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Conserved domains on  [gi|2024455796|ref|XP_040538436|]
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MICOS complex subunit MIC25 isoform X3 [Gallus gallus]

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 ...
32-201 4.62e-50

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: 164.10  E-value: 4.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796  32 TEDVVNRMKE-SQSKRDNQRSPHSSSGTAPFSTAAEGKPKSPTGIQPPTASNSGQKAT-------VAEQELYRRYEQEQA 103
Cdd:pfam05300   1 SENVINRMKEpSAPPPPSAPSPPPPSPPPPSPTPGPSQAPESTSAPPSAESSGGRQPVdeeelrkKIKEELYKRLEQEQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796 104 LVQEELLRLAKREREAAGETLSTALQRERNSTNEERKRVAQLpedldawALELQGREAELKRQEAFYKEQLARIERKNAE 183
Cdd:pfam05300  81 KVQEELARLAEREREAAQESLTRAILRERASTEDERLKAQQL-------AKQLEEKEAELKKQDAFYKEQLARLEEKNAE 153
                         170
                  ....*....|....*...
gi 2024455796 184 IYKLTSEQYQEAATKAEE 201
Cdd:pfam05300 154 FYKVTTEQFHKAATKAEA 171
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
212-246 1.05e-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: 36.06  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2024455796 212 CASLQSEILKCYQENQREVLKCSELAKEYQRCVSA 246
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCVKK 35
 
Name Accession Description Interval E-value
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
32-201 4.62e-50

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: 164.10  E-value: 4.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796  32 TEDVVNRMKE-SQSKRDNQRSPHSSSGTAPFSTAAEGKPKSPTGIQPPTASNSGQKAT-------VAEQELYRRYEQEQA 103
Cdd:pfam05300   1 SENVINRMKEpSAPPPPSAPSPPPPSPPPPSPTPGPSQAPESTSAPPSAESSGGRQPVdeeelrkKIKEELYKRLEQEQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796 104 LVQEELLRLAKREREAAGETLSTALQRERNSTNEERKRVAQLpedldawALELQGREAELKRQEAFYKEQLARIERKNAE 183
Cdd:pfam05300  81 KVQEELARLAEREREAAQESLTRAILRERASTEDERLKAQQL-------AKQLEEKEAELKKQDAFYKEQLARLEEKNAE 153
                         170
                  ....*....|....*...
gi 2024455796 184 IYKLTSEQYQEAATKAEE 201
Cdd:pfam05300 154 FYKVTTEQFHKAATKAEA 171
PRK12705 PRK12705
hypothetical protein; Provisional
85-218 9.22e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 43.93  E-value: 9.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796  85 QKATVAEQELYRRYEQEQALVQEELLRlAKREREAAGETLSTALQRERNSTNEERKRVAQLPEDLDAWALELQGREAELK 164
Cdd:PRK12705   30 RLAKEAERILQEAQKEAEEKLEAALLE-AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLE 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024455796 165 RQEAFYKEQLARIERKNAEIykltSEQYQEAATKAEEWIKrrntDPVCASLQSE 218
Cdd:PRK12705  109 EREKALSARELELEELEKQL----DNELYRVAGLTPEQAR----KLLLKLLDAE 154
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
85-206 5.47e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796  85 QKATVAEQELYRRYEQEQALVQEELLRLAKREREAAGE--TLSTALQRERNSTNEERKRVAQLPEDLDAWALELQGREAE 162
Cdd:COG1196   259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2024455796 163 LKRQEAFYKEQLARIERKNAEIYKLtSEQYQEAATKAEEWIKRR 206
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEA-EEALLEAEAELAEAEEEL 381
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
212-246 1.05e-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: 36.06  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2024455796 212 CASLQSEILKCYQENQREVLKCSELAKEYQRCVSA 246
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCVKK 35
 
Name Accession Description Interval E-value
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
32-201 4.62e-50

