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Conserved domains on  [gi|443156|pdb|1NSC|B]
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Chain B, NEURAMINIDASE

Protein Classification

neuraminidase( domain architecture ID 10203044)

viral neuraminidase or exo-alpha-sialidase catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Influenza_NA cd15483
Sialidase or neuraminidase (EC 3.2.1.18) of Influenza viruses A and B; Sialidases or ...
3-390 0e+00

Sialidase or neuraminidase (EC 3.2.1.18) of Influenza viruses A and B; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates. Viral neuraminidases, such as this family from Influenza viruses A and B, play a vital role in pathogenesis. Influenza neuraminidase cleaves an alpha-ketosidic linkage between sialic acid and a neighboring sugar residue. During budding of virus particles from the infected cell, the sialidase helps to prevent the newly formed viral particles from aggregating. The viral sialidase cleaves terminal sialic acid from glycan structures on the infected cell surface, promoting virus release and the spread of virus to neighboring cells that are not yet infected. Also, sialidase modifies mucins in the respiratory tract and may improve access of the viral particle to its target cells. Sialidases have a six-bladed beta-propeller fold.


:

Pssm-ID: 271235  Cd Length: 386  Bit Score: 601.79  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B        3 EWTYP-RLSCQGSTFQKALLISPHRFGEArgnSAPLIIREPFIACGPKECKHFALTHYAAQPGGYYNGTREDRNKLRHLI 81
Cdd:cd15483   1 EFLNWtKPLCQISGFAIYSKDNGIRIGEG---GDVLVIREPFVSCDPGECRTFALTQGATLNGKHSNGTVHDRSPYRTLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B       82 SVKLGKIPTVENSIFHMAAWSGSACHDGREWTYIGVDGPDSNALIKIKYGEAYTDTYHSYANNILRTQESACNCIGGDCY 161
Cdd:cd15483  78 SVPLGSPPTVYNSRFECIAWSSSACHDGKAWLHIGISGPDNNATAVIKYGGRPTDTIGSWANNILRTQESECVCINGTCY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B      162 LMITDGSASGISKCRFLKIREGRIIKEIFPTGRVEHTEECTCGFASnKTIECACRDNSYTAKRPFVKLNVETDTAEIRLM 241
Cdd:cd15483 158 VVMTDGSASGQASTRILKIKEGKITKEIPLSGSAQHIEECSCYPRY-GKVECVCRDNWKGSNRPVVDIDMEDLTYESGYI 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B      242 CTETYLDTPRPDDGSITGPCESNGDK-GRGGIKGGFVHQRmaskIGRWYSRTMSKTERMGMELYVRYDGDPwTDSDALAH 320
Cdd:cd15483 237 CSGVVTDTPRPDDSSSTGSCRDPNNGrGNNGVKGFSFRQG----NGVWMGRTISKSSRSGYEMLKVPDGWT-PDSKSQVN 311
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1NSC_B      321 SGVMVSMKEPGWYSFGFEIKDK--KCDVPCIGIEMVHDGGK---KTWHSAATAIYCLMGSGQLLWDTVTGVDMAL 390
Cdd:cd15483 312 RQVIVDNKNWSGYSGSFSIEGKegSCIVPCFYVELIRGRPKetrVWWTSNSIVVFCGVSSTYGGWSWPDGANIPF 386
 
Name Accession Description Interval E-value
Influenza_NA cd15483
Sialidase or neuraminidase (EC 3.2.1.18) of Influenza viruses A and B; Sialidases or ...
3-390 0e+00

Sialidase or neuraminidase (EC 3.2.1.18) of Influenza viruses A and B; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates. Viral neuraminidases, such as this family from Influenza viruses A and B, play a vital role in pathogenesis. Influenza neuraminidase cleaves an alpha-ketosidic linkage between sialic acid and a neighboring sugar residue. During budding of virus particles from the infected cell, the sialidase helps to prevent the newly formed viral particles from aggregating. The viral sialidase cleaves terminal sialic acid from glycan structures on the infected cell surface, promoting virus release and the spread of virus to neighboring cells that are not yet infected. Also, sialidase modifies mucins in the respiratory tract and may improve access of the viral particle to its target cells. Sialidases have a six-bladed beta-propeller fold.


