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Conserved domains on  [gi|4759230|ref|NP_004236|]
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protein-glutamine gamma-glutamyltransferase 5 isoform 2 [Homo sapiens]

Protein Classification

Transglut_core and Transglut_C domain-containing protein( domain architecture ID 10256589)

protein containing domains Transglut_N, Transglut_core, and Transglut_C

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
538-635 1.80e-29

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 112.44  E-value: 1.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230    538 PSITINVLGAAVVNQPLSIQVIFSNPLSEQVEDCVL-----TVEGSGLFKKQ--QKVFLGVLKPQHQASIILETVPFKSG 610
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLslsaqTVEYNGVLGAEfkKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*
gi 4759230    611 QRQIQANMRSNKFKDIKGYRNVYVD 635
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVA 105
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 188-281 4.10e-25

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: 98.61  E-value: 4.10e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230     188 CQPVRYGQCWVFAAVMCTVMRCLGIPTRVITNFDSGHDTDGNLIIdeyydntgrilgnkkkdtIWNFHVWNECWMArkdl 267
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYLE---- 58

                           90
                   ....*....|....
gi 4759230     268 ppayGGWQVLDATP 281
Cdd:smart00460  59 ----GGWVPVDPTP 68
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
425-524 4.29e-24

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 97.03  E-value: 4.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230    425 VSLKFKLLDPPNMGQDICFVLLALNMSSQF-KDLKVNLSAQSLLHDGSPLSPFWQDTAFITLSPKEAKTYPCKISYSQYS 503
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 4759230    504 QY-----LSTDKLIRISALGEEKSSP 524
Cdd:pfam00927  81 PRqllveFSSDALAKVKGYRNVLVAQ 106
Transglut_N super family cl02994
Transglutaminase family;
11-63 1.14e-19

Transglutaminase family;


The actual alignment was detected with superfamily member pfam00868:

Pssm-ID: 459971  Cd Length: 114  Bit Score: 84.60  E-value: 1.14e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4759230     11 DLQSSRNNVRHHTEEITVDHLLVRRGQAFNLTLYFrNRSFQPGLDNIIFVVET 63
Cdd:pfam00868   4 DLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRF-NRPFDPQLDKLTLEFET 55
 
Name Accession Description Interval E-value
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
538-635 1.80e-29

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 112.44  E-value: 1.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230    538 PSITINVLGAAVVNQPLSIQVIFSNPLSEQVEDCVL-----TVEGSGLFKKQ--QKVFLGVLKPQHQASIILETVPFKSG 610
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLslsaqTVEYNGVLGAEfkKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*
gi 4759230    611 QRQIQANMRSNKFKDIKGYRNVYVD 635
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVA 105
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 188-281 4.10e-25

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: 98.61  E-value: 4.10e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230     188 CQPVRYGQCWVFAAVMCTVMRCLGIPTRVITNFDSGHDTDGNLIIdeyydntgrilgnkkkdtIWNFHVWNECWMArkdl 267
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYLE---- 58

                           90
                   ....*....|....
gi 4759230     268 ppayGGWQVLDATP 281
Cdd:smart00460  59 ----GGWVPVDPTP 68
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
425-524 4.29e-24

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 97.03  E-value: 4.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230    425 VSLKFKLLDPPNMGQDICFVLLALNMSSQF-KDLKVNLSAQSLLHDGSPLSPFWQDTAFITLSPKEAKTYPCKISYSQYS 503
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 4759230    504 QY-----LSTDKLIRISALGEEKSSP 524
Cdd:pfam00927  81 PRqllveFSSDALAKVKGYRNVLVAQ 106
Transglut_N pfam00868
Transglutaminase family;
11-63 1.14e-19

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 84.60  E-value: 1.14e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4759230     11 DLQSSRNNVRHHTEEITVDHLLVRRGQAFNLTLYFrNRSFQPGLDNIIFVVET 63
Cdd:pfam00868   4 DLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRF-NRPFDPQLDKLTLEFET 55
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 183-279 8.79e-17

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: 76.29  E-value: 8.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230    183 WNATGCQPVRYGQCWVFAAVMCTVMRCLGIPTRVITNFDSGHDTDGNliideyydntgrilgnkkkdtiWNFHVWNECWM 262
Cdd:pfam01841  41 GDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYL 98

                          90
                  ....*....|....*..
gi 4759230    263 arkdlppAYGGWQVLDA 279
Cdd:pfam01841  99 -------PGYGWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 192-280 3.21e-07

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 50.77  E-value: 3.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230  192 RYGQCWVFAAVMCTVMRCLGIPTRVITNFDSGHDTDGNLIIDeyydntgrilgnkkkdtiwNFHVWNECWmarkdLPPAy 271
Cdd:COG1305 112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVY-----LPGA- 166


                ....*....
gi 4759230  272 gGWQVLDAT 280
Cdd:COG1305 167 -GWVPFDPT 174
 
Name Accession Description Interval E-value
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
538-635 1.80e-29

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 112.44  E-value: 1.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230    538 PSITINVLGAAVVNQPLSIQVIFSNPLSEQVEDCVL-----TVEGSGLFKKQ--QKVFLGVLKPQHQASIILETVPFKSG 610
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLslsaqTVEYNGVLGAEfkKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*
gi 4759230    611 QRQIQANMRSNKFKDIKGYRNVYVD 635
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVA 105
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 188-281 4.10e-25

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: 98.61  E-value: 4.10e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230     188 CQPVRYGQCWVFAAVMCTVMRCLGIPTRVITNFDSGHDTDGNLIIdeyydntgrilgnkkkdtIWNFHVWNECWMArkdl 267
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYLE---- 58

                           90
                   ....*....|....
gi 4759230     268 ppayGGWQVLDATP 281
Cdd:smart00460  59 ----GGWVPVDPTP 68
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
425-524 4.29e-24

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 97.03  E-value: 4.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230    425 VSLKFKLLDPPNMGQDICFVLLALNMSSQF-KDLKVNLSAQSLLHDGSPLSPFWQDTAFITLSPKEAKTYPCKISYSQYS 503
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 4759230    504 QY-----LSTDKLIRISALGEEKSSP 524
Cdd:pfam00927  81 PRqllveFSSDALAKVKGYRNVLVAQ 106
Transglut_N pfam00868
Transglutaminase family;
11-63 1.14e-19

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 84.60  E-value: 1.14e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4759230     11 DLQSSRNNVRHHTEEITVDHLLVRRGQAFNLTLYFrNRSFQPGLDNIIFVVET 63
Cdd:pfam00868   4 DLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRF-NRPFDPQLDKLTLEFET 55
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 183-279 8.79e-17

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: 76.29  E-value: 8.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230    183 WNATGCQPVRYGQCWVFAAVMCTVMRCLGIPTRVITNFDSGHDTDGNliideyydntgrilgnkkkdtiWNFHVWNECWM 262
Cdd:pfam01841  41 GDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYL 98

                          90
                  ....*....|....*..
gi 4759230    263 arkdlppAYGGWQVLDA 279
Cdd:pfam01841  99 -------PGYGWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 192-280 3.21e-07

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 50.77  E-value: 3.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759230  192 RYGQCWVFAAVMCTVMRCLGIPTRVITNFDSGHDTDGNLIIDeyydntgrilgnkkkdtiwNFHVWNECWmarkdLPPAy 271
Cdd:COG1305 112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVY-----LPGA- 166


                ....*....
gi 4759230  272 gGWQVLDAT 280
Cdd:COG1305 167 -GWVPFDPT 174
 
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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