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Conserved domains on  [gi|1245897739|ref|NP_001342596|]
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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 ...
 29-179 6.73e-38

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: 129.81  E-value: 6.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  29 SENVIDRMKESSPSGSKSQRY-----------------------------SSVYGASVSDEDLKRRVAEEL----ALEQA 75
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgpsqapestsappsaeSSGGRQPVDEEELRKKIKEELykrlEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  76 KKESEhqrrlkQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLdiedkARQLEEKDRVMRKQDAFYKEQLARLEE 155
Cdd:pfam05300  81 KVQEE------LARLAEREREAAQESLTRAILRERASTEDERLKAQQL-----AKQLEEKEAELKKQDAFYKEQLARLEE 149

                         170       180
                  ....*....|....*....|....
gi 1245897739 156 RSSEFYKVTTEEYQKAAEEVEAKF 179
Cdd:pfam05300 150 KNAEFYKVTTEQFHKAATKAEARF 173
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 188-220 7.59e-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: 7.59e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1245897739 188 CADLQTKILQCYRQNTQQTLSCSALASQYMHCV 220
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 ...
 29-179 6.73e-38

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: 129.81  E-value: 6.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  29 SENVIDRMKESSPSGSKSQRY-----------------------------SSVYGASVSDEDLKRRVAEEL----ALEQA 75
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgpsqapestsappsaeSSGGRQPVDEEELRKKIKEELykrlEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  76 KKESEhqrrlkQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLdiedkARQLEEKDRVMRKQDAFYKEQLARLEE 155
Cdd:pfam05300  81 KVQEE------LARLAEREREAAQESLTRAILRERASTEDERLKAQQL-----AKQLEEKEAELKKQDAFYKEQLARLEE 149

                         170       180
                  ....*....|....*....|....
gi 1245897739 156 RSSEFYKVTTEEYQKAAEEVEAKF 179
Cdd:pfam05300 150 KNAEFYKVTTEQFHKAATKAEARF 173
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 59-178 1.04e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  59 DEDLKRRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLDIEDKARQLEEKDRV 138
Cdd:COG1196   280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1245897739 139 MRKQDAFYKEQLARLEERSSEFYKVTTEEYQKAAEEVEAK 178
Cdd:COG1196   360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
PTZ00121 PTZ00121
MAEBL; Provisional
 60-176 1.36e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739   60 EDLKRRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLTRAVLRERISSEEERMKAKhldiEDKARQLEEKDRVM 139
Cdd:PTZ00121  1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE----EDKKKAEEAKKAEE 1685

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1245897739  140 RKQDAfyKEQLARLEE--RSSEFYKVTTEEYQKAAEEVE 176
Cdd:PTZ00121  1686 DEKKA--AEALKKEAEeaKKAEELKKKEAEEKKKAEELK 1722
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 188-220 7.59e-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: 7.59e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1245897739 188 CADLQTKILQCYRQNTQQTLSCSALASQYMHCV 220
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 ...
 29-179 6.73e-38

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: 129.81  E-value: 6.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  29 SENVIDRMKESSPSGSKSQRY-----------------------------SSVYGASVSDEDLKRRVAEEL----ALEQA 75
Cdd:pfam05300   1 SENVINRMKEPSAPPPPSAPSppppsppppsptpgpsqapestsappsaeSSGGRQPVDEEELRKKIKEELykrlEQEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  76 KKESEhqrrlkQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLdiedkARQLEEKDRVMRKQDAFYKEQLARLEE 155
Cdd:pfam05300  81 KVQEE------LARLAEREREAAQESLTRAILRERASTEDERLKAQQL-----AKQLEEKEAELKKQDAFYKEQLARLEE 149

                         170       180
                  ....*....|....*....|....
gi 1245897739 156 RSSEFYKVTTEEYQKAAEEVEAKF 179
Cdd:pfam05300 150 KNAEFYKVTTEQFHKAATKAEARF 173
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 59-178 1.04e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  59 DEDLKRRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLDIEDKARQLEEKDRV 138
Cdd:COG1196   280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1245897739 139 MRKQDAFYKEQLARLEERSSEFYKVTTEEYQKAAEEVEAK 178
Cdd:COG1196   360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
PTZ00121 PTZ00121
MAEBL; Provisional
 60-176 1.36e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739   60 EDLKRRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLTRAVLRERISSEEERMKAKhldiEDKARQLEEKDRVM 139
Cdd:PTZ00121  1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE----EDKKKAEEAKKAEE 1685

