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Conserved domains on  [gi|2037181015|ref|NP_001381905|]
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nucleolar protein 3 isoform C [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) ...
 5-58 7.91e-11

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: 55.81  E-value: 7.91e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2037181015    5 QERPSETIDRERKRLVETLQADsgLLLDALLARGVLTGPEYEALDALPDAERRA 58
Cdd:smart00114   2 AERDKRLLRRNRVRLGEELGVD--GLLDYLVEKNVLTEKEIEAIKAATTKLRDK 53
metallo-dependent_hydrolases super family cl00281
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 30-115 9.23e-04

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


The actual alignment was detected with superfamily member PRK13404:

Pssm-ID: 469705 [Multi-domain]  Cd Length: 477  Bit Score: 38.91  E-value: 9.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037181015  30 LLDALLARGvLTGPEYEALDALPDAERRAT----------GTAAMTLH---AQATGR-RRHPARGP--HAPGCPELQTLT 93
Cdd:PRK13404  195 LTKRLLAAG-LTAPKYHAISRPMLAEREAThraialaelvDVPILIVHvsgREAAEQiRRARGRGLkiFAETCPQYLFLT 273

                          90       100
                  ....*....|....*....|....*..
gi 2037181015  94 -----RPGALRAPRRCNPGPRRSQSQS 115
Cdd:PRK13404  274 aedldRPGMEGAKYICSPPPRDKANQE 300
 
Name Accession Description Interval E-value
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 5-58 7.91e-11

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: 55.81  E-value: 7.91e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2037181015    5 QERPSETIDRERKRLVETLQADsgLLLDALLARGVLTGPEYEALDALPDAERRA 58
Cdd:smart00114   2 AERDKRLLRRNRVRLGEELGVD--GLLDYLVEKNVLTEKEIEAIKAATTKLRDK 53
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 10-58 1.27e-06

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: 44.47  E-value: 1.27e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2037181015  10 ETIDRERKRLVETLQADSGLLlDALLARGVLTGPEYEALDALPDAERRA 58
Cdd:pfam00619   2 KLLKKNRVALVERLGTLDGLL-DYLLEKNVLTEEEEEKIKANPTRLDKA 49
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 12-58 3.08e-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: 3.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2037181015  12 IDRERKRLVETLQADSglLLDALLARGVLTGPEYEALDALPDAERRA 58
Cdd:cd01671     1 LRKNRVELVEDLDVED--ILDHLIQKGVLTEEDKEEILSEKTRQDKA 45
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 30-115 9.23e-04

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 38.91  E-value: 9.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037181015  30 LLDALLARGvLTGPEYEALDALPDAERRAT----------GTAAMTLH---AQATGR-RRHPARGP--HAPGCPELQTLT 93
Cdd:PRK13404  195 LTKRLLAAG-LTAPKYHAISRPMLAEREAThraialaelvDVPILIVHvsgREAAEQiRRARGRGLkiFAETCPQYLFLT 273

                          90       100
                  ....*....|....*....|....*..
gi 2037181015  94 -----RPGALRAPRRCNPGPRRSQSQS 115
Cdd:PRK13404  274 aedldRPGMEGAKYICSPPPRDKANQE 300
 
Name Accession Description Interval E-value
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 5-58 7.91e-11

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: 55.81  E-value: 7.91e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2037181015    5 QERPSETIDRERKRLVETLQADsgLLLDALLARGVLTGPEYEALDALPDAERRA 58
Cdd:smart00114   2 AERDKRLLRRNRVRLGEELGVD--GLLDYLVEKNVLTEKEIEAIKAATTKLRDK 53
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 10-58 1.27e-06

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: 44.47  E-value: 1.27e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2037181015  10 ETIDRERKRLVETLQADSGLLlDALLARGVLTGPEYEALDALPDAERRA 58
Cdd:pfam00619   2 KLLKKNRVALVERLGTLDGLL-DYLLEKNVLTEEEEEKIKANPTRLDKA 49
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 12-58 3.08e-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: 3.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2037181015  12 IDRERKRLVETLQADSglLLDALLARGVLTGPEYEALDALPDAERRA 58
Cdd:cd01671     1 LRKNRVELVEDLDVED--ILDHLIQKGVLTEEDKEEILSEKTRQDKA 45
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 30-115 9.23e-04

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 38.91  E-value: 9.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037181015  30 LLDALLARGvLTGPEYEALDALPDAERRAT----------GTAAMTLH---AQATGR-RRHPARGP--HAPGCPELQTLT 93
Cdd:PRK13404  195 LTKRLLAAG-LTAPKYHAISRPMLAEREAThraialaelvDVPILIVHvsgREAAEQiRRARGRGLkiFAETCPQYLFLT 273

                          90       100
                  ....*....|....*....|....*..
gi 2037181015  94 -----RPGALRAPRRCNPGPRRSQSQS 115
Cdd:PRK13404  274 aedldRPGMEGAKYICSPPPRDKANQE 300
 
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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