NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|156627577|ref|NP_003232|]
View 

protein-glutamine gamma-glutamyltransferase 4 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
12-122 2.40e-34

Transglutaminase family;


:

Pssm-ID: 459971  Cd Length: 114  Bit Score: 126.58  E-value: 2.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577   12 HIDFLNQDNAVSHHTWEFQTSSPVFRRGQVFHLRLVLNQPLQ-SYHQLKLEFSTGPNPSIAKHTLVVLDPRTPSDHYNWQ 90
Cdd:pfam00868   2 SVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDpQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASSWS 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 156627577   91 ATLQNESGKEVTVAVTSSPNAILGKYQLNVKT 122
Cdd:pfam00868  82 ARVESISGNSLSVSITSPANAPVGRYTLTVET 113
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
587-684 2.36e-24

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 97.80  E-value: 2.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577  587 PEFSIELPNTGRIGQLLVCNCIFKNTLAIPLTDVKFSL-----ESLGISS---LQTSDHGTVQPGETIQSQIKCTPIKTG 658
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGaefKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 156627577  659 PKKFIVKLSSKQVKEINAQKIVLITK 684
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 263-353 5.10e-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: 87.05  E-value: 5.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577   263 VCFGQCWVFAGILTTVLRALGIPARSVTGFDSAHDTERNLTvdtyvnengekitsmthdSVWNFHVWTDAWMKrpdlpkg 342
Cdd:smart00460   4 TKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE------- 58

                           90
                   ....*....|.
gi 156627577   343 yDGWQAVDATP 353
Cdd:smart00460  59 -GGWVPVDPTP 68
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
12-122 2.40e-34

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 126.58  E-value: 2.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577   12 HIDFLNQDNAVSHHTWEFQTSSPVFRRGQVFHLRLVLNQPLQ-SYHQLKLEFSTGPNPSIAKHTLVVLDPRTPSDHYNWQ 90
Cdd:pfam00868   2 SVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDpQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASSWS 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 156627577   91 ATLQNESGKEVTVAVTSSPNAILGKYQLNVKT 122
Cdd:pfam00868  82 ARVESISGNSLSVSITSPANAPVGRYTLTVET 113
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
587-684 2.36e-24

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 97.80  E-value: 2.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577  587 PEFSIELPNTGRIGQLLVCNCIFKNTLAIPLTDVKFSL-----ESLGISS---LQTSDHGTVQPGETIQSQIKCTPIKTG 658
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGaefKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 156627577  659 PKKFIVKLSSKQVKEINAQKIVLITK 684
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 263-353 5.10e-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: 87.05  E-value: 5.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577   263 VCFGQCWVFAGILTTVLRALGIPARSVTGFDSAHDTERNLTvdtyvnengekitsmthdSVWNFHVWTDAWMKrpdlpkg 342
Cdd:smart00460   4 TKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE------- 58

                           90
                   ....*....|.
gi 156627577   343 yDGWQAVDATP 353
Cdd:smart00460  59 -GGWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 266-351 1.36e-13

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: 67.43  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577  266 GQCWVFAGILTTVLRALGIPARSVTGFDSAHDTERNltvdtyvnengekitsmthdsvWNFHVWTDAWMKrpdlpkgYDG 345
Cdd:pfam01841  52 GDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYLP-------GYG 102


                  ....*.
gi 156627577  346 WQAVDA 351
Cdd:pfam01841 103 WVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 255-352 1.24e-07

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 51.93  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577 255 QYYNTKQAVCFGqcwvFAGILTTVLRALGIPARSVTGFDSAHDTERNLTVDtyvnengekitsmthdsvwNFHVWTDAWm 334
Cdd:COG1305  107 ETLERRRGVCRD----FAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVY- 162

                         90
                 ....*....|....*...
gi 156627577 335 krpdLPkGYdGWQAVDAT 352
Cdd:COG1305  163 ----LP-GA-GWVPFDPT 174
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
12-122 2.40e-34

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 126.58  E-value: 2.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577   12 HIDFLNQDNAVSHHTWEFQTSSPVFRRGQVFHLRLVLNQPLQ-SYHQLKLEFSTGPNPSIAKHTLVVLDPRTPSDHYNWQ 90
Cdd:pfam00868   2 SVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDpQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASSWS 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 156627577   91 ATLQNESGKEVTVAVTSSPNAILGKYQLNVKT 122
Cdd:pfam00868  82 ARVESISGNSLSVSITSPANAPVGRYTLTVET 113
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
587-684 2.36e-24

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 97.80  E-value: 2.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577  587 PEFSIELPNTGRIGQLLVCNCIFKNTLAIPLTDVKFSL-----ESLGISS---LQTSDHGTVQPGETIQSQIKCTPIKTG 658
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGaefKKKSLELTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 156627577  659 PKKFIVKLSSKQVKEINAQKIVLITK 684
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 263-353 5.10e-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: 87.05  E-value: 5.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577   263 VCFGQCWVFAGILTTVLRALGIPARSVTGFDSAHDTERNLTvdtyvnengekitsmthdSVWNFHVWTDAWMKrpdlpkg 342
Cdd:smart00460   4 TKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE------- 58

                           90
                   ....*....|.
gi 156627577   343 yDGWQAVDATP 353
Cdd:smart00460  59 -GGWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 266-351 1.36e-13

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: 67.43  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577  266 GQCWVFAGILTTVLRALGIPARSVTGFDSAHDTERNltvdtyvnengekitsmthdsvWNFHVWTDAWMKrpdlpkgYDG 345
Cdd:pfam01841  52 GDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYLP-------GYG 102


                  ....*.
gi 156627577  346 WQAVDA 351
Cdd:pfam01841 103 WVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 255-352 1.24e-07

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 51.93  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156627577 255 QYYNTKQAVCFGqcwvFAGILTTVLRALGIPARSVTGFDSAHDTERNLTVDtyvnengekitsmthdsvwNFHVWTDAWm 334
Cdd:COG1305  107 ETLERRRGVCRD----FAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVY- 162

                         90
                 ....*....|....*...
gi 156627577 335 krpdLPkGYdGWQAVDAT 352
Cdd:COG1305  163 ----LP-GA-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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH