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Conserved domains on  [gi|1734339322|ref|NP_001360721|]
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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 ...
 1358-1633 1.83e-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: 1.83e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1358 PQFVVLTFDDAVNGKTFSDYKKLFENDVlKNPNGCDVKATFFISHEWTNYDAVNWLVQKNMEIASNSISHESLE-NANTN 1436
Cdd:cd10974      1 PQMITLTFDDAINDNNIELYKKIFNGKR-NNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDEnNATYE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1437 RWLNEMDGQRRILAKFGGAPEEEIVGIRSPQLALGGDNQFEMMIGAEFLWDNSMSANPgiHGEPFWPQTMDYQVAWDCNE 1516
Cdd:cd10974     80 DWVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAPP--SNVPLWPYTLDYKMPHECHG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1517 ASCPKSSFPGVWSVPLNQFYGSYMSQIDSFRrssMLRAAVDLNNTVDELEEIITRNFERSYSANRAPYVLSLNADFLQLG 1596
Cdd:cd10974    158 QNCPTRSFPGVWEMVLNELDVRDDPQGDEPL---AMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTK 234

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1734339322 1597 ghNKGMKAVQKFLNRMSAQKDVYIVTIKQLIDWMKRP 1633
Cdd:cd10974    235 --NELLRALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1239-1295 2.00e-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: 52.04  E-value: 2.00e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339322 1239 CAAQHVAIRGICKQKsapafAAPGDTCSMREKCTGGATCFEGMCTCDDHHFAEDGYC 1295
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 ...
 514-569 1.65e-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: 49.35  E-value: 1.65e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339322  514 CLSTHVNIEGRCEKVIYPGQVgCRSDLQCHaahSGTHCIDRICVCPEGQRAVDQTC 569
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 ...
 860-916 2.08e-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: 2.08e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339322  860 CPQDKSEIsQGQCVTprklEVVPGASCNANTVCTKGSTCESGLCRCQPGYIAVSGNC 916
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 ...
 558-615 2.88e-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: 2.88e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734339322  558 CPEGQRAVDQTCVSasepvTSPPGGSCSNLRECTGGSVCREGWCICPDPSMIVNrGIC 615
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 ...
 905-969 3.25e-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: 45.88  E-value: 3.25e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1734339322  905 CQPGYIAVSGNCVAlpmsttpkmrvIAKPLESCENGETCEGGSNCDydTGICMCPPGQIVFNVQC 969
Cdd:pfam01683    1 CPPGQVLVNGQCVP-----------KVAPGESCEADEQCPGGSVCV--NGVCQCPPGFTPVNGRC 52
PHA02682 super family cl31817
ORF080 virion core protein; Provisional
 337-442 5.22e-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: 50.24  E-value: 5.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322  337 QKIVGPGELCDSGETCGKGSICDSVIPVCVCPAQTdlsngecISVPAPTSQPVQVMT--PPPTLPPVQVPIQTLPPQTRp 414
Cdd:PHA02682    74 QRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVT-------CPAPAPACPPATAPTcpPPAVCPAPARPAPACPPSTR- 145

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1734339322  415 pQLPPVqitqPPIQTP-----VQPIFFQTTRPP 442
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 ...
 1191-1250 7.93e-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: 44.72  E-value: 7.93e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1191 CPENYIRQNGQCISKeckhkvAKVGETCKNGEICAGGSICdyDRKRCICAAQHVAIRGIC 1250
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 ...
 1164-1202 4.98e-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: 4.98e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339322 1164 KVAAVGSACRPIDICLGESVCTNGFCHCPENYIRQNGQC 1202
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 667-706 1.50e-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: 1.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1734339322  667 KKIVPGGRCGPIDVCVGGSNCIEGFCLCPAGQQPSNsGRC 706
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 ...
 293-331 4.25e-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: 37.02  E-value: 4.25e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339322  293 TLVGIGALCSDLAECDHGSTCVMGRCTCVSPLVQHEGKC 331
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 958-1032 5.28e-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: 5.28e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339322  958 CPPGQIVFNVQCMP--PPTQPqittrvttpvkaapvvtpkpihstdCEIDANCGENKICVSGKCKCKPGFVDNSGTC 1032
Cdd:pfam01683    1 CPPGQVLVNGQCVPkvAPGES-------------------------CEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1021-1073 9.93e-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: 35.86  E-value: 9.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1734339322 1021 CKPGFVDNSGTCEPlegirgrSLRYGQACDrYQDKCINGAKCIDKICKCAPGF 1073
Cdd:pfam01683    1 CPPGQVLVNGQCVP-------KVAPGESCE-ADEQCPGGSVCVNGVCQCPPGF 45
 
