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Conserved domains on  [gi|530418037|ref|XP_005260436|]
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meiotic recombination protein SPO11 isoform X1 [Homo sapiens]

Protein Classification

SPO11/TOP6A family protein( domain architecture ID 13688712)

SPO11/TOP6A family protein similar to Drosophila melanogaster meiotic recombination protein W68 that is required for meiotic recombination

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Spo11 super family cl34337
DNA topoisomerase VI, subunit A [Replication, recombination and repair];
46-407 1.38e-78

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


The actual alignment was detected with superfamily member COG1697:

Pssm-ID: 441303 [Multi-domain]  Cd Length: 360  Bit Score: 246.68  E-value: 1.38e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037  46 EVLASIENIIQDIITSLARNEAPAFTIDNRSSwENIKFEDSVG-LQMVSHCTTRKIKSdsPKSAQKFSLILKILSMIYKL 124
Cdd:COG1697    9 KALKKLKELAEKIYDQIEKGEIPVLEIPSRTL-SNIEYDEKKGvLKLGDKKSVRSFLN--VKQAKKFMQTLLVASFIKEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 125 VQSNTYATKRDIYY------TDSQLFGNQTVVDNIINDISCMLKVSRRSLHILSTSKGLIAGNLRYIEE-DGTKVNCT-C 196
Cdd:COG1697   86 LEENKTSTLRELYYiskhwiLKENTFDEQDESDALIEDLEVATGVLREEFHIRPEEKGSVVGPLTIRDGtRGDEIDCSkV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 197 GATAVAVPSNIQGIRNLVTDAKFVLIVEKDATFQRLLDDNFCNKLSpCIMITstpvfqhlkskGKGVPDLNTRLLVKKLW 276
Cdd:COG1697  166 GEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVH-----------LKGQPARATRRFLRRLN 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 277 DTFHVPVFTLVDADPHGIEIMCIYKYGSMSMSFEAHHLTVPAIRWLGLLPSDLKRLNVPKDsliPLTKRDQMKLDSILRR 356
Cdd:COG1697  234 EELGLPVYVFTDGDPWGYYIYSVIKYGSIKLAHESERLATPDAKFIGVTPSDIEEYDLPTD---KLKDKDIKRAKELLKD 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530418037 357 P-YVTcqPFWRKEMEIMADSKMKAEIQALTFLSSDYLSRVYLPNKLKFGGWI 407
Cdd:COG1697  311 PwFQT--DYWQKEINLFLKLKKKAEQQALAKKGLDFVTDTYLPEKLEEGGWL 360
SPO11_like pfam03533
SPO11 homolog;
2-44 9.40e-26

SPO11 homolog;


:

Pssm-ID: 460961  Cd Length: 43  Bit Score: 98.34  E-value: 9.40e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530418037    2 AFAPMGPEASFFDVLDRHRESLLAALRRGGREPPTGGSRLASS 44
Cdd:pfam03533   1 AFAPMGPEASFFEVLDRHRASLLAALRRGGGEPPAGGTRLASS 43
 
Name Accession Description Interval E-value
Spo11 COG1697
DNA topoisomerase VI, subunit A [Replication, recombination and repair];
46-407 1.38e-78

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


Pssm-ID: 441303 [Multi-domain]  Cd Length: 360  Bit Score: 246.68  E-value: 1.38e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037  46 EVLASIENIIQDIITSLARNEAPAFTIDNRSSwENIKFEDSVG-LQMVSHCTTRKIKSdsPKSAQKFSLILKILSMIYKL 124
Cdd:COG1697    9 KALKKLKELAEKIYDQIEKGEIPVLEIPSRTL-SNIEYDEKKGvLKLGDKKSVRSFLN--VKQAKKFMQTLLVASFIKEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 125 VQSNTYATKRDIYY------TDSQLFGNQTVVDNIINDISCMLKVSRRSLHILSTSKGLIAGNLRYIEE-DGTKVNCT-C 196
Cdd:COG1697   86 LEENKTSTLRELYYiskhwiLKENTFDEQDESDALIEDLEVATGVLREEFHIRPEEKGSVVGPLTIRDGtRGDEIDCSkV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 197 GATAVAVPSNIQGIRNLVTDAKFVLIVEKDATFQRLLDDNFCNKLSpCIMITstpvfqhlkskGKGVPDLNTRLLVKKLW 276
Cdd:COG1697  166 GEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVH-----------LKGQPARATRRFLRRLN 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 277 DTFHVPVFTLVDADPHGIEIMCIYKYGSMSMSFEAHHLTVPAIRWLGLLPSDLKRLNVPKDsliPLTKRDQMKLDSILRR 356
Cdd:COG1697  234 EELGLPVYVFTDGDPWGYYIYSVIKYGSIKLAHESERLATPDAKFIGVTPSDIEEYDLPTD---KLKDKDIKRAKELLKD 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530418037 357 P-YVTcqPFWRKEMEIMADSKMKAEIQALTFLSSDYLSRVYLPNKLKFGGWI 407
Cdd:COG1697  311 PwFQT--DYWQKEINLFLKLKKKAEQQALAKKGLDFVTDTYLPEKLEEGGWL 360
PRK04342 PRK04342
DNA topoisomerase IV subunit A;
42-407 2.09e-76

