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Conserved domains on  [gi|1827780]
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Chain A, INFLUENZA A SUBTYPE N2 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 ...
2-385 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: 664.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780    2 EYRNWSKPQCQITGFAPFSKDNSIRLSAGGDIWVTREPYVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTLLMNE 81
Cdd:cd15483   1 EFLNWTKPLCQISGFAIYSKDNGIRIGEGGDVLVIREPFVSCDPGECRTFALTQGATLNGKHSNGTVHDRSPYRTLISVP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780   82 LGVPFHLG-TRQVCIAWSSSSCHDGKAWLHVCITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECVCINGTCTVVM 160
Cdd:cd15483  81 LGSPPTVYnSRFECIAWSSSACHDGKAWLHIGISGPDNNATAVIKYGGRPTDTIGSWANNILRTQESECVCINGTCYVVM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780  161 TDGSASGRADTRILFIEEGKIVHISPLAGSAQHVEECSCYPRYPGVRCICRDNWKGSNRPVVDINMEDYSIDSSYVCSGL 240
Cdd:cd15483 161 TDGSASGQASTRILKIKEGKITKEIPLSGSAQHIEECSCYPRYGKVECVCRDNWKGSNRPVVDIDMEDLTYESGYICSGV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780  241 VGDTPRNDDRSSNSNCRDPNNERGTQGVKGWAFDNGNDLWMGRTISKDLRSGYETFKVIGGWsTPNSKSQINRQVIVDSD 320
Cdd:cd15483 241 VTDTPRPDDSSSTGSCRDPNNGRGNNGVKGFSFRQGNGVWMGRTISKSSRSGYEMLKVPDGW-TPDSKSQVNRQVIVDNK 319
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827780  321 NRSGYSGIFSVEGK--SCINRCFYVELIRGRKQETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINF 385
Cdd:cd15483 320 NWSGYSGSFSIEGKegSCIVPCFYVELIRGRPKETRVWWTSNSIVVFCGVSSTYGGWSWPDGANIPF 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 ...
2-385 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: 664.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780    2 EYRNWSKPQCQITGFAPFSKDNSIRLSAGGDIWVTREPYVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTLLMNE 81
Cdd:cd15483   1 EFLNWTKPLCQISGFAIYSKDNGIRIGEGGDVLVIREPFVSCDPGECRTFALTQGATLNGKHSNGTVHDRSPYRTLISVP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780   82 LGVPFHLG-TRQVCIAWSSSSCHDGKAWLHVCITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECVCINGTCTVVM 160
Cdd:cd15483  81 LGSPPTVYnSRFECIAWSSSACHDGKAWLHIGISGPDNNATAVIKYGGRPTDTIGSWANNILRTQESECVCINGTCYVVM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780  161 TDGSASGRADTRILFIEEGKIVHISPLAGSAQHVEECSCYPRYPGVRCICRDNWKGSNRPVVDINMEDYSIDSSYVCSGL 240
Cdd:cd15483 161 TDGSASGQASTRILKIKEGKITKEIPLSGSAQHIEECSCYPRYGKVECVCRDNWKGSNRPVVDIDMEDLTYESGYICSGV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780  241 VGDTPRNDDRSSNSNCRDPNNERGTQGVKGWAFDNGNDLWMGRTISKDLRSGYETFKVIGGWsTPNSKSQINRQVIVDSD 320
Cdd:cd15483 241 VTDTPRPDDSSSTGSCRDPNNGRGNNGVKGFSFRQGNGVWMGRTISKSSRSGYEMLKVPDGW-TPDSKSQVNRQVIVDNK 319
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827780  321 NRSGYSGIFSVEGK--SCINRCFYVELIRGRKQETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINF 385
Cdd:cd15483 320 NWSGYSGSFSIEGKegSCIVPCFYVELIRGRPKETRVWWTSNSIVVFCGVSSTYGGWSWPDGANIPF 386
Neur pfam00064
Neuraminidase; Neuraminidases cleave sialic acid residues from glycoproteins. Belong to the ...
