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Conserved domains on  [gi|1844872245|ref|WP_171577298|]
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MULTISPECIES: cysteine protease LapG [Pseudomonas]

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, ...
56-234 4.07e-77

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


:

Pssm-ID: 442889  Cd Length: 197  Bit Score: 231.44  E-value: 4.07e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844872245  56 DFSQISRKSQALYGPL-------GAGQGRIDAWQNLMATQKqgtELERLQVVNRFFNQQLRYVEDIDLWHEVDYWATPVQ 128
Cdd:COG3672    17 QFAATGGATSAPYGHYefckrypAECAVRVREWRLVELTLD---EWAKLRAVNRFVNRRIRPVTDIDHWGVEDYWATPLE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844872245 129 ALIKGAGDCEDYAIAKYFSLRRMGIPSEKLRITYVKALRQNRAHMVLTYYssPQAQPLVLDSLMDAIKPASQRTDLLPVY 208
Cdd:COG3672    94 FLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQGHAVLTVR--TDAGDLVLDNLTDAILPWSQRYDLLPRQ 171
                         170       180
                  ....*....|....*....|....*.
gi 1844872245 209 AFNGEGLWLTGAAGNKKVGDTKRLSR 234
Cdd:COG3672   172 SFNGPGLWVSIGRGRGSLVGSVRMRA 197
 
Name Accession Description Interval E-value
COG3672 COG3672
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
56-234 4.07e-77

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


Pssm-ID: 442889  Cd Length: 197  Bit Score: 231.44  E-value: 4.07e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844872245  56 DFSQISRKSQALYGPL-------GAGQGRIDAWQNLMATQKqgtELERLQVVNRFFNQQLRYVEDIDLWHEVDYWATPVQ 128
Cdd:COG3672    17 QFAATGGATSAPYGHYefckrypAECAVRVREWRLVELTLD---EWAKLRAVNRFVNRRIRPVTDIDHWGVEDYWATPLE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844872245 129 ALIKGAGDCEDYAIAKYFSLRRMGIPSEKLRITYVKALRQNRAHMVLTYYssPQAQPLVLDSLMDAIKPASQRTDLLPVY 208
Cdd:COG3672    94 FLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQGHAVLTVR--TDAGDLVLDNLTDAILPWSQRYDLLPRQ 171
                         170       180
                  ....*....|....*....|....*.
gi 1844872245 209 AFNGEGLWLTGAAGNKKVGDTKRLSR 234
Cdd:COG3672   172 SFNGPGLWVSIGRGRGSLVGSVRMRA 197
Peptidase_C93 pfam06035
Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are ...
94-200 3.22e-17

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: 76.09  E-value: 3.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844872245  94 LERLQVVNRFFNQQLRYVEDIDLWHEVDYWATPVqaliKGAGDCEDYAIAKYFSLRRMGIPSEKLRITYVKAlRQNRAHM 173
Cdd:pfam06035  39 WKELVEVNRSVNRTIKPMTDMEHYGVEERWTYPT----DGAGDCEDYALLKRKRLIEAGWPRSALLLTVVRD-PNGEGHA 113
                          90       100
                  ....*....|....*....|....*..
gi 1844872245 174 VLTYYSSpqAQPLVLDSLMDAIKPASQ 200
Cdd:pfam06035 114 VLTVRTD--RGDFILDNLTDEVLLWSD 138
 
Name Accession Description Interval E-value
COG3672 COG3672
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
56-234 4.07e-77

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


Pssm-ID: 442889  Cd Length: 197  Bit Score: 231.44  E-value: 4.07e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844872245  56 DFSQISRKSQALYGPL-------GAGQGRIDAWQNLMATQKqgtELERLQVVNRFFNQQLRYVEDIDLWHEVDYWATPVQ 128
Cdd:COG3672    17 QFAATGGATSAPYGHYefckrypAECAVRVREWRLVELTLD---EWAKLRAVNRFVNRRIRPVTDIDHWGVEDYWATPLE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844872245 129 ALIKGAGDCEDYAIAKYFSLRRMGIPSEKLRITYVKALRQNRAHMVLTYYssPQAQPLVLDSLMDAIKPASQRTDLLPVY 208
Cdd:COG3672    94 FLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQGHAVLTVR--TDAGDLVLDNLTDAILPWSQRYDLLPRQ 171
                         170       180
                  ....*....|....*....|....*.
gi 1844872245 209 AFNGEGLWLTGAAGNKKVGDTKRLSR 234
Cdd:COG3672   172 SFNGPGLWVSIGRGRGSLVGSVRMRA 197
Peptidase_C93 pfam06035
Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are ...
94-200 3.22e-17

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: 76.09  E-value: 3.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844872245  94 LERLQVVNRFFNQQLRYVEDIDLWHEVDYWATPVqaliKGAGDCEDYAIAKYFSLRRMGIPSEKLRITYVKAlRQNRAHM 173
Cdd:pfam06035  39 WKELVEVNRSVNRTIKPMTDMEHYGVEERWTYPT----DGAGDCEDYALLKRKRLIEAGWPRSALLLTVVRD-PNGEGHA 113
                          90       100
                  ....*....|....*....|....*..
gi 1844872245 174 VLTYYSSpqAQPLVLDSLMDAIKPASQ 200
Cdd:pfam06035 114 VLTVRTD--RGDFILDNLTDEVLLWSD 138
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
87-155 8.71e-06

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 45.00  E-value: 8.71e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844872245  87 TQKQGTELERLQVVNRFFNQQLRYVEDIDlwhevDYWATPVQALIKGAGDCEDYAIAKYFSLRRMGIPS 155
Cdd:COG1305    71 TGGATTPYEKARALYDWVRDNIRYDPGST-----GVGTTALETLERRRGVCRDFAHLLVALLRALGIPA 134
 
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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