|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
1-429 |
0e+00 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 629.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 1 MIPQNFIDDLLYRLDIADVVGRYVQLKSAGANLQGLCPFHKEKSPSFSVSPSKQFYHCFGCGASGNAIGFVMEHLGMTFP 80
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 81 EAVEQLAGQLGMEVPYEKGMDLPEEVRSERDQIVELLTRSANYYKAQLKQSP---RAVQYLKNRGLTGQIAARYGLGYAP 157
Cdd:COG0358 81 EAVEELAERAGIELPEEEGSPEEREEASERERLYEALELAAKFYQEQLKNTPegkAARDYLKKRGLSDETIERFGLGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 158 ENYQNLESVV--DDYASNVLLDtAGLTKLSEQNsRRYDRFRDRVMFPIRNAKGQVIGFGGRVIEKAEPKYLNSPETPVFH 235
Cdd:COG0358 161 DGWDALLKHLkkKGFSEEELVE-AGLVIEREDG-GYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 236 KGHEVYGLFEARQAIHKKGYVLITEGYMDVVALAQWGFENAVATLGTAVTPDHVQKLFKQTDRLVFAFDGDGAGQKAAWR 315
Cdd:COG0358 239 KGRVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 316 ALQACLSHVNEVKradFIFLPTEHDPDSYVRTEGPDGFEALVAKALSLSDYLLRQVGSQFQVRQVEGSSAAVAFLKPLVA 395
Cdd:COG0358 319 ALELLLKDGLQVR---VLFLPDGEDPDELIRKEGAEAFRELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLA 395
|
410 420 430
....*....|....*....|....*....|....
gi 2526761200 396 QVQPSVFRSALVRSLADLLGMTPVELSSHLGLKR 429
Cdd:COG0358 396 KIPDPILRELYLRELAERLGLDEEALDALARLKR 429
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
1-414 |
2.44e-175 |
|
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: 502.91 E-value: 2.44e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 1 MIPQNFIDDLLYRLDIADVVGRYVQLKSAGANLQGLCPFHKEKSPSFSVSPSKQFYHCFGCGASGNAIGFVMEHLGMTFP 80
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 81 EAVEQLAGQLGMEVPYEKGMDLPEEVRSERDQIVELLTRSANYYKAQLKQSP---RAVQYLKNRGLTGQIAARYGLGYAP 157
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKKEQKSKRKKLYELLELAAKFFKNQLKHTPenrAALDYLQSRGLSDETIDRFELGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 158 ENYQNLESVV---DDYASNVLLDtAGLTKLSEqNSRRYDRFRDRVMFPIRNAKGQVIGFGGRVIEKAEPKYLNSPETPVF 234
Cdd:TIGR01391 161 NNWDFLFDFLqnkKGFDLELLAE-AGLLVKKE-NGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 235 HKGHEVYGLFEARQAIHKKGYVLITEGYMDVVALAQWGFENAVATLGTAVTPDHVQKLFKQTDRLVFAFDGDGAGQKAAW 314
Cdd:TIGR01391 239 KKSELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 315 RALQACLSHVNEVKradFIFLPTEHDPDSYVRTEGPDGFEALVAKALSLSDYLLRQVGSQFQVRQVEGSSAAVAFLKPLV 394
Cdd:TIGR01391 319 RAIELLLPLGINVK---VIKLPGGKDPDEYLRKEGVEALKKLLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLI 395
|
410 420
....*....|....*....|
gi 2526761200 395 AQVQPSVFRSALVRSLADLL 414
Cdd:TIGR01391 396 KKIPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
123-247 |
2.06e-50 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 170.01 E-value: 2.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 123 YYKAQLKQSP--RAVQYLKNRGLTGQIAARYGLGYAPENYQNLESVV--DDYASNVLLDtAGLTKLSEQNsRRYDRFRDR 198
Cdd:pfam08275 1 FYQELLKTNEgaAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLkkKGFSEEELLE-AGLLSKNEDG-RYYDRFRNR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2526761200 199 VMFPIRNAKGQVIGFGGRVIEKAEP-KYLNSPETPVFHKGHEVYGLFEAR 247
Cdd:pfam08275 79 IMFPIKDARGRVVGFGGRALDDDKPpKYLNSPETPLFKKSKLLYGLDEAK 128
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
256-332 |
5.91e-31 |
|
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: 115.30 E-value: 5.91e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526761200 256 VLITEGYMDVVALAQWGFENAVATLGTAVTPDHVQKLFKQTDRLVFAFDGDGAGQKAAWRALQACLSHVNEVKRADF 332
Cdd:cd03364 3 VILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKLGLNVRVLTL 79
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
33-87 |
6.31e-29 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 108.92 E-value: 6.31e-29
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2526761200 33 LQGLCPFHKEKSPSFSVSPSKQFYHCFGCGASGNAIGFVMEHLGMTFPEAVEQLA 87
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| PRK08624 |
PRK08624 |
hypothetical protein; Provisional |
192-294 |
5.06e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 236314 [Multi-domain] Cd Length: 373 Bit Score: 45.70 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 192 YDRFRDRVMFPIRNAKGQVIGFGGRVIEKAE-------PKYLNspETPVFH-KGHEVYGLFEARQAIHKKGYVLITEGYM 263
Cdd:PRK08624 177 LDVISQRIIIPHRDESGELIGIRGRLLDKELvdknkyfPIYVN--DTGYNHpKGKILYGLWQNKKYIKEKKKVIIVESEK 254
|
90 100 110
....*....|....*....|....*....|...
