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Conserved domains on  [gi|567930680|ref|WP_024033060|]
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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, ...
 32-220 1.12e-64

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


:

Pssm-ID: 442889  Cd Length: 197  Bit Score: 199.47  E-value: 1.12e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930680  32 GVFASRLTIQFNTFIELMGQKYGPAR---------VTVARNWQTMlvrTQNKPEQQQILIVNDFFARNLRYQTDIQLWKQ 102
Cdd:COG3672    8 GLAAAAAAAQFAATGGATSAPYGHYEfckrypaecAVRVREWRLV---ELTLDEWAKLRAVNRFVNRRIRPVTDIDHWGV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930680 103 NDYWATPLETLGRGLGDCEDYAIAKYISLRALGVSDDKLRLIYVKAklagTNKTQAHMVLGYFATpnAQPLILDSLITKV 182
Cdd:COG3672   85 EDYWATPLEFLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRD----LPLGQGHAVLTVRTD--AGDLVLDNLTDAI 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 567930680 183 LPAAKRVDLSPVFSFNSQGLW-ANNSTKSVASPTARLSR 220
Cdd:COG3672  159 LPWSQRYDLLPRQSFNGPGLWvSIGRGRGSLVGSVRMRA 197
 
Name Accession Description Interval E-value
COG3672 COG3672
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
 32-220 1.12e-64

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


Pssm-ID: 442889  Cd Length: 197  Bit Score: 199.47  E-value: 1.12e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930680  32 GVFASRLTIQFNTFIELMGQKYGPAR---------VTVARNWQTMlvrTQNKPEQQQILIVNDFFARNLRYQTDIQLWKQ 102
Cdd:COG3672    8 GLAAAAAAAQFAATGGATSAPYGHYEfckrypaecAVRVREWRLV---ELTLDEWAKLRAVNRFVNRRIRPVTDIDHWGV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930680 103 NDYWATPLETLGRGLGDCEDYAIAKYISLRALGVSDDKLRLIYVKAklagTNKTQAHMVLGYFATpnAQPLILDSLITKV 182
Cdd:COG3672   85 EDYWATPLEFLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRD----LPLGQGHAVLTVRTD--AGDLVLDNLTDAI 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 567930680 183 LPAAKRVDLSPVFSFNSQGLW-ANNSTKSVASPTARLSR 220
Cdd:COG3672  159 LPWSQRYDLLPRQSFNGPGLWvSIGRGRGSLVGSVRMRA 197
Peptidase_C93 pfam06035
Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are ...
 78-184 9.59e-08

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: 49.89  E-value: 9.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930680   78 QQILIVNDFFARNLRYQTDIQLWKQNDYWATPletlGRGLGDCEDYAIAKYISLRALGVSDDKLRLIYVKaklagTNKTQ 157
Cdd:pfam06035  40 KELVEVNRSVNRTIKPMTDMEHYGVEERWTYP----TDGAGDCEDYALLKRKRLIEAGWPRSALLLTVVR-----DPNGE 110

                          90       100       110
                  ....*....|....*....|....*....|...
gi 567930680  158 AHMVL------GYFatpnaqplILDSLITKVLP 184
Cdd:pfam06035 111 GHAVLtvrtdrGDF--------ILDNLTDEVLL 135
 
Name Accession Description Interval E-value
COG3672 COG3672
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
 32-220 1.12e-64

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


Pssm-ID: 442889  Cd Length: 197  Bit Score: 199.47  E-value: 1.12e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930680  32 GVFASRLTIQFNTFIELMGQKYGPAR---------VTVARNWQTMlvrTQNKPEQQQILIVNDFFARNLRYQTDIQLWKQ 102
Cdd:COG3672    8 GLAAAAAAAQFAATGGATSAPYGHYEfckrypaecAVRVREWRLV---ELTLDEWAKLRAVNRFVNRRIRPVTDIDHWGV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930680 103 NDYWATPLETLGRGLGDCEDYAIAKYISLRALGVSDDKLRLIYVKAklagTNKTQAHMVLGYFATpnAQPLILDSLITKV 182
Cdd:COG3672   85 EDYWATPLEFLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRD----LPLGQGHAVLTVRTD--AGDLVLDNLTDAI 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 567930680 183 LPAAKRVDLSPVFSFNSQGLW-ANNSTKSVASPTARLSR 220
Cdd:COG3672  159 LPWSQRYDLLPRQSFNGPGLWvSIGRGRGSLVGSVRMRA 197
Peptidase_C93 pfam06035
Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are ...
 78-184 9.59e-08

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: 49.89  E-value: 9.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567930680   78 QQILIVNDFFARNLRYQTDIQLWKQNDYWATPletlGRGLGDCEDYAIAKYISLRALGVSDDKLRLIYVKaklagTNKTQ 157
Cdd:pfam06035  40 KELVEVNRSVNRTIKPMTDMEHYGVEERWTYP----TDGAGDCEDYALLKRKRLIEAGWPRSALLLTVVR-----DPNGE 110

                          90       100       110
                  ....*....|....*....|....*....|...
gi 567930680  158 AHMVL------GYFatpnaqplILDSLITKVLP 184
Cdd:pfam06035 111 GHAVLtvrtdrGDF--------ILDNLTDEVLL 135
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 69-136 6.21e-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: 6.21e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567930680  69 VRTQNKPEQQQILIVNDFFARNLRYQTDIqlwkqNDYWATPLETLGRGLGDCEDYAIAkYIS-LRALGV 136
Cdd:COG1305   70 LTGGATTPYEKARALYDWVRDNIRYDPGS-----TGVGTTALETLERRRGVCRDFAHL-LVAlLRALGI 132
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 74-136 1.89e-03

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 37.00  E-value: 1.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567930680   74 KPEQQQILIVNDFFARNLRYQTDIQLWKQNDywatPLETLGRGLGDCEDYAIAKYISLRALGV 136
Cdd:pfam01841  12 TDPLEKARAIYDYVRKNITYDLPGRSPGDGD----AEEFLFTGKGDCEDFASLFVALLRALGI 70
 
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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