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Conserved domains on  [gi|528518297|ref|XP_005162368|]
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MICOS complex subunit mic25a isoform X1 [Danio rerio]

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 ...
 30-194 5.02e-46

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: 151.38  E-value: 5.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297   30 SEDVLQRMRNTNADPRPPANN--------------KENQGHQTRTPSTSDA--QAPKTQAKTTFPDSKEELKKRYEQQQA 93
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgPSQAPESTSAPPSAESsgGRQPVDEEELRKKIKEELYKRLEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297   94 IIQEELARIARKEREAARQDISRAVQRERAQTRQESERAKQLpaseldawGKQLDKKEAELKALEAFYQEQITQLEKKNE 173
Cdd:pfam05300  81 KVQEELARLAEREREAAQESLTRAILRERASTEDERLKAQQL--------AKQLEEKEAELKKQDAFYKEQLARLEEKNA 152

                         170       180
                  ....*....|....*....|.
gi 528518297  174 ERFRMSAEQFHAAATRSEANI 194
Cdd:pfam05300 153 EFYKVTTEQFHKAATKAEARF 173
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 203-237 3.27e-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: 34.52  E-value: 3.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528518297  203 CLNLQAQILNCYRENREQTLQCSDLAKEYMQCINA 237
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 ...
 30-194 5.02e-46

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: 151.38  E-value: 5.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297   30 SEDVLQRMRNTNADPRPPANN--------------KENQGHQTRTPSTSDA--QAPKTQAKTTFPDSKEELKKRYEQQQA 93
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgPSQAPESTSAPPSAESsgGRQPVDEEELRKKIKEELYKRLEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297   94 IIQEELARIARKEREAARQDISRAVQRERAQTRQESERAKQLpaseldawGKQLDKKEAELKALEAFYQEQITQLEKKNE 173
Cdd:pfam05300  81 KVQEELARLAEREREAAQESLTRAILRERASTEDERLKAQQL--------AKQLEEKEAELKKQDAFYKEQLARLEEKNA 152

                         170       180
                  ....*....|....*....|.
gi 528518297  174 ERFRMSAEQFHAAATRSEANI 194
Cdd:pfam05300 153 EFYKVTTEQFHKAATKAEARF 173
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 79-230 2.13e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297  79 DSKEELKKRYEQQQAIIQEELARiARKEREAARQDISRAVQRERAQTRQ--ESERAKQLPASELDAWGKQLDKKEAELKA 156
Cdd:COG1196  249 EELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAE 327

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528518297 157 LEAFYQEQITQLEKKNEERFRMSAEQFHAAATRSEANIKARNVEPVCLNLQAQILNCYRENREQTLQCSDLAKE 230
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
PRK12704 PRK12704
phosphodiesterase; Provisional
 84-182 1.85e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297  84 LKKRYEQQQAIIQEELARI---ARKEREAARQDISRAVQRERAQTRQESERAKQLPASELDAWGKQL------------- 147
Cdd:PRK12704  25 RKKIAEAKIKEAEEEAKRIleeAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLlqkeenldrklel 104

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 528518297 148 -DKKEAELKALEAFYQEQITQLEKKNEERFRMSAEQ 182
Cdd:PRK12704 105 lEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 203-237 3.27e-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: 34.52  E-value: 3.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528518297  203 CLNLQAQILNCYRENREQTLQCSDLAKEYMQCINA 237
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCVKK 35
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-230 4.41e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.11  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297    81 KEELKKRYEQQQAIIQEELARIARKEREAARQdisravQRERAQTRQESERAkqlpASELDAWGKQLDKKEAELKALEAF 160
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQIL------RERLANLERQLEEL----EAQLEELESKLDELAEELAELEEK 345

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528518297   161 Y---QEQITQLEKKNEErFRMSAEQFHAAATRSEANIKARNVEPVCLNLQAQILNCYRENREQTLQCSDLAKE 230
Cdd:TIGR02168  346 LeelKEELESLEAELEE-LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417
 
Name Accession Description Interval E-value
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
 30-194 5.02e-46

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: 151.38  E-value: 5.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297   30 SEDVLQRMRNTNADPRPPANN--------------KENQGHQTRTPSTSDA--QAPKTQAKTTFPDSKEELKKRYEQQQA 93
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgPSQAPESTSAPPSAESsgGRQPVDEEELRKKIKEELYKRLEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297   94 IIQEELARIARKEREAARQDISRAVQRERAQTRQESERAKQLpaseldawGKQLDKKEAELKALEAFYQEQITQLEKKNE 173
Cdd:pfam05300  81 KVQEELARLAEREREAAQESLTRAILRERASTEDERLKAQQL--------AKQLEEKEAELKKQDAFYKEQLARLEEKNA 152

                         170       180
                  ....*....|....*....|.
gi 528518297  174 ERFRMSAEQFHAAATRSEANI 194
Cdd:pfam05300 153 EFYKVTTEQFHKAATKAEARF 173
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 79-230 2.13e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297  79 DSKEELKKRYEQQQAIIQEELARiARKEREAARQDISRAVQRERAQTRQ--ESERAKQLPASELDAWGKQLDKKEAELKA 156
Cdd:COG1196  249 EELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAE 327

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528518297 157 LEAFYQEQITQLEKKNEERFRMSAEQFHAAATRSEANIKARNVEPVCLNLQAQILNCYRENREQTLQCSDLAKE 230
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
PRK12704 PRK12704
phosphodiesterase; Provisional
 84-182 1.85e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297  84 LKKRYEQQQAIIQEELARI---ARKEREAARQDISRAVQRERAQTRQESERAKQLPASELDAWGKQL------------- 147
Cdd:PRK12704  25 RKKIAEAKIKEAEEEAKRIleeAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLlqkeenldrklel 104

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 528518297 148 -DKKEAELKALEAFYQEQITQLEKKNEERFRMSAEQ 182
Cdd:PRK12704 105 lEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
PRK12705 PRK12705
hypothetical protein; Provisional
 85-196 2.17e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.92  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297  85 KKRYEQQQAIIQEELARIARKEREAARQDISRAVQRERAQTRQESERAKQLPASE----------LDAWGKQLDKKEAEL 154
Cdd:PRK12705  28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeerlvqkeeqLDARAEKLDNLENQL 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 528518297 155 KALEAFYQEQITQLEKKNEERfrmsAEQFHAAATRSEANIKA 196
Cdd:PRK12705 108 EEREKALSARELELEELEKQL----DNELYRVAGLTPEQARK 145
PRK12704 PRK12704
phosphodiesterase; Provisional
 81-182 2.36e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297  81 KEELKKRYEQQQAIIQEELARIARKEReaarqdisRAVQRERaQTRQESERAKQLpASELDAWGKQLDKKEAELKALEAF 160
Cdd:PRK12704  63 KEEIHKLRNEFEKELRERRNELQKLEK--------RLLQKEE-NLDRKLELLEKR-EEELEKKEKELEQKQQELEKKEEE 132

                         90       100
                 ....*....|....*....|..
gi 528518297 161 YQEQITQLEKKNEERFRMSAEQ 182
Cdd:PRK12704 133 LEELIEEQLQELERISGLTAEE 154
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 203-237 3.27e-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: 34.52  E-value: 3.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528518297  203 CLNLQAQILNCYRENREQTLQCSDLAKEYMQCINA 237
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCVKK 35
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-230 4.41e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.11  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297    81 KEELKKRYEQQQAIIQEELARIARKEREAARQdisravQRERAQTRQESERAkqlpASELDAWGKQLDKKEAELKALEAF 160
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQIL------RERLANLERQLEEL----EAQLEELESKLDELAEELAELEEK 345

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528518297   161 Y---QEQITQLEKKNEErFRMSAEQFHAAATRSEANIKARNVEPVCLNLQAQILNCYRENREQTLQCSDLAKE 230
Cdd:TIGR02168  346 LeelKEELESLEAELEE-LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
5-171 9.10e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 37.14  E-value: 9.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297   5 ESTTRRVSFGLDEDD-RVRILRGVKLsEDVLQRMRNTNADPRPPANNKENQgHQTRTPSTSDAQAPKTQAKT-TFPDSKE 82
Cdd:COG2433  353 ERVEKKVPPDVDRDEvKARVIRGLSI-EEALEELIEKELPEEEPEAEREKE-HEERELTEEEEEIRRLEEQVeRLEAEVE 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518297  83 ELKKRYEQQQAIIQE----------ELARIARKEREAARQD--ISRaVQRERAQTRQESERAKQLPASELDAWGKQLDKK 150
Cdd:COG2433  431 ELEAELEEKDERIERlerelsearsEERREIRKDREISRLDreIER-LERELEEERERIEELKRKLERLKELWKLEHSGE 509

                        170       180
                 ....*....|....*....|.
gi 528518297 151 EAELKALEAFYQEQITQLEKK 171
Cdd:COG2433  510 LVPVKVVEKFTKEAIRRLEEE 530
 
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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