|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
3-365 |
1.52e-57 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 205.76 E-value: 1.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 3 RIPEAELQHLKAAVSLVAVVqaqGR--QLVKKGKDFTTLCPFHDEKTPSCVISPEKNLYHCFGCNAGGSVLNWVMQTEKL 80
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVI---GEyvKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 81 SLRKAAERLKAELGdnpavVPLVTRDEPEIFADDEAGRQKL---LGRVVEFYHHTLLNAPE---AVAYLEKRRLNhPELV 154
Cdd:COG0358 78 SFPEAVEELAERAG-----IELPEEEGSPEEREEASERERLyeaLELAAKFYQEQLKNTPEgkaARDYLKKRGLS-DETI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 155 AAFKLGFAnrtlpyrlPAvksrAGEKIRARLKGVGV----LRESG----------HEHFTGSLVVPVMDLNGQIREMYGR 220
Cdd:COG0358 152 ERFGLGYA--------PD----GWDALLKHLKKKGFseeeLVEAGlvieredggyYDRFRGRIMFPIRDLRGRVIGFGGR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 221 KITDR----LRSG-TAL-----HLY-LPGAHggvwneQALIGSSVVILCESLIDAMSFWVAGVRNVTAAYGVNgfTGEMR 289
Cdd:COG0358 220 VLDDGepkyLNSPeTPLfhkgrVLYgLDLAR------KAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTA--LTEEH 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149955363 290 AALLAHGVKQVLIAYDNDPAGNEAAVKLASSLAADGIATFRVLFPAGMDANGYLcqVAEPEQAFSVLLDGAVPMSD 365
Cdd:COG0358 292 IKLLKRYTDEVILCFDGDAAGQKAALRALELLLKDGLQVRVLFLPDGEDPDELI--RKEGAEAFRELLENAKPLIE 365
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
3-365 |
3.46e-53 |
|
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria protein. Most members of this family contain nearly two hundred additional residues C-terminal to the region represented here, but conservation between species is poor and the C-terminal region was not included in the seed alignment. This protein contains a CHC2 zinc finger (pfam01807) and a Toprim domain (pfam01751). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273595 [Multi-domain] Cd Length: 415 Bit Score: 191.67 E-value: 3.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 3 RIPEAELQHLKAAVSLVAVVQAQgRQLVKKGKDFTTLCPFHDEKTPSCVISPEKNLYHCFGCNAGGSVLNWVMQTEKLSL 82
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEY-VKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 83 RKAAERLKAELGdnpavVPLVTRDEPEIFADDEAGRQKL---LGRVVEFYHHTLLNAPE---AVAYLEKRRLNhPELVAA 156
Cdd:TIGR01391 80 VEAVEELAKRAG-----IDLPFEKDQQEKKEQKSKRKKLyelLELAAKFFKNQLKHTPEnraALDYLQSRGLS-DETIDR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 157 FKLGFAnrtlPYRLPAVKSRAGEKIRARLK-----GVGVLRESG--HEHFTGSLVVPVMDLNGQIREMYGRKITDR---- 225
Cdd:TIGR01391 154 FELGYA----PNNWDFLFDFLQNKKGFDLEllaeaGLLVKKENGkyYDRFRNRIMFPIHDPKGRVVGFGGRALGDEkpky 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 226 LRSG-TAL-----HLYLpgahggvWNE--QALIGSSVVILCESLIDAMSFWVAGVRNVTAAYGVNgFTGEmRAALLAHGV 297
Cdd:TIGR01391 230 LNSPeTPLfkkseLLYG-------LHKarKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTA-LTEE-HIKLLKRYA 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149955363 298 KQVLIAYDNDPAGNEAAVKLASSLAADGIATFRVLFPAGMDANGYLCQvaEPEQAFSVLLDGAVPMSD 365
Cdd:TIGR01391 301 DEIILCFDGDKAGRKAALRAIELLLPLGINVKVIKLPGGKDPDEYLRK--EGVEALKKLLENSKSLIE 366
|
|
| zf-CHC2 |
pfam01807 |
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases. |
5-94 |
3.58e-26 |
|
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
Pssm-ID: 426447 [Multi-domain] Cd Length: 95 Bit Score: 103.10 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 5 PEAELQHLKAAVSLVAVVQAQgRQLVKKGKDFTTLCPFHDEKTPSCVISPEKNLYHCFGCNAGGSVLNWVMQTEKLSLRK 84
Cdd:pfam01807 1 PPEFIDDLKNRIDIVDVVGQY-VKLKKRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIKFLMKIEKLSFVE 79
|
90
....*....|
gi 1149955363 85 AAERLKAELG 94
Cdd:pfam01807 80 AVEKLADRYG 89
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
39-89 |
3.43e-19 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 81.96 E-value: 3.43e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1149955363 39 LCPFHDEKTPSCVISPEKNLYHCFGCNAGGSVLNWVMQTEKLSLRKAAERL 89
Cdd:smart00400 4 LCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKL 54
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
255-333 |
1.94e-14 |
|
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase domain found in the active site regions of proteins similar to Escherichia coli DnaG. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM 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. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. E. coli DnaG is a single subunit enzyme.
