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Conserved domains on  [gi|1408378621|ref|WP_111631205|]
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TIR domain-containing protein [Larkinella arboricola]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
STING_bact-like cd22659
Stimulator Of Interferon Genes (STING) protein in bacteria; This model represents the ...
 164-328 7.41e-30

Stimulator Of Interferon Genes (STING) protein in bacteria; This model represents the bacterial Stimulator Of Interferon Genes (STING) protein that exhibits clear homology to the cyclic-dinucleotide-binding domain of human STING, and represents a newly identified prokaryotic member of the STING family of receptors. Bacterial STING occurs primarily as a fusion to a Toll/interleukin-1 receptor (TIR, or Toll and IL-1 receptor) adaptor domain, or more rarely are appended to predicted transmembrane segments; TIR domains can function as beta-nicotinamide adenine dinucleotide (NAD+) hydrolases in plant and animal immunity. Bacterial STING proteins define a minimal homodimeric scaffold that selectively responds to cyclic di-GMP synthesized by a neighboring cGAS/DncV-like nucleotidyltransferase (CD-NTase) enzyme. They couple the recognition of cyclic dinucleotides with the formation of protein filaments to drive oligomerization of TIR effector domains and rapid NAD+ cleavage. Structures of Flavobacteriaceae sp. STING (FsSTING) and Capnocytophaga granulosa STING (CgSTING) show that the overall architecture is conserved with metazoan STING; they adopt a canonical V-shaped, homodimeric architecture with a hydrophobic alpha-helix stem. However, bacterial STING proteins are 20% smaller and notably compact. Comparative structural analysis shows that metazoan-specific insertions into the core bacterial STING fold have enabled a switch from direct effector function to regulation of antiviral transcription.


:

Pssm-ID: 439311  Cd Length: 155  Bit Score: 111.16  E-value: 7.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621 164 LPSTSLAVGYYYNFLREILEAFNNQKSIQIIlerdrtgkptktidYEIKKPYPTIEIRVPQNLASLKKE--VLTWNTSEY 241
Cdd:cd22659     1 LPSTALAIGYFENFVKPVCEELLENKGIEIG--------------EGFKYKDFKLKIIIPKDLDDDIKLqfELYKKKHGL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621 242 KQIFINAAS-RTYPFFLQGEfKEDQILSIFDIPTTLYASYLTIKELFTDSFLKTQNNERKLINKEIRNFERTLSKLID-D 319
Cdd:cd22659    67 KEISIDTKGgRPYPIYFDID-IKDGKLIIYDFPTTLNGINKAIDLYLPKDFIGKSEDKELLEERELRNFKRTLEYLIKrN 145


                  ....*....
gi 1408378621 320 TIEEKFYKF 328
Cdd:cd22659   146 AYTKEIVEI 154
COG4271 COG4271
Predicted nucleotide-binding protein containing TIR -like domain [General function prediction ...
 10-153 3.80e-28

Predicted nucleotide-binding protein containing TIR -like domain [General function prediction only];


:

Pssm-ID: 443412  Cd Length: 153  Bit Score: 106.91  E-value: 3.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621  10 KAMKPTIFIASsGKSSDIAEAIKLNLDK-EAEVDIWTEnIFQQNEGTLETLMNRASYYDFFIGVFAADDTAIIKKKK--K 86
Cdd:COG4271     4 AEKKRKVFIVH-GRDSLVAEALARLLEKlGLEPIIWNE-QFNAGRTIIEKLEEASDQVDFAIVLMTPDDEGRLRGELvgQ 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1408378621  87 DVTRDNVIFEFGLFLGRIGLDRTFFVLEEGIDLFNDWNGITTSTFTrrdnlTSALGASCIRIKERMK 153
Cdd:COG4271    82 PRARQNVIFELGLFIGRLGRERVLLLKEGGVELPSDLAGVTYIRFD-----GGRIGAWKIELARELK 143
 
Name Accession Description Interval E-value
STING_bact-like cd22659
Stimulator Of Interferon Genes (STING) protein in bacteria; This model represents the ...
 164-328 7.41e-30

