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Conserved domains on  [gi|2173144738|ref|WP_233437974|]
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sialate O-acetylesterase [Klebsiella variicola]

Protein Classification

sialate O-acetylesterase family protein( domain architecture ID 4012)

sialate O-acetylesterase family protein similar to Homo sapiens sialate O-acetylesterase and Escherichia coli 9-O-acetyl-N-acetylneuraminic acid deacetylase

CATH:  3.40.50.1110
EC:  3.1.1.-
Gene Ontology:  GO:0001681|GO:0005975
SCOP:  3001315

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SASA super family cl04187
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
417-594 5.49e-05

Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665.


The actual alignment was detected with superfamily member pfam03629:

Pssm-ID: 427409  Cd Length: 227  Bit Score: 45.27  E-value: 5.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173144738 417 AFADEVKRRrnermqkdnDTDVIFGVALCGVAGAPIEDLSKGAaaGYYNRyltalsgIVQAATAAGYEWEVGGIILNHGE 496
Cdd:pfam03629  69 AFANALLRA---------PPGGVIGLVPCAVGGTSIEEWARGG--LLYQE-------MVRRAKAALKGGEIKGILWYQGE 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173144738 497 QNNG--ATAEYYLPYLQTLYGNLIADamtaSGQTTTPIFlINQIGnSFiSGRNFGVVEAQrQFVENNPLAFMVGSyAGLP 574
Cdd:pfam03629 131 SDTSdeEDAAAYKEKLEKLITDLRDD----LGLPDLPII-QVQLA-SG-EGPYEEVVREA-QLGIKLPNVTVVDA-KGLP 201
                         170       180
                  ....*....|....*....|..
gi 2173144738 575 NPVD--HLFANSYRWLGAQFAK 594
Cdd:pfam03629 202 LKDDnlHLTTESQVLLGKRLAE 223
 
Name Accession Description Interval E-value
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
417-594 5.49e-05

Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665.


Pssm-ID: 427409  Cd Length: 227  Bit Score: 45.27  E-value: 5.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173144738 417 AFADEVKRRrnermqkdnDTDVIFGVALCGVAGAPIEDLSKGAaaGYYNRyltalsgIVQAATAAGYEWEVGGIILNHGE 496
Cdd:pfam03629  69 AFANALLRA---------PPGGVIGLVPCAVGGTSIEEWARGG--LLYQE-------MVRRAKAALKGGEIKGILWYQGE 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173144738 497 QNNG--ATAEYYLPYLQTLYGNLIADamtaSGQTTTPIFlINQIGnSFiSGRNFGVVEAQrQFVENNPLAFMVGSyAGLP 574
Cdd:pfam03629 131 SDTSdeEDAAAYKEKLEKLITDLRDD----LGLPDLPII-QVQLA-SG-EGPYEEVVREA-QLGIKLPNVTVVDA-KGLP 201
                         170       180
                  ....*....|....*....|..
gi 2173144738 575 NPVD--HLFANSYRWLGAQFAK 594
Cdd:pfam03629 202 LKDDnlHLTTESQVLLGKRLAE 223
 
Name Accession Description Interval E-value
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
417-594 5.49e-05

Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665.


Pssm-ID: 427409  Cd Length: 227  Bit Score: 45.27  E-value: 5.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173144738 417 AFADEVKRRrnermqkdnDTDVIFGVALCGVAGAPIEDLSKGAaaGYYNRyltalsgIVQAATAAGYEWEVGGIILNHGE 496
Cdd:pfam03629  69 AFANALLRA---------PPGGVIGLVPCAVGGTSIEEWARGG--LLYQE-------MVRRAKAALKGGEIKGILWYQGE 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173144738 497 QNNG--ATAEYYLPYLQTLYGNLIADamtaSGQTTTPIFlINQIGnSFiSGRNFGVVEAQrQFVENNPLAFMVGSyAGLP 574
Cdd:pfam03629 131 SDTSdeEDAAAYKEKLEKLITDLRDD----LGLPDLPII-QVQLA-SG-EGPYEEVVREA-QLGIKLPNVTVVDA-KGLP 201
                         170       180
                  ....*....|....*....|..
gi 2173144738 575 NPVD--HLFANSYRWLGAQFAK 594
Cdd:pfam03629 202 LKDDnlHLTTESQVLLGKRLAE 223
 
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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