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Conserved domains on  [gi|1314862428|gb|AUG19242|]
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9-O-acetyl-N-acetylneuraminic acid deacetylase [Escherichia coli str. K-12 substr. MG1655]

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 ...
11-209 3.74e-15

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: 73.39  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862428  11 YVLtvAGQSNaMAyGEGL-----PLPDREDAPHPRIKQLARFAHTHPGGPPCHFnDIiplthcphDVQDMQGyhhplatn 85
Cdd:pfam03629   5 FLL--AGQSN-MA-GRGGvenwdGVVPPECQPPPRILRLNADLEWEEAREPLHA-DI--------DAKKTCG-------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862428  86 hqtqygtVGQALHIARKLLPfIPDNAGILIVPCCRGGSAFTagsegtyserhgashdacRWGTDTPLYQDLVSRTRAALA 165
Cdd:pfam03629  64 -------VGPGMAFANALLR-APPGGVIGLVPCAVGGTSIE------------------EWARGGLLYQEMVRRAKAALK 117
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1314862428 166 KnpqnkflGAC----WMQGEFDLMT-SDYASHPQHFNHMVEAFRRDLKQ 209
Cdd:pfam03629 118 G-------GEIkgilWYQGESDTSDeEDAAAYKEKLEKLITDLRDDLGL 159
 
Name Accession Description Interval E-value
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
11-209 3.74e-15

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: 73.39  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862428  11 YVLtvAGQSNaMAyGEGL-----PLPDREDAPHPRIKQLARFAHTHPGGPPCHFnDIiplthcphDVQDMQGyhhplatn 85
Cdd:pfam03629   5 FLL--AGQSN-MA-GRGGvenwdGVVPPECQPPPRILRLNADLEWEEAREPLHA-DI--------DAKKTCG-------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862428  86 hqtqygtVGQALHIARKLLPfIPDNAGILIVPCCRGGSAFTagsegtyserhgashdacRWGTDTPLYQDLVSRTRAALA 165
Cdd:pfam03629  64 -------VGPGMAFANALLR-APPGGVIGLVPCAVGGTSIE------------------EWARGGLLYQEMVRRAKAALK 117
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1314862428 166 KnpqnkflGAC----WMQGEFDLMT-SDYASHPQHFNHMVEAFRRDLKQ 209
Cdd:pfam03629 118 G-------GEIkgilWYQGESDTSDeEDAAAYKEKLEKLITDLRDDLGL 159
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
17-100 4.00e-03

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 38.49  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862428  17 GQSNAMAYGEGLPLPDREDAPHPRIKQLARFAHTHPGGPPCHFNDIIPLTHCPHDVQDMQGYHHPLAtnHQTQYGTVGQA 96
Cdd:cd22056   191 EQSCMMAAGGGGFMGQQKPKHQMHSVHPQAFTHHQAAGPGALQGRGGRGGPDCHLLHSSHHHHHHHH--LQYQYMNAPYP 268

                  ....
gi 1314862428  97 LHIA 100
Cdd:cd22056   269 PHYA 272
 
Name Accession Description Interval E-value
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
11-209 3.74e-15

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: 73.39  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862428  11 YVLtvAGQSNaMAyGEGL-----PLPDREDAPHPRIKQLARFAHTHPGGPPCHFnDIiplthcphDVQDMQGyhhplatn 85
Cdd:pfam03629   5 FLL--AGQSN-MA-GRGGvenwdGVVPPECQPPPRILRLNADLEWEEAREPLHA-DI--------DAKKTCG-------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862428  86 hqtqygtVGQALHIARKLLPfIPDNAGILIVPCCRGGSAFTagsegtyserhgashdacRWGTDTPLYQDLVSRTRAALA 165
Cdd:pfam03629  64 -------VGPGMAFANALLR-APPGGVIGLVPCAVGGTSIE------------------EWARGGLLYQEMVRRAKAALK 117
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1314862428 166 KnpqnkflGAC----WMQGEFDLMT-SDYASHPQHFNHMVEAFRRDLKQ 209
Cdd:pfam03629 118 G-------GEIkgilWYQGESDTSDeEDAAAYKEKLEKLITDLRDDLGL 159
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
17-100 4.00e-03

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 38.49  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862428  17 GQSNAMAYGEGLPLPDREDAPHPRIKQLARFAHTHPGGPPCHFNDIIPLTHCPHDVQDMQGYHHPLAtnHQTQYGTVGQA 96
Cdd:cd22056   191 EQSCMMAAGGGGFMGQQKPKHQMHSVHPQAFTHHQAAGPGALQGRGGRGGPDCHLLHSSHHHHHHHH--LQYQYMNAPYP 268

                  ....
gi 1314862428  97 LHIA 100
Cdd:cd22056   269 PHYA 272
 
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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