Stimulator Of Interferon Genes (STING) protein in bacteria; This model represents the bacterial Stimulator Of Interferon Genes (STING) protein that exhibits clear homology to the cyclic-dinucleotide-binding domain of human STING, and represents a newly identified prokaryotic member of the STING family of receptors. Bacterial STING occurs primarily as a fusion to a Toll/interleukin-1 receptor (TIR, or Toll and IL-1 receptor) adaptor domain, or more rarely are appended to predicted transmembrane segments; TIR domains can function as beta-nicotinamide adenine dinucleotide (NAD+) hydrolases in plant and animal immunity. Bacterial STING proteins define a minimal homodimeric scaffold that selectively responds to cyclic di-GMP synthesized by a neighboring cGAS/DncV-like nucleotidyltransferase (CD-NTase) enzyme. They couple the recognition of cyclic dinucleotides with the formation of protein filaments to drive oligomerization of TIR effector domains and rapid NAD+ cleavage. Structures of Flavobacteriaceae sp. STING (FsSTING) and Capnocytophaga granulosa STING (CgSTING) show that the overall architecture is conserved with metazoan STING; they adopt a canonical V-shaped, homodimeric architecture with a hydrophobic alpha-helix stem. However, bacterial STING proteins are 20% smaller and notably compact. Comparative structural analysis shows that metazoan-specific insertions into the core bacterial STING fold have enabled a switch from direct effector function to regulation of antiviral transcription.


Pssm-ID: 439311  Cd Length: 155  Bit Score: 111.16  E-value: 7.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621 164 LPSTSLAVGYYYNFLREILEAFNNQKSIQIIlerdrtgkptktidYEIKKPYPTIEIRVPQNLASLKKE--VLTWNTSEY 241
Cdd:cd22659     1 LPSTALAIGYFENFVKPVCEELLENKGIEIG--------------EGFKYKDFKLKIIIPKDLDDDIKLqfELYKKKHGL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621 242 KQIFINAAS-RTYPFFLQGEfKEDQILSIFDIPTTLYASYLTIKELFTDSFLKTQNNERKLINKEIRNFERTLSKLID-D 319
Cdd:cd22659    67 KEISIDTKGgRPYPIYFDID-IKDGKLIIYDFPTTLNGINKAIDLYLPKDFIGKSEDKELLEERELRNFKRTLEYLIKrN 145


                  ....*....
gi 1408378621 320 TIEEKFYKF 328
Cdd:cd22659   146 AYTKEIVEI 154
COG4271 COG4271
Predicted nucleotide-binding protein containing TIR -like domain [General function prediction ...
 10-153 3.80e-28

Predicted nucleotide-binding protein containing TIR -like domain [General function prediction only];


Pssm-ID: 443412  Cd Length: 153  Bit Score: 106.91  E-value: 3.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621  10 KAMKPTIFIASsGKSSDIAEAIKLNLDK-EAEVDIWTEnIFQQNEGTLETLMNRASYYDFFIGVFAADDTAIIKKKK--K 86
Cdd:COG4271     4 AEKKRKVFIVH-GRDSLVAEALARLLEKlGLEPIIWNE-QFNAGRTIIEKLEEASDQVDFAIVLMTPDDEGRLRGELvgQ 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1408378621  87 DVTRDNVIFEFGLFLGRIGLDRTFFVLEEGIDLFNDWNGITTSTFTrrdnlTSALGASCIRIKERMK 153
Cdd:COG4271    82 PRARQNVIFELGLFIGRLGRERVLLLKEGGVELPSDLAGVTYIRFD-----GGRIGAWKIELARELK 143
TIR-like pfam10137
Predicted nucleotide-binding protein containing TIR-like domain; Members of this family of ...
 16-131 1.30e-24

Predicted nucleotide-binding protein containing TIR-like domain; Members of this family of bacterial nucleotide-binding proteins contain a TIR-like domain. Their exact function has not, as yet, been defined.


