NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|528518299|ref|XP_005162369|]
View 

MICOS complex subunit mic25a isoform X2 [Danio rerio]

Protein Classification

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

DUF737 and CHCH domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 30-186 1.24e-48

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: 157.55  E-value: 1.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299   30 SEDVLQRMRNTNADPRPPANN--------------KENQGHQTRTPSTSDA--QAPKTQAKTTFPDSKEELKKRYEQQQA 93
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgPSQAPESTSAPPSAESsgGRQPVDEEELRKKIKEELYKRLEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299   94 IIQEELARIARKEREAARQDISRAVQRERAQTRQESERAKQLGKQLDKKEAELKALEAFYQEQITQLEKKNEERFRMSAE 173
Cdd:pfam05300  81 KVQEELARLAEREREAAQESLTRAILRERASTEDERLKAQQLAKQLEEKEAELKKQDAFYKEQLARLEEKNAEFYKVTTE 160

                         170
                  ....*....|...
gi 528518299  174 QFHAAATRSEANI 186
Cdd:pfam05300 161 QFHKAATKAEARF 173
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 195-229 3.89e-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: 34.13  E-value: 3.89e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528518299  195 CLNLQAQILNCYRENREQTLQCSDLAKEYMQCINA 229
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 ...
 30-186 1.24e-48

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: 157.55  E-value: 1.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299   30 SEDVLQRMRNTNADPRPPANN--------------KENQGHQTRTPSTSDA--QAPKTQAKTTFPDSKEELKKRYEQQQA 93
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgPSQAPESTSAPPSAESsgGRQPVDEEELRKKIKEELYKRLEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299   94 IIQEELARIARKEREAARQDISRAVQRERAQTRQESERAKQLGKQLDKKEAELKALEAFYQEQITQLEKKNEERFRMSAE 173
Cdd:pfam05300  81 KVQEELARLAEREREAAQESLTRAILRERASTEDERLKAQQLAKQLEEKEAELKKQDAFYKEQLARLEEKNAEFYKVTTE 160

                         170
                  ....*....|...
gi 528518299  174 QFHAAATRSEANI 186
Cdd:pfam05300 161 QFHKAATKAEARF 173
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 82-215 2.63e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299  82 EELKKRYEQQQAIIQEELARIARKEREAA-----RQDISRAVQRERAQTRQESERAKQLGKQLDKKEAELKALEAFYQEQ 156
Cdd:COG1196  277 EELELELEEAQAEEYELLAELARLEQDIArleerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528518299 157 ITQLEKKNEERFRMSAEQFHAAATRSEANIKARNVEPVCLNLQAQILNcyRENREQTLQ 215
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE--LEEAEEALL 413
PRK12704 PRK12704
phosphodiesterase; Provisional
 70-174 1.07e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299  70 KTQAKTTFPDSKEELKKRYEQQQAIIQEELARIARKEReaarqdisrAVQRERAQTRQESERAKQLGKQLDKKEAELKAL 149
Cdd:PRK12704  59 LLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE---------NLDRKLELLEKREEELEKKEKELEQKQQELEKK 129

                         90       100
                 ....*....|....*....|....*
gi 528518299 150 EAFYQEQITQLEKKNEERFRMSAEQ 174
Cdd:PRK12704 130 EEELEELIEEQLQELERISGLTAEE 154
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 195-229 3.89e-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: 34.13  E-value: 3.89e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528518299  195 CLNLQAQILNCYRENREQTLQCSDLAKEYMQCINA 229
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 ...
 30-186 1.24e-48

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: 157.55  E-value: 1.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299   30 SEDVLQRMRNTNADPRPPANN--------------KENQGHQTRTPSTSDA--QAPKTQAKTTFPDSKEELKKRYEQQQA 93
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgPSQAPESTSAPPSAESsgGRQPVDEEELRKKIKEELYKRLEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299   94 IIQEELARIARKEREAARQDISRAVQRERAQTRQESERAKQLGKQLDKKEAELKALEAFYQEQITQLEKKNEERFRMSAE 173
Cdd:pfam05300  81 KVQEELARLAEREREAAQESLTRAILRERASTEDERLKAQQLAKQLEEKEAELKKQDAFYKEQLARLEEKNAEFYKVTTE 160

                         170
                  ....*....|...
gi 528518299  174 QFHAAATRSEANI 186
Cdd:pfam05300 161 QFHKAATKAEARF 173
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 82-215 2.63e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299  82 EELKKRYEQQQAIIQEELARIARKEREAA-----RQDISRAVQRERAQTRQESERAKQLGKQLDKKEAELKALEAFYQEQ 156
Cdd:COG1196  277 EELELELEEAQAEEYELLAELARLEQDIArleerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528518299 157 ITQLEKKNEERFRMSAEQFHAAATRSEANIKARNVEPVCLNLQAQILNcyRENREQTLQ 215
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE--LEEAEEALL 413
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 79-222 5.92e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 5.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299  79 DSKEELKKRYEQQQAIIQEELARiARKEREAARQDISRAVQRERAQTRQ----------ESERAKQLGKQLDKKEAELKA 148
Cdd:COG1196  249 EELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAElarleqdiarLEERRRELEERLEELEEELAE 327

