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Conserved domains on  [gi|2550912439|ref|WP_302278724|]
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sialate O-acetylesterase [Barnesiella intestinihominis]

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 ...
408-526 7.99e-07

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: 50.28  E-value: 7.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550912439 408 PSLLYNAMVNpLVGLSMQ-----GVIWYQGENNTNR---AKEYYDLFPAMINDWRKKWGK-DFPFYWVQLANymdavevP 478
Cdd:pfam03629 101 GGLLYQEMVR-RAKAALKggeikGILWYQGESDTSDeedAAAYKEKLEKLITDLRDDLGLpDLPIIQVQLAS-------G 172
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2550912439 479 SESLWAQVREAQtQTLSLSHTgqaVIIDigeAKDIHPKNKQ---------EVGRRLA 526
Cdd:pfam03629 173 EGPYEEVVREAQ-LGIKLPNV---TVVD---AKGLPLKDDNlhlttesqvLLGKRLA 222
LacZ super family cl43822
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];
261-379 1.34e-05

Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];


The actual alignment was detected with superfamily member COG3250:

Pssm-ID: 442481 [Multi-domain]  Cd Length: 638  Bit Score: 48.22  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550912439 261 PSYSKDDWKEVSVPGLWSEEGLVSLD----------GVVWQTCRFTLSENYVGKEAVLSLHVIDDD-DItWINGQKIGET 329
Cdd:COG3250    16 PDFDDSGWDPITVPGDWELDLYGLPDpfvgpwylynGVGWYRRTFTVPASWKGKRVFLHFEGVDTAaEV-WVNGKKVGYH 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550912439 330 VG------YDVRRLysVPAG-------VLKESNEITLKISDYRGGGGLYGPaneIYLKVGDKT 379
Cdd:COG3250    95 EGgftpfeFDITDY--LKPGenvlavrVDNPSDGSYLEGQDWWRTSGIYRD---VWLEATPKV 152
SASA super family cl04187
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
106-229 1.55e-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: 46.43  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550912439 106 GEVWICSGQSNMEFR--LHAAMNAEKEIADAENYSFLRSFNVKQEMSHRPLSDLQGEWRVCDSGSagdfsavGYFFAREL 183
Cdd:pfam03629   2 KDIFLLAGQSNMAGRggVENWDGVVPPECQPPPRILRLNADLEWEEAREPLHADIDAKKTCGVGP-------GMAFANAL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2550912439 184 YR-KLGVPVGFINTSWGGTDIESWMSMDaidkfPKYKRLQDRMRSSQ 229
Cdd:pfam03629  75 LRaPPGGVIGLVPCAVGGTSIEEWARGG-----LLYQEMVRRAKAAL 116
 
Name Accession Description Interval E-value
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
408-526 7.99e-07

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: 50.28  E-value: 7.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550912439 408 PSLLYNAMVNpLVGLSMQ-----GVIWYQGENNTNR---AKEYYDLFPAMINDWRKKWGK-DFPFYWVQLANymdavevP 478
Cdd:pfam03629 101 GGLLYQEMVR-RAKAALKggeikGILWYQGESDTSDeedAAAYKEKLEKLITDLRDDLGLpDLPIIQVQLAS-------G 172
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2550912439 479 SESLWAQVREAQtQTLSLSHTgqaVIIDigeAKDIHPKNKQ---------EVGRRLA 526
Cdd:pfam03629 173 EGPYEEVVREAQ-LGIKLPNV---TVVD---AKGLPLKDDNlhlttesqvLLGKRLA 222
LacZ COG3250
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];
261-379 1.34e-05

Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];


Pssm-ID: 442481 [Multi-domain]  Cd Length: 638  Bit Score: 48.22  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550912439 261 PSYSKDDWKEVSVPGLWSEEGLVSLD----------GVVWQTCRFTLSENYVGKEAVLSLHVIDDD-DItWINGQKIGET 329
Cdd:COG3250    16 PDFDDSGWDPITVPGDWELDLYGLPDpfvgpwylynGVGWYRRTFTVPASWKGKRVFLHFEGVDTAaEV-WVNGKKVGYH 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550912439 330 VG------YDVRRLysVPAG-------VLKESNEITLKISDYRGGGGLYGPaneIYLKVGDKT 379
Cdd:COG3250    95 EGgftpfeFDITDY--LKPGenvlavrVDNPSDGSYLEGQDWWRTSGIYRD---VWLEATPKV 152
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
106-229 1.55e-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: 46.43  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550912439 106 GEVWICSGQSNMEFR--LHAAMNAEKEIADAENYSFLRSFNVKQEMSHRPLSDLQGEWRVCDSGSagdfsavGYFFAREL 183
Cdd:pfam03629   2 KDIFLLAGQSNMAGRggVENWDGVVPPECQPPPRILRLNADLEWEEAREPLHADIDAKKTCGVGP-------GMAFANAL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2550912439 184 YR-KLGVPVGFINTSWGGTDIESWMSMDaidkfPKYKRLQDRMRSSQ 229
Cdd:pfam03629  75 LRaPPGGVIGLVPCAVGGTSIEEWARGG-----LLYQEMVRRAKAAL 116
 
Name Accession Description Interval E-value
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
408-526 7.99e-07

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: 50.28  E-value: 7.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550912439 408 PSLLYNAMVNpLVGLSMQ-----GVIWYQGENNTNR---AKEYYDLFPAMINDWRKKWGK-DFPFYWVQLANymdavevP 478
Cdd:pfam03629 101 GGLLYQEMVR-RAKAALKggeikGILWYQGESDTSDeedAAAYKEKLEKLITDLRDDLGLpDLPIIQVQLAS-------G 172
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2550912439 479 SESLWAQVREAQtQTLSLSHTgqaVIIDigeAKDIHPKNKQ---------EVGRRLA 526
Cdd:pfam03629 173 EGPYEEVVREAQ-LGIKLPNV---TVVD---AKGLPLKDDNlhlttesqvLLGKRLA 222
LacZ COG3250
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];
261-379 1.34e-05

Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];


Pssm-ID: 442481 [Multi-domain]  Cd Length: 638  Bit Score: 48.22  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550912439 261 PSYSKDDWKEVSVPGLWSEEGLVSLD----------GVVWQTCRFTLSENYVGKEAVLSLHVIDDD-DItWINGQKIGET 329
Cdd:COG3250    16 PDFDDSGWDPITVPGDWELDLYGLPDpfvgpwylynGVGWYRRTFTVPASWKGKRVFLHFEGVDTAaEV-WVNGKKVGYH 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550912439 330 VG------YDVRRLysVPAG-------VLKESNEITLKISDYRGGGGLYGPaneIYLKVGDKT 379
Cdd:COG3250    95 EGgftpfeFDITDY--LKPGenvlavrVDNPSDGSYLEGQDWWRTSGIYRD---VWLEATPKV 152
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
106-229 1.55e-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: 46.43  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550912439 106 GEVWICSGQSNMEFR--LHAAMNAEKEIADAENYSFLRSFNVKQEMSHRPLSDLQGEWRVCDSGSagdfsavGYFFAREL 183
Cdd:pfam03629   2 KDIFLLAGQSNMAGRggVENWDGVVPPECQPPPRILRLNADLEWEEAREPLHADIDAKKTCGVGP-------GMAFANAL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2550912439 184 YR-KLGVPVGFINTSWGGTDIESWMSMDaidkfPKYKRLQDRMRSSQ 229
Cdd:pfam03629  75 LRaPPGGVIGLVPCAVGGTSIEEWARGG-----LLYQEMVRRAKAAL 116
 
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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