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Conserved domains on  [gi|1020158911|ref|NP_001310245|]
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protein-glutamine gamma-glutamyltransferase 2 isoform a [Homo sapiens]

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;
8-122 1.45e-44

Transglutaminase family;


:

Pssm-ID: 459971  Cd Length: 114  Bit Score: 155.09  E-value: 1.45e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911   8 ERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEgRNYEASVDSLTFSVVTGPAPSQEAGTKARFPLRDAVEEGD 87
Cdd:pfam00868   1 MSVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFN-RPFDPQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASS 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1020158911  88 WTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEAS 122
Cdd:pfam00868  80 WSARVESISGNSLSVSITSPANAPVGRYTLTVETS 114
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
473-573 2.19e-29

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 112.44  E-value: 2.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911 473 MAMRIRVGQSMNMGSDFDVFAHITNNTAEE-YVCRLLLCARTVSYNGILGPECGTKYlLNLNLEPFSEKSVPLCILYEKY 551
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKS-LELTLEPGEEKSVPIKITPSKY 79
                          90       100
                  ....*....|....*....|....*..
gi 1020158911 552 --RDCLTE---SNLIKVRALLVEPVIN 573
Cdd:pfam00927  80 gpRQLLVEfssDALAKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
587-686 1.47e-24

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 98.57  E-value: 1.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911 587 PEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTF-----TVEGAGLTE-EQKTVEIPDPVEAGEEVKVRMDLLPLHMG 660
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLslsaqTVEYNGVLGaEFKKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 1020158911 661 LHKLVVNFESDKLKAVKGFRNVIIGP 686
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
269-361 1.38e-22

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: 91.68  E-value: 1.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911  269 CQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLieyfrnefgeiqgdkseMIWNFHCWVESWMTRpdlq 348
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR-----------------SIWEAHAWAEVYLEG---- 59
                           90
                   ....*....|...
gi 1020158911  349 pgyeGWQALDPTP 361
Cdd:smart00460  60 ----GWVPVDPTP 68
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
8-122 1.45e-44

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 155.09  E-value: 1.45e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911   8 ERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEgRNYEASVDSLTFSVVTGPAPSQEAGTKARFPLRDAVEEGD 87
Cdd:pfam00868   1 MSVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFN-RPFDPQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASS 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1020158911  88 WTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEAS 122
Cdd:pfam00868  80 WSARVESISGNSLSVSITSPANAPVGRYTLTVETS 114
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
473-573 2.19e-29

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 112.44  E-value: 2.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911 473 MAMRIRVGQSMNMGSDFDVFAHITNNTAEE-YVCRLLLCARTVSYNGILGPECGTKYlLNLNLEPFSEKSVPLCILYEKY 551
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKS-LELTLEPGEEKSVPIKITPSKY 79
                          90       100
                  ....*....|....*....|....*..
gi 1020158911 552 --RDCLTE---SNLIKVRALLVEPVIN 573
Cdd:pfam00927  80 gpRQLLVEfssDALAKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
587-686 1.47e-24

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 98.57  E-value: 1.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911 587 PEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTF-----TVEGAGLTE-EQKTVEIPDPVEAGEEVKVRMDLLPLHMG 660
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLslsaqTVEYNGVLGaEFKKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 1020158911 661 LHKLVVNFESDKLKAVKGFRNVIIGP 686
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
269-361 1.38e-22

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: 91.68  E-value: 1.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911  269 CQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLieyfrnefgeiqgdkseMIWNFHCWVESWMTRpdlq 348
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR-----------------SIWEAHAWAEVYLEG---- 59
                           90
                   ....*....|...
gi 1020158911  349 pgyeGWQALDPTP 361
Cdd:smart00460  60 ----GWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
271-359 1.24e-16

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: 75.90  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911 271 RVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNllieyfrnefgeiqgdksemiWNFHCWVESWMtrpdlqPG 350
Cdd:pfam01841  48 FTGKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG---------------------GDAHAWVEVYL------PG 100

                  ....*....
gi 1020158911 351 YeGWQALDP 359
Cdd:pfam01841 101 Y-GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
273-360 8.58e-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: 8.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911 273 KYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDqnsnllieyfrNEFGEIQGDksemiwnFHCWVESWMtrpdlqPGYe 352
Cdd:COG1305   112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEP-----------PPGGGRADD-------AHAWVEVYL------PGA- 166

                  ....*...
gi 1020158911 353 GWQALDPT 360
Cdd:COG1305   167 GWVPFDPT 174
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
8-122 1.45e-44

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 155.09  E-value: 1.45e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911   8 ERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEgRNYEASVDSLTFSVVTGPAPSQEAGTKARFPLRDAVEEGD 87
Cdd:pfam00868   1 MSVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFN-RPFDPQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASS 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1020158911  88 WTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEAS 122
Cdd:pfam00868  80 WSARVESISGNSLSVSITSPANAPVGRYTLTVETS 114
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
473-573 2.19e-29

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 112.44  E-value: 2.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911 473 MAMRIRVGQSMNMGSDFDVFAHITNNTAEE-YVCRLLLCARTVSYNGILGPECGTKYlLNLNLEPFSEKSVPLCILYEKY 551
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKS-LELTLEPGEEKSVPIKITPSKY 79
                          90       100
                  ....*....|....*....|....*..
gi 1020158911 552 --RDCLTE---SNLIKVRALLVEPVIN 573
Cdd:pfam00927  80 gpRQLLVEfssDALAKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
587-686 1.47e-24

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 98.57  E-value: 1.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911 587 PEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTF-----TVEGAGLTE-EQKTVEIPDPVEAGEEVKVRMDLLPLHMG 660
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLslsaqTVEYNGVLGaEFKKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 1020158911 661 LHKLVVNFESDKLKAVKGFRNVIIGP 686
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
269-361 1.38e-22

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: 91.68  E-value: 1.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911  269 CQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLieyfrnefgeiqgdkseMIWNFHCWVESWMTRpdlq 348
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR-----------------SIWEAHAWAEVYLEG---- 59
                           90
                   ....*....|...
gi 1020158911  349 pgyeGWQALDPTP 361
Cdd:smart00460  60 ----GWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
271-359 1.24e-16

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: 75.90  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911 271 RVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNllieyfrnefgeiqgdksemiWNFHCWVESWMtrpdlqPG 350
Cdd:pfam01841  48 FTGKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG---------------------GDAHAWVEVYL------PG 100

                  ....*....
gi 1020158911 351 YeGWQALDP 359
Cdd:pfam01841 101 Y-GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
273-360 8.58e-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: 8.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158911 273 KYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDqnsnllieyfrNEFGEIQGDksemiwnFHCWVESWMtrpdlqPGYe 352
Cdd:COG1305   112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEP-----------PPGGGRADD-------AHAWVEVYL------PGA- 166

                  ....*...
gi 1020158911 353 GWQALDPT 360
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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