Pssm-ID: 173784 [Multi-domain] Cd Length: 79 Bit Score: 69.08 E-value: 1.94e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149955363 255 VILCESLIDAMSFWVAGVRNVTAAYGVNgFTGEmRAALLAHGVKQVLIAYDNDPAGNEAAVKLASSLAADGIATFRVLF 333
Cdd:cd03364 3 VILVEGYMDVIALHQAGIKNVVASLGTA-LTEE-QAELLKRLAKEVILAFDGDEAGQKAALRALELLLKLGLNVRVLTL 79
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
237-356 |
5.43e-05 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 45.95 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 237 PGAHGgvWNEQALIGSSVViLCESLIDAMSF-WVAGVRNVTAAyGVNGFT--GEMRAALLAHGVKQVLIAYDNDPAGNEA 313
Cdd:PHA02031 147 PDYVG--WPPELSMPRPVV-LTEDYLSALKVrWACNKPEVFAV-ALLGTRlrDRLAAILLQQTCPRVLIFLDGDPAGVDG 222
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1149955363 314 AVKLASSLAADGIATFRVLFPAGMDANGylcqvAEPEQAFSVL 356
Cdd:PHA02031 223 SAGAMRRLRPLLIEGQVIITPDGFDPKD-----LEREQIRELL 260
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
3-365 |
1.52e-57 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 205.76 E-value: 1.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 3 RIPEAELQHLKAAVSLVAVVqaqGR--QLVKKGKDFTTLCPFHDEKTPSCVISPEKNLYHCFGCNAGGSVLNWVMQTEKL 80
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVI---GEyvKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 81 SLRKAAERLKAELGdnpavVPLVTRDEPEIFADDEAGRQKL---LGRVVEFYHHTLLNAPE---AVAYLEKRRLNhPELV 154
Cdd:COG0358 78 SFPEAVEELAERAG-----IELPEEEGSPEEREEASERERLyeaLELAAKFYQEQLKNTPEgkaARDYLKKRGLS-DETI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 155 AAFKLGFAnrtlpyrlPAvksrAGEKIRARLKGVGV----LRESG----------HEHFTGSLVVPVMDLNGQIREMYGR 220
Cdd:COG0358 152 ERFGLGYA--------PD----GWDALLKHLKKKGFseeeLVEAGlvieredggyYDRFRGRIMFPIRDLRGRVIGFGGR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 221 KITDR----LRSG-TAL-----HLY-LPGAHggvwneQALIGSSVVILCESLIDAMSFWVAGVRNVTAAYGVNgfTGEMR 289
Cdd:COG0358 220 VLDDGepkyLNSPeTPLfhkgrVLYgLDLAR------KAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTA--LTEEH 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149955363 290 AALLAHGVKQVLIAYDNDPAGNEAAVKLASSLAADGIATFRVLFPAGMDANGYLcqVAEPEQAFSVLLDGAVPMSD 365
Cdd:COG0358 292 IKLLKRYTDEVILCFDGDAAGQKAALRALELLLKDGLQVRVLFLPDGEDPDELI--RKEGAEAFRELLENAKPLIE 365
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
3-365 |
3.46e-53 |
|
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria protein. Most members of this family contain nearly two hundred additional residues C-terminal to the region represented here, but conservation between species is poor and the C-terminal region was not included in the seed alignment. This protein contains a CHC2 zinc finger (pfam01807) and a Toprim domain (pfam01751). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273595 [Multi-domain] Cd Length: 415 Bit Score: 191.67 E-value: 3.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 3 RIPEAELQHLKAAVSLVAVVQAQgRQLVKKGKDFTTLCPFHDEKTPSCVISPEKNLYHCFGCNAGGSVLNWVMQTEKLSL 82
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEY-VKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 83 RKAAERLKAELGdnpavVPLVTRDEPEIFADDEAGRQKL---LGRVVEFYHHTLLNAPE---AVAYLEKRRLNhPELVAA 156
Cdd:TIGR01391 80 VEAVEELAKRAG-----IDLPFEKDQQEKKEQKSKRKKLyelLELAAKFFKNQLKHTPEnraALDYLQSRGLS-DETIDR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 157 FKLGFAnrtlPYRLPAVKSRAGEKIRARLK-----GVGVLRESG--HEHFTGSLVVPVMDLNGQIREMYGRKITDR---- 225
Cdd:TIGR01391 154 FELGYA----PNNWDFLFDFLQNKKGFDLEllaeaGLLVKKENGkyYDRFRNRIMFPIHDPKGRVVGFGGRALGDEkpky 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 226 LRSG-TAL-----HLYLpgahggvWNE--QALIGSSVVILCESLIDAMSFWVAGVRNVTAAYGVNgFTGEmRAALLAHGV 297
