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Conserved domains on  [gi|568923597|ref|XP_006501928|]
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small ribosomal subunit protein mS29 isoform X3 [Mus musculus]

Protein Classification

DEAD/DEAH box helicase family protein( domain architecture ID 1000205)

DEAD/DEAH box helicase family protein such as a DEAD/DEAH box-containing ATP-dependent helicase, which catalyzes the unwinding of DNA or RNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
97-339 4.52e-88

N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.


The actual alignment was detected with superfamily member pfam10236:

Pssm-ID: 475120  Cd Length: 310  Bit Score: 266.86  E-value: 4.52e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923597   97 LMVRKPALELLGYLKNTNFAHPAVRYLLYGEKGTGKTLSLCHAVHFCARHDWLILHIPDAHLWVKNCRELLQSTHNKQRF 176
Cdd:pfam10236   1 LLVREETLELIKKLKAADKSKKVVRFVLTGEPGSGKSVLLLQAMAYALEKGWVVLHVPEAELWVNGTTDYAPDESNPKLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923597  177 DQPLEASTWLKNFKTTNERFLSQIKVQEKYVWNKRESTEKGSPLGEVVEQ------------------------------ 226
Cdd:pfam10236  81 DQPMYTAALLRRIKKANEPVLSKIKLSQDYEWLKRESTPAGSTLLELLSLginransawdvfqalwkeltaqskrppvlv 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923597  227 ---------------------IAPEELSLVHNLRKMV--KNDWHGGAIVLSLSQTGSLFKSRTAYLPHELLGKEGFNALE 283
Cdd:pfam10236 161 avdgfnalmgntaykdadfkpIHPHDLTLVRHFLDLLsgKSDFPNGGVVTVLAATSSSNTPRSPTLPIALLQEEARPQLD 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568923597  284 PFL---------------PILIPNYNPKEFESSFQYYLENNWLQHeKASTEEGRKELRFLSNCNPEQLERL 339
Cdd:pfam10236 241 PYVkrydyvleakkgsvePFRVPGLTKEEARGLMEYYADSGWLQE-KVNEELVDEKLFLSGNGNPRELEKL 310
 
Name Accession Description Interval E-value
DAP3 pfam10236
Mitochondrial ribosomal death-associated protein 3; This is a family of conserved proteins ...
97-339 4.52e-88

Mitochondrial ribosomal death-associated protein 3; This is a family of conserved proteins which were originally described as death-associated-protein-3 (DAP-3). The proteins carry a P-loop DNA-binding motif, and induce apoptosis. DAP3 has been shown to be a pro-apoptotic factor in the mitochondrial matrix and to be crucial for mitochondrial biogenesis and so has also been designated as MRP-S29 (mitochondrial ribosomal protein subunit 29).


Pssm-ID: 431160  Cd Length: 310  Bit Score: 266.86  E-value: 4.52e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923597   97 LMVRKPALELLGYLKNTNFAHPAVRYLLYGEKGTGKTLSLCHAVHFCARHDWLILHIPDAHLWVKNCRELLQSTHNKQRF 176
Cdd:pfam10236   1 LLVREETLELIKKLKAADKSKKVVRFVLTGEPGSGKSVLLLQAMAYALEKGWVVLHVPEAELWVNGTTDYAPDESNPKLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923597  177 DQPLEASTWLKNFKTTNERFLSQIKVQEKYVWNKRESTEKGSPLGEVVEQ------------------------------ 226
Cdd:pfam10236  81 DQPMYTAALLRRIKKANEPVLSKIKLSQDYEWLKRESTPAGSTLLELLSLginransawdvfqalwkeltaqskrppvlv 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923597  227 ---------------------IAPEELSLVHNLRKMV--KNDWHGGAIVLSLSQTGSLFKSRTAYLPHELLGKEGFNALE 283
Cdd:pfam10236 161 avdgfnalmgntaykdadfkpIHPHDLTLVRHFLDLLsgKSDFPNGGVVTVLAATSSSNTPRSPTLPIALLQEEARPQLD 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568923597  284 PFL---------------PILIPNYNPKEFESSFQYYLENNWLQHeKASTEEGRKELRFLSNCNPEQLERL 339
Cdd:pfam10236 241 PYVkrydyvleakkgsvePFRVPGLTKEEARGLMEYYADSGWLQE-KVNEELVDEKLFLSGNGNPRELEKL 310
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
105-141 9.25e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 36.36  E-value: 9.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568923597 105 ELLGYLKNTNFAHpavrYLLYGEKGTGKTLsLCHAVH 141
Cdd:cd00009    9 ALREALELPPPKN----LLLYGPPGTGKTT-LARAIA 40
 
Name Accession Description Interval E-value
DAP3 pfam10236
Mitochondrial ribosomal death-associated protein 3; This is a family of conserved proteins ...
97-339 4.52e-88

Mitochondrial ribosomal death-associated protein 3; This is a family of conserved proteins which were originally described as death-associated-protein-3 (DAP-3). The proteins carry a P-loop DNA-binding motif, and induce apoptosis. DAP3 has been shown to be a pro-apoptotic factor in the mitochondrial matrix and to be crucial for mitochondrial biogenesis and so has also been designated as MRP-S29 (mitochondrial ribosomal protein subunit 29).


Pssm-ID: 431160  Cd Length: 310  Bit Score: 266.86  E-value: 4.52e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923597   97 LMVRKPALELLGYLKNTNFAHPAVRYLLYGEKGTGKTLSLCHAVHFCARHDWLILHIPDAHLWVKNCRELLQSTHNKQRF 176
Cdd:pfam10236   1 LLVREETLELIKKLKAADKSKKVVRFVLTGEPGSGKSVLLLQAMAYALEKGWVVLHVPEAELWVNGTTDYAPDESNPKLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923597  177 DQPLEASTWLKNFKTTNERFLSQIKVQEKYVWNKRESTEKGSPLGEVVEQ------------------------------ 226
Cdd:pfam10236  81 DQPMYTAALLRRIKKANEPVLSKIKLSQDYEWLKRESTPAGSTLLELLSLginransawdvfqalwkeltaqskrppvlv 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923597  227 ---------------------IAPEELSLVHNLRKMV--KNDWHGGAIVLSLSQTGSLFKSRTAYLPHELLGKEGFNALE 283
Cdd:pfam10236 161 avdgfnalmgntaykdadfkpIHPHDLTLVRHFLDLLsgKSDFPNGGVVTVLAATSSSNTPRSPTLPIALLQEEARPQLD 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568923597  284 PFL---------------PILIPNYNPKEFESSFQYYLENNWLQHeKASTEEGRKELRFLSNCNPEQLERL 339
Cdd:pfam10236 241 PYVkrydyvleakkgsvePFRVPGLTKEEARGLMEYYADSGWLQE-KVNEELVDEKLFLSGNGNPRELEKL 310
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
105-141 7.96e-03

Protein of unknown function (DUF815); This family consists of several bacterial proteins of unknown function.


Pssm-ID: 428578 [Multi-domain]  Cd Length: 250  Bit Score: 37.51  E-value: 7.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568923597  105 ELLGY-------LKNT-NFA--HPAVRYLLYGEKGTGKTlSLCHAVH 141
Cdd:pfam05673  29 DLVGIerqkealIRNTrRFLagLPANNVLLWGARGTGKS-SLVKALL 74
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
105-141 9.25e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 36.36  E-value: 9.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568923597 105 ELLGYLKNTNFAHpavrYLLYGEKGTGKTLsLCHAVH 141
Cdd:cd00009    9 ALREALELPPPKN----LLLYGPPGTGKTT-LARAIA 40
 
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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