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Conserved domains on  [gi|21313618|ref|NP_079612|]
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MICOS complex subunit Mic19 [Mus musculus]

Protein Classification

DUF737 and CHCH domain-containing protein( domain architecture ID 12062594)

DUF737 and CHCH domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
 29-174 3.41e-40

MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.


:

Pssm-ID: 461615 [Multi-domain]  Cd Length: 173  Bit Score: 135.59  E-value: 3.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618    29 SENVIDRMKESSPSGSKSQRY-----------------------------SSVYGASVSDEDLKRRVAEEL----ALEQA 75
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgpsqapestsappsaeSSGGRQPVDEEELRKKIKEELykrlEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618    76 KKESEhqrrlkQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLARQLEEKDRVMRKQDAFYKEQLARLEERSSEF 155
Cdd:pfam05300  81 KVQEE------LARLAEREREAAQESLTRAILRERASTEDERLKAQQLAKQLEEKEAELKKQDAFYKEQLARLEEKNAEF 154

                         170
                  ....*....|....*....
gi 21313618   156 YKVTTEEYQKAAEEVEAKF 174
Cdd:pfam05300 155 YKVTTEQFHKAATKAEARF 173
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 183-215 7.42e-03

CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called the CHCH motif. Alignment of this protein with related members showed the presence of three subgroups of proteins, which are called the S (Small), N (N-terminal extended) and C (C-terminal extended) subgroups. All three sub-groups of proteins have in common that they contain a predicted conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2] domain (CHCH domain). Within each helix of the CHCH domain, there are two cysteines present in a C-X9-C motif. The N-group contains an additional double helix domain, and each helix contains the C-X9-C motif. This family contains a number of characterized proteins: Cox19 protein - a nuclear gene of Saccharomyces cerevisiae, codes for an 11-kDa protein (Cox19p) required for expression of cytochrome oxidase. Because cox19 mutants are able to synthesize the mitochondrial and nuclear gene products of cytochrome oxidase, Cox19p probably functions post-translationally during assembly of the enzyme. Cox19p is present in the cytoplasm and mitochondria, where it exists as a soluble intermembrane protein. This dual location is similar to what was previously reported for Cox17p, a low molecular weight copper protein thought to be required for maturation of the CuA centre of subunit 2 of cytochrome oxidase. Cox19p have four conserved potential metal ligands, these are three cysteines and one histidine. Mrp10 - belongs to the class of yeast mitochondrial ribosomal proteins that are essential for translation. Eukaryotic NADH-ubiquinone oxidoreductase 19 kDa (NDUFA8) subunit. The CHCH domain was previously called DUF657.


:

Pssm-ID: 429096  Cd Length: 35  Bit Score: 33.36  E-value: 7.42e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 21313618   183 CADLQTKILQCYRQNTQQTLSCSALASQYMHCV 215
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCV 33
 
Name Accession Description Interval E-value
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
 29-174 3.41e-40

MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.


Pssm-ID: 461615 [Multi-domain]  Cd Length: 173  Bit Score: 135.59  E-value: 3.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618    29 SENVIDRMKESSPSGSKSQRY-----------------------------SSVYGASVSDEDLKRRVAEEL----ALEQA 75
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgpsqapestsappsaeSSGGRQPVDEEELRKKIKEELykrlEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618    76 KKESEhqrrlkQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLARQLEEKDRVMRKQDAFYKEQLARLEERSSEF 155
Cdd:pfam05300  81 KVQEE------LARLAEREREAAQESLTRAILRERASTEDERLKAQQLAKQLEEKEAELKKQDAFYKEQLARLEEKNAEF 154

                         170
                  ....*....|....*....
gi 21313618   156 YKVTTEEYQKAAEEVEAKF 174
Cdd:pfam05300 155 YKVTTEQFHKAATKAEARF 173
PTZ00121 PTZ00121
MAEBL; Provisional
 60-171 4.30e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618    60 EDLKRRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLARQLEEKdRVMRKQDA 139
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-KKAEEDEK 1688

                          90       100       110
                  ....*....|....*....|....*....|....
gi 21313618   140 FYKEQLARLEE--RSSEFYKVTTEEYQKAAEEVE 171
Cdd:PTZ00121 1689 KAAEALKKEAEeaKKAEELKKKEAEEKKKAEELK 1722
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 183-215 7.42e-03

CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called the CHCH motif. Alignment of this protein with related members showed the presence of three subgroups of proteins, which are called the S (Small), N (N-terminal extended) and C (C-terminal extended) subgroups. All three sub-groups of proteins have in common that they contain a predicted conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2] domain (CHCH domain). Within each helix of the CHCH domain, there are two cysteines present in a C-X9-C motif. The N-group contains an additional double helix domain, and each helix contains the C-X9-C motif. This family contains a number of characterized proteins: Cox19 protein - a nuclear gene of Saccharomyces cerevisiae, codes for an 11-kDa protein (Cox19p) required for expression of cytochrome oxidase. Because cox19 mutants are able to synthesize the mitochondrial and nuclear gene products of cytochrome oxidase, Cox19p probably functions post-translationally during assembly of the enzyme. Cox19p is present in the cytoplasm and mitochondria, where it exists as a soluble intermembrane protein. This dual location is similar to what was previously reported for Cox17p, a low molecular weight copper protein thought to be required for maturation of the CuA centre of subunit 2 of cytochrome oxidase. Cox19p have four conserved potential metal ligands, these are three cysteines and one histidine. Mrp10 - belongs to the class of yeast mitochondrial ribosomal proteins that are essential for translation. Eukaryotic NADH-ubiquinone oxidoreductase 19 kDa (NDUFA8) subunit. The CHCH domain was previously called DUF657.