DNA topoisomerase IV subunit A;


Pssm-ID: 235287 [Multi-domain]  Cd Length: 367  Bit Score: 241.34  E-value: 2.09e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037  42 ASSSEVLASIENIIQDIITSLARNEAPAFTIDNRSSwENIKFEDSVGLqMVSHCTTRKIKSDSPKSAQKFSLILKILSMI 121
Cdd:PRK04342   9 EDREKALKKLRELAEKIYEDIEKGKRPVLEIPKRTL-SNIEYDEKKGL-LVLGDKKSKRSFLNVKQAKKFMQTVLMAEFI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 122 YKLVQSNTYATKRDIYY--------TDSQLFGNQTVVDNIINDISCMLKVSRRSLHILSTSKGLIAGNLRyIEEDGTKVN 193
Cdd:PRK04342  87 KELLEENKSSTLRELYYmskhwipgLKENTFDDQDESDAVIEDLEVALGVLREELHIRPEEDGSVVGPLR-IRDGTDEID 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 194 CT-CGATAVAVPSNIQGIRNLVTDAKFVLIVEKDATFQRLLDDNFCNKLSpCIMITstpvfqhlkskGKGVPDLNTRLLV 272
Cdd:PRK04342 166 CSkLGEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVH-----------LKGQPARATRRFI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 273 KKLWDTFHVPVFTLVDADPHGIEIMCIYKYGSMSMSFEAHHLTVPAIRWLGLLPSDLKRlNVPKDSLIPLTKRDQMKLDS 352
Cdd:PRK04342 234 KRLNEELGLPVYVFTDGDPWGYYIYSVVKYGSIKLAHLSERLATPDAKFIGVTPSDIVE-YERDLPTIKLKDSDIKRAKE 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530418037 353 ILRRP-YVTcqPFWRKEMEIMADSKMKAEIQALTFLSSDYLSRVYLPNKLKFGGWI 407
Cdd:PRK04342 313 LLNYPwFQT--DFWQKEINLFLKIGKKAEQQALASKGLKFVTDEYLPEKLEEKDWL 366
TOPRIM_TopoIIB_SPO cd00223
TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of ...
218-391 4.02e-73

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: 225.60  E-value: 4.02e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 218 KFVLIVEKDATFQRLLDDNFCNKLsPCIMITstpvfqhlkskGKGVPDLNTRLLVKKLWDTFHVPVFTLVDADPHGIEIM 297
Cdd:cd00223    1 DFVLVVEKEAVFQRLIEEGFHERN-NCILIT-----------GKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISIL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 298 CIYKYGSMSMSFEAHHLTVPAIRWLGLLPSDLKRLnvPKDSLIPLTKRDQMKLDSILRRPYVTCQPFWRKEMEIMADSKM 377
Cdd:cd00223   69 LTYKYGSIKLAYESESLATPDLRWLGLRPSDIIRL--PDLPLLPLSERDLKRAKSLLRRPRFKELPEWKRELQLMLKLGK 146
                        170
                 ....*....|....
gi 530418037 378 KAEIQALTFLSSDY 391
Cdd:cd00223  147 KAEIEALASCGLEF 160
SPO11_like pfam03533
SPO11 homolog;
2-44 9.40e-26

SPO11 homolog;


Pssm-ID: 460961  Cd Length: 43  Bit Score: 98.34  E-value: 9.40e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530418037    2 AFAPMGPEASFFDVLDRHRESLLAALRRGGREPPTGGSRLASS 44
Cdd:pfam03533   1 AFAPMGPEASFFEVLDRHRASLLAALRRGGGEPPAGGTRLASS 43
TP6A_N pfam04406
Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze ...
109-170 4.11e-25