Cdd:TIGR01391 230 LNSPeTPLfkkseLLYG-------LHKarKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTA-LTEE-HIKLLKRYA 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149955363 298 KQVLIAYDNDPAGNEAAVKLASSLAADGIATFRVLFPAGMDANGYLCQvaEPEQAFSVLLDGAVPMSD 365
Cdd:TIGR01391 301 DEIILCFDGDKAGRKAALRAIELLLPLGINVKVIKLPGGKDPDEYLRK--EGVEALKKLLENSKSLIE 366
|
|
| zf-CHC2 |
pfam01807 |
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases. |
5-94 |
3.58e-26 |
|
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
Pssm-ID: 426447 [Multi-domain] Cd Length: 95 Bit Score: 103.10 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 5 PEAELQHLKAAVSLVAVVQAQgRQLVKKGKDFTTLCPFHDEKTPSCVISPEKNLYHCFGCNAGGSVLNWVMQTEKLSLRK 84
Cdd:pfam01807 1 PPEFIDDLKNRIDIVDVVGQY-VKLKKRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIKFLMKIEKLSFVE 79
|
90
....*....|
gi 1149955363 85 AAERLKAELG 94
Cdd:pfam01807 80 AVEKLADRYG 89
|
|
| Toprim_2 |
pfam13155 |
Toprim-like; This is a family or Toprim-like proteins. |
256-343 |
3.23e-20 |
|
Toprim-like; This is a family or Toprim-like proteins.
Pssm-ID: 463793 [Multi-domain] Cd Length: 88 Bit Score: 86.08 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 256 ILCESLIDAMSFWVAGVRNVT--AAYGVNgFTGEMrAALLAHGVKQVLIAYDNDPAGNEAAVKLASSLAADGIATFRVLF 333
Cdd:pfam13155 1 VVFEGYIDALSLAQAGIKNVLyvATLGTA-LTEAQ-IKLLKRYPKEVILAFDNDEAGRKAAKRLAELLKEAGVDVKIRLL 78
|
90
....*....|
gi 1149955363 334 PAGMDANGYL 343
Cdd:pfam13155 79 PDGKDWNEYL 88
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
39-89 |
3.43e-19 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 81.96 E-value: 3.43e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1149955363 39 LCPFHDEKTPSCVISPEKNLYHCFGCNAGGSVLNWVMQTEKLSLRKAAERL 89
Cdd:smart00400 4 LCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKL 54
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
255-333 |
1.94e-14 |
|
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase domain found in the active site regions of proteins similar to Escherichia coli DnaG. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM 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. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. E. coli DnaG is a single subunit enzyme.
Pssm-ID: 173784 [Multi-domain] Cd Length: 79 Bit Score: 69.08 E-value: 1.94e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149955363 255 VILCESLIDAMSFWVAGVRNVTAAYGVNgFTGEmRAALLAHGVKQVLIAYDNDPAGNEAAVKLASSLAADGIATFRVLF 333
Cdd:cd03364 3 VILVEGYMDVIALHQAGIKNVVASLGTA-LTEE-QAELLKRLAKEVILAFDGDEAGQKAALRALELLLKLGLNVRVLTL 79
|
|
| TOPRIM_primases |
cd01029 |
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
255-333 |
1.40e-12 |
|
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in the active site regions of bacterial DnaG-type primases and their homologs. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM 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. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The prototypical bacterial primase. Escherichia coli DnaG is a single subunit enzyme.
Pssm-ID: 173779 [Multi-domain] Cd Length: 79 Bit Score: 63.83 E-value: 1.40e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149955363 255 VILCESLIDAMSFWVAGVRNVTAAYGVNGFTGEMRaaLLAHGVKQVLIAYDNDPAGNEAAVKLASSLAADGIATFRVLF 333
Cdd:cd01029 3 VIIVEGYMDVLALHQAGIKNVVAALGTANTEEQLR--LLKRFARTVILAFDNDEAGKKAAARALELLLALGGRVRVPPL 79
|
|
| Toprim_3 |
pfam13362 |
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ... |
254-345 |
4.41e-09 |
|
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic acid manipulation.
