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Conserved domains on  [gi|124248481|ref|NP_001071181|]
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succinate dehydrogenase assembly factor 3, mitochondrial isoform b precursor [Mus musculus]

Protein Classification

succinate dehydrogenase assembly factor 3( domain architecture ID 14448900)

mitochondrial succinate dehydrogenase assembly factor 3 (SDHAF3) plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol

Gene Ontology:  GO:0006111|GO:0006105|GO:0034553

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Complex1_LYR_SDHAF3_LYRM10 cd20270
LYR (leucine-tyrosine-arginine) motif found in mitochondrial succinate dehydrogenase assembly ...
 9-64 2.62e-32

LYR (leucine-tyrosine-arginine) motif found in mitochondrial succinate dehydrogenase assembly factor 3 (SDHAF3) and similar proteins; SDHAF3, also called SDH assembly factor 3, or LYR motif-containing protein 10 (LYRM10), plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. It promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. SDHAF3 may act together with SDHAF1. Its mutations may be associated with idiopathic SDH-associated diseases. SDHAF3 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: 380765  Cd Length: 56  Bit Score: 108.05  E-value: 2.62e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124248481   9 VRALYRRILLLHRALPPDLKALGDQYVKDEFRRHKTVGPGEAQRFLKEWETYAAVL 64
Cdd:cd20270    1 VLSLYRRILRLHRRLPPEMRALGDQYVKDEFRRHKTADPEQAKQFMAEWEMYADTL 56
 
Name Accession Description Interval E-value
Complex1_LYR_SDHAF3_LYRM10 cd20270
LYR (leucine-tyrosine-arginine) motif found in mitochondrial succinate dehydrogenase assembly ...
 9-64 2.62e-32

LYR (leucine-tyrosine-arginine) motif found in mitochondrial succinate dehydrogenase assembly factor 3 (SDHAF3) and similar proteins; SDHAF3, also called SDH assembly factor 3, or LYR motif-containing protein 10 (LYRM10), plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. It promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. SDHAF3 may act together with SDHAF1. Its mutations may be associated with idiopathic SDH-associated diseases. SDHAF3 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: 380765  Cd Length: 56  Bit Score: 108.05  E-value: 2.62e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124248481   9 VRALYRRILLLHRALPPDLKALGDQYVKDEFRRHKTVGPGEAQRFLKEWETYAAVL 64
Cdd:cd20270    1 VLSLYRRILRLHRRLPPEMRALGDQYVKDEFRRHKTADPEQAKQFMAEWEMYADTL 56
Complex1_LYR_2 pfam13233
Complex1_LYR-like; This is a family of proteins carrying the LYR motif of family Complex1_LYR, ...
 9-67 1.66e-16

Complex1_LYR-like; This is a family of proteins carrying the LYR motif of family Complex1_LYR, pfam05347, likely to be involved in Fe-S cluster biogenesis in mitochondria.


Pssm-ID: 463812  Cd Length: 79  Bit Score: 68.53  E-value: 1.66e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124248481    9 VRALYRRILLLHRALPPDLKALGDQYVKDEFRRHKTV-GPGEAQRFLKEWETYAAVLWQQ 67
Cdd:pfam13233   1 VLSLYRALLRELRELPPNGRSYGRQYLRAEFRRHKHLtDPEEIAEFLKSWREYKELLERY 60
 
Name Accession Description Interval E-value
Complex1_LYR_SDHAF3_LYRM10 cd20270
LYR (leucine-tyrosine-arginine) motif found in mitochondrial succinate dehydrogenase assembly ...
 9-64 2.62e-32

LYR (leucine-tyrosine-arginine) motif found in mitochondrial succinate dehydrogenase assembly factor 3 (SDHAF3) and similar proteins; SDHAF3, also called SDH assembly factor 3, or LYR motif-containing protein 10 (LYRM10), plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. It promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. SDHAF3 may act together with SDHAF1. Its mutations may be associated with idiopathic SDH-associated diseases. SDHAF3 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: 380765  Cd Length: 56  Bit Score: 108.05  E-value: 2.62e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124248481   9 VRALYRRILLLHRALPPDLKALGDQYVKDEFRRHKTVGPGEAQRFLKEWETYAAVL 64
Cdd:cd20270    1 VLSLYRRILRLHRRLPPEMRALGDQYVKDEFRRHKTADPEQAKQFMAEWEMYADTL 56
Complex1_LYR_2 pfam13233
Complex1_LYR-like; This is a family of proteins carrying the LYR motif of family Complex1_LYR, ...
 9-67 1.66e-16

Complex1_LYR-like; This is a family of proteins carrying the LYR motif of family Complex1_LYR, pfam05347, likely to be involved in Fe-S cluster biogenesis in mitochondria.


Pssm-ID: 463812  Cd Length: 79  Bit Score: 68.53  E-value: 1.66e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124248481    9 VRALYRRILLLHRALPPDLKALGDQYVKDEFRRHKTV-GPGEAQRFLKEWETYAAVLWQQ 67
Cdd:pfam13233   1 VLSLYRALLRELRELPPNGRSYGRQYLRAEFRRHKHLtDPEEIAEFLKSWREYKELLERY 60
Complex1_LYR_SF cd20251
LYR (leucine-tyrosine-arginine) motif found in Complex1_LYR-like superfamily; The ...
 9-60 3.14e-06

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: 41.38  E-value: 3.14e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124248481   9 VRALYRRIL-LLHRALPPDLKALGDQYVKDEFRRHKTV-GPGEAQRFLKEWETY 60
Cdd:cd20251    1 VLKLYRDLLrLARKGLPSRKRDALRQRIREEFRKNKNEtDPEKIEELLAEARRG 54
Complex1_LYR pfam05347
Complex 1 protein (LYR family); Proteins in this family include an accessory subunit of the ...
 8-63 5.94e-05

Complex 1 protein (LYR family); Proteins in this family include an accessory subunit of the higher eukaryotic NADH dehydrogenase complex. In Saccharomyces cerevisiae, the Isd11 protein has been shown to play a role in Fe/S cluster biogenesis in mitochondria. We have named this family LYR after a highly conserved tripeptide motif close to the N-terminus of these proteins.


Pssm-ID: 428432  Cd Length: 59  Bit Score: 38.33  E-value: 5.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 124248481    8 RVRALYRRILLLHRALP-PDLKALGDQYVKDEFRRHKTV-GPGEAQRFLKEWETYAAV 63
Cdd:pfam05347   2 QVLSLYRALLRAARKFPdYNFREYFRRRIRDEFRKNKDLtDPEKIEKLLKEGKEELEE 59
Complex1_LYR_LYRM2 cd20262
LYR (leucine-tyrosine-arginine) motif found in LYR motif-containing protein 2 (LYRM2) and ...
 7-45 5.25e-03

LYR (leucine-tyrosine-arginine) motif found in LYR motif-containing protein 2 (LYRM2) and similar proteins; LYRM2 is an uncharacterized LYR motif-containing protein that belongs to the Complex1_LYR-like superfamily which consists of proteins of diverse functions that are exclusively found in eukaryotes; these proteins contain the conserved tripeptide 'LYR' close to the N-terminus.


Pssm-ID: 380757  Cd Length: 63  Bit Score: 33.28  E-value: 5.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 124248481   7 SRVRALYRRIL-LLHRALPPDLKALGDQYVKDEFRRHKTV 45
Cdd:cd20262    4 AQVLSLYRDILrAIRKIPDPSTRRELRDWVREEFERNRNE 43
 
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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