NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|520975337|ref|NP_001265575|]
View 

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 isoform 3 [Homo sapiens]

Protein Classification

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9( domain architecture ID 14448744)

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 (NDUFB9) is an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Complex1_LYR_NDUFB9_LYRM3 cd20263
LYR (leucine-tyrosine-arginine) motif found in NADH dehydrogenase [ubiquinone] 1 beta ...
1-45 1.31e-20

LYR (leucine-tyrosine-arginine) motif found in NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 (NDUFB9) and similar proteins; NDUFB9, also called LYR motif-containing protein 3 (LYRM3), or Complex I-B22 (CI-B22), or NADH-ubiquinone oxidoreductase B22 subunit (UQOR22), is an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (complex I), and is believed to be not involved in catalysis. In general, accessory subunits are integral for assembly and function of Complex I, which functions in the transfer of electrons from NADH to the respiratory chain. NDUFB9 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: 380758  Cd Length: 77  Bit Score: 79.53  E-value: 1.31e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 520975337   1 MRARFEEHKNEKDMAKATQLLKEAEEEFWYRQHPQPYIFPDSPGG 45
Cdd:cd20263   33 LRARFDANKDVKDPRKAEKLLEEGEAELWENQHPDPYIFPTSPGG 77
 
Name Accession Description Interval E-value
Complex1_LYR_NDUFB9_LYRM3 cd20263
LYR (leucine-tyrosine-arginine) motif found in NADH dehydrogenase [ubiquinone] 1 beta ...
1-45 1.31e-20

LYR (leucine-tyrosine-arginine) motif found in NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 (NDUFB9) and similar proteins; NDUFB9, also called LYR motif-containing protein 3 (LYRM3), or Complex I-B22 (CI-B22), or NADH-ubiquinone oxidoreductase B22 subunit (UQOR22), is an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (complex I), and is believed to be not involved in catalysis. In general, accessory subunits are integral for assembly and function of Complex I, which functions in the transfer of electrons from NADH to the respiratory chain. NDUFB9 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: 380758  Cd Length: 77  Bit Score: 79.53  E-value: 1.31e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 520975337   1 MRARFEEHKNEKDMAKATQLLKEAEEEFWYRQHPQPYIFPDSPGG 45
Cdd:cd20263   33 LRARFDANKDVKDPRKAEKLLEEGEAELWENQHPDPYIFPTSPGG 77
Complex1_LYR pfam05347
Complex 1 protein (LYR family); Proteins in this family include an accessory subunit of the ...
2-29 2.38e-04

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: 36.79  E-value: 2.38e-04
                          10        20
                  ....*....|....*....|....*...
gi 520975337    2 RARFEEHKNEKDMAKATQLLKEAEEEFW 29
Cdd:pfam05347  31 RDEFRKNKDLTDPEKIEKLLKEGKEELE 58
 
Name Accession Description Interval E-value
Complex1_LYR_NDUFB9_LYRM3 cd20263
LYR (leucine-tyrosine-arginine) motif found in NADH dehydrogenase [ubiquinone] 1 beta ...
1-45 1.31e-20

LYR (leucine-tyrosine-arginine) motif found in NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 (NDUFB9) and similar proteins; NDUFB9, also called LYR motif-containing protein 3 (LYRM3), or Complex I-B22 (CI-B22), or NADH-ubiquinone oxidoreductase B22 subunit (UQOR22), is an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (complex I), and is believed to be not involved in catalysis. In general, accessory subunits are integral for assembly and function of Complex I, which functions in the transfer of electrons from NADH to the respiratory chain. NDUFB9 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: 380758  Cd Length: 77  Bit Score: 79.53  E-value: 1.31e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 520975337   1 MRARFEEHKNEKDMAKATQLLKEAEEEFWYRQHPQPYIFPDSPGG 45
Cdd:cd20263   33 LRARFDANKDVKDPRKAEKLLEEGEAELWENQHPDPYIFPTSPGG 77
Complex1_LYR pfam05347
Complex 1 protein (LYR family); Proteins in this family include an accessory subunit of the ...
2-29 2.38e-04

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: 36.79  E-value: 2.38e-04
                          10        20
                  ....*....|....*....|....*...
gi 520975337    2 RARFEEHKNEKDMAKATQLLKEAEEEFW 29
Cdd:pfam05347  31 RDEFRKNKDLTDPEKIEKLLKEGKEELE 58
Complex1_LYR_SF cd20251
LYR (leucine-tyrosine-arginine) motif found in Complex1_LYR-like superfamily; The ...
1-30 6.10e-04

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: 35.60  E-value: 6.10e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 520975337   1 MRARFEEHKNEKDMAKATQLLKEAEEEFWY 30
Cdd:cd20251   28 IREEFRKNKNETDPEKIEELLAEARRGLKN 57
Complex1_LYR_LYRM7 cd20267
LYR (leucine-tyrosine-arginine) motif found in LYR motif-containing protein 7 (LYRM7) and ...
1-26 3.94e-03

LYR (leucine-tyrosine-arginine) motif found in LYR motif-containing protein 7 (LYRM7) and similar proteins; LYRM7 is an assembly factor required for Rieske iron sulfur (Fe-S) protein UQCRFS1 incorporation into the cytochrome b-c1 (CIII) complex. It functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. LYRM7 mutations cause a multifocal cavitating leukoencephalopathy with a distinct and recognizable magnetic resonance imaging (MRI) pattern. LYRM7 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: 380762  Cd Length: 72  Bit Score: 34.08  E-value: 3.94e-03
                         10        20
                 ....*....|....*....|....*.
gi 520975337   1 MRARFEEHKNEKDMAKATQLLKEAEE 26
Cdd:cd20267   30 IREEFEKNRNETDPEKIAELLKEARE 55
Complex1_LYR_LYRM4 cd20264
LYR (leucine-tyrosine-arginine) motif found in LYR motif-containing protein 4 (LYRM4) and ...
2-27 6.35e-03

LYR (leucine-tyrosine-arginine) motif found in LYR motif-containing protein 4 (LYRM4) and similar proteins; LYRM4, also called ISD11, is a eukaryote-specific component of the mitochondrial biogenesis of Fe-S clusters which are essential cofactors in multiple processes, including oxidative phosphorylation. It is required for nuclear and mitochondrial iron-sulfur protein biosynthesis by forming a complex with, and stabilizing, the sulfur donor NFS1. LYRM4 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: 380759  Cd Length: 69  Bit Score: 33.26  E-value: 6.35e-03
                         10        20
                 ....*....|....*....|....*...
gi 520975337   2 RAR--FEEHKNEKDMAKATQLLKEAEEE 27
Cdd:cd20264   28 RIRdaFRENKNLKDPEEIKKLYEEGEEQ 55
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH