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Conserved domains on  [gi|119395709|ref|NP_000120.2|]
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coagulation factor XIII A chain precursor [Homo sapiens]

Protein Classification

Transglut_N and Transglut_C domain-containing protein (domain architecture ID 10467682)

protein containing domains Transglut_N, TGc, and Transglut_C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
46-165 1.62e-47

Transglutaminase family;


:

Pssm-ID: 334292  Cd Length: 117  Bit Score: 163.46  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709   46 LNVTSVHLFKERwdtNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSE 125
Cdd:pfam00868   1 LEVKSVDLQKEE---NNKEHHTDEYESDRLIVRRGQPFTITLTFNRPFDPSKDKLRLEFETGPNPSESKGTKAVFPLSSS 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119395709  126 LQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVW 165
Cdd:pfam00868  78 RDPSGWSARVVESSGNSLTVSVTSPANAPIGRYRLTVETS 117
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
519-623 6.30e-26

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 307191  Cd Length: 106  Bit Score: 102.41  E-value: 6.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709  519 VDMDFEV-ENAVLGKDFKLSITFRNNSHNR-YTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLI---QAG 593
Cdd:pfam00927   1 PEMKIEVlGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKItpsKYG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 119395709  594 EYmgQLLeqASLHFFVTARINETRDVLAKQ 623
Cdd:pfam00927  81 LR--QLL--VEFSSDALKKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
631-728 7.88e-26

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 307191  Cd Length: 106  Bit Score: 102.03  E-value: 7.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709  631 PEIIIKVRGTQVVGSDMTVTVEFTNPLKETLRNVWVHL-----DGPGVTRP---MKKMFREIRPNSTVQWEEVCRPWVSG 702
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAefkKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 119395709  703 HRKLIASMSSDSLRHVYGELDVQIQR 728
Cdd:pfam00927  81 LRQLLVEFSSDALKKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
309-400 1.33e-23

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 [Multi-domain]  Cd Length: 68  Bit Score: 94.37  E-value: 1.33e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709   309 PVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLqmdifleedgnvnskltkDSVWNYHCWNEAWMTrpdlpv 388
Cdd:smart00460   3 KTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGL------------------RSIWEAHAWAEVYLE------ 58
                           90
                   ....*....|..
gi 119395709   389 gfGGWQAVDSTP 400
Cdd:smart00460  59 --GGWVPVDPTP 68
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
46-165 1.62e-47

Transglutaminase family;


Pssm-ID: 334292  Cd Length: 117  Bit Score: 163.46  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709   46 LNVTSVHLFKERwdtNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSE 125
Cdd:pfam00868   1 LEVKSVDLQKEE---NNKEHHTDEYESDRLIVRRGQPFTITLTFNRPFDPSKDKLRLEFETGPNPSESKGTKAVFPLSSS 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119395709  126 LQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVW 165
Cdd:pfam00868  78 RDPSGWSARVVESSGNSLTVSVTSPANAPIGRYRLTVETS 117
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
519-623 6.30e-26

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 102.41  E-value: 6.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709  519 VDMDFEV-ENAVLGKDFKLSITFRNNSHNR-YTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLI---QAG 593
Cdd:pfam00927   1 PEMKIEVlGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKItpsKYG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 119395709  594 EYmgQLLeqASLHFFVTARINETRDVLAKQ 623
Cdd:pfam00927  81 LR--QLL--VEFSSDALKKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
631-728 7.88e-26

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 102.03  E-value: 7.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709  631 PEIIIKVRGTQVVGSDMTVTVEFTNPLKETLRNVWVHL-----DGPGVTRP---MKKMFREIRPNSTVQWEEVCRPWVSG 702
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAefkKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 119395709  703 HRKLIASMSSDSLRHVYGELDVQIQR 728
Cdd:pfam00927  81 LRQLLVEFSSDALKKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
309-400 1.33e-23

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 [Multi-domain]  Cd Length: 68  Bit Score: 94.37  E-value: 1.33e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709   309 PVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLqmdifleedgnvnskltkDSVWNYHCWNEAWMTrpdlpv 388
Cdd:smart00460   3 KTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGL------------------RSIWEAHAWAEVYLE------ 58
                           90
                   ....*....|..
gi 119395709   389 gfGGWQAVDSTP 400
Cdd:smart00460  59 --GGWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
311-397 5.99e-15

