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Conserved domains on  [gi|530414178|ref|XP_005266746|]
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mitochondrial import inner membrane translocase subunit Tim21 isoform X1 [Homo sapiens]

Protein Classification

Coa1/Tim21 domain-containing protein( domain architecture ID 231040)

Coa1/Tim21 domain-containing protein such as mitochondrial import inner membrane translocase subunit Tim21, an essential component of the TIM23 complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane

CATH:  3.10.450.320
Gene Ontology:  GO:0098798|GO:0030150
PubMed:  17099692|15797382

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Coa1 super family cl21648
Cytochrome oxidase complex assembly protein 1; Coa1 is an inner mitochondrial membrane protein ...
 74-195 4.93e-47

Cytochrome oxidase complex assembly protein 1; Coa1 is an inner mitochondrial membrane protein that associates with Shy1 and is required for cytochrome oxidase complex IV assembly. It contains a conserved hydrophobic segment (amino acids 74-92) with the potential to form a membrane-spanning helix. The N-terminus of Coa1 is rich in positively charged amino acids and could form an amphipathic alpha helix, characteriztic of a mitochondrial presequence. A cleavage site for the mitochondrial processing peptidase is predicted adjacent to the presequence. Upon in vitro import into mitochondria, Coa1 is processed to a mature form, indicating that it possesses a cleavable presequence. The eukaryotic cytochrome oxidase complex consists of 12-13 subunits, with three mitochondrial encoded subunits, Cox1-Cox3, forming the core enzyme. Translation of the Cox1 transcript requires the two promoters, Pet309 and Mss51, and the latter has an additional role in translational elongation. Coa1 is necessary for linking the activity of Mss51 to Cox1 insertion into the assembly complex.


The actual alignment was detected with superfamily member pfam08294:

Pssm-ID: 451344  Cd Length: 145  Bit Score: 151.29  E-value: 4.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414178   74 GLFYTIFKELFSSSSPSKIYGRALEKCRSHPEVIGVFGESVKGYGEVTRRGR----RQHVRFTEYVKDGLKHTCVKFYIE 149
Cdd:pfam08294  24 LVIYLIFSELFSPSGDTQIFNRAVELVEENERVRDLLGERIKAYGEETRRGRwtrnRPIVSTREYDKDGKEHIRMQFHVE 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 530414178  150 GsePGKQGTVYAQVKENPGSGEYDFRYIFVEIesYPRRTIIIEDNR 195
Cdd:pfam08294 104 G--PRKKGTVHLELVESDDSGQYEFRYLYVDV--PGHKRIYLEDNR 145
 
Name Accession Description Interval E-value
TIM21 pfam08294
TIM21; TIM21 interacts with the outer mitochondrial TOM complex and promotes the insertion of ...
 74-195 4.93e-47

TIM21; TIM21 interacts with the outer mitochondrial TOM complex and promotes the insertion of proteins into the inner mitochondrial membrane.


Pssm-ID: 311963  Cd Length: 145  Bit Score: 151.29  E-value: 4.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414178   74 GLFYTIFKELFSSSSPSKIYGRALEKCRSHPEVIGVFGESVKGYGEVTRRGR----RQHVRFTEYVKDGLKHTCVKFYIE 149
Cdd:pfam08294  24 LVIYLIFSELFSPSGDTQIFNRAVELVEENERVRDLLGERIKAYGEETRRGRwtrnRPIVSTREYDKDGKEHIRMQFHVE 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 530414178  150 GsePGKQGTVYAQVKENPGSGEYDFRYIFVEIesYPRRTIIIEDNR 195
Cdd:pfam08294 104 G--PRKKGTVHLELVESDDSGQYEFRYLYVDV--PGHKRIYLEDNR 145
 
Name Accession Description Interval E-value
TIM21 pfam08294
TIM21; TIM21 interacts with the outer mitochondrial TOM complex and promotes the insertion of ...
 74-195 4.93e-47

TIM21; TIM21 interacts with the outer mitochondrial TOM complex and promotes the insertion of proteins into the inner mitochondrial membrane.


Pssm-ID: 311963  Cd Length: 145  Bit Score: 151.29  E-value: 4.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414178   74 GLFYTIFKELFSSSSPSKIYGRALEKCRSHPEVIGVFGESVKGYGEVTRRGR----RQHVRFTEYVKDGLKHTCVKFYIE 149
Cdd:pfam08294  24 LVIYLIFSELFSPSGDTQIFNRAVELVEENERVRDLLGERIKAYGEETRRGRwtrnRPIVSTREYDKDGKEHIRMQFHVE 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 530414178  150 GsePGKQGTVYAQVKENPGSGEYDFRYIFVEIesYPRRTIIIEDNR 195
Cdd:pfam08294 104 G--PRKKGTVHLELVESDDSGQYEFRYLYVDV--PGHKRIYLEDNR 145
 
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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