Pssm-ID: 271235  Cd Length: 386  Bit Score: 601.79  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B        3 EWTYP-RLSCQGSTFQKALLISPHRFGEArgnSAPLIIREPFIACGPKECKHFALTHYAAQPGGYYNGTREDRNKLRHLI 81
Cdd:cd15483   1 EFLNWtKPLCQISGFAIYSKDNGIRIGEG---GDVLVIREPFVSCDPGECRTFALTQGATLNGKHSNGTVHDRSPYRTLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B       82 SVKLGKIPTVENSIFHMAAWSGSACHDGREWTYIGVDGPDSNALIKIKYGEAYTDTYHSYANNILRTQESACNCIGGDCY 161
Cdd:cd15483  78 SVPLGSPPTVYNSRFECIAWSSSACHDGKAWLHIGISGPDNNATAVIKYGGRPTDTIGSWANNILRTQESECVCINGTCY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B      162 LMITDGSASGISKCRFLKIREGRIIKEIFPTGRVEHTEECTCGFASnKTIECACRDNSYTAKRPFVKLNVETDTAEIRLM 241
Cdd:cd15483 158 VVMTDGSASGQASTRILKIKEGKITKEIPLSGSAQHIEECSCYPRY-GKVECVCRDNWKGSNRPVVDIDMEDLTYESGYI 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B      242 CTETYLDTPRPDDGSITGPCESNGDK-GRGGIKGGFVHQRmaskIGRWYSRTMSKTERMGMELYVRYDGDPwTDSDALAH 320
Cdd:cd15483 237 CSGVVTDTPRPDDSSSTGSCRDPNNGrGNNGVKGFSFRQG----NGVWMGRTISKSSRSGYEMLKVPDGWT-PDSKSQVN 311
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1NSC_B      321 SGVMVSMKEPGWYSFGFEIKDK--KCDVPCIGIEMVHDGGK---KTWHSAATAIYCLMGSGQLLWDTVTGVDMAL 390
Cdd:cd15483 312 RQVIVDNKNWSGYSGSFSIEGKegSCIVPCFYVELIRGRPKetrVWWTSNSIVVFCGVSSTYGGWSWPDGANIPF 386
Neur pfam00064
Neuraminidase; Neuraminidases cleave sialic acid residues from glycoproteins. Belong to the ...
36-371 0e+00

Neuraminidase; Neuraminidases cleave sialic acid residues from glycoproteins. Belong to the sialidase family - but this alignment does not generalize to the other sialidases. Structure is a 6-sheet beta propeller.


Pssm-ID: 395018  Cd Length: 334  Bit Score: 588.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B         36 PLIIREPFIACGPKECKHFALTHYAAQPGGYYNGTREDRNKLRHLISVKLGKIPTVENSIFHMAAWSGSACHDGREWTYI 115
Cdd:pfam00064   1 PFVIREPFVSCSPKECRTFFLTQGALLNDKHSNGTVKDRSPLRHLMSVKVGKIPTVYNSRFEMVAWSASACHDGREWTTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B        116 GVDGPDSNALIKIKYGEAYTDTYHSYANNILRTQESACNCIGGDCYLMITDGSASGISKCRFLKIREGRIIKEIFPTGRV 195
Cdd:pfam00064  81 GVDGPDNDAVAVIKYGGAYTDTYHSWAHNILRTQESACNCIGGDCYLMMTDGPASGIAKYRILKIREGKIIKEILPTGRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B        196 EHTEECTCGFASNKTIECACRDNSYTAKRPFVKLNVETDTAEIRLMCTETYLDTPRPDDGSITGPCESNGDKGRGGIKGG 275
Cdd:pfam00064 161 EHTEECSCGFASNKTVECVCRDNWYGANRPFVKLNVELDTAEIGYMCTGTYLDTPRPEDGSIAGPCESNGDKWLGGVKGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B        276 FVHQRMasKIGRWYSRTMSKTERMGMELYVRYDGDPWTDSDALAHSGVMVSMKEPGWYSFGFEIKDKKCDVPCIGIEMVH 355
Cdd:pfam00064 241 FVHQRM--KIGVWYGRTMSKTSRMGFELIVRYDGDPWTDSDALTLSGVVVSIEEPGWYSFGFELKGKKCDVPCFWVEMIR 318
                         330
                  ....*....|....*.
1NSC_B        356 DGGKKTWHSAATAIYC 371
Cdd:pfam00064 319 GRGKTIWTSASSIIYC 334
 
