NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1242436564|gb|PBH67548|]
View 

hypothetical protein BGU94_02975 [Clostridioides difficile]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1-222 2.11e-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: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242436564   1 MDVFLLIGQSNARGLG-------NPKESIIPNENCFeYLSTDEIINMRCELETSEGDGTIAP------AFSNEW-NKLTG 66
Cdd:pfam03629   2 KDIFLLAGQSNMAGRGgvenwdgVVPPECQPPPRIL-RLNADLEWEEAREPLHADIDAKKTCgvgpgmAFANALlRAPPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242436564  67 NKVCFIHNAKDGSRIKNWNHDN---NWFLNDTIEKFNTGcttlskhyniENKYVIWIQGESDAKYGSDVLYYKESLKKIA 143
Cdd:pfam03629  81 GVIGLVPCAVGGTSIEEWARGGllyQEMVRRAKAALKGG----------EIKGILWYQGESDTSDEEDAAAYKEKLEKLI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242436564 144 YRLKEECMIDKMFVSLTGYWLGEDEYfIRTRRiaAAQESACSECdILCVGSKiamqfhdrGLTI--DDVHYTQEGLNMLG 221
Cdd:pfam03629 151 TDLRDDLGLPDLPIIQVQLASGEGPY-EEVVR--EAQLGIKLPN-VTVVDAK--------GLPLkdDNLHLTTESQVLLG 218

                  .
gi 1242436564 222 E 222
Cdd:pfam03629 219 K 219
 
Name Accession Description Interval E-value
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
1-222 2.11e-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: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242436564   1 MDVFLLIGQSNARGLG-------NPKESIIPNENCFeYLSTDEIINMRCELETSEGDGTIAP------AFSNEW-NKLTG 66
Cdd:pfam03629   2 KDIFLLAGQSNMAGRGgvenwdgVVPPECQPPPRIL-RLNADLEWEEAREPLHADIDAKKTCgvgpgmAFANALlRAPPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242436564  67 NKVCFIHNAKDGSRIKNWNHDN---NWFLNDTIEKFNTGcttlskhyniENKYVIWIQGESDAKYGSDVLYYKESLKKIA 143
Cdd:pfam03629  81 GVIGLVPCAVGGTSIEEWARGGllyQEMVRRAKAALKGG----------EIKGILWYQGESDTSDEEDAAAYKEKLEKLI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242436564 144 YRLKEECMIDKMFVSLTGYWLGEDEYfIRTRRiaAAQESACSECdILCVGSKiamqfhdrGLTI--DDVHYTQEGLNMLG 221
Cdd:pfam03629 151 TDLRDDLGLPDLPIIQVQLASGEGPY-EEVVR--EAQLGIKLPN-VTVVDAK--------GLPLkdDNLHLTTESQVLLG 218

                  .
gi 1242436564 222 E 222
Cdd:pfam03629 219 K 219
 
Name Accession Description Interval E-value
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
1-222 2.11e-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: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242436564   1 MDVFLLIGQSNARGLG-------NPKESIIPNENCFeYLSTDEIINMRCELETSEGDGTIAP------AFSNEW-NKLTG 66
Cdd:pfam03629   2 KDIFLLAGQSNMAGRGgvenwdgVVPPECQPPPRIL-RLNADLEWEEAREPLHADIDAKKTCgvgpgmAFANALlRAPPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242436564  67 NKVCFIHNAKDGSRIKNWNHDN---NWFLNDTIEKFNTGcttlskhyniENKYVIWIQGESDAKYGSDVLYYKESLKKIA 143
Cdd:pfam03629  81 GVIGLVPCAVGGTSIEEWARGGllyQEMVRRAKAALKGG----------EIKGILWYQGESDTSDEEDAAAYKEKLEKLI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242436564 144 YRLKEECMIDKMFVSLTGYWLGEDEYfIRTRRiaAAQESACSECdILCVGSKiamqfhdrGLTI--DDVHYTQEGLNMLG 221
Cdd:pfam03629 151 TDLRDDLGLPDLPIIQVQLASGEGPY-EEVVR--EAQLGIKLPN-VTVVDAK--------GLPLkdDNLHLTTESQVLLG 218

                  .
gi 1242436564 222 E 222
Cdd:pfam03629 219 K 219
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH