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Conserved domains on  [gi|1703311|sp|P52183|]
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RecName: Full=Annulin; AltName: Full=Protein-glutamine gamma-glutamyltransferase; AltName: Full=Transglutaminase

Protein Classification

Transglut_N and TGc domain-containing protein (domain architecture ID 10467673)

protein containing domains Transglut_N, TGc, and Transglut_C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
66-191 3.20e-39

Transglutaminase family;


:

Pssm-ID: 334292  Cd Length: 117  Bit Score: 140.74  E-value: 3.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311     66 SVKEVDVLLAENGDAHRTRHYELmdrekePRLVVRRGQPFAVSVTLSRPYNPDIDAISFVFTVedAEKPSYGQGTLVAVP 145
Cdd:pfam00868   2 EVKSVDLQKEENNKEHHTDEYES------DRLIVRRGQPFTITLTFNRPFDPSKDKLRLEFET--GPNPSESKGTKAVFP 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1703311    146 LLAKGAESGaaWNAVLDSSADDILRIQITPAADAIVGKWKMDIDTK 191
Cdd:pfam00868  74 LSSSRDPSG--WSARVVESSGNSLTVSVTSPANAPIGRYRLTVETS 117
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
335-430 6.29e-23

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 [Multi-domain]  Cd Length: 68  Bit Score: 92.45  E-value: 6.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311     335 PVKYGQCWVFAGVLTTVCRALGLPARTVTTYSAAHDTQNSLTvdyfvddkgeimeemnsdSIWNFHVWTEVWMErpdlmp 414
Cdd:smart00460   3 KTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE------ 58
                           90
                   ....*....|....*.
gi 1703311     415 gdgahyGGWQAVDSTP 430
Cdd:smart00460  59 ------GGWVPVDPTP 68
Transglut_C super family cl08295
Transglutaminase family, C-terminal ig like domain;
549-655 1.72e-17

Transglutaminase family, C-terminal ig like domain;


The actual alignment was detected with superfamily member pfam00927:

Pssm-ID: 307191  Cd Length: 106  Bit Score: 78.15  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311    549 IHFNFELRDDIVIGSPFSVVVVMKNRSNQQDYTVTVLLRVDTVLYTGHVKDGVKKEKVERLIKAGAVEEVRIDVSYEDY- 627
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYg 80
                          90       100
                  ....*....|....*....|....*....
gi 1703311    628 -YKHLVDqcaFNIACLATVHDTNYEYFAQ 655
Cdd:pfam00927  81 lRQLLVE---FSSDALKKVKGYRNVLVAQ 106
Transglut_C super family cl08295
Transglutaminase family, C-terminal ig like domain;
663-761 1.10e-12

Transglutaminase family, C-terminal ig like domain;


The actual alignment was detected with superfamily member pfam00927:

Pssm-ID: 307191  Cd Length: 106  Bit Score: 64.66  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311    663 PDIKIKLEGEPVQGQEMSAVATLKNPLPIPVKKGQFLI-----EGPGI--AKTQKIKLSQNIAPGEEASVNFKFTPKYDG 735
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVlgAEFKKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 1703311    736 RATIAAKFSSKELDDVDGFLNFMVEP 761
Cdd:pfam00927  81 LRQLLVEFSSDALKKVKGYRNVLVAQ 106
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
66-191 3.20e-39

Transglutaminase family;


Pssm-ID: 334292  Cd Length: 117  Bit Score: 140.74  E-value: 3.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311     66 SVKEVDVLLAENGDAHRTRHYELmdrekePRLVVRRGQPFAVSVTLSRPYNPDIDAISFVFTVedAEKPSYGQGTLVAVP 145
Cdd:pfam00868   2 EVKSVDLQKEENNKEHHTDEYES------DRLIVRRGQPFTITLTFNRPFDPSKDKLRLEFET--GPNPSESKGTKAVFP 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1703311    146 LLAKGAESGaaWNAVLDSSADDILRIQITPAADAIVGKWKMDIDTK 191
Cdd:pfam00868  74 LSSSRDPSG--WSARVVESSGNSLTVSVTSPANAPIGRYRLTVETS 117
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
335-430 6.29e-23

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 [Multi-domain]  Cd Length: 68  Bit Score: 92.45  E-value: 6.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311     335 PVKYGQCWVFAGVLTTVCRALGLPARTVTTYSAAHDTQNSLTvdyfvddkgeimeemnsdSIWNFHVWTEVWMErpdlmp 414
Cdd:smart00460   3 KTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE------ 58
                           90
                   ....*....|....*.
gi 1703311     415 gdgahyGGWQAVDSTP 430
Cdd:smart00460  59 ------GGWVPVDPTP 68
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
549-655 1.72e-17

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 78.15  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311    549 IHFNFELRDDIVIGSPFSVVVVMKNRSNQQDYTVTVLLRVDTVLYTGHVKDGVKKEKVERLIKAGAVEEVRIDVSYEDY- 627
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYg 80
                          90       100
                  ....*....|....*....|....*....
gi 1703311    628 -YKHLVDqcaFNIACLATVHDTNYEYFAQ 655
Cdd:pfam00927  81 lRQLLVE---FSSDALKKVKGYRNVLVAQ 106
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
337-427 1.00e-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: 334704  Cd Length: 108  Bit Score: 67.81  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311    337 KYGQCWVFAGVLTTVCRALGLPARTVTTYSAAHDTqnsltvdyfvddkgeimeemnsDSIWNFHVWTEVWMErpdlmpgd 416
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDT----------------------VRGGDAHAWVEVYLP-------- 99
                          90
                  ....*....|.
gi 1703311    417 gahYGGWQAVD 427
Cdd:pfam01841 100 ---GYGWVPVD 107
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
663-761 1.10e-12

