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Conserved domains on  [gi|2069622609|ref|XP_042352869|]
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protein-glutamine gamma-glutamyltransferase 2 [Plectropomus leopardus]

Protein Classification

protein-glutamine gamma-glutamyltransferase( domain architecture ID 10467673)

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;
10-112 2.03e-25

Transglutaminase family;


:

Pssm-ID: 459971  Cd Length: 114  Bit Score: 101.16  E-value: 2.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609  10 DVDLRSNENNLAHRTREIDRQRLIVRRGQPFSITLQCSES-LPRQHHVELVLHLGKRDEVVIKTQ-----REHGAGDKWW 83
Cdd:pfam00868   2 SVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPfDPQLDKLTLEFETGPKPSESKGTLvvfplGKSGDASSWS 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2069622609  84 FSQQGAQDEML-LTVHSPADAIIGHYRLAV 112
Cdd:pfam00868  82 ARVESISGNSLsVSITSPANAPVGRYTLTV 111
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 264-356 2.72e-21

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: 87.82  E-value: 2.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609  264 ARAVKYGQCWVFAAVACTVLRCLGIPTRLITNFSSAHDVDGDLNidtllneslrllkdqreSSWNFHCWVESWMrrddlp 343
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR-----------------SIWEAHAWAEVYL------ 57

                           90
                   ....*....|...
gi 2069622609  344 kgNDGWQVLDPTP 356
Cdd:smart00460  58 --EGGWVPVDPTP 68
Transglut_C super family cl08295
Transglutaminase family, C-terminal ig like domain;
582-678 2.80e-16

Transglutaminase family, C-terminal ig like domain;


The actual alignment was detected with superfamily member pfam00927:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 75.07  E-value: 2.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609 582 PELLVQVPGKAVVWEPVTALISFTNPLP-----VRLRGGMFTVEGAGLLTA--TEIRVNGDISPGQKVSVKLSFTPTRTG 654
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSeplkdVVLSLSAQTVEYNGVLGAefKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....
gi 2069622609 655 VRKLLVDFDSDRLKDMKGDATVVV 678
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLV 104
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
10-112 2.03e-25

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 101.16  E-value: 2.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609  10 DVDLRSNENNLAHRTREIDRQRLIVRRGQPFSITLQCSES-LPRQHHVELVLHLGKRDEVVIKTQ-----REHGAGDKWW 83
Cdd:pfam00868   2 SVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPfDPQLDKLTLEFETGPKPSESKGTLvvfplGKSGDASSWS 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2069622609  84 FSQQGAQDEML-LTVHSPADAIIGHYRLAV 112
Cdd:pfam00868  82 ARVESISGNSLsVSITSPANAPVGRYTLTV 111
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 264-356 2.72e-21

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: 87.82  E-value: 2.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609  264 ARAVKYGQCWVFAAVACTVLRCLGIPTRLITNFSSAHDVDGDLNidtllneslrllkdqreSSWNFHCWVESWMrrddlp 343
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR-----------------SIWEAHAWAEVYL------ 57

                           90
                   ....*....|...
gi 2069622609  344 kgNDGWQVLDPTP 356
Cdd:smart00460  58 --EGGWVPVDPTP 68
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
582-678 2.80e-16

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 75.07  E-value: 2.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609 582 PELLVQVPGKAVVWEPVTALISFTNPLP-----VRLRGGMFTVEGAGLLTA--TEIRVNGDISPGQKVSVKLSFTPTRTG 654
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSeplkdVVLSLSAQTVEYNGVLGAefKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....
gi 2069622609 655 VRKLLVDFDSDRLKDMKGDATVVV 678
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLV 104
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 268-354 1.82e-14

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: 69.74  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609 268 KYGQCWVFAAVACTVLRCLGIPTRLITNFSSAHDVDGdlnidtllneslrllkdqresSWNFHCWVESWMrrddlpkGND 347
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVR---------------------GGDAHAWVEVYL-------PGY 101


                  ....*..
gi 2069622609 348 GWQVLDP 354
Cdd:pfam01841 102 GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 268-355 5.60e-07

