NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767806545|ref|NP_001292363|]
View 

meiotic recombination protein SPO11 isoform d [Mus musculus]

Protein Classification

TP6A_N and TOPRIM_TopoIIB_SPO domain-containing protein( domain architecture ID 10507686)

protein containing domains SPO11_like, TP6A_N, and TOPRIM_TopoIIB_SPO

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
176-338 1.57e-74

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: 227.52  E-value: 1.57e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 176 KFLLIVEKDATFQRLLDDNFCSRmSPCIMVTGKGVPDLNTRLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMS 255
Cdd:cd00223    1 DFVLVVEKEAVFQRLIEEGFHER-NNCILITGKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISILLTYKYGSIKLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 256 FEAHNLTIPTIRWLGLLPSDIQRlnIPKDSLIPLTKHDQMKLDSILKRPYITYQPLWKKELEMMADSKMKAEIQALTLLS 335
Cdd:cd00223   80 YESESLATPDLRWLGLRPSDIIR--LPDLPLLPLSERDLKRAKSLLRRPRFKELPEWKRELQLMLKLGKKAEIEALASCG 157

                 ...
gi 767806545 336 SDY 338
Cdd:cd00223  158 LEF 160
TP6A_N pfam04406
Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze ...
71-132 8.68e-27

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: 100.62  E-value: 8.68e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767806545   71 KKFALILKVLSMIYKLIQSDTYATKRDIYYTDSQLFGNQAAVDSAIDDISCMLKVPRRSLHV 132
Cdd:pfam04406   1 KKFAQLLRLLELIHELLLEGKTSTKRDIYYRDVELFKSQSEVDRLIDDLEVLLGVPREDLNV 62
SPO11_like pfam03533
SPO11 homolog;
2-43 3.74e-23

SPO11 homolog;


:

Pssm-ID: 460961  Cd Length: 43  Bit Score: 90.64  E-value: 3.74e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 767806545    2 AFAPMGPEASFFDALDRHRASLLAMVKRGAGETPAGATRVAS 43
Cdd:pfam03533   1 AFAPMGPEASFFEVLDRHRASLLAALRRGGGEPPAGGTRLAS 42
 
Name Accession Description Interval E-value
TOPRIM_TopoIIB_SPO cd00223
TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of ...
176-338 1.57e-74

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: 227.52  E-value: 1.57e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 176 KFLLIVEKDATFQRLLDDNFCSRmSPCIMVTGKGVPDLNTRLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMS 255
Cdd:cd00223    1 DFVLVVEKEAVFQRLIEEGFHER-NNCILITGKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISILLTYKYGSIKLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 256 FEAHNLTIPTIRWLGLLPSDIQRlnIPKDSLIPLTKHDQMKLDSILKRPYITYQPLWKKELEMMADSKMKAEIQALTLLS 335
Cdd:cd00223   80 YESESLATPDLRWLGLRPSDIIR--LPDLPLLPLSERDLKRAKSLLRRPRFKELPEWKRELQLMLKLGKKAEIEALASCG 157

                 ...
gi 767806545 336 SDY 338
Cdd:cd00223  158 LEF 160
Spo11 COG1697
DNA topoisomerase VI, subunit A [Replication, recombination and repair];
68-354 5.51e-74

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


Pssm-ID: 441303 [Multi-domain]  Cd Length: 360  Bit Score: 233.20  E-value: 5.51e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545  68 KSVKKFALILKVLSMIYKLIQSDTYATKRDIYY------TDSQLFGNQAAVDSAIDDISCMLKVPRRSLHVLSTSKGLIA 141
Cdd:COG1697   67 KQAKKFMQTLLVASFIKELLEENKTSTLRELYYiskhwiLKENTFDEQDESDALIEDLEVATGVLREEFHIRPEEKGSVV 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 142 GNLRYMEE-DGTRVQCTCSAT-ATAVPTNIQGMQ----HAKFLLIVEKDATFQRLLDDNFCSRMSpCIMVTGKGVPDLNT 215
Cdd:COG1697  147 GPLTIRDGtRGDEIDCSKVGEgGYSIPPNVDNIEfvdvDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVHLKGQPARAT 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 216 RLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIPTIRWLGLLPSDIQRLNIPKDsliPLTKHDQM 295
Cdd:COG1697  226 RRFLRRLNEELGLPVYVFTDGDPWGYYIYSVIKYGSIKLAHESERLATPDAKFIGVTPSDIEEYDLPTD---KLKDKDIK 302
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767806545 296 KLDSILKRPYITYqPLWKKELEMMADSKMKAEIQALTLLSSDYLSRVYLPNKLRFGGWI 354
Cdd:COG1697  303 RAKELLKDPWFQT-DYWQKEINLFLKLKKKAEQQALAKKGLDFVTDTYLPEKLEEGGWL 360
PRK04342 PRK04342
DNA topoisomerase IV subunit A;
68-354 1.81e-73

DNA topoisomerase IV subunit A;