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: 334704  Cd Length: 108  Bit Score: 70.89  E-value: 5.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709  311 RYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANlqmdifleedgnvnskltkdsvWNYHCWNEAWMtrpdlpvGF 390
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYL-------PG 100

                  ....*..
gi 119395709  391 GGWQAVD 397
Cdd:pfam01841 101 YGWVPVD 107
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
284-408 1.24e-06

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


Pssm-ID: 224224 [Multi-domain]  Cd Length: 319  Bit Score: 50.82  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709 284 YAYGVPPSAWTGSVDILLEYRssenpvrYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAhdndanlqmdifleeDGNVNS 363
Cdd:COG1305  173 IRYSPGPTPVTGSASDALRLG-------RGVCRDFAHLLVALLRAAGIPARYVSGYLGA---------------EVEPLS 230
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119395709 364 KLTKDSVWNYHCWNEAWmtrpdlpVGFGGWQAVDSTPQENSDGMY 408
Cdd:COG1305  231 GRPLVRNDDAHAWAEVY-------LPGRGWVPLDPTNGLLAGGRY 268
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
46-165 1.62e-47

Transglutaminase family;


Pssm-ID: 334292  Cd Length: 117  Bit Score: 163.46  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709   46 LNVTSVHLFKERwdtNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSE 125
Cdd:pfam00868   1 LEVKSVDLQKEE---NNKEHHTDEYESDRLIVRRGQPFTITLTFNRPFDPSKDKLRLEFETGPNPSESKGTKAVFPLSSS 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119395709  126 LQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVW 165
Cdd:pfam00868  78 RDPSGWSARVVESSGNSLTVSVTSPANAPIGRYRLTVETS 117
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
519-623 6.30e-26

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 102.41  E-value: 6.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709  519 VDMDFEV-ENAVLGKDFKLSITFRNNSHNR-YTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLI---QAG 593
Cdd:pfam00927   1 PEMKIEVlGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKItpsKYG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 119395709  594 EYmgQLLeqASLHFFVTARINETRDVLAKQ 623
Cdd:pfam00927  81 LR--QLL--VEFSSDALKKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
631-728 7.88e-26

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 102.03  E-value: 7.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709  631 PEIIIKVRGTQVVGSDMTVTVEFTNPLKETLRNVWVHL-----DGPGVTRP---MKKMFREIRPNSTVQWEEVCRPWVSG 702
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAefkKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 119395709  703 HRKLIASMSSDSLRHVYGELDVQIQR 728
Cdd:pfam00927  81 LRQLLVEFSSDALKKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
309-400 1.33e-23

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 [Multi-domain]  Cd Length: 68  Bit Score: 94.37  E-value: 1.33e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709   309 PVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLqmdifleedgnvnskltkDSVWNYHCWNEAWMTrpdlpv 388
Cdd:smart00460   3 KTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGL------------------RSIWEAHAWAEVYLE------ 58
                           90
                   ....*....|..
gi 119395709   389 gfGGWQAVDSTP 400
Cdd:smart00460  59 --GGWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
311-397 5.99e-15

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: 334704  Cd Length: 108  Bit Score: 70.89  E-value: 5.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709  311 RYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANlqmdifleedgnvnskltkdsvWNYHCWNEAWMtrpdlpvGF 390
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYL-------PG 100

                  ....*..
gi 119395709  391 GGWQAVD 397
Cdd:pfam01841 101 YGWVPVD 107
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
284-408 1.24e-06

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


Pssm-ID: 224224 [Multi-domain]  Cd Length: 319  Bit Score: 50.82  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395709 284 YAYGVPPSAWTGSVDILLEYRssenpvrYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAhdndanlqmdifleeDGNVNS 363
Cdd:COG1305  173 IRYSPGPTPVTGSASDALRLG-------RGVCRDFAHLLVALLRAAGIPARYVSGYLGA---------------EVEPLS 230
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119395709 364 KLTKDSVWNYHCWNEAWmtrpdlpVGFGGWQAVDSTPQENSDGMY 408
Cdd:COG1305  231 GRPLVRNDDAHAWAEVY-------LPGRGWVPLDPTNGLLAGGRY 268
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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