Pssm-ID: 431080  Cd Length: 120  Bit Score: 96.46  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621  16 IFIaSSGKSSDIAEAIKLNLDK-EAEVDIWTENIFQQNEGTLETLMNRASYYDFFIGVFAADD-TAIIKKKKKDVTRDNV 93
Cdd:pfam10137   2 VFI-VHGEDLDAALEVKRFLEKlGLEPIIWHEGTFKGSPTIIEKLEEASSQVDFAIVLFTPDDiVRSRGEELQPRARDNV 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1408378621  94 IFEFGLFLGRIGLDRTFFVLEEGIDLFNDWNGITTSTF 131
Cdd:pfam10137  81 IFELGLFIGKLGRNRVIILRKGGVELPSDLAGITYIRF 118
prok_STING pfam20300
Prokaryotic STING domain; This is a STING sensor domain found in certain prokaryotic ...
 165-313 2.14e-17

Prokaryotic STING domain; This is a STING sensor domain found in certain prokaryotic nucleotide-activated effector conflict systems. Binding to a nucleotide activates fused effector proteins in conflict response against invasive elements. Certain versions in prokaryotes may additionally regulate bacterial ion channels. Transferred to eukaryotes on multiple occasions, representatives observed are in animal-choanoflagellate, haptophyte/stramenopile, and fungal lineages.


Pssm-ID: 466450  Cd Length: 137  Bit Score: 77.38  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621 165 PSTSLAVGYYYNFLREILEafnnqksiQIILERDRTGKPTKTIDYEIKkpyptieIRVPQNL-ASLKKEV-LTWNTSEYK 242
Cdd:pfam20300   1 PSTALAYGYFENFLKPVCR--------HLLKDGGFRIEGLKYEDLKLK-------IVIPDDLsDDLRDDAeVLKRKLGLE 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1408378621 243 QIFINAASRTYPFFLQGEFKEDQILSIFDIPTTLYASYLTIKELFTDSFLKTQNNERKLINKEIRNFERTL 313
Cdd:pfam20300  66 EVKIETGGRPRPFWLRADIDDDGLLILIDFPTTLYALNKAIELLLPKDFNGESSEWERLEERELDNFIRTL 136
 
Name Accession Description Interval E-value
STING_bact-like cd22659
Stimulator Of Interferon Genes (STING) protein in bacteria; This model represents the ...
 164-328 7.41e-30

Stimulator Of Interferon Genes (STING) protein in bacteria; This model represents the bacterial Stimulator Of Interferon Genes (STING) protein that exhibits clear homology to the cyclic-dinucleotide-binding domain of human STING, and represents a newly identified prokaryotic member of the STING family of receptors. Bacterial STING occurs primarily as a fusion to a Toll/interleukin-1 receptor (TIR, or Toll and IL-1 receptor) adaptor domain, or more rarely are appended to predicted transmembrane segments; TIR domains can function as beta-nicotinamide adenine dinucleotide (NAD+) hydrolases in plant and animal immunity. Bacterial STING proteins define a minimal homodimeric scaffold that selectively responds to cyclic di-GMP synthesized by a neighboring cGAS/DncV-like nucleotidyltransferase (CD-NTase) enzyme. They couple the recognition of cyclic dinucleotides with the formation of protein filaments to drive oligomerization of TIR effector domains and rapid NAD+ cleavage. Structures of Flavobacteriaceae sp. STING (FsSTING) and Capnocytophaga granulosa STING (CgSTING) show that the overall architecture is conserved with metazoan STING; they adopt a canonical V-shaped, homodimeric architecture with a hydrophobic alpha-helix stem. However, bacterial STING proteins are 20% smaller and notably compact. Comparative structural analysis shows that metazoan-specific insertions into the core bacterial STING fold have enabled a switch from direct effector function to regulation of antiviral transcription.


