NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568917999|ref|XP_006500051|]
View 

protein-glutamine gamma-glutamyltransferase Z isoform X1 [Mus musculus]

Protein Classification

TGc and Transglut_C domain-containing protein( domain architecture ID 10648733)

TGc and Transglut_C domain-containing protein

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_C super family cl08295
Transglutaminase family, C-terminal ig like domain;
319-417 7.41e-19

Transglutaminase family, C-terminal ig like domain;


The actual alignment was detected with superfamily member pfam00927:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 81.23  E-value: 7.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568917999  319 PHLSIEVFERAEVGKALDIHITLTNTLMVPLNNCTMVL-----EGSGLINGQMTKDL--GTLMAGHTIRIHLELYPIKAG 391
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAEFKKKSleLTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 568917999  392 PHQLQVLISSSEVKEIKGYKDILVAA 417
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 1-75 1.12e-12

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: 62.79  E-value: 1.12e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568917999     1 MRCLGVPTRVVSNFHSAHNTDGNLTIdtyydrtaemltaqrpdkIWNFHVWNECWMirkdlppgYNGWQVLDPTP 75
Cdd:smart00460  20 LRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYL--------EGGWVPVDPTP 68
Transglut_C super family cl08295
Transglutaminase family, C-terminal ig like domain;
210-301 8.99e-04

Transglutaminase family, C-terminal ig like domain;


The actual alignment was detected with superfamily member pfam00927:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 38.48  E-value: 8.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568917999  210 APMWGQDLPLMLYVQ---RVPVRDhvqgsvgLTVRFCAQALLHGGGTRKPFWRHIVHLNVDFEKELQWPFLLPYSSY--R 284
Cdd:pfam00927  10 SAVVGQDLTVSVTLSnplSEPLKD-------VVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYgpR 82

                          90       100
                  ....*....|....*....|
gi 568917999  285 DKLTDER---LIRVAGIAEV 301
Cdd:pfam00927  83 QLLVEFSsdaLAKVKGYRNV 102
 
Name Accession Description Interval E-value
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
319-417 7.41e-19

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 81.23  E-value: 7.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568917999  319 PHLSIEVFERAEVGKALDIHITLTNTLMVPLNNCTMVL-----EGSGLINGQMTKDL--GTLMAGHTIRIHLELYPIKAG 391
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAEFKKKSleLTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 568917999  392 PHQLQVLISSSEVKEIKGYKDILVAA 417
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 1-75 1.12e-12

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: 62.79  E-value: 1.12e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568917999     1 MRCLGVPTRVVSNFHSAHNTDGNLTIdtyydrtaemltaqrpdkIWNFHVWNECWMirkdlppgYNGWQVLDPTP 75
Cdd:smart00460  20 LRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYL--------EGGWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 1-73 9.56e-09

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: 52.79  E-value: 9.56e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568917999    1 MRCLGVPTRVVSNFHSAHNTDGNltidtyydrtaemltaqrpdkiWNFHVWNECWMirkdlpPGYnGWQVLDP 73
Cdd:pfam01841  65 LRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYL------PGY-GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 1-74 3.14e-04

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 41.14  E-value: 3.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568917999   1 MRCLGVPTRVVSNFHSAHNTDGNLTIDtyydrtaemltaqrpdkiwNFHVWNECWMirkdlpPGYnGWQVLDPT 74
Cdd:COG1305  127 LRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVYL------PGA-GWVPFDPT 174
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
210-301 8.99e-04

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 38.48  E-value: 8.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568917999  210 APMWGQDLPLMLYVQ---RVPVRDhvqgsvgLTVRFCAQALLHGGGTRKPFWRHIVHLNVDFEKELQWPFLLPYSSY--R 284
Cdd:pfam00927  10 SAVVGQDLTVSVTLSnplSEPLKD-------VVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYgpR 82

                          90       100
                  ....*....|....*....|
gi 568917999  285 DKLTDER---LIRVAGIAEV 301
Cdd:pfam00927  83 QLLVEFSsdaLAKVKGYRNV 102
 
Name Accession Description Interval E-value
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
319-417 7.41e-19

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 81.23  E-value: 7.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568917999  319 PHLSIEVFERAEVGKALDIHITLTNTLMVPLNNCTMVL-----EGSGLINGQMTKDL--GTLMAGHTIRIHLELYPIKAG 391
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAEFKKKSleLTLEPGEEKSVPIKITPSKYG 80

                          90       100
                  ....*....|....*....|....*.
gi 568917999  392 PHQLQVLISSSEVKEIKGYKDILVAA 417
Cdd:pfam00927  81 PRQLLVEFSSDALAKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 1-75 1.12e-12

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: 62.79  E-value: 1.12e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568917999     1 MRCLGVPTRVVSNFHSAHNTDGNLTIdtyydrtaemltaqrpdkIWNFHVWNECWMirkdlppgYNGWQVLDPTP 75
Cdd:smart00460  20 LRSLGIPARVVSGYLKAPDTIGGLRS------------------IWEAHAWAEVYL--------EGGWVPVDPTP 68
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 1-73 9.56e-09

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: 52.79  E-value: 9.56e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568917999    1 MRCLGVPTRVVSNFHSAHNTDGNltidtyydrtaemltaqrpdkiWNFHVWNECWMirkdlpPGYnGWQVLDP 73
Cdd:pfam01841  65 LRALGIPARYVTGYLRGPDTVRG----------------------GDAHAWVEVYL------PGY-GWVPVDP 108
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 1-74 3.14e-04

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 41.14  E-value: 3.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568917999   1 MRCLGVPTRVVSNFHSAHNTDGNLTIDtyydrtaemltaqrpdkiwNFHVWNECWMirkdlpPGYnGWQVLDPT 74
Cdd:COG1305  127 LRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVYL------PGA-GWVPFDPT 174
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
210-301 8.99e-04

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 38.48  E-value: 8.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568917999  210 APMWGQDLPLMLYVQ---RVPVRDhvqgsvgLTVRFCAQALLHGGGTRKPFWRHIVHLNVDFEKELQWPFLLPYSSY--R 284
Cdd:pfam00927  10 SAVVGQDLTVSVTLSnplSEPLKD-------VVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYgpR 82

                          90       100
                  ....*....|....*....|
gi 568917999  285 DKLTDER---LIRVAGIAEV 301
Cdd:pfam00927  83 QLLVEFSsdaLAKVKGYRNV 102
 
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