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Conserved domains on  [gi|1907066808|ref|XP_036021571|]
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myeloid cell nuclear differentiation antigen-like protein isoform X1 [Mus musculus]

Protein Classification

protein kinase family protein( domain architecture ID 10169747)

protein kinase family protein containing a Death domain (DD), may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates

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 ...
 311-479 1.06e-90

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: 275.24  E-value: 1.06e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066808 311 HSEPLTVMVLTATDPFEYESPEHEvKNMFHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVL 390
Cdd:pfam02760   1 QKGPKEVMVLKATEPFEYESQEGK-KKMFHATVATESEFFRVKVFNINLKEKFIPKKVIAISDYFGRNGFLEVNEASSVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066808 391 KADPDQMIEVPNNIIRNANASPKICDIQKGTSGAVFYGVFTLHKKKVKTQNTSYEIKDGSGSIEVEGSGQWHNINCKEGD 470
Cdd:pfam02760  80 EAGPDQKMEVPKSIIRKANETPKINKLKKQPSGTIVNGLFTVHKKTVNKKNTIYEIQDNTGKMEVVVYGKLTNIKCEEGD 159


                  ....*....
gi 1907066808 471 KLHLFCFHL 479
Cdd:pfam02760 160 KLRLFCFEL 168
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 9-82 1.58e-27

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: 105.08  E-value: 1.58e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907066808   9 LLKGLESMEDYQFRTVKSLLRKELKLTKKLQEDYDRIQLADWMEDKFPKYAGLDKLIKVCEHIKdLKDLAKKLK 82
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 ...
 311-479 1.06e-90

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: 275.24  E-value: 1.06e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066808 311 HSEPLTVMVLTATDPFEYESPEHEvKNMFHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVL 390
Cdd:pfam02760   1 QKGPKEVMVLKATEPFEYESQEGK-KKMFHATVATESEFFRVKVFNINLKEKFIPKKVIAISDYFGRNGFLEVNEASSVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066808 391 KADPDQMIEVPNNIIRNANASPKICDIQKGTSGAVFYGVFTLHKKKVKTQNTSYEIKDGSGSIEVEGSGQWHNINCKEGD 470
Cdd:pfam02760  80 EAGPDQKMEVPKSIIRKANETPKINKLKKQPSGTIVNGLFTVHKKTVNKKNTIYEIQDNTGKMEVVVYGKLTNIKCEEGD 159


                  ....*....
gi 1907066808 471 KLHLFCFHL 479
Cdd:pfam02760 160 KLRLFCFEL 168
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 9-82 1.58e-27

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: 105.08  E-value: 1.58e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907066808   9 LLKGLESMEDYQFRTVKSLLRKELKLTKKLQEDYDRIQLADWMEDKFPKYAGLDKLIKVCEHIKdLKDLAKKLK 82
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 ...
 9-79 1.20e-11

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: 60.30  E-value: 1.20e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907066808   9 LLKGLESMEDYQFRTVKSLLRKE-----LKLTKKLQEDYDRIQLADWMEDKFPKYAGLDKLIKVCEHIKdLKDLAK 79
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEpeeglRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKIN-LKDLAE 76
PHA03058 PHA03058
Hypothetical protein; Provisional
 13-130 5.00e-03

Hypothetical protein; Provisional


Pssm-ID: 222966  Cd Length: 124  Bit Score: 37.08  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066808  13 LESMEDYQFRTVKSLLRKELKLTKKLQEDYDRIQLADWMEDKFPKYAGLDKLIKVCEHIKDLKDLAKKLK--TEKAKVQK 90
Cdd:PHA03058   11 LENLTDYQFKMLIFLTQDDLNIEEEEKEKLDRIDLAEKISEKYPGIRSIYFLKKVISEIPNTEYVDSLLSraIKDFNVTD 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907066808  91 KKQGKCKTAVKKKGqdelsssesLFINKESYKSVPSSKKK 130
Cdd:PHA03058   91 VTFGKVQKTIKRKH---------RFRNPKVLKNLSSSERR 121
 
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 ...
 311-479 1.06e-90

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: 275.24  E-value: 1.06e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066808 311 HSEPLTVMVLTATDPFEYESPEHEvKNMFHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVL 390
Cdd:pfam02760   1 QKGPKEVMVLKATEPFEYESQEGK-KKMFHATVATESEFFRVKVFNINLKEKFIPKKVIAISDYFGRNGFLEVNEASSVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066808 391 KADPDQMIEVPNNIIRNANASPKICDIQKGTSGAVFYGVFTLHKKKVKTQNTSYEIKDGSGSIEVEGSGQWHNINCKEGD 470
Cdd:pfam02760  80 EAGPDQKMEVPKSIIRKANETPKINKLKKQPSGTIVNGLFTVHKKTVNKKNTIYEIQDNTGKMEVVVYGKLTNIKCEEGD 159


                  ....*....
gi 1907066808 471 KLHLFCFHL 479
Cdd:pfam02760 160 KLRLFCFEL 168
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 9-82 1.58e-27

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: 105.08  E-value: 1.58e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907066808   9 LLKGLESMEDYQFRTVKSLLRKELKLTKKLQEDYDRIQLADWMEDKFPKYAGLDKLIKVCEHIKdLKDLAKKLK 82
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 ...
 9-79 1.20e-11

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: 60.30  E-value: 1.20e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907066808   9 LLKGLESMEDYQFRTVKSLLRKE-----LKLTKKLQEDYDRIQLADWMEDKFPKYAGLDKLIKVCEHIKdLKDLAK 79
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEpeeglRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKIN-LKDLAE 76
PHA03058 PHA03058
Hypothetical protein; Provisional
 13-130 5.00e-03

Hypothetical protein; Provisional


Pssm-ID: 222966  Cd Length: 124  Bit Score: 37.08  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066808  13 LESMEDYQFRTVKSLLRKELKLTKKLQEDYDRIQLADWMEDKFPKYAGLDKLIKVCEHIKDLKDLAKKLK--TEKAKVQK 90
Cdd:PHA03058   11 LENLTDYQFKMLIFLTQDDLNIEEEEKEKLDRIDLAEKISEKYPGIRSIYFLKKVISEIPNTEYVDSLLSraIKDFNVTD 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907066808  91 KKQGKCKTAVKKKGqdelsssesLFINKESYKSVPSSKKK 130
Cdd:PHA03058   91 VTFGKVQKTIKRKH---------RFRNPKVLKNLSSSERR 121
 
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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