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: 164.10  E-value: 4.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796  32 TEDVVNRMKE-SQSKRDNQRSPHSSSGTAPFSTAAEGKPKSPTGIQPPTASNSGQKAT-------VAEQELYRRYEQEQA 103
Cdd:pfam05300   1 SENVINRMKEpSAPPPPSAPSPPPPSPPPPSPTPGPSQAPESTSAPPSAESSGGRQPVdeeelrkKIKEELYKRLEQEQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796 104 LVQEELLRLAKREREAAGETLSTALQRERNSTNEERKRVAQLpedldawALELQGREAELKRQEAFYKEQLARIERKNAE 183
Cdd:pfam05300  81 KVQEELARLAEREREAAQESLTRAILRERASTEDERLKAQQL-------AKQLEEKEAELKKQDAFYKEQLARLEEKNAE 153
                         170
                  ....*....|....*...
gi 2024455796 184 IYKLTSEQYQEAATKAEE 201
Cdd:pfam05300 154 FYKVTTEQFHKAATKAEA 171
PRK12705 PRK12705
hypothetical protein; Provisional
85-218 9.22e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 43.93  E-value: 9.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796  85 QKATVAEQELYRRYEQEQALVQEELLRlAKREREAAGETLSTALQRERNSTNEERKRVAQLPEDLDAWALELQGREAELK 164
Cdd:PRK12705   30 RLAKEAERILQEAQKEAEEKLEAALLE-AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLE 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024455796 165 RQEAFYKEQLARIERKNAEIykltSEQYQEAATKAEEWIKrrntDPVCASLQSE 218
Cdd:PRK12705  109 EREKALSARELELEELEKQL----DNELYRVAGLTPEQAR----KLLLKLLDAE 154
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
85-206 5.47e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796  85 QKATVAEQELYRRYEQEQALVQEELLRLAKREREAAGE--TLSTALQRERNSTNEERKRVAQLPEDLDAWALELQGREAE 162
Cdd:COG1196   259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2024455796 163 LKRQEAFYKEQLARIERKNAEIYKLtSEQYQEAATKAEEWIKRR 206
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEA-EEALLEAEAELAEAEEEL 381
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
212-246 1.05e-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: 36.06  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2024455796 212 CASLQSEILKCYQENQREVLKCSELAKEYQRCVSA 246
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCVKK 35
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
85-242 2.81e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796  85 QKATVAEQELYRRYEQEQALVQEEL--LRLAKREREAAGETLSTALQRERNSTNEERKRVAQLPEDLDAWALELQGREAE 162
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELeeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796 163 LKRQEAFYKEQLARIERKNAEIYKLTSEQYQEAATKAEEWIKRRNTDPVCASLQSEILKCYQENQREVLKCSELAKEYQR 242
Cdd:COG1196   325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
11-180 6.22e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796  11 RKVSFGLDeRDQV--RVLQGIRLtEDVVNRMKESQSKRDNQRSPHSSSGTAPFSTAAEGKPKSPTG-IQPPTASNSGQKA 87
Cdd:COG2433   357 KKVPPDVD-RDEVkaRVIRGLSI-EEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEqVERLEAEVEELEA 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796  88 TVAEQELY-RRYEQEQALVQEELLRLAKREREAagetlsTALQRE----RNSTNEERKRVAQLPEDLD----AWALELQG 158
Cdd:COG2433   435 ELEEKDERiERLERELSEARSEERREIRKDREI------SRLDREierlERELEEERERIEELKRKLErlkeLWKLEHSG 508
                         170       180
                  ....*....|....*....|..
gi 2024455796 159 REAELKRQEAFYKEQLARIERK 180
Cdd:COG2433   509 ELVPVKVVEKFTKEAIRRLEEE 530
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
97-184 9.83e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 35.69  E-value: 9.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455796  97 RYEQEQALVQEELLRLAKREREA---------AGETLSTALQRERNSTNEERKRVAQLPEDLDAWALELQGREAELKRQE 167
Cdd:pfam07926  19 DAEAQLQKLQEDLEKQAEIAREAqqnyerelvLHAEDIKALQALREELNELKAEIAELKAEAESAKAELEESEESWEEQK 98
                          90
                  ....*....|....*..
gi 2024455796 168 AFYKEQLARIERKNAEI 184
Cdd:pfam07926  99 KELEKELSELEKRIEDL 115
 
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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