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Conserved domains on  [gi|1383484825|ref|NP_001349653|]
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protein-glutamine gamma-glutamyltransferase 5 isoform 2 [Mus musculus]

Protein Classification

TGc and Transglut_C domain-containing protein( domain architecture ID 10648757)

TGc and Transglut_C domain-containing protein

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;
390-487 8.91e-29

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 109.35  E-value: 8.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383484825 390 PGIMINVLGAAFVNQPLTVQVVFSNPLSEPVEDCVLTL-----EGSGLFRKQ--QRVLIGVLKPHHKASITLKTVPFKSG 462
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAEfkKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*
gi 1383484825 463 QRQIQANLRSNRFKDIKGYKNVYVD 487
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVA 105
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
277-372 9.12e-24

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 95.49  E-value: 9.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383484825 277 VSLKFELLDSPKMGQDINFVLLAVNMSPQF-KDLKLNLSAQSLLHDGSPLVPFWQDTAFITLFPEEEKSYPCKILYSQYS 355
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|..
gi 1383484825 356 QY-----LSTDKLIRISALGEE 372
Cdd:pfam00927  81 PRqllveFSSDALAKVKGYRNV 102
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 57-134 6.48e-15

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: 69.33  E-value: 6.48e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1383484825   57 VGVMRCLGIPTRVITNFDSGHDTDGNLIIdeyydntgrilenmkkdtVWNFHVWNECWMArkdlppgyGGWQVLDATP 134
Cdd:smart00460  17 VALLRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYLE--------GGWVPVDPTP 68
 
Name Accession Description Interval E-value
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
390-487 8.91e-29

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 109.35  E-value: 8.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383484825 390 PGIMINVLGAAFVNQPLTVQVVFSNPLSEPVEDCVLTL-----EGSGLFRKQ--QRVLIGVLKPHHKASITLKTVPFKSG 462
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAEfkKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*
gi 1383484825 463 QRQIQANLRSNRFKDIKGYKNVYVD 487
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVA 105
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
277-372 9.12e-24

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 95.49  E-value: 9.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383484825 277 VSLKFELLDSPKMGQDINFVLLAVNMSPQF-KDLKLNLSAQSLLHDGSPLVPFWQDTAFITLFPEEEKSYPCKILYSQYS 355
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|..
gi 1383484825 356 QY-----LSTDKLIRISALGEE 372
Cdd:pfam00927  81 PRqllveFSSDALAKVKGYRNV 102
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 57-134 6.48e-15

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: 69.33  E-value: 6.48e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1383484825   57 VGVMRCLGIPTRVITNFDSGHDTDGNLIIdeyydntgrilenmkkdtVWNFHVWNECWMArkdlppgyGGWQVLDATP 134
Cdd:smart00460  17 VALLRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYLE--------GGWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 57-132 3.67e-10

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: 57.03  E-value: 3.67e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1383484825  57 VGVMRCLGIPTRVITNFDSGHDTDGNliideyydntgrilenmkkdtvWNFHVWNECWMarkdlpPGYgGWQVLDA 132
Cdd:pfam01841  62 VALLRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYL------PGY-GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 57-133 5.80e-04

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 40.76  E-value: 5.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1383484825  57 VGVMRCLGIPTRVITNFDSGHDTDGNliideyydntgrilenmkkDTVWNFHVWNECWMarkdlpPGYgGWQVLDAT 133
Cdd:COG1305   124 VALLRALGIPARYVSGYLPGEPPPGG-------------------GRADDAHAWVEVYL------PGA-GWVPFDPT 174
 
Name Accession Description Interval E-value
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
390-487 8.91e-29

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 109.35  E-value: 8.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383484825 390 PGIMINVLGAAFVNQPLTVQVVFSNPLSEPVEDCVLTL-----EGSGLFRKQ--QRVLIGVLKPHHKASITLKTVPFKSG 462
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAEfkKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*
gi 1383484825 463 QRQIQANLRSNRFKDIKGYKNVYVD 487
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVA 105
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
277-372 9.12e-24

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 95.49  E-value: 9.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383484825 277 VSLKFELLDSPKMGQDINFVLLAVNMSPQF-KDLKLNLSAQSLLHDGSPLVPFWQDTAFITLFPEEEKSYPCKILYSQYS 355
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|..
gi 1383484825 356 QY-----LSTDKLIRISALGEE 372
Cdd:pfam00927  81 PRqllveFSSDALAKVKGYRNV 102
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 57-134 6.48e-15

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: 69.33  E-value: 6.48e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1383484825   57 VGVMRCLGIPTRVITNFDSGHDTDGNLIIdeyydntgrilenmkkdtVWNFHVWNECWMArkdlppgyGGWQVLDATP 134
Cdd:smart00460  17 VALLRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYLE--------GGWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 57-132 3.67e-10

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: 57.03  E-value: 3.67e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1383484825  57 VGVMRCLGIPTRVITNFDSGHDTDGNliideyydntgrilenmkkdtvWNFHVWNECWMarkdlpPGYgGWQVLDA 132
Cdd:pfam01841  62 VALLRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYL------PGY-GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 57-133 5.80e-04

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 40.76  E-value: 5.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1383484825  57 VGVMRCLGIPTRVITNFDSGHDTDGNliideyydntgrilenmkkDTVWNFHVWNECWMarkdlpPGYgGWQVLDAT 133
Cdd:COG1305   124 VALLRALGIPARYVSGYLPGEPPPGG-------------------GRADDAHAWVEVYL------PGA-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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