Name Accession Description Interval E-value
Influenza_NA cd15483
Sialidase or neuraminidase (EC 3.2.1.18) of Influenza viruses A and B; Sialidases or ...
3-390 0e+00

Sialidase or neuraminidase (EC 3.2.1.18) of Influenza viruses A and B; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates. Viral neuraminidases, such as this family from Influenza viruses A and B, play a vital role in pathogenesis. Influenza neuraminidase cleaves an alpha-ketosidic linkage between sialic acid and a neighboring sugar residue. During budding of virus particles from the infected cell, the sialidase helps to prevent the newly formed viral particles from aggregating. The viral sialidase cleaves terminal sialic acid from glycan structures on the infected cell surface, promoting virus release and the spread of virus to neighboring cells that are not yet infected. Also, sialidase modifies mucins in the respiratory tract and may improve access of the viral particle to its target cells. Sialidases have a six-bladed beta-propeller fold.


Pssm-ID: 271235  Cd Length: 386  Bit Score: 601.79  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B        3 EWTYP-RLSCQGSTFQKALLISPHRFGEArgnSAPLIIREPFIACGPKECKHFALTHYAAQPGGYYNGTREDRNKLRHLI 81
Cdd:cd15483   1 EFLNWtKPLCQISGFAIYSKDNGIRIGEG---GDVLVIREPFVSCDPGECRTFALTQGATLNGKHSNGTVHDRSPYRTLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B       82 SVKLGKIPTVENSIFHMAAWSGSACHDGREWTYIGVDGPDSNALIKIKYGEAYTDTYHSYANNILRTQESACNCIGGDCY 161
Cdd:cd15483  78 SVPLGSPPTVYNSRFECIAWSSSACHDGKAWLHIGISGPDNNATAVIKYGGRPTDTIGSWANNILRTQESECVCINGTCY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B      162 LMITDGSASGISKCRFLKIREGRIIKEIFPTGRVEHTEECTCGFASnKTIECACRDNSYTAKRPFVKLNVETDTAEIRLM 241
Cdd:cd15483 158 VVMTDGSASGQASTRILKIKEGKITKEIPLSGSAQHIEECSCYPRY-GKVECVCRDNWKGSNRPVVDIDMEDLTYESGYI 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B      242 CTETYLDTPRPDDGSITGPCESNGDK-GRGGIKGGFVHQRmaskIGRWYSRTMSKTERMGMELYVRYDGDPwTDSDALAH 320
Cdd:cd15483 237 CSGVVTDTPRPDDSSSTGSCRDPNNGrGNNGVKGFSFRQG----NGVWMGRTISKSSRSGYEMLKVPDGWT-PDSKSQVN 311
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1NSC_B      321 SGVMVSMKEPGWYSFGFEIKDK--KCDVPCIGIEMVHDGGK---KTWHSAATAIYCLMGSGQLLWDTVTGVDMAL 390
Cdd:cd15483 312 RQVIVDNKNWSGYSGSFSIEGKegSCIVPCFYVELIRGRPKetrVWWTSNSIVVFCGVSSTYGGWSWPDGANIPF 386
Neur pfam00064
Neuraminidase; Neuraminidases cleave sialic acid residues from glycoproteins. Belong to the ...
36-371 0e+00

Neuraminidase; Neuraminidases cleave sialic acid residues from glycoproteins. Belong to the sialidase family - but this alignment does not generalize to the other sialidases. Structure is a 6-sheet beta propeller.