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 50.39  E-value: 5.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609 268 KYGQCWVFAAVACTVLRCLGIPTRLITNFSSAHDVDGDLNIDtllneslrllkdqresswNFHCWVESWMrrddlpkGND 347
Cdd:COG1305   112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD------------------DAHAWVEVYL-------PGA 166


                  ....*...
gi 2069622609 348 GWQVLDPT 355
Cdd:COG1305   167 GWVPFDPT 174
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 572-676 2.09e-04

bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 44.60  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609 572 MTMATIPLSMPELLVQV--PGKAVVWEPVTALiSFTNPL------PVRLRGGMFTVEGAGLLTATEIRVNGDIS------ 637
Cdd:PRK14806  464 LPMASAQVKSCLLLAGLyaEGETSVTEPAPTR-DHTERMlrgfgyPVKVEGNTISVEGGGKLTATDIEVPADISsaaffl 542

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2069622609 638 ------PGQKVSVK-LSFTPTRTGVrkllVDFdsdrLKDMKGDATV 676
Cdd:PRK14806  543 vaasiaEGSELTLEhVGINPTRTGV----IDI----LKLMGADITL 580
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
10-112 2.03e-25

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 101.16  E-value: 2.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609  10 DVDLRSNENNLAHRTREIDRQRLIVRRGQPFSITLQCSES-LPRQHHVELVLHLGKRDEVVIKTQ-----REHGAGDKWW 83
Cdd:pfam00868   2 SVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPfDPQLDKLTLEFETGPKPSESKGTLvvfplGKSGDASSWS 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2069622609  84 FSQQGAQDEML-LTVHSPADAIIGHYRLAV 112
Cdd:pfam00868  82 ARVESISGNSLsVSITSPANAPVGRYTLTV 111
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 264-356 2.72e-21

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: 87.82  E-value: 2.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609  264 ARAVKYGQCWVFAAVACTVLRCLGIPTRLITNFSSAHDVDGDLNidtllneslrllkdqreSSWNFHCWVESWMrrddlp 343
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR-----------------SIWEAHAWAEVYL------ 57

                           90
                   ....*....|...
gi 2069622609  344 kgNDGWQVLDPTP 356
Cdd:smart00460  58 --EGGWVPVDPTP 68
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
582-678 2.80e-16

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 75.07  E-value: 2.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609 582 PELLVQVPGKAVVWEPVTALISFTNPLP-----VRLRGGMFTVEGAGLLTA--TEIRVNGDISPGQKVSVKLSFTPTRTG 654
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSeplkdVVLSLSAQTVEYNGVLGAefKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....
gi 2069622609 655 VRKLLVDFDSDRLKDMKGDATVVV 678
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLV 104
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 268-354 1.82e-14

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: 69.74  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609 268 KYGQCWVFAAVACTVLRCLGIPTRLITNFSSAHDVDGdlnidtllneslrllkdqresSWNFHCWVESWMrrddlpkGND 347
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVR---------------------GGDAHAWVEVYL-------PGY 101


                  ....*..
gi 2069622609 348 GWQVLDP 354
Cdd:pfam01841 102 GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 268-355 5.60e-07

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 50.39  E-value: 5.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609 268 KYGQCWVFAAVACTVLRCLGIPTRLITNFSSAHDVDGDLNIDtllneslrllkdqresswNFHCWVESWMrrddlpkGND 347
Cdd:COG1305   112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD------------------DAHAWVEVYL-------PGA 166


                  ....*...
gi 2069622609 348 GWQVLDPT 355
Cdd:COG1305   167 GWVPFDPT 174
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 572-676 2.09e-04

bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 44.60  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069622609 572 MTMATIPLSMPELLVQV--PGKAVVWEPVTALiSFTNPL------PVRLRGGMFTVEGAGLLTATEIRVNGDIS------ 637
Cdd:PRK14806  464 LPMASAQVKSCLLLAGLyaEGETSVTEPAPTR-DHTERMlrgfgyPVKVEGNTISVEGGGKLTATDIEVPADISsaaffl 542

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2069622609 638 ------PGQKVSVK-LSFTPTRTGVrkllVDFdsdrLKDMKGDATV 676
Cdd:PRK14806  543 vaasiaEGSELTLEhVGINPTRTGV----IDI----LKLMGADITL 580
 
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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