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 64.66  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311    663 PDIKIKLEGEPVQGQEMSAVATLKNPLPIPVKKGQFLI-----EGPGI--AKTQKIKLSQNIAPGEEASVNFKFTPKYDG 735
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVlgAEFKKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 1703311    736 RATIAAKFSSKELDDVDGFLNFMVEP 761
Cdd:pfam00927  81 LRQLLVEFSSDALKKVKGYRNVLVAQ 106
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
337-438 2.24e-06

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


Pssm-ID: 224224 [Multi-domain]  Cd Length: 319  Bit Score: 50.05  E-value: 2.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311  337 KYGQCWVFAGVLTTVCRALGLPARTVTTYSAAhdtqnslTVDYFVDDKGEImeemnsdsIWNFHVWTEVWMERpdlmpgd 416
Cdd:COG1305 193 GRGVCRDFAHLLVALLRAAGIPARYVSGYLGA-------EVEPLSGRPLVR--------NDDAHAWAEVYLPG------- 250
                        90       100
                ....*....|....*....|..
gi 1703311  417 gahyGGWQAVDSTPQELSDNMY 438
Cdd:COG1305 251 ----RGWVPLDPTNGLLAGGRY 268
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
66-191 3.20e-39

Transglutaminase family;


Pssm-ID: 334292  Cd Length: 117  Bit Score: 140.74  E-value: 3.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311     66 SVKEVDVLLAENGDAHRTRHYELmdrekePRLVVRRGQPFAVSVTLSRPYNPDIDAISFVFTVedAEKPSYGQGTLVAVP 145
Cdd:pfam00868   2 EVKSVDLQKEENNKEHHTDEYES------DRLIVRRGQPFTITLTFNRPFDPSKDKLRLEFET--GPNPSESKGTKAVFP 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1703311    146 LLAKGAESGaaWNAVLDSSADDILRIQITPAADAIVGKWKMDIDTK 191
Cdd:pfam00868  74 LSSSRDPSG--WSARVVESSGNSLTVSVTSPANAPIGRYRLTVETS 117
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
335-430 6.29e-23

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 [Multi-domain]  Cd Length: 68  Bit Score: 92.45  E-value: 6.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311     335 PVKYGQCWVFAGVLTTVCRALGLPARTVTTYSAAHDTQNSLTvdyfvddkgeimeemnsdSIWNFHVWTEVWMErpdlmp 414
Cdd:smart00460   3 KTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE------ 58
                           90
                   ....*....|....*.
gi 1703311     415 gdgahyGGWQAVDSTP 430
Cdd:smart00460  59 ------GGWVPVDPTP 68
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
549-655 1.72e-17

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 78.15  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311    549 IHFNFELRDDIVIGSPFSVVVVMKNRSNQQDYTVTVLLRVDTVLYTGHVKDGVKKEKVERLIKAGAVEEVRIDVSYEDY- 627
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYg 80
                          90       100
                  ....*....|....*....|....*....
gi 1703311    628 -YKHLVDqcaFNIACLATVHDTNYEYFAQ 655
Cdd:pfam00927  81 lRQLLVE---FSSDALKKVKGYRNVLVAQ 106
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
337-427 1.00e-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: 334704  Cd Length: 108  Bit Score: 67.81  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311    337 KYGQCWVFAGVLTTVCRALGLPARTVTTYSAAHDTqnsltvdyfvddkgeimeemnsDSIWNFHVWTEVWMErpdlmpgd 416
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDT----------------------VRGGDAHAWVEVYLP-------- 99
                          90
                  ....*....|.
gi 1703311    417 gahYGGWQAVD 427
Cdd:pfam01841 100 ---GYGWVPVD 107
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
663-761 1.10e-12

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 64.66  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311    663 PDIKIKLEGEPVQGQEMSAVATLKNPLPIPVKKGQFLI-----EGPGI--AKTQKIKLSQNIAPGEEASVNFKFTPKYDG 735
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVlgAEFKKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 1703311    736 RATIAAKFSSKELDDVDGFLNFMVEP 761
Cdd:pfam00927  81 LRQLLVEFSSDALKKVKGYRNVLVAQ 106
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
337-438 2.24e-06

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


Pssm-ID: 224224 [Multi-domain]  Cd Length: 319  Bit Score: 50.05  E-value: 2.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703311  337 KYGQCWVFAGVLTTVCRALGLPARTVTTYSAAhdtqnslTVDYFVDDKGEImeemnsdsIWNFHVWTEVWMERpdlmpgd 416
Cdd:COG1305 193 GRGVCRDFAHLLVALLRAAGIPARYVSGYLGA-------EVEPLSGRPLVR--------NDDAHAWAEVYLPG------- 250
                        90       100
                ....*....|....*....|..
gi 1703311  417 gahyGGWQAVDSTPQELSDNMY 438
Cdd:COG1305 251 ----RGWVPLDPTNGLLAGGRY 268
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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