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Conserved domains on  [gi|297632352|ref|NP_001171986|]
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nucleolar protein 3 isoform Nop30 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 5-92 1.53e-14

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. 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. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


The actual alignment was detected with superfamily member smart00114:

Pssm-ID: 472698  Cd Length: 88  Bit Score: 66.59  E-value: 1.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297632352     5 QERPSETIDRERKRLVETLQADsgLLLDALLARGVLTGPEYEALDALPDAERRVRRLLLLVQGKGEAACQELLRCAQRT- 83
Cdd:smart00114   2 AERDKRLLRRNRVRLGEELGVD--GLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQETd 79


                   ....*....
gi 297632352    84 AGAPDPAWD 92
Cdd:smart00114  80 QKLADFLEL 88
 
Name Accession Description Interval E-value
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 5-92 1.53e-14

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 66.59  E-value: 1.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297632352     5 QERPSETIDRERKRLVETLQADsgLLLDALLARGVLTGPEYEALDALPDAERRVRRLLLLVQGKGEAACQELLRCAQRT- 83
Cdd:smart00114   2 AERDKRLLRRNRVRLGEELGVD--GLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQETd 79


                   ....*....
gi 297632352    84 AGAPDPAWD 92
Cdd:smart00114  80 QKLADFLEL 88
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 10-95 1.36e-09

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 52.95  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297632352   10 ETIDRERKRLVETLQADSGLLlDALLARGVLTGPEYEALDALPDAERRVRRLLLLVQGKGEAACQELLRCAQRtaGAPDP 89
Cdd:pfam00619   2 KLLKKNRVALVERLGTLDGLL-DYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE--GDPDL 78


                  ....*.
gi 297632352   90 AWDWQH 95
Cdd:pfam00619  79 ASDLEG 84
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 12-83 3.67e-04

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 37.88  E-value: 3.67e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297632352  12 IDRERKRLVETLQADSglLLDALLARGVLTGPEYEALDALPDAERRVRRLLLLVQGKGEAACQELLRCAQRT 83
Cdd:cd01671    1 LRKNRVELVEDLDVED--ILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRET 70
 
Name Accession Description Interval E-value
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 5-92 1.53e-14

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 66.59  E-value: 1.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297632352     5 QERPSETIDRERKRLVETLQADsgLLLDALLARGVLTGPEYEALDALPDAERRVRRLLLLVQGKGEAACQELLRCAQRT- 83
Cdd:smart00114   2 AERDKRLLRRNRVRLGEELGVD--GLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQETd 79


                   ....*....
gi 297632352    84 AGAPDPAWD 92
Cdd:smart00114  80 QKLADFLEL 88
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 10-95 1.36e-09

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 52.95  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297632352   10 ETIDRERKRLVETLQADSGLLlDALLARGVLTGPEYEALDALPDAERRVRRLLLLVQGKGEAACQELLRCAQRtaGAPDP 89
Cdd:pfam00619   2 KLLKKNRVALVERLGTLDGLL-DYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE--GDPDL 78


                  ....*.
gi 297632352   90 AWDWQH 95
Cdd:pfam00619  79 ASDLEG 84
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 12-83 3.67e-04

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 37.88  E-value: 3.67e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297632352  12 IDRERKRLVETLQADSglLLDALLARGVLTGPEYEALDALPDAERRVRRLLLLVQGKGEAACQELLRCAQRT 83
Cdd:cd01671    1 LRKNRVELVEDLDVED--ILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRET 70
 
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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