Pssm-ID: 439311  Cd Length: 155  Bit Score: 111.16  E-value: 7.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621 164 LPSTSLAVGYYYNFLREILEAFNNQKSIQIIlerdrtgkptktidYEIKKPYPTIEIRVPQNLASLKKE--VLTWNTSEY 241
Cdd:cd22659     1 LPSTALAIGYFENFVKPVCEELLENKGIEIG--------------EGFKYKDFKLKIIIPKDLDDDIKLqfELYKKKHGL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621 242 KQIFINAAS-RTYPFFLQGEfKEDQILSIFDIPTTLYASYLTIKELFTDSFLKTQNNERKLINKEIRNFERTLSKLID-D 319
Cdd:cd22659    67 KEISIDTKGgRPYPIYFDID-IKDGKLIIYDFPTTLNGINKAIDLYLPKDFIGKSEDKELLEERELRNFKRTLEYLIKrN 145


                  ....*....
gi 1408378621 320 TIEEKFYKF 328
Cdd:cd22659   146 AYTKEIVEI 154
STING-like cd22587
C-terminal domain of metazoan Stimulator Of Interferon Genes (STING) protein, bacterial STING, ...
 164-328 6.85e-29

C-terminal domain of metazoan Stimulator Of Interferon Genes (STING) protein, bacterial STING, and similar proteins; This model represents the cytoplasmic ligand-binding domain (LBD, or cyclic-dinucleotide-binding domain) of Stimulator Of Interferon Genes (STING) protein, also called transmembrane protein 173 (TMEM173), mediator of IRF3 activation (MITA), endoplasmic reticulum IFN stimulator (ERIS), or N-terminal methionine-proline-tyrosine-serine plasma membrane tetraspanner (MYSA) of metazoa, as well as STING proteins in bacteria. STING is a receptor that senses foreign cyclic dinucleotides that are released during bacterial infections as well as in endogenous cyclic GMP-AMP (cGAMP) signaling during viral infection and anti-tumor immunity. STING activates downstream transcription factor IRF3 (interferon regulatory factor 3) and STAT (signal transducer and activator of transcription) via TBK1 ((Tank binding kinase 1), which are responsible for antiviral and innate immune response against intracellular pathogens. STING's activation of IRF3 and STAT induces the production of type 1 interferon and target genes involved in immune cell homing such as chemokines, respectively. STING may also function as a direct cytosolic DNA sensor. STING also has a role in B cell adaptive immunity through modulating B cell receptor signaling via PI3K (phosphatidylinositol 3-kinase). STING is encoded by the STING1 gene in mammals. It is an endoplasmic reticulum (ER) membrane protein that contains four transmembrane helices followed by a cytoplasmic ligand-binding and signaling domain. The cytoplasmic domain forms a homodimer, which undergoes conformational changes upon binding to cGAMP. Bacterial STING proteins are functional cyclic dinucleotide receptors and define a minimal homodimeric scaffold that selectively responds to cyclic di-GMP. They couple the recognition of cyclic dinucleotides with the formation of protein filaments to drive oligomerization of TIR effector domains and rapid NAD+ cleavage. Bacterial STING occurs primarily as a fusion to a Toll/interleukin-1 receptor (TIR, or Toll and IL-1 receptor) adaptor domain; TIR domains can function as beta-nicotinamide adenine dinucleotide (NAD+) hydrolases in plant and animal immunity. Bacterial STING homologs are 20% smaller and markedly compact, such that the metazoan insertions into the core bacterial fold are necessary for induction of autophagy, and the C-terminal tail contains motifs for the recruitment of kinases and transcription factors in vertebrates.


Pssm-ID: 439309  Cd Length: 157  Bit Score: 108.86  E-value: 6.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621 164 LPSTSLAVGYYYNFLREILEAFNNQKSIQIIlerdrtgkptktiDYEIKKPYPTIEIRVPQNLASL--KKEVLTWNTSEY 241
Cdd:cd22587     1 LPSTALAIGYYENFLKPVCPELLENKGIENN-------------NEGKKYKDFKLKILIPLDLDDDdkLQFEAYKNIHGL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621 242 KQIFINAAS-RTYPFFLQGEFKEDQILSIFDIPTTLYASYLTIKELFTDSFLKTQNNERKLINKEIRNFERTLSKLID-D 319
Cdd:cd22587    68 KELSIKTKDgRPYPFSIYVDIDNEGKLCILDFPTTLNGLNEAIQLYLPKDFIGKSEDKELLEERELRNFYRTLKYLIErN 147


