTFDDAvngkTFSDYKKLFEndVLKNpNGcdVKATFFI------------SHEWTNYDAVNW-----LVQKNMEIASN 1474
Cdd:cd10918      2 VVLTFDDG----YRDNYTYALP--ILKK-YG--LPATFFVitgyigggnpwwAPAPPRPPYLTWdqlreLAASGVEIGSH 72

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1734339320 1475 SISHESLENANTNRWLNEMDGQRRILAKFGGAP 1507
Cdd:cd10918     73 THTHPDLTTLSDEELRRELAESKERLEEELGKP 105
PRK11633 PRK11633
cell division protein DedD; Provisional
 431-492 2.31e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 41.53  E-value: 2.31e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339320  431 SVPAPTSQPVQVMTPPPTLPPVQVPIQTLPPQTRPPQLPPVQITQPPIQTPV-----QPIFFQTTRP 492
Cdd:PRK11633    79 DAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPApkpepKPVVEEKAAP 145
PHA03247 PHA03247
large tegument protein UL36; Provisional
 430-484 2.37e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 2.37e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1734339320  430 ISVPAPTSQPVQVMTPPPTLPPVQVPIQTLPPQTRPPQLPPVQiTQPPIQTPVQP 484
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ-PQPPPPPPPRP 2939
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1009-1083 6.37e-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: 36.64  E-value: 6.37e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339320 1009 CPPGQIVFNVQCMP--PPTQPqittrvttpvkaapvvtpkpihstdCEIDANCGENKICVSGKCKCKPGFVDNSGTC 1083
Cdd:pfam01683    1 CPPGQVLVNGQCVPkvAPGES-------------------------CEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 431-484 9.56e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 9.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734339320  431 SVPAPTSQPVQVMTPPPTLPPVQVPIQTLPPQTRPPQLPPvQITQPPIQTPVQP 484
Cdd:PHA03247  2800 SPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP-PPPPGPPPPSLPL 2852
 
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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