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Conserved domains on  [gi|15598010|ref|NP_251504|]
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hypothetical protein PA2814 [Pseudomonas aeruginosa PAO1]

Protein Classification

transglutaminase-like domain-containing protein( domain architecture ID 11441893)

transglutaminase-like domain-containing protein may act as a cysteine protease

CATH:  3.10.620.30
PubMed:  10452618|15288868

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 2-137 2.63e-17

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


:

Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 76.20  E-value: 2.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598010   2 QSYLQSGRFVDSDHPVVVEFAEKSRGNSAKPRDQAVALYYAVRDGVRYNPYVfsrDPQTLKASHALQQGESYCVPKAILL 81
Cdd:COG1305  47 LLAGPGELLSASYDPELRALAAELTGGATTPYEKARALYDWVRDNIRYDPGS---TGVGTTALETLERRRGVCRDFAHLL 123

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598010  82 AACARHCRIPARIGLADVRNHlATPRLLEAlrsevFAMHGYTELYLEGR-WVKATPA 137
Cdd:COG1305 124 VALLRALGIPARYVSGYLPGE-PPPGGGRA-----DDAHAWVEVYLPGAgWVPFDPT 174
 
Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 2-137 2.63e-17

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 76.20  E-value: 2.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598010   2 QSYLQSGRFVDSDHPVVVEFAEKSRGNSAKPRDQAVALYYAVRDGVRYNPYVfsrDPQTLKASHALQQGESYCVPKAILL 81
Cdd:COG1305  47 LLAGPGELLSASYDPELRALAAELTGGATTPYEKARALYDWVRDNIRYDPGS---TGVGTTALETLERRRGVCRDFAHLL 123

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598010  82 AACARHCRIPARIGLADVRNHlATPRLLEAlrsevFAMHGYTELYLEGR-WVKATPA 137
Cdd:COG1305 124 VALLRALGIPARYVSGYLPGE-PPPGGGRA-----DDAHAWVEVYLPGAgWVPFDPT 174
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 20-136 2.61e-14

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: 66.66  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598010    20 EFAEKSRGNSAKPRDQAVALYYAVRDGVRYNPYVfsRDPQTLKASHALQQGESYCVPKAILLAACARHCRIPARIGLADV 99
Cdd:pfam01841   2 ALADRITGGATDPLEKARAIYDYVRKNITYDLPG--RSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYL 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15598010   100 RNHlatprlleaLRSEVFAMHGYTELYLEG-RWVKATP 136
Cdd:pfam01841  80 RGP---------DTVRGGDAHAWVEVYLPGyGWVPVDP 108
 
Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 2-137 2.63e-17

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 76.20  E-value: 2.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598010   2 QSYLQSGRFVDSDHPVVVEFAEKSRGNSAKPRDQAVALYYAVRDGVRYNPYVfsrDPQTLKASHALQQGESYCVPKAILL 81
Cdd:COG1305  47 LLAGPGELLSASYDPELRALAAELTGGATTPYEKARALYDWVRDNIRYDPGS---TGVGTTALETLERRRGVCRDFAHLL 123

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598010  82 AACARHCRIPARIGLADVRNHlATPRLLEAlrsevFAMHGYTELYLEGR-WVKATPA 137
Cdd:COG1305 124 VALLRALGIPARYVSGYLPGE-PPPGGGRA-----DDAHAWVEVYLPGAgWVPFDPT 174
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 20-136 2.61e-14

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: 66.66  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598010    20 EFAEKSRGNSAKPRDQAVALYYAVRDGVRYNPYVfsRDPQTLKASHALQQGESYCVPKAILLAACARHCRIPARIGLADV 99
Cdd:pfam01841   2 ALADRITGGATDPLEKARAIYDYVRKNITYDLPG--RSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYL 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15598010   100 RNHlatprlleaLRSEVFAMHGYTELYLEG-RWVKATP 136
Cdd:pfam01841  80 RGP---------DTVRGGDAHAWVEVYLPGyGWVPVDP 108
 
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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