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Conserved domains on  [gi|1020158942|ref|NP_001310246|]
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protein-glutamine gamma-glutamyltransferase 2 isoform c [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;
392-492 1.72e-29

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 112.44  E-value: 1.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942 392 MAMRIRVGQSMNMGSDFDVFAHITNNTAEE-YVCRLLLCARTVSYNGILGPECGTKYlLNLNLEPFSEKSVPLCILYEKY 470
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKS-LELTLEPGEEKSVPIKITPSKY 79

                          90       100
                  ....*....|....*....|....*..
gi 1020158942 471 --RDCLTE---SNLIKVRALLVEPVIN 492
Cdd:pfam00927  80 gpRQLLVEfssDALAKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
506-605 1.25e-24

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 98.57  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942 506 PEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTF-----TVEGAGLTE-EQKTVEIPDPVEAGEEVKVRMDLLPLHMG 579
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLslsaqTVEYNGVLGaEFKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 1020158942 580 LHKLVVNFESDKLKAVKGFRNVIIGP 605
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 188-280 8.40e-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  Cd Length: 68  Bit Score: 92.06  E-value: 8.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942  188 CQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLieyfrnefgeiqgdkseMIWNFHCWVESWMTRpdlq 267
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR-----------------SIWEAHAWAEVYLEG---- 59

                           90
                   ....*....|...
gi 1020158942  268 pgyeGWQALDPTP 280
Cdd:smart00460  60 ----GWVPVDPTP 68
Transglut_N super family cl02994
Transglutaminase family;
8-63 1.93e-17

Transglutaminase family;


The actual alignment was detected with superfamily member pfam00868:

Pssm-ID: 459971  Cd Length: 114  Bit Score: 78.43  E-value: 1.93e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1020158942   8 ERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEgRNYEASVDSLTFSVVT 63
Cdd:pfam00868   1 MSVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFN-RPFDPQLDKLTLEFET 55
 
Name Accession Description Interval E-value
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
392-492 1.72e-29

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 112.44  E-value: 1.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942 392 MAMRIRVGQSMNMGSDFDVFAHITNNTAEE-YVCRLLLCARTVSYNGILGPECGTKYlLNLNLEPFSEKSVPLCILYEKY 470
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKS-LELTLEPGEEKSVPIKITPSKY 79

                          90       100
                  ....*....|....*....|....*..
gi 1020158942 471 --RDCLTE---SNLIKVRALLVEPVIN 492
Cdd:pfam00927  80 gpRQLLVEfssDALAKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
506-605 1.25e-24

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 98.57  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942 506 PEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTF-----TVEGAGLTE-EQKTVEIPDPVEAGEEVKVRMDLLPLHMG 579
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLslsaqTVEYNGVLGaEFKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 1020158942 580 LHKLVVNFESDKLKAVKGFRNVIIGP 605
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 188-280 8.40e-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  Cd Length: 68  Bit Score: 92.06  E-value: 8.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942  188 CQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLieyfrnefgeiqgdkseMIWNFHCWVESWMTRpdlq 267
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR-----------------SIWEAHAWAEVYLEG---- 59

                           90
                   ....*....|...
gi 1020158942  268 pgyeGWQALDPTP 280
Cdd:smart00460  60 ----GWVPVDPTP 68
Transglut_N pfam00868
Transglutaminase family;
8-63 1.93e-17

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 78.43  E-value: 1.93e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1020158942   8 ERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEgRNYEASVDSLTFSVVT 63
Cdd:pfam00868   1 MSVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFN-RPFDPQLDKLTLEFET 55
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 190-278 8.39e-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: 8.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942 190 RVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNllieyfrnefgeiqgdksemiWNFHCWVESWMtrpdlqPG 269
Cdd:pfam01841  48 FTGKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG---------------------GDAHAWVEVYL------PG 100


                  ....*....
gi 1020158942 270 YeGWQALDP 278
Cdd:pfam01841 101 Y-GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 192-279 7.39e-10

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 58.48  E-value: 7.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942 192 KYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDqnsnllieyfrNEFGEIQGDksemiwnFHCWVESWMtrpdlqPGYe 271
Cdd:COG1305   112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEP-----------PPGGGRADD-------AHAWVEVYL------PGA- 166


                  ....*...
gi 1020158942 272 GWQALDPT 279
Cdd:COG1305   167 GWVPFDPT 174
 
Name Accession Description Interval E-value
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
392-492 1.72e-29

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 112.44  E-value: 1.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942 392 MAMRIRVGQSMNMGSDFDVFAHITNNTAEE-YVCRLLLCARTVSYNGILGPECGTKYlLNLNLEPFSEKSVPLCILYEKY 470
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKS-LELTLEPGEEKSVPIKITPSKY 79

                          90       100
                  ....*....|....*....|....*..
gi 1020158942 471 --RDCLTE---SNLIKVRALLVEPVIN 492
Cdd:pfam00927  80 gpRQLLVEfssDALAKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
506-605 1.25e-24

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 98.57  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942 506 PEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTF-----TVEGAGLTE-EQKTVEIPDPVEAGEEVKVRMDLLPLHMG 579
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLslsaqTVEYNGVLGaEFKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 1020158942 580 LHKLVVNFESDKLKAVKGFRNVIIGP 605
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 188-280 8.40e-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  Cd Length: 68  Bit Score: 92.06  E-value: 8.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942  188 CQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLieyfrnefgeiqgdkseMIWNFHCWVESWMTRpdlq 267
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR-----------------SIWEAHAWAEVYLEG---- 59

                           90
                   ....*....|...
gi 1020158942  268 pgyeGWQALDPTP 280
Cdd:smart00460  60 ----GWVPVDPTP 68
Transglut_N pfam00868
Transglutaminase family;
8-63 1.93e-17

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 78.43  E-value: 1.93e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1020158942   8 ERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEgRNYEASVDSLTFSVVT 63
Cdd:pfam00868   1 MSVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFN-RPFDPQLDKLTLEFET 55
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 190-278 8.39e-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: 8.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942 190 RVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNllieyfrnefgeiqgdksemiWNFHCWVESWMtrpdlqPG 269
Cdd:pfam01841  48 FTGKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG---------------------GDAHAWVEVYL------PG 100


                  ....*....
gi 1020158942 270 YeGWQALDP 278
Cdd:pfam01841 101 Y-GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 192-279 7.39e-10

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 58.48  E-value: 7.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158942 192 KYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDqnsnllieyfrNEFGEIQGDksemiwnFHCWVESWMtrpdlqPGYe 271
Cdd:COG1305   112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEP-----------PPGGGRADD-------AHAWVEVYL------PGA- 166


                  ....*...
gi 1020158942 272 GWQALDPT 279
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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