Name Accession Description Interval E-value
CE4_CDA_like_1 cd10974
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ...
 1358-1633 1.83e-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: 1.83e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1358 PQFVVLTFDDAVNGKTFSDYKKLFENDVlKNPNGCDVKATFFISHEWTNYDAVNWLVQKNMEIASNSISHESLE-NANTN 1436
Cdd:cd10974      1 PQMITLTFDDAINDNNIELYKKIFNGKR-NNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDEnNATYE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1437 RWLNEMDGQRRILAKFGGAPEEEIVGIRSPQLALGGDNQFEMMIGAEFLWDNSMSANPgiHGEPFWPQTMDYQVAWDCNE 1516
Cdd:cd10974     80 DWVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAPP--SNVPLWPYTLDYKMPHECHG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1517 ASCPKSSFPGVWSVPLNQFYGSYMSQIDSFRrssMLRAAVDLNNTVDELEEIITRNFERSYSANRAPYVLSLNADFLQLG 1596
Cdd:cd10974    158 QNCPTRSFPGVWEMVLNELDVRDDPQGDEPL---AMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTK 234

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1734339322 1597 ghNKGMKAVQKFLNRMSAQKDVYIVTIKQLIDWMKRP 1633
Cdd:cd10974    235 --NELLRALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1239-1295 2.00e-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: 52.04  E-value: 2.00e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339322 1239 CAAQHVAIRGICKQKsapafAAPGDTCSMREKCTGGATCFEGMCTCDDHHFAEDGYC 1295
Cdd:pfam01683    1 CPPGQVLVNGQCVPK-----VAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
 1345-1466 3.31e-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: 3.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1345 GRRAPGGLRPDETPQ-FVVLTFDDAVNgktfSDYKKLFenDVLKNpngCDVKATFFISHEW--TNYDAVNWLVQKNMEIA 1421
Cdd:COG0726      5 LDELLPALRWGPLPKkAVALTFDDGPR----EGTPRLL--DLLKK---YGVKATFFVVGSAveRHPELVREIAAAGHEIG 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1734339322 1422 SNSISHESLENANTNRWLNEMDGQRRILAKFGGAPeeeIVGIRSP 1466
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 ...
 514-569 1.65e-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: 49.35  E-value: 1.65e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339322  514 CLSTHVNIEGRCEKVIYPGQVgCRSDLQCHaahSGTHCIDRICVCPEGQRAVDQTC 569
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 ...
 860-916 2.08e-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: 2.08e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339322  860 CPQDKSEIsQGQCVTprklEVVPGASCNANTVCTKGSTCESGLCRCQPGYIAVSGNC 916
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 ...
 558-615 2.88e-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: 2.88e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734339322  558 CPEGQRAVDQTCVSasepvTSPPGGSCSNLRECTGGSVCREGWCICPDPSMIVNrGIC 615
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 ...
 905-969 3.25e-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: 45.88  E-value: 3.25e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1734339322  905 CQPGYIAVSGNCVAlpmsttpkmrvIAKPLESCENGETCEGGSNCDydTGICMCPPGQIVFNVQC 969
Cdd:pfam01683    1 CPPGQVLVNGQCVP-----------KVAPGESCEADEQCPGGSVCV--NGVCQCPPGFTPVNGRC 52
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 337-442 5.22e-06

