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Conserved domains on  [gi|157019418|gb|EAA05541|]
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AGAP010898-PA, partial [Anopheles gambiae str. PEST]

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 ...
 105-263 9.76e-57

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: 179.37  E-value: 9.76e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418 105 KLVLVVEKDTVFKRLLEDGILSTFPdtLVLITAKGYPDVSTRLLLKKISDWTHVPIYGLMDADPHGIEIFCVYKFGSLAM 184
Cdd:cd00223    1 DFVLVVEKEAVFQRLIEEGFHERNN--CILITGKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISILLTYKYGSIKL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418 185 VHQQRSLAVPTMRWIGLFPSDI-ELLGLQGVPLREGELKRIEQMTKRPY--TEGHIQRELLLLRQLATKVEIESLYNIAS 261
Cdd:cd00223   79 AYESESLATPDLRWLGLRPSDIiRLPDLPLLPLSERDLKRAKSLLRRPRfkELPEWKRELQLMLKLGKKAEIEALASCGL 158


                 ..
gi 157019418 262 DF 263
Cdd:cd00223  159 EF 160
TP6A_N pfam04406
Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze ...
 2-58 1.45e-11

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: 58.64  E-value: 1.45e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157019418    2 MVQLLATIYQLLTTGSSCTKRELYYLHLELAQTPAYTYATLEDVCALLDADPWELHV 58
Cdd:pfam04406   6 LLRLLELIHELLLEGKTSTKRDIYYRDVELFKSQSEVDRLIDDLEVLLGVPREDLNV 62
 
Name Accession Description Interval E-value
TOPRIM_TopoIIB_SPO cd00223
TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of ...
 105-263 9.76e-57

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: 179.37  E-value: 9.76e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418 105 KLVLVVEKDTVFKRLLEDGILSTFPdtLVLITAKGYPDVSTRLLLKKISDWTHVPIYGLMDADPHGIEIFCVYKFGSLAM 184
Cdd:cd00223    1 DFVLVVEKEAVFQRLIEEGFHERNN--CILITGKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISILLTYKYGSIKL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418 185 VHQQRSLAVPTMRWIGLFPSDI-ELLGLQGVPLREGELKRIEQMTKRPY--TEGHIQRELLLLRQLATKVEIESLYNIAS 261
Cdd:cd00223   79 AYESESLATPDLRWLGLRPSDIiRLPDLPLLPLSERDLKRAKSLLRRPRfkELPEWKRELQLMLKLGKKAEIEALASCGL 158


                 ..
gi 157019418 262 DF 263
Cdd:cd00223  159 EF 160
Spo11 COG1697
DNA topoisomerase VI, subunit A [Replication, recombination and repair];
2-275 3.64e-45

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


Pssm-ID: 441303 [Multi-domain]  Cd Length: 360  Bit Score: 155.78  E-value: 3.64e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418   2 MVQLLATIYQLLTTGSSCTKRELYYLHLELAQTPAyTYAT-------LEDVCALLDADPWELHVYNTSKGLIAGPIVL-T 73
Cdd:COG1697   75 TLLVASFIKELLEENKTSTLRELYYISKHWILKEN-TFDEqdesdalIEDLEVATGVLREEFHIRPEEKGSVVGPLTIrD 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418  74 LSDGQRIDCN--GRWGTAVPLDVGSVTEIRLAAKLVLVVEKDTVFKRLLEDGilstFPDTL--VLITAKGYPDVSTRLLL 149
Cdd:COG1697  154 GTRGDEIDCSkvGEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEG----FWKKYnaILVHLKGQPARATRRFL 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418 150 KKISDWTHVPIYGLMDADPHGIEIFCVYKFGSLAMVHQQRSLAVPTMRWIGLFPSDIELLGLQGVPLREGELKRIEQMTK 229
Cdd:COG1697  230 RRLNEELGLPVYVFTDGDPWGYYIYSVIKYGSIKLAHESERLATPDAKFIGVTPSDIEEYDLPTDKLKDKDIKRAKELLK 309

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 157019418 230 RP-YTEGHIQRELLLLRQLATKVEIESLYNIASDFITTVYLKGKLKE 275
Cdd:COG1697  310 DPwFQTDYWQKEINLFLKLKKKAEQQALAKKGLDFVTDTYLPEKLEE 356
PRK04342 PRK04342
DNA topoisomerase IV subunit A;
2-275 3.56e-43

DNA topoisomerase IV subunit A;