Pssm-ID: 429096  Cd Length: 35  Bit Score: 33.36  E-value: 7.42e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 21313618   183 CADLQTKILQCYRQNTQQTLSCSALASQYMHCV 215
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCV 33
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 59-172 8.22e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 36.84  E-value: 8.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618  59 DEDLKRRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLTRAVLRERISSEEERMKAkhLARQLEEKDRVMRKQD 138
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE--LEEELEEAEEELEEAE 357

                        90       100       110
                ....*....|....*....|....*....|....
gi 21313618 139 AFYKEQLARLEERSSEFYKVTTEEYQKAAEEVEA 172
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
 
Name Accession Description Interval E-value
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
 29-174 3.41e-40

MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.


Pssm-ID: 461615 [Multi-domain]  Cd Length: 173  Bit Score: 135.59  E-value: 3.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618    29 SENVIDRMKESSPSGSKSQRY-----------------------------SSVYGASVSDEDLKRRVAEEL----ALEQA 75
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgpsqapestsappsaeSSGGRQPVDEEELRKKIKEELykrlEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618    76 KKESEhqrrlkQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLARQLEEKDRVMRKQDAFYKEQLARLEERSSEF 155
Cdd:pfam05300  81 KVQEE------LARLAEREREAAQESLTRAILRERASTEDERLKAQQLAKQLEEKEAELKKQDAFYKEQLARLEEKNAEF 154

                         170
                  ....*....|....*....
gi 21313618   156 YKVTTEEYQKAAEEVEAKF 174
Cdd:pfam05300 155 YKVTTEQFHKAATKAEARF 173
PTZ00121 PTZ00121
MAEBL; Provisional
 60-171 4.30e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618    60 EDLKRRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLARQLEEKdRVMRKQDA 139
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-KKAEEDEK 1688

                          90       100       110
                  ....*....|....*....|....*....|....
gi 21313618   140 FYKEQLARLEE--RSSEFYKVTTEEYQKAAEEVE 171
Cdd:PTZ00121 1689 KAAEALKKEAEeaKKAEELKKKEAEEKKKAEELK 1722
PTZ00121 PTZ00121
MAEBL; Provisional
 58-175 3.24e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618    58 SDEDLKRRVAEELALEQAKK-ESEHQRRLKQARDLERERAAANEQLTRavlreriSSEEERMKAKHLARQLEEKDRVMRK 136
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKkEAEEKKKAEELKKAEEENKIKAEEAKK-------EAEEDKKKAEEAKKDEEEKKKIAHL 1762

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 21313618   137 QDAFYKEQLARLEERSSEFYKVTTEEYQKAAEEVEAKFK 175
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
PTZ00121 PTZ00121
MAEBL; Provisional
 64-173 7.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618    64 RRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLaRQLEEKDRVMRKQDAFYKE 143
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL-KKAEEKKKADEAKKAEEKK 1302

                          90       100       110
                  ....*....|....*....|....*....|
gi 21313618   144 QLARLEERSSEFYKvtTEEYQKAAEEVEAK 173
Cdd:PTZ00121 1303 KADEAKKKAEEAKK--ADEAKKKAEEAKKK 1330
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 183-215 7.42e-03

CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called the CHCH motif. Alignment of this protein with related members showed the presence of three subgroups of proteins, which are called the S (Small), N (N-terminal extended) and C (C-terminal extended) subgroups. All three sub-groups of proteins have in common that they contain a predicted conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2] domain (CHCH domain). Within each helix of the CHCH domain, there are two cysteines present in a C-X9-C motif. The N-group contains an additional double helix domain, and each helix contains the C-X9-C motif. This family contains a number of characterized proteins: Cox19 protein - a nuclear gene of Saccharomyces cerevisiae, codes for an 11-kDa protein (Cox19p) required for expression of cytochrome oxidase. Because cox19 mutants are able to synthesize the mitochondrial and nuclear gene products of cytochrome oxidase, Cox19p probably functions post-translationally during assembly of the enzyme. Cox19p is present in the cytoplasm and mitochondria, where it exists as a soluble intermembrane protein. This dual location is similar to what was previously reported for Cox17p, a low molecular weight copper protein thought to be required for maturation of the CuA centre of subunit 2 of cytochrome oxidase. Cox19p have four conserved potential metal ligands, these are three cysteines and one histidine. Mrp10 - belongs to the class of yeast mitochondrial ribosomal proteins that are essential for translation. Eukaryotic NADH-ubiquinone oxidoreductase 19 kDa (NDUFA8) subunit. The CHCH domain was previously called DUF657.


Pssm-ID: 429096  Cd Length: 35  Bit Score: 33.36  E-value: 7.42e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 21313618   183 CADLQTKILQCYRQNTQQTLSCSALASQYMHCV 215
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCV 33
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 59-172 8.22e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 36.84  E-value: 8.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313618  59 DEDLKRRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLTRAVLRERISSEEERMKAkhLARQLEEKDRVMRKQD 138
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE--LEEELEEAEEELEEAE 357

                        90       100       110
                ....*....|....*....|....*....|....
gi 21313618 139 AFYKEQLARLEERSSEFYKVTTEEYQKAAEEVEA 172
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
 
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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