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Conserved domains on  [gi|6321765|ref|NP_011841|]
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DNA topoisomerase (ATP-hydrolyzing) [Saccharomyces cerevisiae S288C]

Protein Classification

topoisomerase 6A family protein( domain architecture ID 10516509)

topoisomerase 6A (TOP6A) family protein similar to Caenorhabditis elegans meiotic recombination protein spo-11 that mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TOPRIM_TopoIIB_SPO cd00223
TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of ...
 227-397 4.34e-45

TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in the type IIB family of DNA topoisomerases and Spo11. This subgroup contains proteins similar to Sulfolobus shibatae topoisomerase VI (TopoVI) and Saccharomyces cerevisiae meiotic recombination factor: Spo11. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. TopoVI enzymes are heterotetramers found in archaea and plants. Spo11 plays a role in generating the double strand breaks that initiate homologous recombination during meiosis. S. shibatae TopoVI relaxes both positive and negative supercoils, and in addition has a strong decatenase activity. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD. For topoisomerases the conserved glutamate is believed to act as a general base in strand joining and, as a general acid in strand cleavage. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


:

Pssm-ID: 173774  Cd Length: 160  Bit Score: 153.18  E-value: 4.34e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  227 CNIVIVEKEAVFTKLVNNYHKLSTNTMLITGKGFPDFLTRLFLKKLEQycsKLISDCSIFTDADPYGISIALNYTHSNER 306
Cdd:cd00223   1 DFVLVVEKEAVFQRLIEEGFHERNNCILITGKGYPDRATRRFLRRLHE---ELDLPVYILVDGDPYGISILLTYKYGSIK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  307 NAYIC-----TMANYKGIRITQVLaqnnevHNKSIQLLSLNQRDYSLAKNLIASLTAnswdiatSPLKNVIIECQREIFF 381
Cdd:cd00223  78 LAYESeslatPDLRWLGLRPSDII------RLPDLPLLPLSERDLKRAKSLLRRPRF-------KELPEWKRELQLMLKL 144

                       170
                ....*....|....*.
gi 6321765  382 QKKAEMNEIDARIFEY 397
Cdd:cd00223 145 GKKAEIEALASCGLEF 160
TP6A_N pfam04406
Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze ...
 106-168 5.94e-13

Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze the ATP-dependent transport of one DNA duplex through a second DNA segment via a transient double-strand break. Type II DNA topoisomerases are now subdivided into two sub-families, type IIA and IIB DNA topoisomerases. TP6A_N is present in type IIB topoisomerase and is thought to be involved in DNA binding owing to its sequence similarity to E. coli catabolite activator protein (CAP).


:

Pssm-ID: 461294 [Multi-domain]  Cd Length: 62  Bit Score: 63.26  E-value: 5.94e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321765    106 KRCAILLNLLKVVMEKLPLGKNTTVRDIFYSNVELFQRQANVVQWLDVIRFNFKLsPRKSLNI 168
Cdd:pfam04406   1 KKFAQLLRLLELIHELLLEGKTSTKRDIYYRDVELFKSQSEVDRLIDDLEVLLGV-PREDLNV 62
 
Name Accession Description Interval E-value
TOPRIM_TopoIIB_SPO cd00223
TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of ...
 227-397 4.34e-45

TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in the type IIB family of DNA topoisomerases and Spo11. This subgroup contains proteins similar to Sulfolobus shibatae topoisomerase VI (TopoVI) and Saccharomyces cerevisiae meiotic recombination factor: Spo11. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. TopoVI enzymes are heterotetramers found in archaea and plants. Spo11 plays a role in generating the double strand breaks that initiate homologous recombination during meiosis. S. shibatae TopoVI relaxes both positive and negative supercoils, and in addition has a strong decatenase activity. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD. For topoisomerases the conserved glutamate is believed to act as a general base in strand joining and, as a general acid in strand cleavage. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173774  Cd Length: 160  Bit Score: 153.18  E-value: 4.34e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  227 CNIVIVEKEAVFTKLVNNYHKLSTNTMLITGKGFPDFLTRLFLKKLEQycsKLISDCSIFTDADPYGISIALNYTHSNER 306
Cdd:cd00223   1 DFVLVVEKEAVFQRLIEEGFHERNNCILITGKGYPDRATRRFLRRLHE---ELDLPVYILVDGDPYGISILLTYKYGSIK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  307 NAYIC-----TMANYKGIRITQVLaqnnevHNKSIQLLSLNQRDYSLAKNLIASLTAnswdiatSPLKNVIIECQREIFF 381
Cdd:cd00223  78 LAYESeslatPDLRWLGLRPSDII------RLPDLPLLPLSERDLKRAKSLLRRPRF-------KELPEWKRELQLMLKL 144

