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Conserved domains on  [gi|695730357|ref|WP_032656897|]
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MULTISPECIES: L-2-amino-thiazoline-4-carboxylic acid hydrolase [Enterobacter]

Protein Classification

L-2-amino-thiazoline-4-carboxylic acid hydrolase( domain architecture ID 10624570)

L-2-amino-thiazoline-4-carboxylic acid (L-ATC) hydrolase catalyzes the conversion of L-ATC to o N-carbamoyl-L-cysteine by cleaving the carbon-sulfur bond in the ring structure of L-ATC

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATC_hydrolase pfam14196
L-2-amino-thiazoline-4-carboxylic acid hydrolase; This family of enzymes catalyzes the ...
 12-153 6.24e-48

L-2-amino-thiazoline-4-carboxylic acid hydrolase; This family of enzymes catalyzes the conversion of L-2-amino-delta2-thiazoline-4-carboxylic acid (L-ATC) to N-carbamoyl-L-cysteine. It cleaves the carbon-sulphur bond in the ring structure of L-ATC to produce N-carbamoyl-L-cysteine.


:

Pssm-ID: 464100  Cd Length: 145  Bit Score: 152.15  E-value: 6.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695730357   12 RRKIEAEIIKPIYEILVREIGKTRAQAVIGEAIEQAAIDAGKAFASKEPNGADVKSFIAL----QYLWEKDNALDVKVID 87
Cdd:pfam14196   1 RRLLEARALIALYDALRKEIGPEEAKAIIRKALERLGRERGKKLAKKLGDKGDKADLEKFlalySEIFKKGNAWGFEVLP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695730357   88 ADDQQYNYNVTRCRYAEMYHEMGLGEIGHLLsCARDEKFIVGYAPDVKLTRTTTIMQGGSCCDFRY 153
Cdd:pfam14196  81 DDKDELEIDFTRCPYCEAWRKLGCPELGPLL-CDIDYAFYEGINPKLKLTRTKTLAEGGDCCDFRF 145
 
Name Accession Description Interval E-value
ATC_hydrolase pfam14196
L-2-amino-thiazoline-4-carboxylic acid hydrolase; This family of enzymes catalyzes the ...
 12-153 6.24e-48

L-2-amino-thiazoline-4-carboxylic acid hydrolase; This family of enzymes catalyzes the conversion of L-2-amino-delta2-thiazoline-4-carboxylic acid (L-ATC) to N-carbamoyl-L-cysteine. It cleaves the carbon-sulphur bond in the ring structure of L-ATC to produce N-carbamoyl-L-cysteine.


Pssm-ID: 464100  Cd Length: 145  Bit Score: 152.15  E-value: 6.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695730357   12 RRKIEAEIIKPIYEILVREIGKTRAQAVIGEAIEQAAIDAGKAFASKEPNGADVKSFIAL----QYLWEKDNALDVKVID 87
Cdd:pfam14196   1 RRLLEARALIALYDALRKEIGPEEAKAIIRKALERLGRERGKKLAKKLGDKGDKADLEKFlalySEIFKKGNAWGFEVLP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695730357   88 ADDQQYNYNVTRCRYAEMYHEMGLGEIGHLLsCARDEKFIVGYAPDVKLTRTTTIMQGGSCCDFRY 153
Cdd:pfam14196  81 DDKDELEIDFTRCPYCEAWRKLGCPELGPLL-CDIDYAFYEGINPKLKLTRTKTLAEGGDCCDFRF 145
 
Name Accession Description Interval E-value
ATC_hydrolase pfam14196
L-2-amino-thiazoline-4-carboxylic acid hydrolase; This family of enzymes catalyzes the ...
 12-153 6.24e-48

L-2-amino-thiazoline-4-carboxylic acid hydrolase; This family of enzymes catalyzes the conversion of L-2-amino-delta2-thiazoline-4-carboxylic acid (L-ATC) to N-carbamoyl-L-cysteine. It cleaves the carbon-sulphur bond in the ring structure of L-ATC to produce N-carbamoyl-L-cysteine.


Pssm-ID: 464100  Cd Length: 145  Bit Score: 152.15  E-value: 6.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695730357   12 RRKIEAEIIKPIYEILVREIGKTRAQAVIGEAIEQAAIDAGKAFASKEPNGADVKSFIAL----QYLWEKDNALDVKVID 87
Cdd:pfam14196   1 RRLLEARALIALYDALRKEIGPEEAKAIIRKALERLGRERGKKLAKKLGDKGDKADLEKFlalySEIFKKGNAWGFEVLP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695730357   88 ADDQQYNYNVTRCRYAEMYHEMGLGEIGHLLsCARDEKFIVGYAPDVKLTRTTTIMQGGSCCDFRY 153
Cdd:pfam14196  81 DDKDELEIDFTRCPYCEAWRKLGCPELGPLL-CDIDYAFYEGINPKLKLTRTKTLAEGGDCCDFRF 145
 
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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