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 50.24  E-value: 5.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322  337 QKIVGPGELCDSGETCGKGSICDSVIPVCVCPAQTdlsngecISVPAPTSQPVQVMT--PPPTLPPVQVPIQTLPPQTRp 414
Cdd:PHA02682    74 QRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVT-------CPAPAPACPPATAPTcpPPAVCPAPARPAPACPPSTR- 145

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1734339322  415 pQLPPVqitqPPIQTP-----VQPIFFQTTRPP 442
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 ...
 1191-1250 7.93e-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: 44.72  E-value: 7.93e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1191 CPENYIRQNGQCISKeckhkvAKVGETCKNGEICAGGSICdyDRKRCICAAQHVAIRGIC 1250
Cdd:pfam01683    1 CPPGQVLVNGQCVPK------VAPGESCEADEQCPGGSVC--VNGVCQCPPGFTPVNGRC 52
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 1361-1466 4.44e-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: 4.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1361 VVLTFDDAVNgktfSDYKKLFenDVLK-NpngcDVKATFFISHEW--TNYDAVNWLVQKNMEIASNSISHESLENANTNR 1437
Cdd:pfam01522    9 VALTFDDGPS----ENTPAIL--DVLKkY----GVKATFFVIGGNveRYPDLVKRMVEAGHEIGNHTWSHPNLTGLSPEE 78

                           90       100
                   ....*....|....*....|....*....
gi 1734339322 1438 WLNEMDGQRRILAKFGGAPeeeIVGIRSP 1466
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 ...
 1164-1202 4.98e-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: 4.98e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339322 1164 KVAAVGSACRPIDICLGESVCTNGFCHCPENYIRQNGQC 1202
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 323-472 5.76e-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: 44.76  E-value: 5.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322  323 PLVQHEGKCVLRQQQKIVGPGELCDSGETCGKGSIcdsviPVCVCPAQTDLSNGECISVPAPTSQPVQVMTPPPTLPPVQ 402
Cdd:pfam03154  172 PVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSV-----PPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPH 246

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322  403 VPIQTLPPQTRPPQLPPVQITQPPIQTPVQPIffqttrpPMPTYATTPATTQFIPKQIYTTPPQMPKNSI 472
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 ...
 667-706 1.50e-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: 1.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1734339322  667 KKIVPGGRCGPIDVCVGGSNCIEGFCLCPAGQQPSNsGRC 706
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVN-GRC 52
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 380-443 2.22e-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: 40.54  E-value: 2.22e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339322   380 SVPAPTSQPV--QVMTPPPTLPpvqvPIQTLPPQTRPPQLPPvqitqppiQTPVQPIFFQTTRPPM 443
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 ...
 293-331 4.25e-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: 37.02  E-value: 4.25e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339322  293 TLVGIGALCSDLAECDHGSTCVMGRCTCVSPLVQHEGKC 331
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 958-1032 5.28e-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: 5.28e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339322  958 CPPGQIVFNVQCMP--PPTQPqittrvttpvkaapvvtpkpihstdCEIDANCGENKICVSGKCKCKPGFVDNSGTC 1032
Cdd:pfam01683    1 CPPGQVLVNGQCVPkvAPGES-------------------------CEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1021-1073 9.93e-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: 35.86  E-value: 9.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1734339322 1021 CKPGFVDNSGTCEPlegirgrSLRYGQACDrYQDKCINGAKCIDKICKCAPGF 1073
Cdd:pfam01683    1 CPPGQVLVNGQCVP-------KVAPGESCE-ADEQCPGGSVCVNGVCQCPPGF 45
 