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1245897739  140 RKQDAfyKEQLARLEE--RSSEFYKVTTEEYQKAAEEVE 176
Cdd:PTZ00121  1686 DEKKA--AEALKKEAEeaKKAEELKKKEAEEKKKAEELK 1722
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 12-170 1.74e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 38.95  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  12 FEADENENITVVKGIRLSENVIDRMKESSPSGSKSQ--RYSSVYGASVSDEDLKRRVAEELALEQAKKESEHQRRLKQAR 89
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEmdRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAM 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  90 DLERERAAANEQLTRAVLRERISSEEERMKAKHLDIEDKARQLEEKDRVMRK----QDAFYKEQLARL-EERSSEFYKVT 164
Cdd:pfam17380 373 EISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQiraeQEEARQREVRRLeEERAREMERVR 452


                  ....*.
gi 1245897739 165 TEEYQK 170
Cdd:pfam17380 453 LEEQER 458
PTZ00121 PTZ00121
MAEBL; Provisional
 64-178 2.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739   64 RRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLDIEDKARQLEEKDRVMRKQD 143
Cdd:PTZ00121  1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1245897739  144 AFYKEQLARlEERSSEFYKVTTEEYQKAAEEVEAK 178
Cdd:PTZ00121  1304 ADEAKKKAE-EAKKADEAKKKAEEAKKKADAAKKK 1337
PRK12705 PRK12705
hypothetical protein; Provisional
 63-175 2.77e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.54  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  63 KRRVAEELA--LEQAKKESEHQRRLKQARDLERERAAANEQLTRAVL-RERISSEEERMKAKHLDIEDKARQLEEKDRVM 139
Cdd:PRK12705   28 RQRLAKEAEriLQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARReREELQREEERLVQKEEQLDARAEKLDNLENQL 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1245897739 140 RKQDAFYKEQLARLEERSS----EFYKVTTEEYQKAAEEV 175
Cdd:PRK12705  108 EEREKALSARELELEELEKqldnELYRVAGLTPEQARKLL 147
PRK12704 PRK12704
phosphodiesterase; Provisional
 67-170 3.57e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  67 AEELA---LEQAKKESEHQRR----------LKQARDLERERAAANEQLTRAvlrerisseEERMKAKHLDIEDKARQLE 133
Cdd:PRK12704   36 AEEEAkriLEEAKKEAEAIKKealleakeeiHKLRNEFEKELRERRNELQKL---------EKRLLQKEENLDRKLELLE 106

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1245897739 134 EKDRVMRKQDAFYKEQLARLEERSSEFYKVTTEEYQK 170
Cdd:PRK12704  107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 59-183 5.72e-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: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  59 DEDLKRRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLtrAVLRERISSEEERMKAKHLDIEDKARQLEEKDRV 138
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE--YELLAELARLEQDIARLEERRRELEERLEELEEE 324

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1245897739 139 MRKQDAFYKEQLARLEERSSEFyKVTTEEYQKAAEEVEAKFKRYE 183
Cdd:COG1196   325 LAELEEELEELEEELEELEEEL-EEAEEELEEAEAELAEAEEALL 368
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
 188-220 7.59e-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: 7.59e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1245897739 188 CADLQTKILQCYRQNTQQTLSCSALASQYMHCV 220
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCV 33
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 60-177 8.72e-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: 8.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245897739  60 EDLKRRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQL-----TRAVLRERISSEEERMKAKHLD---IEDKARQ 131
Cdd:COG1196   220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELaeleaELEELRLELEELELELEEAQAEeyeLLAELAR 299

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1245897739 132 LEEKDRVMRKQDAFYKEQLARLEERSSEfykvTTEEYQKAAEEVEA 177
Cdd:COG1196   300 LEQDIARLEERRRELEERLEELEEELAE----LEEELEELEEELEE 341
 
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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