                       170
                ....*....|....*.
gi 6321765  382 QKKAEMNEIDARIFEY 397
Cdd:cd00223 145 GKKAEIEALASCGLEF 160
TP6A_N pfam04406
Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze ...
 106-168 5.94e-13

Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze the ATP-dependent transport of one DNA duplex through a second DNA segment via a transient double-strand break. Type II DNA topoisomerases are now subdivided into two sub-families, type IIA and IIB DNA topoisomerases. TP6A_N is present in type IIB topoisomerase and is thought to be involved in DNA binding owing to its sequence similarity to E. coli catabolite activator protein (CAP).


Pssm-ID: 461294 [Multi-domain]  Cd Length: 62  Bit Score: 63.26  E-value: 5.94e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321765    106 KRCAILLNLLKVVMEKLPLGKNTTVRDIFYSNVELFQRQANVVQWLDVIRFNFKLsPRKSLNI 168
Cdd:pfam04406   1 KKFAQLLRLLELIHELLLEGKTSTKRDIYYRDVELFKSQSEVDRLIDDLEVLLGV-PREDLNV 62
PRK04342 PRK04342
DNA topoisomerase IV subunit A;
103-352 1.11e-09

DNA topoisomerase IV subunit A;


Pssm-ID: 235287 [Multi-domain]  Cd Length: 367  Bit Score: 59.53  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765   103 FKLKRCAILLNLLKvvmEKLPLGKNTTVRDIFYSN--------VELFQRQA---NVVQWLDVIrfnfkLS-PRKSLNIIP 170
Cdd:PRK04342  74 KKFMQTVLMAEFIK---ELLEENKSSTLRELYYMSkhwipglkENTFDDQDesdAVIEDLEVA-----LGvLREELHIRP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765   171 AQKGLVYSPFPIDIYDNILTCEnepKMQK--QTIfPGKPCLIPFFQDDAVIklgttsmcnIVIVEKEAVFTKLVNNYHKL 248
Cdd:PRK04342 146 EEDGSVVGPLRIRDGTDEIDCS---KLGEggYSI-PPNVDNIEFVDVDADF---------VLAVEKGGMFQRLVEEGFWK 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765   249 STNTMLITGKGFPDFLTRLFLKKL-EQYcsKLisDCSIFTDADPYGISIA-------LNYTHSNERNAyiCTMANYKGIR 320
Cdd:PRK04342 213 KYNAILVHLKGQPARATRRFIKRLnEEL--GL--PVYVFTDGDPWGYYIYsvvkygsIKLAHLSERLA--TPDAKFIGVT 286

                        250       260       270
                 ....*....|....*....|....*....|..
gi 6321765   321 ITQVlaQNNEVHNKSIQllsLNQRDYSLAKNL 352
Cdd:PRK04342 287 PSDI--VEYERDLPTIK---LKDSDIKRAKEL 313
Spo11 COG1697
DNA topoisomerase VI, subunit A [Replication, recombination and repair];
125-352 1.51e-08

DNA topoisomerase VI, subunit A [Replication, recombination and repair];


Pssm-ID: 441303 [Multi-domain]  Cd Length: 360  Bit Score: 56.01  E-value: 1.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  125 GKNTTVRDIFY------SNVELFQRQA---NVVQWLDVIrfnFKLsPRKSLNIIPAQKGLVYSPFPI--DIYDNILTCen 193
Cdd:COG1697  89 NKTSTLRELYYiskhwiLKENTFDEQDesdALIEDLEVA---TGV-LREEFHIRPEEKGSVVGPLTIrdGTRGDEIDC-- 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  194 epkmqkQTIFPGkPCLIPFFQDDavIKLGTTSMCNIVIVEKEAVFTKLV-NNYHKlSTNTMLITGKGFPDFLTRLFLKKL 272
Cdd:COG1697 163 ------SKVGEG-GYSIPPNVDN--IEFVDVDADFVLAVEKGGMFQRLVeEGFWK-KYNAILVHLKGQPARATRRFLRRL 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  273 -EQYcsKLisDCSIFTDADPYGISI-------ALNYTHSNERNAyiCTMANYKGIRITQVLAqNNEVHNKsiqllsLNQR 344
Cdd:COG1697 233 nEEL--GL--PVYVFTDGDPWGYYIysvikygSIKLAHESERLA--TPDAKFIGVTPSDIEE-YDLPTDK------LKDK 299