Pssm-ID: 395018  Cd Length: 334  Bit Score: 588.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B         36 PLIIREPFIACGPKECKHFALTHYAAQPGGYYNGTREDRNKLRHLISVKLGKIPTVENSIFHMAAWSGSACHDGREWTYI 115
Cdd:pfam00064   1 PFVIREPFVSCSPKECRTFFLTQGALLNDKHSNGTVKDRSPLRHLMSVKVGKIPTVYNSRFEMVAWSASACHDGREWTTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B        116 GVDGPDSNALIKIKYGEAYTDTYHSYANNILRTQESACNCIGGDCYLMITDGSASGISKCRFLKIREGRIIKEIFPTGRV 195
Cdd:pfam00064  81 GVDGPDNDAVAVIKYGGAYTDTYHSWAHNILRTQESACNCIGGDCYLMMTDGPASGIAKYRILKIREGKIIKEILPTGRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B        196 EHTEECTCGFASNKTIECACRDNSYTAKRPFVKLNVETDTAEIRLMCTETYLDTPRPDDGSITGPCESNGDKGRGGIKGG 275
Cdd:pfam00064 161 EHTEECSCGFASNKTVECVCRDNWYGANRPFVKLNVELDTAEIGYMCTGTYLDTPRPEDGSIAGPCESNGDKWLGGVKGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B        276 FVHQRMasKIGRWYSRTMSKTERMGMELYVRYDGDPWTDSDALAHSGVMVSMKEPGWYSFGFEIKDKKCDVPCIGIEMVH 355
Cdd:pfam00064 241 FVHQRM--KIGVWYGRTMSKTSRMGFELIVRYDGDPWTDSDALTLSGVVVSIEEPGWYSFGFELKGKKCDVPCFWVEMIR 318
                         330
                  ....*....|....*.
1NSC_B        356 DGGKKTWHSAATAIYC 371
Cdd:pfam00064 319 GRGKTIWTSASSIIYC 334
Sialidase cd00260
sialidases/neuraminidases; Sialidases or neuraminidases function to bind and hydrolyze ...
22-373 1.79e-145

sialidases/neuraminidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates as well as playing roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed beta-propeller fold. This hierarchy includes eubacterial, eukaryotic, and viral sialidases.


Pssm-ID: 271229  Cd Length: 361  Bit Score: 416.70  E-value: 1.79e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B       22 ISPHRFGEArgnSAPLIIREPFIACGPKECKHFALTHYaaqpggyynGTREDRNkLRHLISVKLGK-------IPTVENS 94
Cdd:cd00260   1 NFIPRPGEM---SGSLCTRIPSVDCSPTECCYFALVIL---------GTCRDRS-HRHLISALLVLrttagriPPTVENS 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B       95 IFHMA---AWSGSACHDGREWTYIGVDGPDS---------NALIKIKYG-----EAYTDTYHSY---ANNILRTQESACN 154
Cdd:cd00260  68 ISLDDtqnRWSCSVCHDGRGCDMICSKGPETeeedynsavNALMAIGYLgfdgqYHPVDLDVTTlfeAWNILRTGEGGGS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B      155 CIGGDCYLMITDGSASGISKCRFLKIREG---RIIKEIFPTGRVEHTEECTCGFASnKTIECACRDNSYTAKRPFVKLNV 231
Cdd:cd00260 148 CIDGRCWFSVTDGSAPGRIQQRILSIKEGtlgRIPKLTVPTGTVLHGAEGTILTVG-TSHFCYCRDSSYFSPRPVYPMTV 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NSC_B      232 ETDTAEIRLMCTETYLDTPRPddgsiTGPCESNGDKGRGGIKGGFVHQRMASKIGRWYSRTMSKTERMGMELYVRYDGdp 311
Cdd:cd00260 227 STATLHSPYTCNAFTRDGPRP-----CQASARCPNSCVTGVKGDPYPLIFYTLRGTWGTRTDSETSRLGMESAVFYDA-- 299
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1NSC_B      312 wtDSDALAHSGVMVSMKEPGWYSFGFEIKDKK--CDVPCIGIEMVHDGGKKTWHSAATAIYCLM 373
Cdd:cd00260 300 --DATKRSRGTRVVSSKTKGGYSTSTCFKDVKtnCYYCCSIVEISNTLDKGKWGSFAIVPLCVE 361
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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