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Conserved domains on  [gi|755495471|ref|XP_011237064|]
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interferon-activable protein 203 isoform X2 [Mus musculus]

Protein Classification

Pyrin and HIN domain-containing protein( domain architecture ID 10169747)

protein containing domains Pyrin, DUF5585, and HIN

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HIN pfam02760
HIN-200/IF120x domain; This domain has no know function. It is found in one or two copies per ...
 665-831 5.60e-93

HIN-200/IF120x domain; This domain has no know function. It is found in one or two copies per protein, and is found associated with the PAAD/DAPIN domain pfam02758.


:

Pssm-ID: 460680  Cd Length: 168  Bit Score: 289.88  E-value: 5.60e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495471  665 HQGPKQVMVLKVTEPFTYDF-EETKRMFHATVATETEFFRVKVFDTALMSKFIPGKIIAISHYIGCNGFLEIYRASCVSD 743
Cdd:pfam02760   1 QKGPKEVMVLKATEPFEYESqEGKKKMFHATVATESEFFRVKVFNINLKEKFIPKKVIAISDYFGRNGFLEVNEASSVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495471  744 VNINPTMIISNTLSESAIATPKISYLLSQAKGTFVNGEFVVFKKSERHECICYGIGDDTGKMAVVVYGRLTNVRCEPGSK 823
Cdd:pfam02760  81 AGPDQKMEVPKSIIRKANETPKINKLKKQPSGTIVNGLFTVHKKTVNKKNTIYEIQDNTGKMEVVVYGKLTNIKCEEGDK 160


                  ....*...
gi 755495471  824 LRLVCFEL 831
Cdd:pfam02760 161 LRLFCFEL 168
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 10-83 1.81e-32

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260019  Cd Length: 73  Bit Score: 120.10  E-value: 1.81e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495471  10 LLKGLENMEDYQFRTVKSLLRKELKLTKKMQEDYDRIQLADWIEDKFPKDAGLDKLIKVCEHIKdLKDLAKKLK 83
Cdd:cd08305    1 LLTGLENITDEEFKMFKSLLASELKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMP-LRSLANQLQ 73
 
Name Accession Description Interval E-value
HIN pfam02760
HIN-200/IF120x domain; This domain has no know function. It is found in one or two copies per ...
 665-831 5.60e-93

HIN-200/IF120x domain; This domain has no know function. It is found in one or two copies per protein, and is found associated with the PAAD/DAPIN domain pfam02758.


Pssm-ID: 460680  Cd Length: 168  Bit Score: 289.88  E-value: 5.60e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495471  665 HQGPKQVMVLKVTEPFTYDF-EETKRMFHATVATETEFFRVKVFDTALMSKFIPGKIIAISHYIGCNGFLEIYRASCVSD 743
Cdd:pfam02760   1 QKGPKEVMVLKATEPFEYESqEGKKKMFHATVATESEFFRVKVFNINLKEKFIPKKVIAISDYFGRNGFLEVNEASSVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495471  744 VNINPTMIISNTLSESAIATPKISYLLSQAKGTFVNGEFVVFKKSERHECICYGIGDDTGKMAVVVYGRLTNVRCEPGSK 823
Cdd:pfam02760  81 AGPDQKMEVPKSIIRKANETPKINKLKKQPSGTIVNGLFTVHKKTVNKKNTIYEIQDNTGKMEVVVYGKLTNIKCEEGDK 160


                  ....*...
gi 755495471  824 LRLVCFEL 831
Cdd:pfam02760 161 LRLFCFEL 168
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 10-83 1.81e-32

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260019  Cd Length: 73  Bit Score: 120.10  E-value: 1.81e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495471  10 LLKGLENMEDYQFRTVKSLLRKELKLTKKMQEDYDRIQLADWIEDKFPKDAGLDKLIKVCEHIKdLKDLAKKLK 83
Cdd:cd08305    1 LLTGLENITDEEFKMFKSLLASELKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMP-LRSLANQLQ 73
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-80 1.94e-13

PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the same fold as the pfam00531 domain. This similarity may mean that this is a protein-protein interaction domain.


Pssm-ID: 460678  Cd Length: 76  Bit Score: 66.07  E-value: 1.94e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755495471   10 LLKGLENMEDYQFRTVKSLLRKELKL------TKKMqEDYDRIQLADWIEDKFPKDAGLDKLIKVCEHIKdLKDLAK 80
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEPEEglrsipRGKL-EKADRLDLADLLVEHYGEDAAVDVTIEILKKIN-LKDLAE 76
PHA03058 PHA03058
Hypothetical protein; Provisional
 14-132 1.43e-05

Hypothetical protein; Provisional


Pssm-ID: 222966  Cd Length: 124  Bit Score: 45.17  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495471  14 LENMEDYQFRTVKSLLRKELKLTKKMQEDYDRIQLADWIEDKFPKDAGLDKLIKVCEHIKDLKDLAKKLKTEKAKVQKKK 93
Cdd:PHA03058  11 LENLTDYQFKMLIFLTQDDLNIEEEEKEKLDRIDLAEKISEKYPGIRSIYFLKKVISEIPNTEYVDSLLSRAIKDFNVTD 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755495471  94 EGKCKTAGKKKGQDelsssesLFNNKESNKSVPSSKKKR 132
Cdd:PHA03058  91 VTFGKVQKTIKRKH-------RFRNPKVLKNLSSSERRK 122
 
Name Accession Description Interval E-value
HIN pfam02760
HIN-200/IF120x domain; This domain has no know function. It is found in one or two copies per ...
 665-831 5.60e-93

HIN-200/IF120x domain; This domain has no know function. It is found in one or two copies per protein, and is found associated with the PAAD/DAPIN domain pfam02758.


