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Conserved domains on  [gi|15832533|ref|NP_311306|]
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hypothetical protein ECs_3279 [Escherichia coli O157:H7 str. Sakai]

Protein Classification

Ntn hydrolase family protein( domain architecture ID 307)

Ntn (N-terminal nucleophile) hydrolase family protein is activated autocatalytically via an N-terminally located nucleophilic amino acid, and may catalyze the hydrolysis of amide bonds in either protein or small molecule substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ntn_hydrolase super family cl00467
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
19-72 6.18e-03

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


The actual alignment was detected with superfamily member cd01912:

Pssm-ID: 469781  Cd Length: 189  Bit Score: 34.34  E-value: 6.18e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15832533  19 RASQGSDVASqiaRISQQIIKLTQHIkeIVDTSGSAEDKQKQAELIQQQITLLE 72
Cdd:cd01912  19 RASAGSLVAS---RNFDKIFKISDNI--LLGTAGSAADTQALTRLLKRNLRLYE 67
 
Name Accession Description Interval E-value
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
19-72 6.18e-03

proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 238893  Cd Length: 189  Bit Score: 34.34  E-value: 6.18e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15832533  19 RASQGSDVASqiaRISQQIIKLTQHIkeIVDTSGSAEDKQKQAELIQQQITLLE 72
Cdd:cd01912  19 RASAGSLVAS---RNFDKIFKISDNI--LLGTAGSAADTQALTRLLKRNLRLYE 67
FlxA pfam14282
FlxA-like protein; This family includes FlxA from E. coli. The expression of FlxA is regulated ...
12-92 7.96e-03

FlxA-like protein; This family includes FlxA from E. coli. The expression of FlxA is regulated by the FliA sigma factor, a transcription factor specific for class 3 flagellar operons. However FlxA is not required for flagellar function or formation.


Pssm-ID: 433836 [Multi-domain]  Cd Length: 101  Bit Score: 33.15  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832533    12 IQTQSSNRASQGSDVASQIARISQQIIKLTQHIKEIVDTSG-SAEDKQKQAELIQQQITLLETQLAQLQRQQAEKAQEKE 90
Cdd:pfam14282   1 SSSSSASSATSSSGSASQIASLQKQIKNLTKQLKELSNSDEmTKEEKKQQQQLIQAQIQQLQAQIAQLQSQQAQKAQESQ 80

                  ..
gi 15832533    91 QR 92
Cdd:pfam14282  81 QS 82
 
Name Accession Description Interval E-value
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
19-72 6.18e-03

proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 238893  Cd Length: 189  Bit Score: 34.34  E-value: 6.18e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15832533  19 RASQGSDVASqiaRISQQIIKLTQHIkeIVDTSGSAEDKQKQAELIQQQITLLE 72
Cdd:cd01912  19 RASAGSLVAS---RNFDKIFKISDNI--LLGTAGSAADTQALTRLLKRNLRLYE 67
FlxA pfam14282
FlxA-like protein; This family includes FlxA from E. coli. The expression of FlxA is regulated ...
12-92 7.96e-03

FlxA-like protein; This family includes FlxA from E. coli. The expression of FlxA is regulated by the FliA sigma factor, a transcription factor specific for class 3 flagellar operons. However FlxA is not required for flagellar function or formation.


Pssm-ID: 433836 [Multi-domain]  Cd Length: 101  Bit Score: 33.15  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832533    12 IQTQSSNRASQGSDVASQIARISQQIIKLTQHIKEIVDTSG-SAEDKQKQAELIQQQITLLETQLAQLQRQQAEKAQEKE 90
Cdd:pfam14282   1 SSSSSASSATSSSGSASQIASLQKQIKNLTKQLKELSNSDEmTKEEKKQQQQLIQAQIQQLQAQIAQLQSQQAQKAQESQ 80

                  ..
gi 15832533    91 QR 92
Cdd:pfam14282  81 QS 82
 
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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