33-366 7.31e-102

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: 304.91  E-value: 7.31e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780     33 IWVTREPYVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTLLMNELG-VPFHLGTRQVCIAWSSSSCHDGKAWLHV 111
Cdd:pfam00064   1 PFVIREPFVSCSPKECRTFFLTQGALLNDKHSNGTVKDRSPLRHLMSVKVGkIPTVYNSRFEMVAWSASACHDGREWTTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780    112 CITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECVCINGTCTVVMTDGSASGRADTRILFIEEGKIVHISPLAGSA 191
Cdd:pfam00064  81 GVDGPDNDAVAVIKYGGAYTDTYHSWAHNILRTQESACNCIGGDCYLMMTDGPASGIAKYRILKIREGKIIKEILPTGRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780    192 QHVEECSCYPRYPG-VRCICRDNWKGSNRPVVDINMEDYSIDSSYVCSGLVGDTPRNDDRSSNSNCRDPNNERGtQGVKG 270
Cdd:pfam00064 161 EHTEECSCGFASNKtVECVCRDNWYGANRPFVKLNVELDTAEIGYMCTGTYLDTPRPEDGSIAGPCESNGDKWL-GGVKG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780    271 WAF--DNGNDLWMGRTISKDLRSGYETFKVIGGWsTPNSKSQINRQVIVDSDNRSG-YSGIFSVEGKSCINRCFYVELIR 347
Cdd:pfam00064 240 GFVhqRMKIGVWYGRTMSKTSRMGFELIVRYDGD-PWTDSDALTLSGVVVSIEEPGwYSFGFELKGKKCDVPCFWVEMIR 318
                         330
                  ....*....|....*....
gi 1827780    348 GRKQETrvwWTSNSIVVFC 366
Cdd:pfam00064 319 GRGKTI---WTSASSIIYC 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 ...
2-385 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: 664.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780    2 EYRNWSKPQCQITGFAPFSKDNSIRLSAGGDIWVTREPYVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTLLMNE 81
Cdd:cd15483   1 EFLNWTKPLCQISGFAIYSKDNGIRIGEGGDVLVIREPFVSCDPGECRTFALTQGATLNGKHSNGTVHDRSPYRTLISVP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780   82 LGVPFHLG-TRQVCIAWSSSSCHDGKAWLHVCITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECVCINGTCTVVM 160
Cdd:cd15483  81 LGSPPTVYnSRFECIAWSSSACHDGKAWLHIGISGPDNNATAVIKYGGRPTDTIGSWANNILRTQESECVCINGTCYVVM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780  161 TDGSASGRADTRILFIEEGKIVHISPLAGSAQHVEECSCYPRYPGVRCICRDNWKGSNRPVVDINMEDYSIDSSYVCSGL 240
Cdd:cd15483 161 TDGSASGQASTRILKIKEGKITKEIPLSGSAQHIEECSCYPRYGKVECVCRDNWKGSNRPVVDIDMEDLTYESGYICSGV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780  241 VGDTPRNDDRSSNSNCRDPNNERGTQGVKGWAFDNGNDLWMGRTISKDLRSGYETFKVIGGWsTPNSKSQINRQVIVDSD 320
Cdd:cd15483 241 VTDTPRPDDSSSTGSCRDPNNGRGNNGVKGFSFRQGNGVWMGRTISKSSRSGYEMLKVPDGW-TPDSKSQVNRQVIVDNK 319
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827780  321 NRSGYSGIFSVEGK--SCINRCFYVELIRGRKQETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINF 385
Cdd:cd15483 320 NWSGYSGSFSIEGKegSCIVPCFYVELIRGRPKETRVWWTSNSIVVFCGVSSTYGGWSWPDGANIPF 386
Neur pfam00064
Neuraminidase; Neuraminidases cleave sialic acid residues from glycoproteins. Belong to the ...