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528518299 149 LEAFYQEQITQLEKKNEERFRMSAEQFHAAATRSEANIKARNVEPVCLNLQAQILNCYRENREQTLQCSDLAKE 222
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
PRK12704 PRK12704
phosphodiesterase; Provisional
 70-174 1.07e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299  70 KTQAKTTFPDSKEELKKRYEQQQAIIQEELARIARKEReaarqdisrAVQRERAQTRQESERAKQLGKQLDKKEAELKAL 149
Cdd:PRK12704  59 LLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE---------NLDRKLELLEKREEELEKKEKELEQKQQELEKK 129

                         90       100
                 ....*....|....*....|....*
gi 528518299 150 EAFYQEQITQLEKKNEERFRMSAEQ 174
Cdd:PRK12704 130 EEELEELIEEQLQELERISGLTAEE 154
PRK12705 PRK12705
hypothetical protein; Provisional
 85-188 1.16e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.69  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299  85 KKRYEQQQAIIQEELARIARKEREAARQDISRAVQRERAQTRQES-----------ERAKQLGKQLDKKEAELKALE--- 150
Cdd:PRK12705  28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEArrereelqreeERLVQKEEQLDARAEKLDNLEnql 107

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 528518299 151 AFYQEQITQLEKKNEERFRMSAEQFHAAATRSEANIKA 188
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRVAGLTPEQARK 145
PRK12704 PRK12704
phosphodiesterase; Provisional
 62-174 2.46e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299  62 STSDAQAPKTQAKTTFPDSKEELKKRYEQQQAIIQEELARIaRKEREAARQDISRAVQRERAQTRQESERAKQLGKQLDK 141
Cdd:PRK12704  29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKL-RNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107

                         90       100       110
                 ....*....|....*....|....*....|...
gi 528518299 142 KEAELKALEAFYQEQITQLEKKNEERFRMSAEQ 174
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 195-229 3.89e-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: 34.13  E-value: 3.89e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528518299  195 CLNLQAQILNCYRENREQTLQCSDLAKEYMQCINA 229
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCVKK 35
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 80-158 4.13e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.14  E-value: 4.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528518299  80 SKEELKKrYEQQQAIIQEELAriARKEREAARQDISRAVQRERAQTRQESERAKQLGKQLDKKEAELKALEAFYQEQIT 158
Cdd:COG0542  438 SFERLAE-LRDELAELEEELE--ALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 89-184 4.26e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 38.01  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299   89 EQQQAIIQEELARIARKEREAARQDISRAVQRERAQtrQESERAKQLGKQLDKKEAELKALEAFYQEQITQLEKKNEERF 168
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQ--QELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKR 218

                          90
                  ....*....|....*.
gi 528518299  169 RMSAEQFHAAATRSEA 184
Cdd:PRK11448  219 KEITDQAAKRLELSEE 234
PRK12705 PRK12705
hypothetical protein; Provisional
 63-168 6.32e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 37.38  E-value: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299  63 TSDAQAPKTQAKTTFPDSKEELKKRYEQQQAIIQEELARIARKEREAARQDISRAVQRERAQtrqeSERAKQLGKQLDKK 142
Cdd:PRK12705  32 AKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQL----DARAEKLDNLENQL 107

                         90       100
                 ....*....|....*....|....*.
gi 528518299 143 EAELKALEAfYQEQITQLEKKNEERF 168
Cdd:PRK12705 108 EEREKALSA-RELELEELEKQLDNEL 132
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 79-225 6.40e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.61  E-value: 6.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299  79 DSKEELKKRYEQQQAIIQEELARIA--RKEREAARQDISRAVQRERAQTRQESERAKQLGKQLDKKEAELKALEAFYQEQ 156
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528518299 157 ITQLEKKNEERFRMSAEQFHAAATRSEANIKARNVEPVCLNLQAQILNCYRENREQTLQCSDLAKEYMQ 225
Cdd:COG1196  406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
PRK11281 PRK11281
mechanosensitive channel MscK;
47-161 8.80e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 37.20  E-value: 8.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518299   47 PANNKENQGHQTRTPSTSDAQAPKTQAKTTFPDSKEELKKRYEQQQAIiQEELAriarkerEAARQDISRAVQRERAQTR 126
Cdd:PRK11281   93 PAKLRQAQAELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNA-QNDLA-------EYNSQLVSLQTQPERAQAA 164

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 528518299  127 --QESERAKQLGKQLDKKEAELKALEAfyqEQITQLE 161
Cdd:PRK11281  165 lyANSQRLQQIRNLLKGGKVGGKALRP---SQRVLLQ 198
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 81-147 8.82e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 37.11  E-value: 8.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528518299  81 KEELKKRYEQQQAIIQ---EELARIARKEREAARQDISRAVQRER--------AQTRQE-SERAKQLGKQLDKKEAELK 147
Cdd:PRK00409 550 KEELEEKKEKLQEEEDkllEEAEKEAQQAIKEAKKEADEIIKELRqlqkggyaSVKAHElIEARKRLNKANEKKEKKKK 628
 
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