Pssm-ID: 235287 [Multi-domain]  Cd Length: 367  Bit Score: 150.82  E-value: 3.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418   2 MVQLLATIYQLLTTGSSCTKRELYYLHLelAQTPAYTYATL----------EDVCALLDADPWELHVYNTSKGLIAGPIV 71
Cdd:PRK04342  79 TVLMAEFIKELLEENKSSTLRELYYMSK--HWIPGLKENTFddqdesdaviEDLEVALGVLREELHIRPEEDGSVVGPLR 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418  72 LTlSDGQRIDCN--GRWGTAVPLDVGSVTEIRLAAKLVLVVEKDTVFKRLLEDGilstFPDTL--VLITAKGYPDVSTRL 147
Cdd:PRK04342 157 IR-DGTDEIDCSklGEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEG----FWKKYnaILVHLKGQPARATRR 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418 148 LLKKISDWTHVPIYGLMDADPHGIEIFCVYKFGSLAMVHQQRSLAVPTMRWIGLFPSDIE--LLGLQGVPLREGELKRIE 225
Cdd:PRK04342 232 FIKRLNEELGLPVYVFTDGDPWGYYIYSVVKYGSIKLAHLSERLATPDAKFIGVTPSDIVeyERDLPTIKLKDSDIKRAK 311

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157019418 226 QMTKRPYTEGHI-QRELLLLRQLATKVEIESLYNIASDFITTVYLKGKLKE 275
Cdd:PRK04342 312 ELLNYPWFQTDFwQKEINLFLKIGKKAEQQALASKGLKFVTDEYLPEKLEE 362
TP6A_N pfam04406
Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze ...
 2-58 1.45e-11

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: 58.64  E-value: 1.45e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157019418    2 MVQLLATIYQLLTTGSSCTKRELYYLHLELAQTPAYTYATLEDVCALLDADPWELHV 58
Cdd:pfam04406   6 LLRLLELIHELLLEGKTSTKRDIYYRDVELFKSQSEVDRLIDDLEVLLGVPREDLNV 62
 
Name Accession Description Interval E-value
TOPRIM_TopoIIB_SPO cd00223
TOPRIM_TopoIIB_SPO: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of ...
 105-263 9.76e-57

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: 179.37  E-value: 9.76e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418 105 KLVLVVEKDTVFKRLLEDGILSTFPdtLVLITAKGYPDVSTRLLLKKISDWTHVPIYGLMDADPHGIEIFCVYKFGSLAM 184
Cdd:cd00223    1 DFVLVVEKEAVFQRLIEEGFHERNN--CILITGKGYPDRATRRFLRRLHEELDLPVYILVDGDPYGISILLTYKYGSIKL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418 185 VHQQRSLAVPTMRWIGLFPSDI-ELLGLQGVPLREGELKRIEQMTKRPY--TEGHIQRELLLLRQLATKVEIESLYNIAS 261
Cdd:cd00223   79 AYESESLATPDLRWLGLRPSDIiRLPDLPLLPLSERDLKRAKSLLRRPRfkELPEWKRELQLMLKLGKKAEIEALASCGL 158


                 ..
gi 157019418 262 DF 263
Cdd:cd00223  159 EF 160
Spo11 COG1697
DNA topoisomerase VI, subunit A [Replication, recombination and repair];
2-275 3.64e-45

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


Pssm-ID: 441303 [Multi-domain]  Cd Length: 360  Bit Score: 155.78  E-value: 3.64e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418   2 MVQLLATIYQLLTTGSSCTKRELYYLHLELAQTPAyTYAT-------LEDVCALLDADPWELHVYNTSKGLIAGPIVL-T 73
Cdd:COG1697   75 TLLVASFIKELLEENKTSTLRELYYISKHWILKEN-TFDEqdesdalIEDLEVATGVLREEFHIRPEEKGSVVGPLTIrD 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418  74 LSDGQRIDCN--GRWGTAVPLDVGSVTEIRLAAKLVLVVEKDTVFKRLLEDGilstFPDTL--VLITAKGYPDVSTRLLL 149
Cdd:COG1697  154 GTRGDEIDCSkvGEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEG----FWKKYnaILVHLKGQPARATRRFL 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418 150 KKISDWTHVPIYGLMDADPHGIEIFCVYKFGSLAMVHQQRSLAVPTMRWIGLFPSDIELLGLQGVPLREGELKRIEQMTK 229
Cdd:COG1697  230 RRLNEELGLPVYVFTDGDPWGYYIYSVIKYGSIKLAHESERLATPDAKFIGVTPSDIEEYDLPTDKLKDKDIKRAKELLK 309

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 157019418 230 RP-YTEGHIQRELLLLRQLATKVEIESLYNIASDFITTVYLKGKLKE 275
Cdd:COG1697  310 DPwFQTDYWQKEINLFLKLKKKAEQQALAKKGLDFVTDTYLPEKLEE 356
PRK04342 PRK04342
DNA topoisomerase IV subunit A;
2-275 3.56e-43