Name Accession Description Interval E-value
CE4_CDA_like_1 cd10974
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ...
 1358-1633 1.83e-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: 1.83e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1358 PQFVVLTFDDAVNGKTFSDYKKLFENDVlKNPNGCDVKATFFISHEWTNYDAVNWLVQKNMEIASNSISHESLE-NANTN 1436
Cdd:cd10974      1 PQMITLTFDDAINDNNIELYKKIFNGKR-NNPNGCPIKGTFFVSHEYTNYQAVQKLHRKGHEIAVHSITHNDDEnNATYE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1437 RWLNEMDGQRRILAKFGGAPEEEIVGIRSPQLALGGDNQFEMMIGAEFLWDNSMSANPgiHGEPFWPQTMDYQVAWDCNE 1516
Cdd:cd10974     80 DWVKEMVGMREILEKFANITDNEIVGMRAPFLRVGGNRQFEMMEEFGFLYDSSITAPP--SNVPLWPYTLDYKMPHECHG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1517 ASCPKSSFPGVWSVPLNQFYGSYMSQIDSFRrssMLRAAVDLNNTVDELEEIITRNFERSYSANRAPYVLSLNADFLQLG 1596
Cdd:cd10974    158 QNCPTRSFPGVWEMVLNELDVRDDPQGDEPL---AMDDSCLNILSGDQVYEWLQHNFERHYLTNRAPYGLYFHTNWLKTK 234

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1734339322 1597 ghNKGMKAVQKFLNRMSAQKDVYIVTIKQLIDWMKRP 1633
Cdd:cd10974    235 --NELLRALQKFLDEILQLPDVYFVTMTQAIQWMQNP 269
CE4_CDA_like_2 cd10975
Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3. ...
 1358-1633 3.35e-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: 3.35e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1358 PQFVVLTFDDAVNGKTFSDYKKLFENdvLKNPNGCDVKATFFISHEWTNYDAVNWLVQKNMEIASNSISHESLE----NA 1433
Cdd:cd10975      1 PQLVTLTFDDAVNTLNYPYYEKLFGN--RKNPNGCPIGATFFVSHEYTDYRLVQELYNDGHEIALHSISHRSPQdywrNA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1434 NTNRWLNEMDGQRRILAKFGGAPEEEIVGIRSPQLALGGDNQFEMMIGAEFLWDNSMSAnPGIHGEPFWPQTMDYQVAWD 1513
Cdd:cd10975     79 SVDEWEREFGGQREILAHFANIPAEDIKGFRAPFLQLGGDATFKALKQLGLTYDSSWPT-QSFTNPPLWPYTLDYGSTQD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1514 CNEASCPKSSFPGVWSVPLNQFYGSymsqiDSFRRSSMlrAAVDLNNTVDELEEIITRNFERSYSANRAPYVLSLNADFL 1593
Cdd:cd10975    158 CVIPPCPTDSYPGFWVVPMVDWQDL-----NGVPCSML--AACPPPGTADEVYDWLLSNFERHYNTNRAPFGLYLHASWF 230

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1734339322 1594 QLGGHNKgmKAVQKFLNRMSAQKDVYIVTIKQLIDWMKRP 1633
Cdd:cd10975    231 EFTPNRL--EGFKKFLDELLSLDDVYLVTISQAIEWMRNP 268
CE4_CDA_like cd10919
Putative catalytic domain of chitin deacetylase-like proteins from insects and similar ...
 1358-1633 1.06e-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: 1.06e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1358 PQFVVLTFDDAVN-GKTFSDYKKLFENDvlKNPNGCDVKATFFISHEWTNYDAVNWLVQKNMEIASNSISHESLE-NANT 1435
Cdd:cd10919      1 PQFVLFTFDDAINeLNTDAVIQEIADGT--NNNGGCPIPATFFVSTNYTDCSLVKQLWREGHEIATHTVTHVPDDsNASV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1436 NRWLNEMDGQRRILAKFGGAPEEEIVGIRSPQLAlGGDNQFEMMIGAEFLWDNSMSANPGIHGEPF-WPQTMDYQVAWDC 1514
Cdd:cd10919     79 DEWEEEIAGQREWLNKTCGIPLEKVVGFRAPYLA-YNPNTREVLEENGFLYDSSIPEPYTPSGTNRlWPYTLDYGIPQDC 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1515 NEASC---PKSSFPGVWSVPLnqfygsYMSQIDSFRRSSMLRAAVDLNN-TVDELEEIITRNFERSYSANRAPYVLSLNA 1590
Cdd:cd10919    158 NLVPGscsPTERYPGLWEVPL------YTLQDGNDTTGDSYYCTPDDGPlNGDSFYALLKYNFDRHYNGNRAPFGIYLHA 231