Pssm-ID: 433146 [Multi-domain] Cd Length: 97 Bit Score: 54.71 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 254 VVILCESLIDAMSfwVAGVRNVTAAYGVNGF-TGEMRAALLAHGVKQVLIAYDNDPA--GNEAAVKLASSLAADGIATFR 330
Cdd:pfam13362 1 RLIIGEGIETALS--LTQRLNPPGTPVIALLsAANLKAVAWPERVKRVYIAADNDAAndGQAAAEKLAERLEAAGIEAVL 78
|
90
....*....|....*
gi 1149955363 331 VLFPAGMDANGYLCQ 345
Cdd:pfam13362 79 LEPEAGEDWNDDLQQ 93
|
|
| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
253-333 |
1.60e-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: 52.43 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 253 SVVILCESLIDAMSFWVAGVR--NVTAAYGVNGFTGEMRAALLAHGVKQVLIAYDNDPAGNEAAVKLASSLAADGIATFR 330
Cdd:cd00188 1 KKLIIVEGPSDALALAQAGGYggAVVALGGHALNKTRELLKRLLGEAKEVIIATDADREGEAIALRLLELLKSLGKKVRR 80
|
...
gi 1149955363 331 VLF 333
Cdd:cd00188 81 LLL 83
|
|
| Toprim_4 |
pfam13662 |
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ... |
253-331 |
3.75e-07 |
|
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic acid manipulation.
Pssm-ID: 433387 [Multi-domain] Cd Length: 85 Bit Score: 48.82 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 253 SVVILCESLIDAMSFWVAGVRNVTAAYGVN-----GFTGEMRAALLAHGVKQVLIAYDNDPAGNEAAVKLASSLAADGIA 327
Cdd:pfam13662 1 SEIIVVEGYADVIALEKAGYKGAVAVLGGAlspldGIGPEDLNIDSLGGIKEVILALDGDVAGEKTALYLAEALLEEGVK 80
|
....
gi 1149955363 328 TFRV 331
Cdd:pfam13662 81 VSRL 84
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
237-356 |
5.43e-05 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 45.95 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 237 PGAHGgvWNEQALIGSSVViLCESLIDAMSF-WVAGVRNVTAAyGVNGFT--GEMRAALLAHGVKQVLIAYDNDPAGNEA 313
Cdd:PHA02031 147 PDYVG--WPPELSMPRPVV-LTEDYLSALKVrWACNKPEVFAV-ALLGTRlrDRLAAILLQQTCPRVLIFLDGDPAGVDG 222
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1149955363 314 AVKLASSLAADGIATFRVLFPAGMDANGylcqvAEPEQAFSVL 356
Cdd:PHA02031 223 SAGAMRRLRPLLIEGQVIITPDGFDPKD-----LEREQIRELL 260
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
128-224 |
5.13e-04 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 40.97 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 128 FYHHTLLNAP--EAVAYLEKRRLNhPELVAAFKLGFA---NRTLPYRLPAVKSRAGEKIRArlkGVGVLRESG--HEHFT 200
Cdd:pfam08275 1 FYQELLKTNEgaAALDYLKSRGLS-DETIERFQIGYApdgWDNLLKFLKKKGFSEEELLEA---GLLSKNEDGryYDRFR 76
|
90 100
....*....|....*....|....
gi 1149955363 201 GSLVVPVMDLNGQIREMYGRKITD 224
Cdd:pfam08275 77 NRIMFPIKDARGRVVGFGGRALDD 100
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
254-333 |
1.12e-03 |
|
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim domain common to DnaG primases, topoisomerases, OLD family nucleases and RecR proteins. Both DnaG motifs IV and V are present in the alignment, the DxD (V) motif may be involved in Mg2+ binding and mutations to the conserved glutamate (IV) completely abolish DnaG type primase activity. DNA primase EC:2.7.7.6 is a nucleotidyltransferase it synthesizes the oligoribonucleotide primers required for DNA replication on the lagging strand of the replication fork; it can also prime the leading stand and has been implicated in cell division. This family also includes the atypical archaeal A subunit from type II DNA topoisomerases. Type II DNA topoisomerases catalyze the relaxation of DNA supercoiling by causing transient double strand breaks.
Pssm-ID: 396354 [Multi-domain] Cd Length: 93 Bit Score: 39.26 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149955363 254 VVILCESLIDAMS---FWVAGVRNVTAAYG-----VNGFTGEMRAAL--LAHGVKQVLIAYDNDPAGNEAAVKLASSLAA 323
Cdd:pfam01751 1 ELIIVEGPSDAIAlekALGGGFQAVVAVLGhllslEKGPKKKALKALkeLALKAKEVILATDPDREGEAIALKLLELKEL 80
|
90
....*....|
gi 1149955363 324 DGIATFRVLF 333
Cdd:pfam01751 81 LENAGGRVEF 90
|
|
| |
