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Conserved domains on  [gi|499862294|ref|WP_011543028|]
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transglutaminase-like cysteine peptidase [Sphingopyxis alaskensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3672 super family cl43929
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
177-314 1.93e-45

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


The actual alignment was detected with superfamily member COG3672:

Pssm-ID: 442889  Cd Length: 197  Bit Score: 153.63  E-value: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499862294 177 LSETELLARVNQWVNREIAYVGDDRNYRRRDFWATADETLARGSGDCEDFAILKMQMLRAAGIDANRMKLVLLRDLAANA 256
Cdd:COG3672   56 LDEWAKLRAVNRFVNRRIRPVTDIDHWGVEDYWATPLEFLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQ 135
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499862294 257 DHAFLLVDTGGGKLVLDNVTDRLYDGARPQAVRPVLSFSADRRWVHAYRTAAETPAAT 314
Cdd:COG3672  136 GHAVLTVRTDAGDLVLDNLTDAILPWSQRYDLLPRQSFNGPGLWVSIGRGRGSLVGSV 193
 
Name Accession Description Interval E-value
COG3672 COG3672
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
177-314 1.93e-45

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


Pssm-ID: 442889  Cd Length: 197  Bit Score: 153.63  E-value: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499862294 177 LSETELLARVNQWVNREIAYVGDDRNYRRRDFWATADETLARGSGDCEDFAILKMQMLRAAGIDANRMKLVLLRDLAANA 256
Cdd:COG3672   56 LDEWAKLRAVNRFVNRRIRPVTDIDHWGVEDYWATPLEFLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQ 135
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499862294 257 DHAFLLVDTGGGKLVLDNVTDRLYDGARPQAVRPVLSFSADRRWVHAYRTAAETPAAT 314
Cdd:COG3672  136 GHAVLTVRTDAGDLVLDNLTDAILPWSQRYDLLPRQSFNGPGLWVSIGRGRGSLVGSV 193
Peptidase_C93 pfam06035
Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are ...
182-277 4.62e-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: 77.24  E-value: 4.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499862294  182 LLARVNQWVNREIAYVGDDRNYRRRDFWATADetlaRGSGDCEDFAILKMQMLRAAGIDANRMKLVLLRDlaANAD-HAF 260
Cdd:pfam06035  41 ELVEVNRSVNRTIKPMTDMEHYGVEERWTYPT----DGAGDCEDYALLKRKRLIEAGWPRSALLLTVVRD--PNGEgHAV 114
                          90
                  ....*....|....*..
gi 499862294  261 LLVDTGGGKLVLDNVTD 277
Cdd:pfam06035 115 LTVRTDRGDFILDNLTD 131
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
215-273 1.63e-03

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 36.59  E-value: 1.63e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499862294   215 TLARGSGDCEDFAILKMQMLRAAGIDA------NRMKLVLLRDLAANADHAFLLVDTGGGKLVLD 273
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPArvvsgyLKAPDTIGGLRSIWEAHAWAEVYLEGGWVPVD 65
 
Name Accession Description Interval E-value
COG3672 COG3672
Predicted transglutaminase-like protein [Posttranslational modification, protein turnover, ...
177-314 1.93e-45

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


Pssm-ID: 442889  Cd Length: 197  Bit Score: 153.63  E-value: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499862294 177 LSETELLARVNQWVNREIAYVGDDRNYRRRDFWATADETLARGSGDCEDFAILKMQMLRAAGIDANRMKLVLLRDLAANA 256
Cdd:COG3672   56 LDEWAKLRAVNRFVNRRIRPVTDIDHWGVEDYWATPLEFLGDGAGDCEDYAIAKYFTLIELGVPASALRLTVVRDLPLGQ 135
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499862294 257 DHAFLLVDTGGGKLVLDNVTDRLYDGARPQAVRPVLSFSADRRWVHAYRTAAETPAAT 314
Cdd:COG3672  136 GHAVLTVRTDAGDLVLDNLTDAILPWSQRYDLLPRQSFNGPGLWVSIGRGRGSLVGSV 193
Peptidase_C93 pfam06035
Bacterial transglutaminase-like cysteine proteinase BTLCP; Members of this family are ...
182-277 4.62e-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: 77.24  E-value: 4.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499862294  182 LLARVNQWVNREIAYVGDDRNYRRRDFWATADetlaRGSGDCEDFAILKMQMLRAAGIDANRMKLVLLRDlaANAD-HAF 260
Cdd:pfam06035  41 ELVEVNRSVNRTIKPMTDMEHYGVEERWTYPT----DGAGDCEDYALLKRKRLIEAGWPRSALLLTVVRD--PNGEgHAV 114
                          90
                  ....*....|....*..
gi 499862294  261 LLVDTGGGKLVLDNVTD 277
Cdd:pfam06035 115 LTVRTDRGDFILDNLTD 131
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
181-241 6.26e-10

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 57.71  E-value: 6.26e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499862294 181 ELLARVNQWVNREIAYVgddrnYRRRDFWATADETLARGSGDCEDFAILKMQMLRAAGIDA 241
Cdd:COG1305   79 EKARALYDWVRDNIRYD-----PGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPA 134
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
178-241 1.06e-07

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: 49.71  E-value: 1.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499862294  178 SETELLARVNQWVNREIAYVGDDRNYRRRDfwatADETLARGSGDCEDFAILKMQMLRAAGIDA 241
Cdd:pfam01841  13 DPLEKARAIYDYVRKNITYDLPGRSPGDGD----AEEFLFTGKGDCEDFASLFVALLRALGIPA 72
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
215-273 1.63e-03

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 36.59  E-value: 1.63e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499862294   215 TLARGSGDCEDFAILKMQMLRAAGIDA------NRMKLVLLRDLAANADHAFLLVDTGGGKLVLD 273
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPArvvsgyLKAPDTIGGLRSIWEAHAWAEVYLEGGWVPVD 65
 
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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