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: 96.77  E-value: 4.11e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530418037  109 QKFSLILKILSMIYKLVQSNTYATKRDIYYTDSQLFGNQTVVDNIINDISCMLKVSRRSLHI 170
Cdd:pfam04406   1 KKFAQLLRLLELIHELLLEGKTSTKRDIYYRDVELFKSQSEVDRLIDDLEVLLGVPREDLNV 62
 
Name Accession Description Interval E-value
Spo11 COG1697
DNA topoisomerase VI, subunit A [Replication, recombination and repair];
46-407 1.38e-78

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


Pssm-ID: 441303 [Multi-domain]  Cd Length: 360  Bit Score: 246.68  E-value: 1.38e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037  46 EVLASIENIIQDIITSLARNEAPAFTIDNRSSwENIKFEDSVG-LQMVSHCTTRKIKSdsPKSAQKFSLILKILSMIYKL 124
Cdd:COG1697    9 KALKKLKELAEKIYDQIEKGEIPVLEIPSRTL-SNIEYDEKKGvLKLGDKKSVRSFLN--VKQAKKFMQTLLVASFIKEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 125 VQSNTYATKRDIYY------TDSQLFGNQTVVDNIINDISCMLKVSRRSLHILSTSKGLIAGNLRYIEE-DGTKVNCT-C 196
Cdd:COG1697   86 LEENKTSTLRELYYiskhwiLKENTFDEQDESDALIEDLEVATGVLREEFHIRPEEKGSVVGPLTIRDGtRGDEIDCSkV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 197 GATAVAVPSNIQGIRNLVTDAKFVLIVEKDATFQRLLDDNFCNKLSpCIMITstpvfqhlkskGKGVPDLNTRLLVKKLW 276
Cdd:COG1697  166 GEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVH-----------LKGQPARATRRFLRRLN 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 277 DTFHVPVFTLVDADPHGIEIMCIYKYGSMSMSFEAHHLTVPAIRWLGLLPSDLKRLNVPKDsliPLTKRDQMKLDSILRR 356
Cdd:COG1697  234 EELGLPVYVFTDGDPWGYYIYSVIKYGSIKLAHESERLATPDAKFIGVTPSDIEEYDLPTD---KLKDKDIKRAKELLKD 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530418037 357 P-YVTcqPFWRKEMEIMADSKMKAEIQALTFLSSDYLSRVYLPNKLKFGGWI 407
Cdd:COG1697  311 PwFQT--DYWQKEINLFLKLKKKAEQQALAKKGLDFVTDTYLPEKLEEGGWL 360
PRK04342 PRK04342
DNA topoisomerase IV subunit A;
42-407 2.09e-76

DNA topoisomerase IV subunit A;


Pssm-ID: 235287 [Multi-domain]  Cd Length: 367  Bit Score: 241.34  E-value: 2.09e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037  42 ASSSEVLASIENIIQDIITSLARNEAPAFTIDNRSSwENIKFEDSVGLqMVSHCTTRKIKSDSPKSAQKFSLILKILSMI 121
Cdd:PRK04342   9 EDREKALKKLRELAEKIYEDIEKGKRPVLEIPKRTL-SNIEYDEKKGL-LVLGDKKSKRSFLNVKQAKKFMQTVLMAEFI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 122 YKLVQSNTYATKRDIYY--------TDSQLFGNQTVVDNIINDISCMLKVSRRSLHILSTSKGLIAGNLRyIEEDGTKVN 193
Cdd:PRK04342  87 KELLEENKSSTLRELYYmskhwipgLKENTFDDQDESDAVIEDLEVALGVLREELHIRPEEDGSVVGPLR-IRDGTDEID 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 194 CT-CGATAVAVPSNIQGIRNLVTDAKFVLIVEKDATFQRLLDDNFCNKLSpCIMITstpvfqhlkskGKGVPDLNTRLLV 272
Cdd:PRK04342 166 CSkLGEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEGFWKKYN-AILVH-----------LKGQPARATRRFI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 273 KKLWDTFHVPVFTLVDADPHGIEIMCIYKYGSMSMSFEAHHLTVPAIRWLGLLPSDLKRlNVPKDSLIPLTKRDQMKLDS 352
Cdd:PRK04342 234 KRLNEELGLPVYVFTDGDPWGYYIYSVVKYGSIKLAHLSERLATPDAKFIGVTPSDIVE-YERDLPTIKLKDSDIKRAKE 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530418037 353 ILRRP-YVTcqPFWRKEMEIMADSKMKAEIQALTFLSSDYLSRVYLPNKLKFGGWI 407
Cdd:PRK04342 313 LLNYPwFQT--DFWQKEINLFLKIGKKAEQQALASKGLKFVTDEYLPEKLEEKDWL 366
TOPRIM_TopoIIB_SPO cd00223
TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of ...
218-391 4.02e-73

