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Conserved domains on  [gi|1543101396|ref|WP_126006642|]
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MULTISPECIES: transglutaminase-like cysteine peptidase [Pseudoalteromonas]

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, ...
7-198 1.11e-71

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


:

Pssm-ID: 442889  Cd Length: 197  Bit Score: 216.42  E-value: 1.11e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543101396   7 LVLIVSFFVCAQDMLLYLRNSDIIARAE--QQYGGSGHNRIKNWlTFIDDSADksEWQKIHLVNDFFNKNIKYKSDDELW 84
Cdd:COG3672     6 LLGLAAAAAAAQFAATGGATSAPYGHYEfcKRYPAECAVRVREW-RLVELTLD--EWAKLRAVNRFVNRRIRPVTDIDHW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543101396  85 QKKDYWATPLESLGVGMGDCEDYVIAKYFTLIALGLPEEKIRLMYVRQKTVNQPHMVLIYieQPNQVPYVLGNFNTKLLP 164
Cdd:COG3672    83 GVEDYWATPLEFLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQGHAVLTV--RTDAGDLVLDNLTDAILP 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1543101396 165 ATQRPDLTPIYSFNGQGLWLAKSKGLGNKVKNSR 198
Cdd:COG3672   161 WSQRYDLLPRQSFNGPGLWVSIGRGRGSLVGSVR 194
 
Name Accession Description Interval E-value
COG3672 COG3672
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
7-198 1.11e-71

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


Pssm-ID: 442889  Cd Length: 197  Bit Score: 216.42  E-value: 1.11e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543101396   7 LVLIVSFFVCAQDMLLYLRNSDIIARAE--QQYGGSGHNRIKNWlTFIDDSADksEWQKIHLVNDFFNKNIKYKSDDELW 84
Cdd:COG3672     6 LLGLAAAAAAAQFAATGGATSAPYGHYEfcKRYPAECAVRVREW-RLVELTLD--EWAKLRAVNRFVNRRIRPVTDIDHW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543101396  85 QKKDYWATPLESLGVGMGDCEDYVIAKYFTLIALGLPEEKIRLMYVRQKTVNQPHMVLIYieQPNQVPYVLGNFNTKLLP 164
Cdd:COG3672    83 GVEDYWATPLEFLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQGHAVLTV--RTDAGDLVLDNLTDAILP 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1543101396 165 ATQRPDLTPIYSFNGQGLWLAKSKGLGNKVKNSR 198
Cdd:COG3672   161 WSQRYDLLPRQSFNGPGLWVSIGRGRGSLVGSVR 194
Peptidase_C93 pfam06035
Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are ...
32-142 2.11e-16

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: 73.39  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543101396  32 RAEQQYGGSGHNRIKnwLTfiddsadKSEWQKIHLVNDFFNKNIKYKSDDELWQKKDYWATPleslGVGMGDCEDYVIAK 111
Cdd:pfam06035  19 PAECAARSAEPGPVK--LT-------PDRWKELVEVNRSVNRTIKPMTDMEHYGVEERWTYP----TDGAGDCEDYALLK 85
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1543101396 112 YFTLIALGLPEEKIRLMYVRQKTvNQPHMVL 142
Cdd:pfam06035  86 RKRLIEAGWPRSALLLTVVRDPN-GEGHAVL 115
 
Name Accession Description Interval E-value
COG3672 COG3672
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
7-198 1.11e-71

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


Pssm-ID: 442889  Cd Length: 197  Bit Score: 216.42  E-value: 1.11e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543101396   7 LVLIVSFFVCAQDMLLYLRNSDIIARAE--QQYGGSGHNRIKNWlTFIDDSADksEWQKIHLVNDFFNKNIKYKSDDELW 84
Cdd:COG3672     6 LLGLAAAAAAAQFAATGGATSAPYGHYEfcKRYPAECAVRVREW-RLVELTLD--EWAKLRAVNRFVNRRIRPVTDIDHW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543101396  85 QKKDYWATPLESLGVGMGDCEDYVIAKYFTLIALGLPEEKIRLMYVRQKTVNQPHMVLIYieQPNQVPYVLGNFNTKLLP 164
Cdd:COG3672    83 GVEDYWATPLEFLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQGHAVLTV--RTDAGDLVLDNLTDAILP 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1543101396 165 ATQRPDLTPIYSFNGQGLWLAKSKGLGNKVKNSR 198
Cdd:COG3672   161 WSQRYDLLPRQSFNGPGLWVSIGRGRGSLVGSVR 194
Peptidase_C93 pfam06035
Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are ...
32-142 2.11e-16

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: 73.39  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543101396  32 RAEQQYGGSGHNRIKnwLTfiddsadKSEWQKIHLVNDFFNKNIKYKSDDELWQKKDYWATPleslGVGMGDCEDYVIAK 111
Cdd:pfam06035  19 PAECAARSAEPGPVK--LT-------PDRWKELVEVNRSVNRTIKPMTDMEHYGVEERWTYP----TDGAGDCEDYALLK 85
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1543101396 112 YFTLIALGLPEEKIRLMYVRQKTvNQPHMVL 142
Cdd:pfam06035  86 RKRLIEAGWPRSALLLTVVRDPN-GEGHAVL 115
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
58-121 5.43e-04

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 39.22  E-value: 5.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1543101396  58 KSEWQKIHLVNDFFNKNIKYKSDDElwqkkDYWATPLESLGVGMGDCEDYVIAkyftLIAL----GLP 121
Cdd:COG1305    75 TTPYEKARALYDWVRDNIRYDPGST-----GVGTTALETLERRRGVCRDFAHL----LVALlralGIP 133
 
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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