Pssm-ID: 235287 [Multi-domain]  Cd Length: 367  Bit Score: 232.10  E-value: 1.81e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545  68 KSVKKFALILKVLSMIYKLIQSDTYATKRDIYY--------TDSQLFGNQAAVDSAIDDISCMLKVPRRSLHVLSTSKGL 139
Cdd:PRK04342  71 KQAKKFMQTVLMAEFIKELLEENKSSTLRELYYmskhwipgLKENTFDDQDESDAVIEDLEVALGVLREELHIRPEEDGS 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 140 IAGNLRyMEEDGTRVQCT-CSATATAVPTNIQGMQ----HAKFLLIVEKDATFQRLLDDNFCSRMSpCIMVTGKGVPDLN 214
Cdd:PRK04342 151 VVGPLR-IRDGTDEIDCSkLGEGGYSIPPNVDNIEfvdvDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVHLKGQPARA 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 215 TRLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIPTIRWLGLLPSDIQRlNIPKDSLIPLTKHDQ 294
Cdd:PRK04342 229 TRRFIKRLNEELGLPVYVFTDGDPWGYYIYSVVKYGSIKLAHLSERLATPDAKFIGVTPSDIVE-YERDLPTIKLKDSDI 307
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767806545 295 MKLDSILKRPYitYQ-PLWKKELEMMADSKMKAEIQALTLLSSDYLSRVYLPNKLRFGGWI 354
Cdd:PRK04342 308 KRAKELLNYPW--FQtDFWQKEINLFLKIGKKAEQQALASKGLKFVTDEYLPEKLEEKDWL 366
TP6A_N pfam04406
Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze ...
71-132 8.68e-27

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: 100.62  E-value: 8.68e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767806545   71 KKFALILKVLSMIYKLIQSDTYATKRDIYYTDSQLFGNQAAVDSAIDDISCMLKVPRRSLHV 132
Cdd:pfam04406   1 KKFAQLLRLLELIHELLLEGKTSTKRDIYYRDVELFKSQSEVDRLIDDLEVLLGVPREDLNV 62
SPO11_like pfam03533
SPO11 homolog;
2-43 3.74e-23

SPO11 homolog;


Pssm-ID: 460961  Cd Length: 43  Bit Score: 90.64  E-value: 3.74e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 767806545    2 AFAPMGPEASFFDALDRHRASLLAMVKRGAGETPAGATRVAS 43
Cdd:pfam03533   1 AFAPMGPEASFFEVLDRHRASLLAALRRGGGEPPAGGTRLAS 42
 
Name Accession Description Interval E-value
TOPRIM_TopoIIB_SPO cd00223
TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of ...
176-338 1.57e-74

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: 227.52  E-value: 1.57e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 176 KFLLIVEKDATFQRLLDDNFCSRmSPCIMVTGKGVPDLNTRLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMS 255
Cdd:cd00223    1 DFVLVVEKEAVFQRLIEEGFHER-NNCILITGKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISILLTYKYGSIKLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 256 FEAHNLTIPTIRWLGLLPSDIQRlnIPKDSLIPLTKHDQMKLDSILKRPYITYQPLWKKELEMMADSKMKAEIQALTLLS 335
Cdd:cd00223   80 YESESLATPDLRWLGLRPSDIIR--LPDLPLLPLSERDLKRAKSLLRRPRFKELPEWKRELQLMLKLGKKAEIEALASCG 157

                 ...
gi 767806545 336 SDY 338
Cdd:cd00223  158 LEF 160
Spo11 COG1697
DNA topoisomerase VI, subunit A [Replication, recombination and repair];
68-354 5.51e-74

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


Pssm-ID: 441303 [Multi-domain]  Cd Length: 360  Bit Score: 233.20  E-value: 5.51e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545  68 KSVKKFALILKVLSMIYKLIQSDTYATKRDIYY------TDSQLFGNQAAVDSAIDDISCMLKVPRRSLHVLSTSKGLIA 141
Cdd:COG1697   67 KQAKKFMQTLLVASFIKELLEENKTSTLRELYYiskhwiLKENTFDEQDESDALIEDLEVATGVLREEFHIRPEEKGSVV 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 142 GNLRYMEE-DGTRVQCTCSAT-ATAVPTNIQGMQ----HAKFLLIVEKDATFQRLLDDNFCSRMSpCIMVTGKGVPDLNT 215
Cdd:COG1697  147 GPLTIRDGtRGDEIDCSKVGEgGYSIPPNVDNIEfvdvDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVHLKGQPARAT 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 216 RLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIPTIRWLGLLPSDIQRLNIPKDsliPLTKHDQM 295
Cdd:COG1697  226 RRFLRRLNEELGLPVYVFTDGDPWGYYIYSVIKYGSIKLAHESERLATPDAKFIGVTPSDIEEYDLPTD---KLKDKDIK 302
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767806545 296 KLDSILKRPYITYqPLWKKELEMMADSKMKAEIQALTLLSSDYLSRVYLPNKLRFGGWI 354
Cdd:COG1697  303 RAKELLKDPWFQT-DYWQKEINLFLKLKKKAEQQALAKKGLDFVTDTYLPEKLEEGGWL 360
PRK04342 PRK04342
DNA topoisomerase IV subunit A;
68-354 1.81e-73