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1734339322 1591 DFLQLGGHNKgMKAVQKFLNRMSAQKDVYIVTIKQLIDWMKRP 1633
Cdd:cd10919    232 AWLSPPYSER-RAALEKFLDYALSKPDVWFVTNSQLLDWMQNP 273
CE4_CDA_like_3 cd10976
Putative catalytic domain of uncharacterized bacterial hypothetical proteins similar to insect ...
 1438-1632 1.14e-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: 1.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1438 WLNEMDGQRRIL----AKFGGAPEE--------EIVGIRSPQLAlGGDNQFEMMIGAEFLWDNSMSANpgihgEPFWPQT 1505
Cdd:cd10976    110 WKREFDQFYRFVenayAINGIEGAPpwpafapnSIKGFRAPCLE-GSKGLQPALKKHGFTYDASSVTQ-----GPYWPQK 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1506 MDyqvawdcneascpkssfpGVWSVPLNQFY--GSYMSQI----DSFRRSSMlraAVDLNNTVDELEEI---ITRN-FER 1575
Cdd:cd10976    184 VD------------------GIWNFPLPLVPegPTSRPVIamdyNLFVRHSG---GVEAPAKAAEFEARmlaTYRNaFDR 242

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1734339322 1576 SYSANRAPyvlslnadfLQLGGH----NKG--MKAVQKFLNRMSAQKDVYIVTIKQLIDWMKR 1632
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 ...
 1239-1295 2.00e-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: 52.04  E-value: 2.00e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339322 1239 CAAQHVAIRGICKQKsapafAAPGDTCSMREKCTGGATCFEGMCTCDDHHFAEDGYC 1295
Cdd:pfam01683    1 CPPGQVLVNGQCVPK-----VAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
 1345-1466 3.31e-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: 3.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1345 GRRAPGGLRPDETPQ-FVVLTFDDAVNgktfSDYKKLFenDVLKNpngCDVKATFFISHEW--TNYDAVNWLVQKNMEIA 1421
Cdd:COG0726      5 LDELLPALRWGPLPKkAVALTFDDGPR----EGTPRLL--DLLKK---YGVKATFFVVGSAveRHPELVREIAAAGHEIG 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1734339322 1422 SNSISHESLENANTNRWLNEMDGQRRILAKFGGAPeeeIVGIRSP 1466
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 ...
 514-569 1.65e-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: 49.35  E-value: 1.65e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339322  514 CLSTHVNIEGRCEKVIYPGQVgCRSDLQCHaahSGTHCIDRICVCPEGQRAVDQTC 569
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 ...
 860-916 2.08e-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: 2.08e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339322  860 CPQDKSEIsQGQCVTprklEVVPGASCNANTVCTKGSTCESGLCRCQPGYIAVSGNC 916
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 ...
 558-615 2.88e-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: 2.88e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734339322  558 CPEGQRAVDQTCVSasepvTSPPGGSCSNLRECTGGSVCREGWCICPDPSMIVNrGIC 615
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 ...
 1361-1456 9.80e-07

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


Pssm-ID: 213022 [Multi-domain]  Cd Length: 171  Bit Score: 50.70  E-value: 9.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1361 VVLTFDDAVNGKTFSDYkkLfenDVLKNpNGcdVKATFFISHEW--TNYDAVNWLVQKNMEIASNSISHESLENANTNRW 1438
Cdd:cd10917      3 VALTFDDGPDPEYTPKI--L---DILAE-YG--VKATFFVVGENveKHPDLVRRIVAEGHEIGNHTYSHPDLTKLSPEEI 74

                           90
                   ....*....|....*...
gi 1734339322 1439 LNEMDGQRRILAKFGGAP 1456
Cdd:cd10917     75 RAEIERTQDAIEEATGVR 92
CE4_GLA_like_6s cd10967
Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is ...
 1361-1456 1.63e-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: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1361 VVLTFDDAVNgktfSDYK--KLFEndvlKNpngcDVKATFFIS------HEWTNYDAVNWLVQKNMEIASNSISHESLEN 1432
Cdd:cd10967      3 VSLTFDDGYA----QDLRaaPLLA----KY----GLKGTFFVNsgllgrRGYLDLEELRELAAAGHEIGSHTVTHPDLTS 70

                           90       100
                   ....*....|....*....|....
gi 1734339322 1433 ANTNRWLNEMDGQRRILAKFGGAP 1456
Cdd:cd10967     71 LPPAELRREIAESRAALEEIGGFP 94
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 905-969 3.25e-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: 45.88  E-value: 3.25e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1734339322  905 CQPGYIAVSGNCVAlpmsttpkmrvIAKPLESCENGETCEGGSNCDydTGICMCPPGQIVFNVQC 969
Cdd:pfam01683    1 CPPGQVLVNGQCVP-----------KVAPGESCEADEQCPGGSVCV--NGVCQCPPGFTPVNGRC 52
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 337-442 5.22e-06

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 50.24  E-value: 5.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322  337 QKIVGPGELCDSGETCGKGSICDSVIPVCVCPAQTdlsngecISVPAPTSQPVQVMT--PPPTLPPVQVPIQTLPPQTRp 414
Cdd:PHA02682    74 QRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVT-------CPAPAPACPPATAPTcpPPAVCPAPARPAPACPPSTR- 145

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1734339322  415 pQLPPVqitqPPIQTP-----VQPIFFQTTRPP 442
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 ...
 1191-1250 7.93e-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: 44.72  E-value: 7.93e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1191 CPENYIRQNGQCISKeckhkvAKVGETCKNGEICAGGSICdyDRKRCICAAQHVAIRGIC 1250
Cdd:pfam01683    1 CPPGQVLVNGQCVPK------VAPGESCEADEQCPGGSVC--VNGVCQCPPGFTPVNGRC 52
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 1361-1466 4.44e-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: 4.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1361 VVLTFDDAVNgktfSDYKKLFenDVLK-NpngcDVKATFFISHEW--TNYDAVNWLVQKNMEIASNSISHESLENANTNR 1437
Cdd:pfam01522    9 VALTFDDGPS----ENTPAIL--DVLKkY----GVKATFFVIGGNveRYPDLVKRMVEAGHEIGNHTWSHPNLTGLSPEE 78

                           90       100
                   ....*....|....*....|....*....
gi 1734339322 1438 WLNEMDGQRRILAKFGGAPeeeIVGIRSP 1466
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 ...
 1164-1202 4.98e-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: 4.98e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339322 1164 KVAAVGSACRPIDICLGESVCTNGFCHCPENYIRQNGQC 1202
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 323-472 5.76e-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: 44.76  E-value: 5.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322  323 PLVQHEGKCVLRQQQKIVGPGELCDSGETCGKGSIcdsviPVCVCPAQTDLSNGECISVPAPTSQPVQVMTPPPTLPPVQ 402
Cdd:pfam03154  172 PVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSV-----PPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPH 246

