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Conserved domains on  [gi|1540583156|ref|NP_001354794|]
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sialidase-3 isoform d [Homo sapiens]

Protein Classification

sialidase family protein( domain architecture ID 10202570)

sialidase (glycoside hydrolase 33) family protein such as non-viral exo-alpha-sialidase that catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins, oligosaccharides and gangliosides

CATH:  2.120.10.10
CAZY:  GH33
EC:  3.2.1.-
PubMed:  7934919|8994884
SCOP:  3001607

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sialidase_non-viral cd15482
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
 44-173 8.46e-17

Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.


:

Pssm-ID: 271234 [Multi-domain]  Cd Length: 339  Bit Score: 76.34  E-value: 8.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540583156  44 SPLFRQEDDRGITYRIPALLYIPPThTFLAFAEKRSTRRDE--DALHLVLRRGLRIGQlvQWGPLKPLMEA-TLPGHRTM 120
Cdd:cd15482     1 VLLFVPGDEGSDSYRIPSLVTTPNG-TLLAFADGRYEGAGDlgGDIDIVVRRSTDGGK--TWSEPVTVVDGgGSGGASYG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1540583156 121 NPCPVWEQKSGCVFLFFICVRGHvteRQQIVSGRNAARLCFIYSQDAGCSWSE 173
Cdd:cd15482    78 DPSLVVDPDTGRIFLFYTSGPGG---GGEALTGDGTVRVRLSTSDDDGKTWSE 127
 
Name Accession Description Interval E-value
Sialidase_non-viral cd15482
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
 44-173 8.46e-17

Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.


Pssm-ID: 271234 [Multi-domain]  Cd Length: 339  Bit Score: 76.34  E-value: 8.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540583156  44 SPLFRQEDDRGITYRIPALLYIPPThTFLAFAEKRSTRRDE--DALHLVLRRGLRIGQlvQWGPLKPLMEA-TLPGHRTM 120
Cdd:cd15482     1 VLLFVPGDEGSDSYRIPSLVTTPNG-TLLAFADGRYEGAGDlgGDIDIVVRRSTDGGK--TWSEPVTVVDGgGSGGASYG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1540583156 121 NPCPVWEQKSGCVFLFFICVRGHvteRQQIVSGRNAARLCFIYSQDAGCSWSE 173
Cdd:cd15482    78 DPSLVVDPDTGRIFLFYTSGPGG---GGEALTGDGTVRVRLSTSDDDGKTWSE 127
NanH COG4409
Neuraminidase (sialidase) NanH, contains C-terminal autotransporter domain [Carbohydrate ...
 46-173 2.50e-12

Neuraminidase (sialidase) NanH, contains C-terminal autotransporter domain [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443531 [Multi-domain]  Cd Length: 376  Bit Score: 63.80  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540583156  46 LFRQEDDRGITYRIPALLYIPPThTFLAFAEKR-STRRD--EDaLHLVLRRGLRIGQlvQWGPLKPLM---EATLPGHRT 119
Cdd:COG4409    26 VFTSGDDGYASYRIPALVTTPKG-TLLAFADARyNGSGDlpGD-IDIVMRRSTDGGK--TWSPPQVILdygEGGGLSAGV 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540583156 120 MNPCPVWEQKSGCVFLFFicVRGH------VTERQQIVSGRNAARLCFIYSQDAGCSWSE 173
Cdd:COG4409   102 GDPAPVVDRKTGRIFLLA--DWMPgndgegWSGSEPGTDPKGTRQLWVTYSDDDGKTWSE 159
 
Name Accession Description Interval E-value
Sialidase_non-viral cd15482
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
 44-173 8.46e-17

Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.


Pssm-ID: 271234 [Multi-domain]  Cd Length: 339  Bit Score: 76.34  E-value: 8.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540583156  44 SPLFRQEDDRGITYRIPALLYIPPThTFLAFAEKRSTRRDE--DALHLVLRRGLRIGQlvQWGPLKPLMEA-TLPGHRTM 120
Cdd:cd15482     1 VLLFVPGDEGSDSYRIPSLVTTPNG-TLLAFADGRYEGAGDlgGDIDIVVRRSTDGGK--TWSEPVTVVDGgGSGGASYG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1540583156 121 NPCPVWEQKSGCVFLFFICVRGHvteRQQIVSGRNAARLCFIYSQDAGCSWSE 173
Cdd:cd15482    78 DPSLVVDPDTGRIFLFYTSGPGG---GGEALTGDGTVRVRLSTSDDDGKTWSE 127
NanH COG4409
Neuraminidase (sialidase) NanH, contains C-terminal autotransporter domain [Carbohydrate ...
 46-173 2.50e-12

Neuraminidase (sialidase) NanH, contains C-terminal autotransporter domain [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443531 [Multi-domain]  Cd Length: 376  Bit Score: 63.80  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540583156  46 LFRQEDDRGITYRIPALLYIPPThTFLAFAEKR-STRRD--EDaLHLVLRRGLRIGQlvQWGPLKPLM---EATLPGHRT 119
Cdd:COG4409    26 VFTSGDDGYASYRIPALVTTPKG-TLLAFADARyNGSGDlpGD-IDIVMRRSTDGGK--TWSPPQVILdygEGGGLSAGV 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540583156 120 MNPCPVWEQKSGCVFLFFicVRGH------VTERQQIVSGRNAARLCFIYSQDAGCSWSE 173
Cdd:COG4409   102 GDPAPVVDRKTGRIFLLA--DWMPgndgegWSGSEPGTDPKGTRQLWVTYSDDDGKTWSE 159
 
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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