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Conserved domains on  [gi|227500026|ref|NP_808579|]
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protein-glutamine gamma-glutamyltransferase 4 [Mus musculus]

Protein Classification

protein-glutamine gamma-glutamyltransferase( domain architecture ID 10467682)

protein-glutamine gamma-glutamyltransferase catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
12-117 1.10e-28

Transglutaminase family;


:

Pssm-ID: 459971  Cd Length: 114  Bit Score: 110.40  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026   12 VNVERKLNAAAHHTSEYQTKKLVLRRGQIFTLKVILNRPLQPQ-DELKVTFTSGQRdPPY----MVELDPVTSYRSKGWQ 86
Cdd:pfam00868   3 VDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDPQlDKLTLEFETGPK-PSEskgtLVVFPLGKSGDASSWS 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 227500026   87 VKIAKQSGVEVILNVISAADAVVGRYKMRVN 117
Cdd:pfam00868  82 ARVESISGNSLSVSITSPANAPVGRYTLTVE 112
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
574-670 1.93e-20

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 86.63  E-value: 1.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026  574 AFSVEMPSTGKVKQPLVITSKFTNTLPIPLTNIKFS-----VESLGLAN---MKSWEQETVPPGKTITFQMECTPVKAGP 645
Cdd:pfam00927   2 EMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSlsaqtVEYNGVLGaefKKKSLELTLEPGEEKSVPIKITPSKYGP 81

                          90       100
                  ....*....|....*....|....*
gi 227500026  646 QKFIVKFISRQVKEVHAEKVVLISK 670
Cdd:pfam00927  82 RQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 248-340 1.32e-19

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: 83.20  E-value: 1.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026   248 MPVRYGQCWVFSGILTTALRAVGIPARSVTNFESAHDTEKNLTvdiyldesgktiphltkdSVWNFHVWTDAWMKrqdlp 327
Cdd:smart00460   2 LKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE----- 58

                           90
                   ....*....|...
gi 227500026   328 hgyDGWQVLDSTP 340
Cdd:smart00460  59 ---GGWVPVDPTP 68
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
12-117 1.10e-28

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 110.40  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026   12 VNVERKLNAAAHHTSEYQTKKLVLRRGQIFTLKVILNRPLQPQ-DELKVTFTSGQRdPPY----MVELDPVTSYRSKGWQ 86
Cdd:pfam00868   3 VDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDPQlDKLTLEFETGPK-PSEskgtLVVFPLGKSGDASSWS 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 227500026   87 VKIAKQSGVEVILNVISAADAVVGRYKMRVN 117
Cdd:pfam00868  82 ARVESISGNSLSVSITSPANAPVGRYTLTVE 112
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
574-670 1.93e-20

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 86.63  E-value: 1.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026  574 AFSVEMPSTGKVKQPLVITSKFTNTLPIPLTNIKFS-----VESLGLAN---MKSWEQETVPPGKTITFQMECTPVKAGP 645
Cdd:pfam00927   2 EMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSlsaqtVEYNGVLGaefKKKSLELTLEPGEEKSVPIKITPSKYGP 81

                          90       100
                  ....*....|....*....|....*
gi 227500026  646 QKFIVKFISRQVKEVHAEKVVLISK 670
Cdd:pfam00927  82 RQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 248-340 1.32e-19

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: 83.20  E-value: 1.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026   248 MPVRYGQCWVFSGILTTALRAVGIPARSVTNFESAHDTEKNLTvdiyldesgktiphltkdSVWNFHVWTDAWMKrqdlp 327
Cdd:smart00460   2 LKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE----- 58

                           90
                   ....*....|...
gi 227500026   328 hgyDGWQVLDSTP 340
Cdd:smart00460  59 ---GGWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 251-337 3.33e-12

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: 63.19  E-value: 3.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026  251 RYGQCWVFSGILTTALRAVGIPARSVTNFESAHDTeknltvdiyldesgktiphltkDSVWNFHVWTDAWMKrqdlphgY 330
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDT----------------------VRGGDAHAWVEVYLP-------G 100


                  ....*..
gi 227500026  331 DGWQVLD 337
Cdd:pfam01841 101 YGWVPVD 107
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 251-339 1.31e-05

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 46.15  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026 251 RYGQCWVFSGILTTALRAVGIPARSVTNFESAHDTEKNLTVDiyldesgktiphltkdsvwNFHVWTDAWmkrqdLPhGY 330
Cdd:COG1305  112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVY-----LP-GA 166


                 ....*....
gi 227500026 331 dGWQVLDST 339
Cdd:COG1305  167 -GWVPFDPT 174
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
12-117 1.10e-28

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 110.40  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026   12 VNVERKLNAAAHHTSEYQTKKLVLRRGQIFTLKVILNRPLQPQ-DELKVTFTSGQRdPPY----MVELDPVTSYRSKGWQ 86
Cdd:pfam00868   3 VDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDPQlDKLTLEFETGPK-PSEskgtLVVFPLGKSGDASSWS 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 227500026   87 VKIAKQSGVEVILNVISAADAVVGRYKMRVN 117
Cdd:pfam00868  82 ARVESISGNSLSVSITSPANAPVGRYTLTVE 112
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
574-670 1.93e-20

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 86.63  E-value: 1.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026  574 AFSVEMPSTGKVKQPLVITSKFTNTLPIPLTNIKFS-----VESLGLAN---MKSWEQETVPPGKTITFQMECTPVKAGP 645
Cdd:pfam00927   2 EMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSlsaqtVEYNGVLGaefKKKSLELTLEPGEEKSVPIKITPSKYGP 81

                          90       100
                  ....*....|....*....|....*
gi 227500026  646 QKFIVKFISRQVKEVHAEKVVLISK 670
Cdd:pfam00927  82 RQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 248-340 1.32e-19

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: 83.20  E-value: 1.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026   248 MPVRYGQCWVFSGILTTALRAVGIPARSVTNFESAHDTEKNLTvdiyldesgktiphltkdSVWNFHVWTDAWMKrqdlp 327
Cdd:smart00460   2 LKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE----- 58

                           90
                   ....*....|...
gi 227500026   328 hgyDGWQVLDSTP 340
Cdd:smart00460  59 ---GGWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 251-337 3.33e-12

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: 63.19  E-value: 3.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026  251 RYGQCWVFSGILTTALRAVGIPARSVTNFESAHDTeknltvdiyldesgktiphltkDSVWNFHVWTDAWMKrqdlphgY 330
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDT----------------------VRGGDAHAWVEVYLP-------G 100


                  ....*..
gi 227500026  331 DGWQVLD 337
Cdd:pfam01841 101 YGWVPVD 107
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 251-339 1.31e-05

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 46.15  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500026 251 RYGQCWVFSGILTTALRAVGIPARSVTNFESAHDTEKNLTVDiyldesgktiphltkdsvwNFHVWTDAWmkrqdLPhGY 330
Cdd:COG1305  112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVY-----LP-GA 166


                 ....*....
gi 227500026 331 dGWQVLDST 339
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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