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: 225.60  E-value: 4.02e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 218 KFVLIVEKDATFQRLLDDNFCNKLsPCIMITstpvfqhlkskGKGVPDLNTRLLVKKLWDTFHVPVFTLVDADPHGIEIM 297
Cdd:cd00223    1 DFVLVVEKEAVFQRLIEEGFHERN-NCILIT-----------GKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISIL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 298 CIYKYGSMSMSFEAHHLTVPAIRWLGLLPSDLKRLnvPKDSLIPLTKRDQMKLDSILRRPYVTCQPFWRKEMEIMADSKM 377
Cdd:cd00223   69 LTYKYGSIKLAYESESLATPDLRWLGLRPSDIIRL--PDLPLLPLSERDLKRAKSLLRRPRFKELPEWKRELQLMLKLGK 146
                        170
                 ....*....|....
gi 530418037 378 KAEIQALTFLSSDY 391
Cdd:cd00223  147 KAEIEALASCGLEF 160
PLN00060 PLN00060
meiotic recombination protein SPO11-2; Provisional
106-407 6.58e-55

meiotic recombination protein SPO11-2; Provisional


Pssm-ID: 177691 [Multi-domain]  Cd Length: 384  Bit Score: 186.24  E-value: 6.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 106 KSAQKFSLILKILSMIYKLVQSNTYATKRDIYYT----DSQLFGNQTVVDNIINDISCMLKVSRRSLHILSTSKGLIAGN 181
Cdd:PLN00060  93 GSAKAFVRVWKVMEMCYQILGEGKLVTQRELFYKllcdSPEYFSCQRHVNQTVQDVVSLLRCSRYSLGIMASSRGALIGR 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 182 LRYIEEDGTKVNCT-CGATAVAVPSNIQGIRNLV--TDAKFVLIVEKDATFQRLLDDNFCNKLsPCIMITStpvfqhlks 258
Cdd:PLN00060 173 LVLQEPNEEPVDCSiLGISGHAITGDLNLLSNLIlsSDARYIIVVEKDAIFQRLAEDRFFNHI-PCILITA--------- 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 259 kgKGVPDLNTRLLVKKLWDTF-HVPVFTLVDADPHGIEIMCIYKYGSMSMSFEAHHLtVPAIRWLGLLPSDLKRlnVPKD 337
Cdd:PLN00060 243 --KGYPDLATRFILHRLSQTFpNLPILALVDWNPAGLAILCTYKFGSIGMGLEAYRY-ACNVKWLGLRGDDLQL--IPPE 317
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 338 SLIPLTKRDQMKLDSILRRPYVtcQPFWRKEMEIMADSKMKAEIQALTFLSSDYLSRvYLPNKLKFGGWI 407
Cdd:PLN00060 318 AFVELKPRDLQIAKSLLSSKFL--QNRYREELTLMVQTGKRAEIEALYSHGYDYLGK-YVARKIVQGDYI 384
SPO11_like pfam03533
SPO11 homolog;
2-44 9.40e-26

SPO11 homolog;


Pssm-ID: 460961  Cd Length: 43  Bit Score: 98.34  E-value: 9.40e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530418037    2 AFAPMGPEASFFDVLDRHRESLLAALRRGGREPPTGGSRLASS 44
Cdd:pfam03533   1 AFAPMGPEASFFEVLDRHRASLLAALRRGGGEPPAGGTRLASS 43
TP6A_N pfam04406
Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze ...
109-170 4.11e-25

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: 96.77  E-value: 4.11e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530418037  109 QKFSLILKILSMIYKLVQSNTYATKRDIYYTDSQLFGNQTVVDNIINDISCMLKVSRRSLHI 170
Cdd:pfam04406   1 KKFAQLLRLLELIHELLLEGKTSTKRDIYYRDVELFKSQSEVDRLIDDLEVLLGVPREDLNV 62
TOPRIM cd00188
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ...
218-304 8.04e-05

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: 40.87  E-value: 8.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418037 218 KFVLIVEKDATFQRLLDDNFCNklspCIMITStpvfqhlkskgKGVPDLNTRLLVKKLWDtFHVPVFTLVDADPHGIEIM 297
Cdd:cd00188    1 KKLIIVEGPSDALALAQAGGYG----GAVVAL-----------GGHALNKTRELLKRLLG-EAKEVIIATDADREGEAIA 64

                 ....*...
gi 530418037 298 -CIYKYGS 304
Cdd:cd00188   65 lRLLELLK 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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