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Conserved domains on  [gi|1777435572|pdb|6IST|C]
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Chain C, Lysin

Protein Classification

CHAP domain-containing protein( domain architecture ID 10526148)

cysteine, histidine-dependent amidohydrolase/peptidase (CHAP) domain-containing protein may function as an amidase involved in the cleavage of peptidoglycans

CATH:  3.90.1720.10
Gene Ontology:  GO:0042834|GO:0004040
PubMed:  12765834

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 20-110 1.06e-05

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


:

Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 42.41  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6IST_C         20 DADGWYGTQCMDLTVDVMQRFFGWrpYGNAIALVDQPlpagfQRIRTTSSTQIKAGDVMIWGLG-YYAQYGHTGIATEDg 98
Cdd:pfam05257   1 YGNGYPWGQCTWFVYWRVAQLGIY--LGNAGDWADAA-----AGAYKVGSTTPKVGDIVVFDPGgGGASYGHVAIVEKV- 72

                          90
                  ....*....|..
6IST_C         99 rADGTFVSVDQN 110
Cdd:pfam05257  73 -NDGSITVSEQN 83
 
Name Accession Description Interval E-value
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 20-110 1.06e-05

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 42.41  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6IST_C         20 DADGWYGTQCMDLTVDVMQRFFGWrpYGNAIALVDQPlpagfQRIRTTSSTQIKAGDVMIWGLG-YYAQYGHTGIATEDg 98
Cdd:pfam05257   1 YGNGYPWGQCTWFVYWRVAQLGIY--LGNAGDWADAA-----AGAYKVGSTTPKVGDIVVFDPGgGGASYGHVAIVEKV- 72

                          90
                  ....*....|..
6IST_C         99 rADGTFVSVDQN 110
Cdd:pfam05257  73 -NDGSITVSEQN 83
 
Name Accession Description Interval E-value
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 20-110 1.06e-05

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 42.41  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6IST_C         20 DADGWYGTQCMDLTVDVMQRFFGWrpYGNAIALVDQPlpagfQRIRTTSSTQIKAGDVMIWGLG-YYAQYGHTGIATEDg 98
Cdd:pfam05257   1 YGNGYPWGQCTWFVYWRVAQLGIY--LGNAGDWADAA-----AGAYKVGSTTPKVGDIVVFDPGgGGASYGHVAIVEKV- 72

                          90
                  ....*....|..
6IST_C         99 rADGTFVSVDQN 110
Cdd:pfam05257  73 -NDGSITVSEQN 83
 
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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