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Conserved domains on  [gi|2165618043|ref|WP_231984758|]
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cysteine protease LapG [Pseudomonas libanensis]

Protein Classification

transglutaminase-like cysteine peptidase( domain architecture ID 10007820)

transglutaminase-like cysteine peptidase contains an invariant Cys-His-Asp catalytic triad and is predicted to possess a papain-like cysteine proteinase fold and to catalyze post-translational protein modification through transamidase, acetylase or hydrolase activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3672 COG3672
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
10-188 1.42e-75

Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 442889  Cd Length: 197  Bit Score: 225.66  E-value: 1.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165618043  10 DFSQISREATAVYGPL-------GQGQQRIDAWQRLLATEkqvSESEQLKVVNLFFNKQMTYVEDIDLWHVIDYWETPVE 82
Cdd:COG3672    17 QFAATGGATSAPYGHYefckrypAECAVRVREWRLVELTL---DEWAKLRAVNRFVNRRIRPVTDIDHWGVEDYWATPLE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165618043  83 ALWKGAGDCEDYAIAKYFSLRHLGVSSEKLRITYVKALRQNRAHMVLTYYstPDAIPLVLDSLMDEILPATRRTDLVPVY 162
Cdd:COG3672    94 FLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQGHAVLTVR--TDAGDLVLDNLTDAILPWSQRYDLLPRQ 171
                         170       180
                  ....*....|....*....|....*.
gi 2165618043 163 SFNAEGLYLPGAKGNKKVGDTKRLSR 188
Cdd:COG3672   172 SFNGPGLWVSIGRGRGSLVGSVRMRA 197
 
Name Accession Description Interval E-value
COG3672 COG3672
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
10-188 1.42e-75

Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442889  Cd Length: 197  Bit Score: 225.66  E-value: 1.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165618043  10 DFSQISREATAVYGPL-------GQGQQRIDAWQRLLATEkqvSESEQLKVVNLFFNKQMTYVEDIDLWHVIDYWETPVE 82
Cdd:COG3672    17 QFAATGGATSAPYGHYefckrypAECAVRVREWRLVELTL---DEWAKLRAVNRFVNRRIRPVTDIDHWGVEDYWATPLE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165618043  83 ALWKGAGDCEDYAIAKYFSLRHLGVSSEKLRITYVKALRQNRAHMVLTYYstPDAIPLVLDSLMDEILPATRRTDLVPVY 162
Cdd:COG3672    94 FLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQGHAVLTVR--TDAGDLVLDNLTDAILPWSQRYDLLPRQ 171
                         170       180
                  ....*....|....*....|....*.
gi 2165618043 163 SFNAEGLYLPGAKGNKKVGDTKRLSR 188
Cdd:COG3672   172 SFNGPGLWVSIGRGRGSLVGSVRMRA 197
Peptidase_C93 pfam06035
Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are ...
50-151 1.90e-15

Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are predicted to be bacterial transglutaminase-like cysteine proteinases. They contain a conserved Cys-His-Asp catalytic triad. Their structure is predicted to be similar to that of Salmonella typhimurium N-hydroxyarylamine O-acetyltransferase in pfam00797, however they lack the sub-domain which is important for arylamine recognition.


Pssm-ID: 428732  Cd Length: 161  Bit Score: 70.31  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165618043  50 QLKVVNLFFNKQMTYVEDIDLWHVIDYWETPVealwKGAGDCEDYAIAKYFSLRHLGVSSEKLRITYVKAlRQNRAHMVL 129
Cdd:pfam06035  41 ELVEVNRSVNRTIKPMTDMEHYGVEERWTYPT----DGAGDCEDYALLKRKRLIEAGWPRSALLLTVVRD-PNGEGHAVL 115
                          90       100
                  ....*....|....*....|..
gi 2165618043 130 TyYSTpDAIPLVLDSLMDEILP 151
Cdd:pfam06035 116 T-VRT-DRGDFILDNLTDEVLL 135
 
Name Accession Description Interval E-value
COG3672 COG3672
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
10-188 1.42e-75

Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442889  Cd Length: 197  Bit Score: 225.66  E-value: 1.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165618043  10 DFSQISREATAVYGPL-------GQGQQRIDAWQRLLATEkqvSESEQLKVVNLFFNKQMTYVEDIDLWHVIDYWETPVE 82
Cdd:COG3672    17 QFAATGGATSAPYGHYefckrypAECAVRVREWRLVELTL---DEWAKLRAVNRFVNRRIRPVTDIDHWGVEDYWATPLE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165618043  83 ALWKGAGDCEDYAIAKYFSLRHLGVSSEKLRITYVKALRQNRAHMVLTYYstPDAIPLVLDSLMDEILPATRRTDLVPVY 162
Cdd:COG3672    94 FLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQGHAVLTVR--TDAGDLVLDNLTDAILPWSQRYDLLPRQ 171
                         170       180
                  ....*....|....*....|....*.
gi 2165618043 163 SFNAEGLYLPGAKGNKKVGDTKRLSR 188
Cdd:COG3672   172 SFNGPGLWVSIGRGRGSLVGSVRMRA 197
Peptidase_C93 pfam06035
Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are ...
50-151 1.90e-15

Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are predicted to be bacterial transglutaminase-like cysteine proteinases. They contain a conserved Cys-His-Asp catalytic triad. Their structure is predicted to be similar to that of Salmonella typhimurium N-hydroxyarylamine O-acetyltransferase in pfam00797, however they lack the sub-domain which is important for arylamine recognition.


Pssm-ID: 428732  Cd Length: 161  Bit Score: 70.31  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165618043  50 QLKVVNLFFNKQMTYVEDIDLWHVIDYWETPVealwKGAGDCEDYAIAKYFSLRHLGVSSEKLRITYVKAlRQNRAHMVL 129
Cdd:pfam06035  41 ELVEVNRSVNRTIKPMTDMEHYGVEERWTYPT----DGAGDCEDYALLKRKRLIEAGWPRSALLLTVVRD-PNGEGHAVL 115
                          90       100
                  ....*....|....*....|..
gi 2165618043 130 TyYSTpDAIPLVLDSLMDEILP 151
Cdd:pfam06035 116 T-VRT-DRGDFILDNLTDEVLL 135
 
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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