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Conserved domains on  [gi|1907140066|ref|XP_036018141|]
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meiotic recombination protein SPO11 isoform X7 [Mus musculus]

Protein Classification

TOPRIM_TopoIIB_SPO domain-containing protein( domain architecture ID 10083112)

TOPRIM_TopoIIB_SPO domain-containing protein

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 ...
 34-196 2.39e-75

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: 224.06  E-value: 2.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066  34 KFLLIVEKDATFQRLLDDNFCSRmSPCIMVTGKGVPDLNTRLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMS 113
Cdd:cd00223     1 DFVLVVEKEAVFQRLIEEGFHER-NNCILITGKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISILLTYKYGSIKLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066 114 FEAHNLTIPTIRWLGLLPSDIQRlnIPKDSLIPLTKHDQMKLDSILKRPYITYQPLWKKELEMMADSKMKAEIQALTLLS 193
Cdd:cd00223    80 YESESLATPDLRWLGLRPSDIIR--LPDLPLLPLSERDLKRAKSLLRRPRFKELPEWKRELQLMLKLGKKAEIEALASCG 157


                  ...
gi 1907140066 194 SDY 196
Cdd:cd00223   158 LEF 160
 
Name Accession Description Interval E-value
TOPRIM_TopoIIB_SPO cd00223
TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of ...
 34-196 2.39e-75

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: 224.06  E-value: 2.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066  34 KFLLIVEKDATFQRLLDDNFCSRmSPCIMVTGKGVPDLNTRLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMS 113
Cdd:cd00223     1 DFVLVVEKEAVFQRLIEEGFHER-NNCILITGKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISILLTYKYGSIKLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066 114 FEAHNLTIPTIRWLGLLPSDIQRlnIPKDSLIPLTKHDQMKLDSILKRPYITYQPLWKKELEMMADSKMKAEIQALTLLS 193
Cdd:cd00223    80 YESESLATPDLRWLGLRPSDIIR--LPDLPLLPLSERDLKRAKSLLRRPRFKELPEWKRELQLMLKLGKKAEIEALASCG 157


                  ...
gi 1907140066 194 SDY 196
Cdd:cd00223   158 LEF 160
PRK04342 PRK04342
DNA topoisomerase IV subunit A;
3-212 5.29e-54

DNA topoisomerase IV subunit A;


Pssm-ID: 235287 [Multi-domain]  Cd Length: 367  Bit Score: 176.63  E-value: 5.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066   3 EDGTRV-QCT-CSATATAVPTNIQGMQHLITDAKFLLIVEKDATFQRLLDDNFCSRMSpCIMVTGKGVPDLNTRLLVKKL 80
Cdd:PRK04342  158 RDGTDEiDCSkLGEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVHLKGQPARATRRFIKRL 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066  81 WDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIPTIRWLGLLPSDIQRlNIPKDSLIPLTKHDQMKLDSILK 160
Cdd:PRK04342  237 NEELGLPVYVFTDGDPWGYYIYSVVKYGSIKLAHLSERLATPDAKFIGVTPSDIVE-YERDLPTIKLKDSDIKRAKELLN 315

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907140066 161 RPYitYQ-PLWKKELEMMADSKMKAEIQALTLLSSDYLSRVYLPNKLRFGGWI 212
Cdd:PRK04342  316 YPW--FQtDFWQKEINLFLKIGKKAEQQALASKGLKFVTDEYLPEKLEEKDWL 366
Spo11 COG1697
DNA topoisomerase VI, subunit A [Replication, recombination and repair];
2-212 1.47e-53

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


Pssm-ID: 441303 [Multi-domain]  Cd Length: 360  Bit Score: 175.04  E-value: 1.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066   2 EEDGTRVQCTCSAT-ATAVPTNIQGMQHLITDAKFLLIVEKDATFQRLLDDNFCSRMSpCIMVTGKGVPDLNTRLLVKKL 80
Cdd:COG1697   154 GTRGDEIDCSKVGEgGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVHLKGQPARATRRFLRRL 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066  81 WDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIPTIRWLGLLPSDIQRLNIPKDsliPLTKHDQMKLDSILK 160
Cdd:COG1697   233 NEELGLPVYVFTDGDPWGYYIYSVIKYGSIKLAHESERLATPDAKFIGVTPSDIEEYDLPTD---KLKDKDIKRAKELLK 309

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907140066 161 RPYITYqPLWKKELEMMADSKMKAEIQALTLLSSDYLSRVYLPNKLRFGGWI 212
Cdd:COG1697   310 DPWFQT-DYWQKEINLFLKLKKKAEQQALAKKGLDFVTDTYLPEKLEEGGWL 360
 
Name Accession Description Interval E-value
TOPRIM_TopoIIB_SPO cd00223
TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of ...
 34-196 2.39e-75

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: 224.06  E-value: 2.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066  34 KFLLIVEKDATFQRLLDDNFCSRmSPCIMVTGKGVPDLNTRLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMS 113
Cdd:cd00223     1 DFVLVVEKEAVFQRLIEEGFHER-NNCILITGKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISILLTYKYGSIKLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066 114 FEAHNLTIPTIRWLGLLPSDIQRlnIPKDSLIPLTKHDQMKLDSILKRPYITYQPLWKKELEMMADSKMKAEIQALTLLS 193
Cdd:cd00223    80 YESESLATPDLRWLGLRPSDIIR--LPDLPLLPLSERDLKRAKSLLRRPRFKELPEWKRELQLMLKLGKKAEIEALASCG 157


                  ...
gi 1907140066 194 SDY 196
Cdd:cd00223   158 LEF 160
PRK04342 PRK04342
DNA topoisomerase IV subunit A;
3-212 5.29e-54

DNA topoisomerase IV subunit A;


Pssm-ID: 235287 [Multi-domain]  Cd Length: 367  Bit Score: 176.63  E-value: 5.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066   3 EDGTRV-QCT-CSATATAVPTNIQGMQHLITDAKFLLIVEKDATFQRLLDDNFCSRMSpCIMVTGKGVPDLNTRLLVKKL 80
Cdd:PRK04342  158 RDGTDEiDCSkLGEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVHLKGQPARATRRFIKRL 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066  81 WDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIPTIRWLGLLPSDIQRlNIPKDSLIPLTKHDQMKLDSILK 160
Cdd:PRK04342  237 NEELGLPVYVFTDGDPWGYYIYSVVKYGSIKLAHLSERLATPDAKFIGVTPSDIVE-YERDLPTIKLKDSDIKRAKELLN 315

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907140066 161 RPYitYQ-PLWKKELEMMADSKMKAEIQALTLLSSDYLSRVYLPNKLRFGGWI 212
Cdd:PRK04342  316 YPW--FQtDFWQKEINLFLKIGKKAEQQALASKGLKFVTDEYLPEKLEEKDWL 366
Spo11 COG1697
DNA topoisomerase VI, subunit A [Replication, recombination and repair];
2-212 1.47e-53

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


Pssm-ID: 441303 [Multi-domain]  Cd Length: 360  Bit Score: 175.04  E-value: 1.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066   2 EEDGTRVQCTCSAT-ATAVPTNIQGMQHLITDAKFLLIVEKDATFQRLLDDNFCSRMSpCIMVTGKGVPDLNTRLLVKKL 80
Cdd:COG1697   154 GTRGDEIDCSKVGEgGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVHLKGQPARATRRFLRRL 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066  81 WDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIPTIRWLGLLPSDIQRLNIPKDsliPLTKHDQMKLDSILK 160
Cdd:COG1697   233 NEELGLPVYVFTDGDPWGYYIYSVIKYGSIKLAHESERLATPDAKFIGVTPSDIEEYDLPTD---KLKDKDIKRAKELLK 309

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907140066 161 RPYITYqPLWKKELEMMADSKMKAEIQALTLLSSDYLSRVYLPNKLRFGGWI 212
Cdd:COG1697   310 DPWFQT-DYWQKEINLFLKLKKKAEQQALAKKGLDFVTDTYLPEKLEEGGWL 360
PLN00060 PLN00060
meiotic recombination protein SPO11-2; Provisional
 2-212 2.96e-39

meiotic recombination protein SPO11-2; Provisional


Pssm-ID: 177691 [Multi-domain]  Cd Length: 384  Bit Score: 138.47  E-value: 2.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066   2 EEDGTRVQCT-CSATATAVPTNIQGMQHLI--TDAKFLLIVEKDATFQRLLDDNFCSRMsPCIMVTGKGVPDLNTRLLVK 78
Cdd:PLN00060  177 EPNEEPVDCSiLGISGHAITGDLNLLSNLIlsSDARYIIVVEKDAIFQRLAEDRFFNHI-PCILITAKGYPDLATRFILH 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140066  79 KLWDTF-HIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIpTIRWLGLLPSDIQRlnIPKDSLIPLTKHDQMKLDS 157
Cdd:PLN00060  256 RLSQTFpNLPILALVDWNPAGLAILCTYKFGSIGMGLEAYRYAC-NVKWLGLRGDDLQL--IPPEAFVELKPRDLQIAKS 332

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907140066 158 ILKRPYItyQPLWKKELEMMADSKMKAEIQALTLLSSDYLSRvYLPNKLRFGGWI 212
Cdd:PLN00060  333 LLSSKFL--QNRYREELTLMVQTGKRAEIEALYSHGYDYLGK-YVARKIVQGDYI 384
TOPRIM cd00188
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ...
 34-109 5.96e-08

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: 48.58  E-value: 5.96e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907140066  34 KFLLIVEKDATFQRLLDDNFCSrmspCIMVTGKGVPDLNTRLLVKKLWDtFHIPVFTLVDADPYGIEIM-CIYKYGS 109
Cdd:cd00188     1 KKLIIVEGPSDALALAQAGGYG----GAVVALGGHALNKTRELLKRLLG-EAKEVIIATDADREGEAIAlRLLELLK 72
 
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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