33-366 7.31e-102

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: 304.91  E-value: 7.31e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780     33 IWVTREPYVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTLLMNELG-VPFHLGTRQVCIAWSSSSCHDGKAWLHV 111
Cdd:pfam00064   1 PFVIREPFVSCSPKECRTFFLTQGALLNDKHSNGTVKDRSPLRHLMSVKVGkIPTVYNSRFEMVAWSASACHDGREWTTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780    112 CITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECVCINGTCTVVMTDGSASGRADTRILFIEEGKIVHISPLAGSA 191
Cdd:pfam00064  81 GVDGPDNDAVAVIKYGGAYTDTYHSWAHNILRTQESACNCIGGDCYLMMTDGPASGIAKYRILKIREGKIIKEILPTGRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780    192 QHVEECSCYPRYPG-VRCICRDNWKGSNRPVVDINMEDYSIDSSYVCSGLVGDTPRNDDRSSNSNCRDPNNERGtQGVKG 270
Cdd:pfam00064 161 EHTEECSCGFASNKtVECVCRDNWYGANRPFVKLNVELDTAEIGYMCTGTYLDTPRPEDGSIAGPCESNGDKWL-GGVKG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780    271 WAF--DNGNDLWMGRTISKDLRSGYETFKVIGGWsTPNSKSQINRQVIVDSDNRSG-YSGIFSVEGKSCINRCFYVELIR 347
Cdd:pfam00064 240 GFVhqRMKIGVWYGRTMSKTSRMGFELIVRYDGD-PWTDSDALTLSGVVVSIEEPGwYSFGFELKGKKCDVPCFWVEMIR 318
                         330
                  ....*....|....*....
gi 1827780    348 GRKQETrvwWTSNSIVVFC 366
Cdd:pfam00064 319 GRGKTI---WTSASSIIYC 334
Sialidase cd00260
sialidases/neuraminidases; Sialidases or neuraminidases function to bind and hydrolyze ...
22-366 3.82e-58

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: 193.29  E-value: 3.82e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780   22 DNSIRLSAGGDIWVTREPYVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTllMNELGVPFHLGTRQVCI---AWS 98
Cdd:cd00260   1 NFIPRPGEMSGSLCTRIPSVDCSPTECCYFALVILGTCRDRSHRHLISALLVLRT--TAGRIPPTVENSISLDDtqnRWS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780   99 SSSCHDGKAWLHVCITG------DDKNATASFIYDGRL--------VDSIGSWSQ---NILRTQESECVCINGTCTVVMT 161
Cdd:cd00260  79 CSVCHDGRGCDMICSKGpeteeeDYNSAVNALMAIGYLgfdgqyhpVDLDVTTLFeawNILRTGEGGGSCIDGRCWFSVT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780  162 DGSASGRADTRILFIEEG---KIVHISPLAGSAQHVEECSCYPRYPGVRCICRDNWKGSNRPVVDINMEDYSIDSSYVCS 238
Cdd:cd00260 159 DGSAPGRIQQRILSIKEGtlgRIPKLTVPTGTVLHGAEGTILTVGTSHFCYCRDSSYFSPRPVYPMTVSTATLHSPYTCN 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827780  239 GLVGDTPRnddrssNSNCRDPNNERGTQGVKG----WAFDNGNDLWMGRTISKDLRSGYETFKVIGGWSTPNSKSqinrQ 314
Cdd:cd00260 239 AFTRDGPR------PCQASARCPNSCVTGVKGdpypLIFYTLRGTWGTRTDSETSRLGMESAVFYDADATKRSRG----T 308
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 1827780  315 VIVDSDNRSGYSGIF--SVEGKSCINRCFYVELIRGRKqetRVWWTSNSIVVFC 366
Cdd:cd00260 309 RVVSSKTKGGYSTSTcfKDVKTNCYYCCSIVEISNTLD---KGKWGSFAIVPLC 359
 
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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