                ....*...
gi 6321765  345 DYSLAKNL 352
Cdd:COG1697 300 DIKRAKEL 307
 
Name Accession Description Interval E-value
TOPRIM_TopoIIB_SPO cd00223
TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of ...
 227-397 4.34e-45

TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in the type IIB family of DNA topoisomerases and Spo11. This subgroup contains proteins similar to Sulfolobus shibatae topoisomerase VI (TopoVI) and Saccharomyces cerevisiae meiotic recombination factor: Spo11. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. TopoVI enzymes are heterotetramers found in archaea and plants. Spo11 plays a role in generating the double strand breaks that initiate homologous recombination during meiosis. S. shibatae TopoVI relaxes both positive and negative supercoils, and in addition has a strong decatenase activity. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD. For topoisomerases the conserved glutamate is believed to act as a general base in strand joining and, as a general acid in strand cleavage. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173774  Cd Length: 160  Bit Score: 153.18  E-value: 4.34e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  227 CNIVIVEKEAVFTKLVNNYHKLSTNTMLITGKGFPDFLTRLFLKKLEQycsKLISDCSIFTDADPYGISIALNYTHSNER 306
Cdd:cd00223   1 DFVLVVEKEAVFQRLIEEGFHERNNCILITGKGYPDRATRRFLRRLHE---ELDLPVYILVDGDPYGISILLTYKYGSIK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  307 NAYIC-----TMANYKGIRITQVLaqnnevHNKSIQLLSLNQRDYSLAKNLIASLTAnswdiatSPLKNVIIECQREIFF 381
Cdd:cd00223  78 LAYESeslatPDLRWLGLRPSDII------RLPDLPLLPLSERDLKRAKSLLRRPRF-------KELPEWKRELQLMLKL 144

                       170
                ....*....|....*.
gi 6321765  382 QKKAEMNEIDARIFEY 397
Cdd:cd00223 145 GKKAEIEALASCGLEF 160
TP6A_N pfam04406
Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze ...
 106-168 5.94e-13

Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze the ATP-dependent transport of one DNA duplex through a second DNA segment via a transient double-strand break. Type II DNA topoisomerases are now subdivided into two sub-families, type IIA and IIB DNA topoisomerases. TP6A_N is present in type IIB topoisomerase and is thought to be involved in DNA binding owing to its sequence similarity to E. coli catabolite activator protein (CAP).


Pssm-ID: 461294 [Multi-domain]  Cd Length: 62  Bit Score: 63.26  E-value: 5.94e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321765    106 KRCAILLNLLKVVMEKLPLGKNTTVRDIFYSNVELFQRQANVVQWLDVIRFNFKLsPRKSLNI 168
Cdd:pfam04406   1 KKFAQLLRLLELIHELLLEGKTSTKRDIYYRDVELFKSQSEVDRLIDDLEVLLGV-PREDLNV 62
PRK04342 PRK04342
DNA topoisomerase IV subunit A;
103-352 1.11e-09

DNA topoisomerase IV subunit A;


Pssm-ID: 235287 [Multi-domain]  Cd Length: 367  Bit Score: 59.53  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765   103 FKLKRCAILLNLLKvvmEKLPLGKNTTVRDIFYSN--------VELFQRQA---NVVQWLDVIrfnfkLS-PRKSLNIIP 170
Cdd:PRK04342  74 KKFMQTVLMAEFIK---ELLEENKSSTLRELYYMSkhwipglkENTFDDQDesdAVIEDLEVA-----LGvLREELHIRP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765   171 AQKGLVYSPFPIDIYDNILTCEnepKMQK--QTIfPGKPCLIPFFQDDAVIklgttsmcnIVIVEKEAVFTKLVNNYHKL 248
Cdd:PRK04342 146 EEDGSVVGPLRIRDGTDEIDCS---KLGEggYSI-PPNVDNIEFVDVDADF---------VLAVEKGGMFQRLVEEGFWK 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765   249 STNTMLITGKGFPDFLTRLFLKKL-EQYcsKLisDCSIFTDADPYGISIA-------LNYTHSNERNAyiCTMANYKGIR 320
Cdd:PRK04342 213 KYNAILVHLKGQPARATRRFIKRLnEEL--GL--PVYVFTDGDPWGYYIYsvvkygsIKLAHLSERLA--TPDAKFIGVT 286

                        250       260       270
                 ....*....|....*....|....*....|..
gi 6321765   321 ITQVlaQNNEVHNKSIQllsLNQRDYSLAKNL 352
Cdd:PRK04342 287 PSDI--VEYERDLPTIK---LKDSDIKRAKEL 313
Spo11 COG1697
DNA topoisomerase VI, subunit A [Replication, recombination and repair];
125-352 1.51e-08

DNA topoisomerase VI, subunit A [Replication, recombination and repair];


Pssm-ID: 441303 [Multi-domain]  Cd Length: 360  Bit Score: 56.01  E-value: 1.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  125 GKNTTVRDIFY------SNVELFQRQA---NVVQWLDVIrfnFKLsPRKSLNIIPAQKGLVYSPFPI--DIYDNILTCen 193
Cdd:COG1697  89 NKTSTLRELYYiskhwiLKENTFDEQDesdALIEDLEVA---TGV-LREEFHIRPEEKGSVVGPLTIrdGTRGDEIDC-- 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  194 epkmqkQTIFPGkPCLIPFFQDDavIKLGTTSMCNIVIVEKEAVFTKLV-NNYHKlSTNTMLITGKGFPDFLTRLFLKKL 272
Cdd:COG1697 163 ------SKVGEG-GYSIPPNVDN--IEFVDVDADFVLAVEKGGMFQRLVeEGFWK-KYNAILVHLKGQPARATRRFLRRL 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  273 -EQYcsKLisDCSIFTDADPYGISI-------ALNYTHSNERNAyiCTMANYKGIRITQVLAqNNEVHNKsiqllsLNQR 344
Cdd:COG1697 233 nEEL--GL--PVYVFTDGDPWGYYIysvikygSIKLAHESERLA--TPDAKFIGVTPSDIEE-YDLPTDK------LKDK 299


                ....*...
gi 6321765  345 DYSLAKNL 352
Cdd:COG1697 300 DIKRAKEL 307
PLN00060 PLN00060
meiotic recombination protein SPO11-2; Provisional
 100-355 6.83e-07

meiotic recombination protein SPO11-2; Provisional


Pssm-ID: 177691 [Multi-domain]  Cd Length: 384  Bit Score: 51.03  E-value: 6.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765   100 THQFKLKRCAILLNLLKVVMEKLPLGKNTTVRDIFYS----NVELFQRQANVVQWL-DVIRFnFKLSpRKSLNIIPAQKG 174
Cdd:PLN00060  90 TKAGSAKAFVRVWKVMEMCYQILGEGKLVTQRELFYKllcdSPEYFSCQRHVNQTVqDVVSL-LRCS-RYSLGIMASSRG 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765   175 LVYSPFPIdiydniltceNEPkmQKQTIFPGKPCLIPFFQDDAVIKLGTTSMCN----IVIVEKEAVFTKLVNNYHKLST 250
Cdd:PLN00060 168 ALIGRLVL----------QEP--NEEPVDCSILGISGHAITGDLNLLSNLILSSdaryIIVVEKDAIFQRLAEDRFFNHI 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765   251 NTMLITGKGFPDFLTRLFLKKLeqycSKLISDCSIF--TDADPYGISIALNYTHSN-----ERNAYICTMaNYKGIRITQ 323
Cdd:PLN00060 236 PCILITAKGYPDLATRFILHRL----SQTFPNLPILalVDWNPAGLAILCTYKFGSigmglEAYRYACNV-KWLGLRGDD 310

                        250       260       270
                 ....*....|....*....|....*....|..
gi 6321765   324 VlaqnNEVHNKSIQLLSlnQRDYSLAKNLIAS 355
Cdd:PLN00060 311 L----QLIPPEAFVELK--PRDLQIAKSLLSS 336
TOPRIM cd00188
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ...
 229-298 1.43e-06

Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type IA, type IIA and type IIB topoisomerases, bacterial DnaG-type primases, small primase-like proteins from bacteria and archaea, OLD family nucleases from bacterial and archaea, and bacterial DNA repair proteins of the RecR/M family. This domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases and in strand joining in topoisomerases and, as a general acid in strand cleavage by topisomerases and nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173773 [Multi-domain]  Cd Length: 83  Bit Score: 45.88  E-value: 1.43e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321765  229 IVIVEKEAVFTKLVNNYHKlstNTMLITGKGFPDFLTRLFLKKLEQYCSKLIsdcsIFTDADPYGISIAL 298
Cdd:cd00188   3 LIIVEGPSDALALAQAGGY---GGAVVALGGHALNKTRELLKRLLGEAKEVI----IATDADREGEAIAL 65
 
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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