                  ....*....
gi 1408378621 320 TIEEKFYKF 328
Cdd:cd22587   148 PECRGIVEI 156
COG4271 COG4271
Predicted nucleotide-binding protein containing TIR -like domain [General function prediction ...
 10-153 3.80e-28

Predicted nucleotide-binding protein containing TIR -like domain [General function prediction only];


Pssm-ID: 443412  Cd Length: 153  Bit Score: 106.91  E-value: 3.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621  10 KAMKPTIFIASsGKSSDIAEAIKLNLDK-EAEVDIWTEnIFQQNEGTLETLMNRASYYDFFIGVFAADDTAIIKKKK--K 86
Cdd:COG4271     4 AEKKRKVFIVH-GRDSLVAEALARLLEKlGLEPIIWNE-QFNAGRTIIEKLEEASDQVDFAIVLMTPDDEGRLRGELvgQ 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1408378621  87 DVTRDNVIFEFGLFLGRIGLDRTFFVLEEGIDLFNDWNGITTSTFTrrdnlTSALGASCIRIKERMK 153
Cdd:COG4271    82 PRARQNVIFELGLFIGRLGRERVLLLKEGGVELPSDLAGVTYIRFD-----GGRIGAWKIELARELK 143
TIR-like pfam10137
Predicted nucleotide-binding protein containing TIR-like domain; Members of this family of ...
 16-131 1.30e-24

Predicted nucleotide-binding protein containing TIR-like domain; Members of this family of bacterial nucleotide-binding proteins contain a TIR-like domain. Their exact function has not, as yet, been defined.


Pssm-ID: 431080  Cd Length: 120  Bit Score: 96.46  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621  16 IFIaSSGKSSDIAEAIKLNLDK-EAEVDIWTENIFQQNEGTLETLMNRASYYDFFIGVFAADD-TAIIKKKKKDVTRDNV 93
Cdd:pfam10137   2 VFI-VHGEDLDAALEVKRFLEKlGLEPIIWHEGTFKGSPTIIEKLEEASSQVDFAIVLFTPDDiVRSRGEELQPRARDNV 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1408378621  94 IFEFGLFLGRIGLDRTFFVLEEGIDLFNDWNGITTSTF 131
Cdd:pfam10137  81 IFELGLFIGKLGRNRVIILRKGGVELPSDLAGITYIRF 118
prok_STING pfam20300
Prokaryotic STING domain; This is a STING sensor domain found in certain prokaryotic ...
 165-313 2.14e-17

Prokaryotic STING domain; This is a STING sensor domain found in certain prokaryotic nucleotide-activated effector conflict systems. Binding to a nucleotide activates fused effector proteins in conflict response against invasive elements. Certain versions in prokaryotes may additionally regulate bacterial ion channels. Transferred to eukaryotes on multiple occasions, representatives observed are in animal-choanoflagellate, haptophyte/stramenopile, and fungal lineages.


Pssm-ID: 466450  Cd Length: 137  Bit Score: 77.38  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408378621 165 PSTSLAVGYYYNFLREILEafnnqksiQIILERDRTGKPTKTIDYEIKkpyptieIRVPQNL-ASLKKEV-LTWNTSEYK 242
Cdd:pfam20300   1 PSTALAYGYFENFLKPVCR--------HLLKDGGFRIEGLKYEDLKLK-------IVIPDDLsDDLRDDAeVLKRKLGLE 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1408378621 243 QIFINAASRTYPFFLQGEFKEDQILSIFDIPTTLYASYLTIKELFTDSFLKTQNNERKLINKEIRNFERTL 313
Cdd:pfam20300  66 EVKIETGGRPRPFWLRADIDDDGLLILIDFPTTLYALNKAIELLLPKDFNGESSEWERLEERELDNFIRTL 136
 
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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