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322  403 VPIQTLPPQTRPPQLPPVQITQPPIQTPVQPIffqttrpPMPTYATTPATTQFIPKQIYTTPPQMPKNSI 472
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 ...
 667-706 1.50e-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: 1.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1734339322  667 KKIVPGGRCGPIDVCVGGSNCIEGFCLCPAGQQPSNsGRC 706
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVN-GRC 52
CE4_NodB_like_5s_6s cd10918
Putative catalytic NodB homology domain of PgaB, IcaB, and similar proteins which consist of a ...
 1361-1456 2.09e-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: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322 1361 VVLTFDDAvngkTFSDYKKLFEndVLKNpNGcdVKATFFI------------SHEWTNYDAVNW-----LVQKNMEIASN 1423
Cdd:cd10918      2 VVLTFDDG----YRDNYTYALP--ILKK-YG--LPATFFVitgyigggnpwwAPAPPRPPYLTWdqlreLAASGVEIGSH 72

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1734339322 1424 SISHESLENANTNRWLNEMDGQRRILAKFGGAP 1456
Cdd:cd10918     73 THTHPDLTTLSDEELRRELAESKERLEEELGKP 105
PRK11633 PRK11633
cell division protein DedD; Provisional
 380-441 2.22e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 41.53  E-value: 2.22e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339322  380 SVPAPTSQPVQVMTPPPTLPPVQVPIQTLPPQTRPPQLPPVQITQPPIQTPV-----QPIFFQTTRP 441
Cdd:PRK11633    79 DAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPApkpepKPVVEEKAAP 145
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 380-443 2.22e-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: 40.54  E-value: 2.22e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1734339322   380 SVPAPTSQPV--QVMTPPPTLPpvqvPIQTLPPQTRPPQLPPvqitqppiQTPVQPIFFQTTRPPM 443
Cdd:smart00818   91 NLPQPAQQPFqpQPLQPPQPQQ----PMQPQPPVHPIPPLPP--------QPPLPPMFPMQPLPPL 144
PHA03247 PHA03247
large tegument protein UL36; Provisional
 379-433 2.31e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 2.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1734339322  379 ISVPAPTSQPVQVMTPPPTLPPVQVPIQTLPPQTRPPQLPPVQiTQPPIQTPVQP 433
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 ...
 293-331 4.25e-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: 37.02  E-value: 4.25e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1734339322  293 TLVGIGALCSDLAECDHGSTCVMGRCTCVSPLVQHEGKC 331
Cdd:pfam01683   14 PKVAPGESCEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 958-1032 5.28e-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: 5.28e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734339322  958 CPPGQIVFNVQCMP--PPTQPqittrvttpvkaapvvtpkpihstdCEIDANCGENKICVSGKCKCKPGFVDNSGTC 1032
Cdd:pfam01683    1 CPPGQVLVNGQCVPkvAPGES-------------------------CEADEQCPGGSVCVNGVCQCPPGFTPVNGRC 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 380-433 9.10e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 9.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734339322  380 SVPAPTSQPVQVMTPPPTLPPVQVPIQTLPPQTRPPQLPPvQITQPPIQTPVQP 433
Cdd:PHA03247  2800 SPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP-PPPPGPPPPSLPL 2852
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 380-468 9.79e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.56  E-value: 9.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734339322  380 SVPAPTSQPVQVMTPPPTLP---PVQVPiqTLPPQTRPPQLPPVQITQPPIQTPVQPIFFQTTRPPMPTYATTPATTQFI 456
Cdd:PRK14950   362 PVPAPQPAKPTAAAPSPVRPtpaPSTRP--KAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVD 439

                           90
                   ....*....|..
gi 1734339322  457 PKQIYTTPPQMP 468
Cdd:PRK14950   440 EKPKYTPPAPPK 451
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 1021-1073 9.93e-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: 35.86  E-value: 9.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1734339322 1021 CKPGFVDNSGTCEPlegirgrSLRYGQACDrYQDKCINGAKCIDKICKCAPGF 1073
Cdd:pfam01683    1 CPPGQVLVNGQCVP-------KVAPGESCE-ADEQCPGGSVCVNGVCQCPPGF 45
 
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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