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Conserved domains on  [gi|16445035|ref|NP_443187|]
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protein-glutamine gamma-glutamyltransferase Z [Homo sapiens]

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;
10-123 3.55e-51

Transglutaminase family;


:

Pssm-ID: 459971  Cd Length: 114  Bit Score: 173.19  E-value: 3.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035    10 ESVDLQSSRNNKEHHTQEMGVKRLTVRRGQPFYLRLSFSRPFQSQNDHITFVAETGPKPSELLGTRATFFLTRVQPGNVW 89
Cdd:pfam00868   1 MSVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDPQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASSW 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 16445035    90 SASDFTIDSNSLQVSLFTPANAVIGHYTLKIEIS 123
Cdd:pfam00868  81 SARVESISGNSLSVSITSPANAPVGRYTLTVETS 114
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 272-364 1.46e-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: 1.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035    272 QPVKYGQCWVFASVMCTVMRCLGVPTRVVSNFRSAHNVDRNLTIdtyydrnaemlstqkrdkIWNFHVWNECWMirkdlp 351
Cdd:smart00460   2 LKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYL------ 57

                           90
                   ....*....|...
gi 16445035    352 pgYNGWQVLDPTP 364
Cdd:smart00460  58 --EGGWVPVDPTP 68
Transglut_C super family cl08295
Transglutaminase family, C-terminal ig like domain;
608-705 3.62e-17

Transglutaminase family, C-terminal ig like domain;


The actual alignment was detected with superfamily member pfam00927:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 77.38  E-value: 3.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035   608 PHLSIEVSERAEVGKALRVHVTLTNTL-----MVALSSCTMVLEGSGLINGQIAKDL--GTLVAGHTLQIQLDLYPTKAG 680
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLseplkDVVLSLSAQTVEYNGVLGAEFKKKSleLTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*
gi 16445035   681 PRQLQVLISSNEVKEIKGYKDIFVT 705
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVA 105
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
10-123 3.55e-51

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 173.19  E-value: 3.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035    10 ESVDLQSSRNNKEHHTQEMGVKRLTVRRGQPFYLRLSFSRPFQSQNDHITFVAETGPKPSELLGTRATFFLTRVQPGNVW 89
Cdd:pfam00868   1 MSVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDPQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASSW 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 16445035    90 SASDFTIDSNSLQVSLFTPANAVIGHYTLKIEIS 123
Cdd:pfam00868  81 SARVESISGNSLSVSITSPANAPVGRYTLTVETS 114
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 272-364 1.46e-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: 1.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035    272 QPVKYGQCWVFASVMCTVMRCLGVPTRVVSNFRSAHNVDRNLTIdtyydrnaemlstqkrdkIWNFHVWNECWMirkdlp 351
Cdd:smart00460   2 LKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYL------ 57

                           90
                   ....*....|...
gi 16445035    352 pgYNGWQVLDPTP 364
Cdd:smart00460  58 --EGGWVPVDPTP 68
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
608-705 3.62e-17

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 77.38  E-value: 3.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035   608 PHLSIEVSERAEVGKALRVHVTLTNTL-----MVALSSCTMVLEGSGLINGQIAKDL--GTLVAGHTLQIQLDLYPTKAG 680
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLseplkDVVLSLSAQTVEYNGVLGAEFKKKSleLTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*
gi 16445035   681 PRQLQVLISSNEVKEIKGYKDIFVT 705
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVA 105
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 275-362 1.27e-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: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035   275 KYGQCWVFASVMCTVMRCLGVPTRVVSNFRSAHNVDRNltidtyydrnaemlstqkrdkiWNFHVWNECWMirkdlpPGY 354
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYL------PGY 101


                  ....*...
gi 16445035   355 nGWQVLDP 362
Cdd:pfam01841 102 -GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 275-363 2.05e-08

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 54.24  E-value: 2.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035 275 KYGQCWVFASVMCTVMRCLGVPTRVVSNFRSAHNVDRNLTIDtyydrnaemlstqkrdkiwNFHVWNECWMirkdlpPGY 354
Cdd:COG1305 112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVYL------PGA 166


                ....*....
gi 16445035 355 nGWQVLDPT 363
Cdd:COG1305 167 -GWVPFDPT 174
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
10-123 3.55e-51

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 173.19  E-value: 3.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035    10 ESVDLQSSRNNKEHHTQEMGVKRLTVRRGQPFYLRLSFSRPFQSQNDHITFVAETGPKPSELLGTRATFFLTRVQPGNVW 89
Cdd:pfam00868   1 MSVDLQKNENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDPQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASSW 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 16445035    90 SASDFTIDSNSLQVSLFTPANAVIGHYTLKIEIS 123
Cdd:pfam00868  81 SARVESISGNSLSVSITSPANAPVGRYTLTVETS 114
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 272-364 1.46e-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: 1.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035    272 QPVKYGQCWVFASVMCTVMRCLGVPTRVVSNFRSAHNVDRNLTIdtyydrnaemlstqkrdkIWNFHVWNECWMirkdlp 351
Cdd:smart00460   2 LKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYL------ 57

                           90
                   ....*....|...
gi 16445035    352 pgYNGWQVLDPTP 364
Cdd:smart00460  58 --EGGWVPVDPTP 68
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
608-705 3.62e-17

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 77.38  E-value: 3.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035   608 PHLSIEVSERAEVGKALRVHVTLTNTL-----MVALSSCTMVLEGSGLINGQIAKDL--GTLVAGHTLQIQLDLYPTKAG 680
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLseplkDVVLSLSAQTVEYNGVLGAEFKKKSleLTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*
gi 16445035   681 PRQLQVLISSNEVKEIKGYKDIFVT 705
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVA 105
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 275-362 1.27e-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: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035   275 KYGQCWVFASVMCTVMRCLGVPTRVVSNFRSAHNVDRNltidtyydrnaemlstqkrdkiWNFHVWNECWMirkdlpPGY 354
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYL------PGY 101


                  ....*...
gi 16445035   355 nGWQVLDP 362
Cdd:pfam01841 102 -GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 275-363 2.05e-08

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 54.24  E-value: 2.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16445035 275 KYGQCWVFASVMCTVMRCLGVPTRVVSNFRSAHNVDRNLTIDtyydrnaemlstqkrdkiwNFHVWNECWMirkdlpPGY 354
Cdd:COG1305 112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVYL------PGA 166


                ....*....
gi 16445035 355 nGWQVLDPT 363
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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