DNA topoisomerase IV subunit A;


Pssm-ID: 235287 [Multi-domain]  Cd Length: 367  Bit Score: 232.10  E-value: 1.81e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545  68 KSVKKFALILKVLSMIYKLIQSDTYATKRDIYY--------TDSQLFGNQAAVDSAIDDISCMLKVPRRSLHVLSTSKGL 139
Cdd:PRK04342  71 KQAKKFMQTVLMAEFIKELLEENKSSTLRELYYmskhwipgLKENTFDDQDESDAVIEDLEVALGVLREELHIRPEEDGS 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 140 IAGNLRyMEEDGTRVQCT-CSATATAVPTNIQGMQ----HAKFLLIVEKDATFQRLLDDNFCSRMSpCIMVTGKGVPDLN 214
Cdd:PRK04342 151 VVGPLR-IRDGTDEIDCSkLGEGGYSIPPNVDNIEfvdvDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVHLKGQPARA 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 215 TRLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIPTIRWLGLLPSDIQRlNIPKDSLIPLTKHDQ 294
Cdd:PRK04342 229 TRRFIKRLNEELGLPVYVFTDGDPWGYYIYSVVKYGSIKLAHLSERLATPDAKFIGVTPSDIVE-YERDLPTIKLKDSDI 307
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767806545 295 MKLDSILKRPYitYQ-PLWKKELEMMADSKMKAEIQALTLLSSDYLSRVYLPNKLRFGGWI 354
Cdd:PRK04342 308 KRAKELLNYPW--FQtDFWQKEINLFLKIGKKAEQQALASKGLKFVTDEYLPEKLEEKDWL 366
PLN00060 PLN00060
meiotic recombination protein SPO11-2; Provisional
68-354 1.45e-51

meiotic recombination protein SPO11-2; Provisional


Pssm-ID: 177691 [Multi-domain]  Cd Length: 384  Bit Score: 175.84  E-value: 1.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545  68 KSVKKFALILKVLSMIYKLIQSDTYATKRDIYYT----DSQLFGNQAAVDSAIDDISCMLKVPRRSLHVLSTSKGLIAGN 143
Cdd:PLN00060  93 GSAKAFVRVWKVMEMCYQILGEGKLVTQRELFYKllcdSPEYFSCQRHVNQTVQDVVSLLRCSRYSLGIMASSRGALIGR 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 144 LRYMEEDGTRVQCT-CSATATAVPTNIQGMQH------AKFLLIVEKDATFQRLLDDNFCSRMsPCIMVTGKGVPDLNTR 216
Cdd:PLN00060 173 LVLQEPNEEPVDCSiLGISGHAITGDLNLLSNlilssdARYIIVVEKDAIFQRLAEDRFFNHI-PCILITAKGYPDLATR 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767806545 217 LLVKKLWDTF-HIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIpTIRWLGLLPSDIQRlnIPKDSLIPLTKHDQM 295
Cdd:PLN00060 252 FILHRLSQTFpNLPILALVDWNPAGLAILCTYKFGSIGMGLEAYRYAC-NVKWLGLRGDDLQL--IPPEAFVELKPRDLQ 328
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767806545 296 KLDSILKRPYItyQPLWKKELEMMADSKMKAEIQALTLLSSDYLSRvYLPNKLRFGGWI 354
Cdd:PLN00060 329 IAKSLLSSKFL--QNRYREELTLMVQTGKRAEIEALYSHGYDYLGK-YVARKIVQGDYI 384
TP6A_N pfam04406
Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze ...
71-132 8.68e-27

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: 100.62  E-value: 8.68e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767806545   71 KKFALILKVLSMIYKLIQSDTYATKRDIYYTDSQLFGNQAAVDSAIDDISCMLKVPRRSLHV 132
Cdd:pfam04406   1 KKFAQLLRLLELIHELLLEGKTSTKRDIYYRDVELFKSQSEVDRLIDDLEVLLGVPREDLNV 62
SPO11_like pfam03533
SPO11 homolog;
2-43 3.74e-23

SPO11 homolog;


Pssm-ID: 460961  Cd Length: 43  Bit Score: 90.64  E-value: 3.74e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 767806545    2 AFAPMGPEASFFDALDRHRASLLAMVKRGAGETPAGATRVAS 43
Cdd:pfam03533   1 AFAPMGPEASFFEVLDRHRASLLAALRRGGGEPPAGGTRLAS 42
TOPRIM cd00188
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ...
176-251 1.63e-07

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: 48.19  E-value: 1.63e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767806545 176 KFLLIVEKDATFQRLLDDNFCSrmspCIMVTGKGVPDLNTRLLVKKLWDtFHIPVFTLVDADPYGIEIM-CIYKYGS 251
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH