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Conserved domains on  [gi|14250110|gb|AAH08467|]
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Chromosome 7 open reading frame 55 [Homo sapiens]

Protein Classification

protein FMC1 homolog( domain architecture ID 14448926)

protein FMC1 homolog plays a role in the assembly/stability of the mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V)

Gene Symbol:  FMC1
Gene Ontology:  GO:0033615
PubMed:  24059529

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Complex1_LYR_FMC1 cd20271
LYR (leucine-tyrosine-arginine) motif found in formation of mitochondrial complex V assembly ...
 7-103 7.30e-49

LYR (leucine-tyrosine-arginine) motif found in formation of mitochondrial complex V assembly factor 1 (FMC1) and similar proteins; FMC1, also known as formation of mitochondrial complexes protein 1, is an ATP synthase assembly factor that plays a role in the assembly/stability of the mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V). It belongs to the Complex1_LYR-like superfamily that consists of proteins of diverse functions that are exclusively found in eukaryotes and contain the conserved tripeptide 'LYR' close to the N-terminus.


:

Pssm-ID: 380766  Cd Length: 95  Bit Score: 150.45  E-value: 7.30e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14250110   7 PAHTFRGLLRELRYLSAatGRPYRDTAAYRYLVKAFRAHRVTSEKLCRAQHELHFQAATYLCLLRSIRKHVALHQEFHGK 86
Cdd:cd20271   1 SLSVLRGLLRELRHINP--KGKLRDSPAYRYIMEQFRKNQVTDEQLCRAQQELQFLAETYLCYLESTRKHKELHDEYHGK 78

                        90
                ....*....|....*..
gi 14250110  87 GERSVEESAGLVGLKLP 103
Cdd:cd20271  79 GERSVEETANLVGLKLP 95
 
Name Accession Description Interval E-value
Complex1_LYR_FMC1 cd20271
LYR (leucine-tyrosine-arginine) motif found in formation of mitochondrial complex V assembly ...
 7-103 7.30e-49

LYR (leucine-tyrosine-arginine) motif found in formation of mitochondrial complex V assembly factor 1 (FMC1) and similar proteins; FMC1, also known as formation of mitochondrial complexes protein 1, is an ATP synthase assembly factor that plays a role in the assembly/stability of the mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V). It belongs to the Complex1_LYR-like superfamily that consists of proteins of diverse functions that are exclusively found in eukaryotes and contain the conserved tripeptide 'LYR' close to the N-terminus.


Pssm-ID: 380766  Cd Length: 95  Bit Score: 150.45  E-value: 7.30e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14250110   7 PAHTFRGLLRELRYLSAatGRPYRDTAAYRYLVKAFRAHRVTSEKLCRAQHELHFQAATYLCLLRSIRKHVALHQEFHGK 86
Cdd:cd20271   1 SLSVLRGLLRELRHINP--KGKLRDSPAYRYIMEQFRKNQVTDEQLCRAQQELQFLAETYLCYLESTRKHKELHDEYHGK 78

                        90
                ....*....|....*..
gi 14250110  87 GERSVEESAGLVGLKLP 103
Cdd:cd20271  79 GERSVEETANLVGLKLP 95
 
Name Accession Description Interval E-value
Complex1_LYR_FMC1 cd20271
LYR (leucine-tyrosine-arginine) motif found in formation of mitochondrial complex V assembly ...
 7-103 7.30e-49

LYR (leucine-tyrosine-arginine) motif found in formation of mitochondrial complex V assembly factor 1 (FMC1) and similar proteins; FMC1, also known as formation of mitochondrial complexes protein 1, is an ATP synthase assembly factor that plays a role in the assembly/stability of the mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V). It belongs to the Complex1_LYR-like superfamily that consists of proteins of diverse functions that are exclusively found in eukaryotes and contain the conserved tripeptide 'LYR' close to the N-terminus.


Pssm-ID: 380766  Cd Length: 95  Bit Score: 150.45  E-value: 7.30e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14250110   7 PAHTFRGLLRELRYLSAatGRPYRDTAAYRYLVKAFRAHRVTSEKLCRAQHELHFQAATYLCLLRSIRKHVALHQEFHGK 86
Cdd:cd20271   1 SLSVLRGLLRELRHINP--KGKLRDSPAYRYIMEQFRKNQVTDEQLCRAQQELQFLAETYLCYLESTRKHKELHDEYHGK 78

                        90
                ....*....|....*..
gi 14250110  87 GERSVEESAGLVGLKLP 103
Cdd:cd20271  79 GERSVEETANLVGLKLP 95
Complex1_LYR_SF cd20251
LYR (leucine-tyrosine-arginine) motif found in Complex1_LYR-like superfamily; The ...
 9-69 3.00e-05

LYR (leucine-tyrosine-arginine) motif found in Complex1_LYR-like superfamily; The Complex1_LYR-like superfamily consists of proteins of diverse functions that are exclusively found in eukaryotes and contain the conserved tripeptide 'LYR' close to the N-terminus. The human genome has at least ten LYR proteins that were predominantly identified as mitochondrial proteins. Some family members were also found in the cytosol or nucleus. LYR motif-containing protein 4 (LYRM4) represents the only LYR protein that is directly involved in the first steps of Fe-S cluster generation. Other LYR proteins have been identified as accessory subunits or assembly factors of mitochondrial OXPHOS (oxidative phosphorylation) complexes I, II, III and V, and they play specific roles in acetate metabolism.


Pssm-ID: 380755  Cd Length: 57  Bit Score: 38.68  E-value: 3.00e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14250110   9 HTFRGLLRELRYlsaaTGRPYRDTAAYRYLVKAFRAHRvtSEKLCRAQHELHFQAATYLCL 69
Cdd:cd20251   3 KLYRDLLRLARK----GLPSRKRDALRQRIREEFRKNK--NETDPEKIEELLAEARRGLKN 57
 
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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