Pssm-ID: 460680  Cd Length: 168  Bit Score: 289.88  E-value: 5.60e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495471  665 HQGPKQVMVLKVTEPFTYDF-EETKRMFHATVATETEFFRVKVFDTALMSKFIPGKIIAISHYIGCNGFLEIYRASCVSD 743
Cdd:pfam02760   1 QKGPKEVMVLKATEPFEYESqEGKKKMFHATVATESEFFRVKVFNINLKEKFIPKKVIAISDYFGRNGFLEVNEASSVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495471  744 VNINPTMIISNTLSESAIATPKISYLLSQAKGTFVNGEFVVFKKSERHECICYGIGDDTGKMAVVVYGRLTNVRCEPGSK 823
Cdd:pfam02760  81 AGPDQKMEVPKSIIRKANETPKINKLKKQPSGTIVNGLFTVHKKTVNKKNTIYEIQDNTGKMEVVVYGKLTNIKCEEGDK 160


                  ....*...
gi 755495471  824 LRLVCFEL 831
Cdd:pfam02760 161 LRLFCFEL 168
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 10-83 1.81e-32

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260019  Cd Length: 73  Bit Score: 120.10  E-value: 1.81e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495471  10 LLKGLENMEDYQFRTVKSLLRKELKLTKKMQEDYDRIQLADWIEDKFPKDAGLDKLIKVCEHIKdLKDLAKKLK 83
Cdd:cd08305    1 LLTGLENITDEEFKMFKSLLASELKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMP-LRSLANQLQ 73
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-80 1.94e-13

PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the same fold as the pfam00531 domain. This similarity may mean that this is a protein-protein interaction domain.


Pssm-ID: 460678  Cd Length: 76  Bit Score: 66.07  E-value: 1.94e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755495471   10 LLKGLENMEDYQFRTVKSLLRKELKL------TKKMqEDYDRIQLADWIEDKFPKDAGLDKLIKVCEHIKdLKDLAK 80
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEPEEglrsipRGKL-EKADRLDLADLLVEHYGEDAAVDVTIEILKKIN-LKDLAE 76
PHA03058 PHA03058
Hypothetical protein; Provisional
 14-132 1.43e-05

Hypothetical protein; Provisional


Pssm-ID: 222966  Cd Length: 124  Bit Score: 45.17  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495471  14 LENMEDYQFRTVKSLLRKELKLTKKMQEDYDRIQLADWIEDKFPKDAGLDKLIKVCEHIKDLKDLAKKLKTEKAKVQKKK 93
Cdd:PHA03058  11 LENLTDYQFKMLIFLTQDDLNIEEEEKEKLDRIDLAEKISEKYPGIRSIYFLKKVISEIPNTEYVDSLLSRAIKDFNVTD 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755495471  94 EGKCKTAGKKKGQDelsssesLFNNKESNKSVPSSKKKR 132
Cdd:PHA03058  91 VTFGKVQKTIKRKH-------RFRNPKVLKNLSSSERRK 122
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 10-83 9.61e-04

Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated speck-like protein containing a CARD) and similar proteins. ASC is an adaptor molecule that functions in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. ASC contains two domains from the Death Domain (DD) superfamily, an N-terminal pyrin-like domain and a C-terminal Caspase activation and recruitment domain (CARD). Through these 2 domains, ASC serves as an adaptor for inflammasome integrity and oligomerizes to form supramolecular assemblies. Included in this family is human PYNOD (also known as NLRP10 or NOD8) which via its Pyrin domain suppresses oligomerization of ASC, and ASC-mediated NF-kappaB activation. Other members of this subfamily are associated with ATPase domains and their function remains unknown. In general, Pyrin is a subfamily of the DD superfamily and functions in several signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260033  Cd Length: 82  Bit Score: 38.66  E-value: 9.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495471  10 LLKGLENMEDYQFRTVKSllrkelKLTKKMQEDY-----------DRIQLADWIEDKFPKDAGLDKLIKVCEHIkDLKDL 78
Cdd:cd08321    4 LLDALEDLGEEELKKFKW------KLRDIPLEGYpriprgklenaDRVDLVDLLVSYYGEDYAVEVTVEVLRAI-NQNDL 76


                 ....*
gi 755495471  79 AKKLK 83
Cdd:cd08321   77 AEKLQ 81
W2_eIF4G1_like cd11559
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar ...
 28-91 6.40e-03

C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar proteins; eIF4G1 is a component of the multi-subunit eukaryotic translation initiation factor 4F, which facilitates recruitment of the mRNA to the ribosome, a rate-limiting step during translation initiation. This C-terminal domain, whose structure resembles that of a set of concatenated HEAT repeats, has been associated with binding to/recruiting the kinase Mnk1, which phosphorylates eIF4E.


Pssm-ID: 211397  Cd Length: 134  Bit Score: 37.65  E-value: 6.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495471  28 LLRKELKLTKKMQEDYDRIQLADWIEDKF-PKDAGLDKLIK-----VCEHIKDLKDLAKKLKTEKAKVQK 91
Cdd:cd11559    3 LLRVQAELLKLLQEDPNPDELYKWIKENVsPELYASPGFVRalmtaVLKYAIEEKSLPEKEKALLEKYAP 72
 
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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