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Conserved domains on  [gi|2261542595|ref|NP_001395813|]
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ATP synthase mitochondrial F1 complex assembly factor 2 isoform 3 [Mus musculus]

Protein Classification

ATP12 family chaperone protein( domain architecture ID 4941)

ATP12 family chaperone protein similar to Homo sapiens ATP synthase mitochondrial F1 complex assembly factor 2 that may play a role in the assembly of the F1 component of the mitochondrial ATP synthase (ATPase)

CATH:  1.10.3580.10|3.30.2180.10
Gene Ontology:  GO:0043461
SCOP:  4002624

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP12 super family cl02228
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ...
 9-165 5.91e-34

ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesized as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment. These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly.


The actual alignment was detected with superfamily member COG5387:

Pssm-ID: 470498  Cd Length: 235  Bit Score: 120.29  E-value: 5.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261542595   9 TTLCNTSLDN-PTQRskDQLIRAAVKFLDTDTICYRVEEPETLVELQKNEWDPVIEWAEKRYGMEIGSSTSIMGPSIPTQ 87
Cdd:COG5387    68 TRLANTAIDRvAPQR--AAVADELAAYAGSDLLCYRADSPEELVARQAAAWDPLLDWAAERLGARLVLTEGVMHVPQPPE 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261542595  88 TREVLTSHLSSYNMWALQGIEFVVAQLKSMLLTLGLIDLRLTVEQAVLLSRLEEEYQIQKWGniewaHDYELQELRAR 165
Cdd:COG5387   146 ALAALRAALEALDPFRLAALHDLTTLTGSLVLALALAEGRLDAEEAWAAAHLDEDWQIEQWG-----EDEEAAARRAA 218
 
Name Accession Description Interval E-value
Atp12 COG5387
Mitochondrial FoF1-type ATP synthase assembly chaperone ATP12 [Posttranslational modification, ...
 9-165 5.91e-34

Mitochondrial FoF1-type ATP synthase assembly chaperone ATP12 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444150  Cd Length: 235  Bit Score: 120.29  E-value: 5.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261542595   9 TTLCNTSLDN-PTQRskDQLIRAAVKFLDTDTICYRVEEPETLVELQKNEWDPVIEWAEKRYGMEIGSSTSIMGPSIPTQ 87
Cdd:COG5387    68 TRLANTAIDRvAPQR--AAVADELAAYAGSDLLCYRADSPEELVARQAAAWDPLLDWAAERLGARLVLTEGVMHVPQPPE 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261542595  88 TREVLTSHLSSYNMWALQGIEFVVAQLKSMLLTLGLIDLRLTVEQAVLLSRLEEEYQIQKWGniewaHDYELQELRAR 165
Cdd:COG5387   146 ALAALRAALEALDPFRLAALHDLTTLTGSLVLALALAEGRLDAEEAWAAAHLDEDWQIEQWG-----EDEEAAARRAA 218
ATP12 pfam07542
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ...
 9-66 1.07e-19

ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesized as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment. These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly.


Pssm-ID: 462201  Cd Length: 121  Bit Score: 80.22  E-value: 1.07e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261542595   9 TTLCNTSLD--NPTQRSKDQLIRAAVKFLDTDTICYRVEEPETLVELQKNEWDPVIEWAE 66
Cdd:pfam07542  62 TSLASRAIDlrVPDAGDREAIVDDLLRYLDTDTLLYRAEEPEALRARQAEAWDPLLDWAE 121
 
Name Accession Description Interval E-value
Atp12 COG5387
Mitochondrial FoF1-type ATP synthase assembly chaperone ATP12 [Posttranslational modification, ...
 9-165 5.91e-34

Mitochondrial FoF1-type ATP synthase assembly chaperone ATP12 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444150  Cd Length: 235  Bit Score: 120.29  E-value: 5.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261542595   9 TTLCNTSLDN-PTQRskDQLIRAAVKFLDTDTICYRVEEPETLVELQKNEWDPVIEWAEKRYGMEIGSSTSIMGPSIPTQ 87
Cdd:COG5387    68 TRLANTAIDRvAPQR--AAVADELAAYAGSDLLCYRADSPEELVARQAAAWDPLLDWAAERLGARLVLTEGVMHVPQPPE 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261542595  88 TREVLTSHLSSYNMWALQGIEFVVAQLKSMLLTLGLIDLRLTVEQAVLLSRLEEEYQIQKWGniewaHDYELQELRAR 165
Cdd:COG5387   146 ALAALRAALEALDPFRLAALHDLTTLTGSLVLALALAEGRLDAEEAWAAAHLDEDWQIEQWG-----EDEEAAARRAA 218
ATP12 pfam07542
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ...
 9-66 1.07e-19

ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesized as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment. These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly.


Pssm-ID: 462201  Cd Length: 121  Bit Score: 80.22  E-value: 1.07e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261542595   9 TTLCNTSLD--NPTQRSKDQLIRAAVKFLDTDTICYRVEEPETLVELQKNEWDPVIEWAE 66
Cdd:pfam07542  62 TSLASRAIDlrVPDAGDREAIVDDLLRYLDTDTLLYRAEEPEALRARQAEAWDPLLDWAE 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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