DNA topoisomerase IV subunit A;


Pssm-ID: 235287 [Multi-domain]  Cd Length: 367  Bit Score: 150.82  E-value: 3.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418   2 MVQLLATIYQLLTTGSSCTKRELYYLHLelAQTPAYTYATL----------EDVCALLDADPWELHVYNTSKGLIAGPIV 71
Cdd:PRK04342  79 TVLMAEFIKELLEENKSSTLRELYYMSK--HWIPGLKENTFddqdesdaviEDLEVALGVLREELHIRPEEDGSVVGPLR 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418  72 LTlSDGQRIDCN--GRWGTAVPLDVGSVTEIRLAAKLVLVVEKDTVFKRLLEDGilstFPDTL--VLITAKGYPDVSTRL 147
Cdd:PRK04342 157 IR-DGTDEIDCSklGEGGYSIPPNVDNIEFVDVDADFVLAVEKGGMFQRLVEEG----FWKKYnaILVHLKGQPARATRR 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418 148 LLKKISDWTHVPIYGLMDADPHGIEIFCVYKFGSLAMVHQQRSLAVPTMRWIGLFPSDIE--LLGLQGVPLREGELKRIE 225
Cdd:PRK04342 232 FIKRLNEELGLPVYVFTDGDPWGYYIYSVVKYGSIKLAHLSERLATPDAKFIGVTPSDIVeyERDLPTIKLKDSDIKRAK 311

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157019418 226 QMTKRPYTEGHI-QRELLLLRQLATKVEIESLYNIASDFITTVYLKGKLKE 275
Cdd:PRK04342 312 ELLNYPWFQTDFwQKEINLFLKIGKKAEQQALASKGLKFVTDEYLPEKLEE 362
PLN00060 PLN00060
meiotic recombination protein SPO11-2; Provisional
 4-264 8.75e-35

meiotic recombination protein SPO11-2; Provisional


Pssm-ID: 177691 [Multi-domain]  Cd Length: 384  Bit Score: 128.84  E-value: 8.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418   4 QLLATIYQLLTTGSSCTKRELYYLHLelAQTPAY------TYATLEDVCALLDADPWELHVYNTSKGLIAGPIVLTLSDG 77
Cdd:PLN00060 103 KVMEMCYQILGEGKLVTQRELFYKLL--CDSPEYfscqrhVNQTVQDVVSLLRCSRYSLGIMASSRGALIGRLVLQEPNE 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418  78 QRIDCN--GRWGTAVP--LDVGSVTEIRLAAKLVLVVEKDTVFKRLLEDGILSTFPdtLVLITAKGYPDVSTRLLLKKIS 153
Cdd:PLN00060 181 EPVDCSilGISGHAITgdLNLLSNLILSSDARYIIVVEKDAIFQRLAEDRFFNHIP--CILITAKGYPDLATRFILHRLS 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157019418 154 -DWTHVPIYGLMDADPHGIEIFCVYKFGSLAMVHQQRSLAVpTMRWIGLFPSDIELLGLQG-VPLREGELKRIEQMTKRP 231
Cdd:PLN00060 259 qTFPNLPILALVDWNPAGLAILCTYKFGSIGMGLEAYRYAC-NVKWLGLRGDDLQLIPPEAfVELKPRDLQIAKSLLSSK 337

                        250       260       270
                 ....*....|....*....|....*....|...
gi 157019418 232 YTEGHIQRELLLLRQLATKVEIESLYNIASDFI 264
Cdd:PLN00060 338 FLQNRYREELTLMVQTGKRAEIEALYSHGYDYL 370
TP6A_N pfam04406
Type IIB DNA topoisomerase; Type II DNA topoisomerases are ubiquitous enzymes that catalyze ...
 2-58 1.45e-11

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: 58.64  E-value: 1.45e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157019418    2 MVQLLATIYQLLTTGSSCTKRELYYLHLELAQTPAYTYATLEDVCALLDADPWELHV 58
Cdd:pfam04406   6 LLRLLELIHELLLEGKTSTKRDIYYRDVELFKSQSEVDRLIDDLEVLLGVPREDLNV 62
TOPRIM cd00188
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ...
 105-181 1.17e-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: 42.80  E-value: 1.17e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157019418 105 KLVLVVEKDTVFKRLLEDGILSTfpdtlVLITAKGYPDVSTRLLLKKISDwTHVPIYGLMDADPHGIEI-FCVYKFGS 181
Cdd:cd00188    1 KKLIIVEGPSDALALAQAGGYGG-----AVVALGGHALNKTRELLKRLLG-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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