gi 2526761200 264 DVVALAQ-WGFEN-AVATLGTAVTPDHVQKLFK 294
Cdd:PRK08624 255 SVLFSDKfYGEGNfVVAICGSNISEVQAEKLLR 287
|
|
| DnaG_DnaB_bind |
smart00766 |
DNA primase DnaG DnaB-binding; DnaG_DnaB_bind defines a domain of primase required for ... |
460-567 |
2.44e-03 |
|
DNA primase DnaG DnaB-binding; DnaG_DnaB_bind defines a domain of primase required for functional interaction with DnaB that attracts primase to the replication fork. DnaG_DnaB_bind is responsible for the interaction between DnaG and DnaB.
Pssm-ID: 197866 Cd Length: 125 Bit Score: 38.40 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 460 LLGLaarLVRAPQCVGECFSLVELyeksDALPQEGHS-FIHLVEKIKENPNLLMARLPNAFNDQVHQSWVNGVVQEAQQL 538
Cdd:smart00766 4 LIRL---LLQNPELASLVPDLLPL----ELFTHPGLAlLAELLALCRGAPGLTTGQLLEHWRDTPYRELLSELAVWDHLI 76
|
90 100
....*....|....*....|....*....
gi 2526761200 539 DDEIDfETELKDAVYQCSEAWFKSELARL 567
Cdd:smart00766 77 DEENL-EEEFQDALARLRKQLLERRIEEL 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
1-429 |
0e+00 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 629.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 1 MIPQNFIDDLLYRLDIADVVGRYVQLKSAGANLQGLCPFHKEKSPSFSVSPSKQFYHCFGCGASGNAIGFVMEHLGMTFP 80
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 81 EAVEQLAGQLGMEVPYEKGMDLPEEVRSERDQIVELLTRSANYYKAQLKQSP---RAVQYLKNRGLTGQIAARYGLGYAP 157
Cdd:COG0358 81 EAVEELAERAGIELPEEEGSPEEREEASERERLYEALELAAKFYQEQLKNTPegkAARDYLKKRGLSDETIERFGLGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 158 ENYQNLESVV--DDYASNVLLDtAGLTKLSEQNsRRYDRFRDRVMFPIRNAKGQVIGFGGRVIEKAEPKYLNSPETPVFH 235
Cdd:COG0358 161 DGWDALLKHLkkKGFSEEELVE-AGLVIEREDG-GYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 236 KGHEVYGLFEARQAIHKKGYVLITEGYMDVVALAQWGFENAVATLGTAVTPDHVQKLFKQTDRLVFAFDGDGAGQKAAWR 315
Cdd:COG0358 239 KGRVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 316 ALQACLSHVNEVKradFIFLPTEHDPDSYVRTEGPDGFEALVAKALSLSDYLLRQVGSQFQVRQVEGSSAAVAFLKPLVA 395
Cdd:COG0358 319 ALELLLKDGLQVR---VLFLPDGEDPDELIRKEGAEAFRELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLA 395
|
410 420 430
....*....|....*....|....*....|....
gi 2526761200 396 QVQPSVFRSALVRSLADLLGMTPVELSSHLGLKR 429
Cdd:COG0358 396 KIPDPILRELYLRELAERLGLDEEALDALARLKR 429
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
1-414 |
2.44e-175 |
|
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: 502.91 E-value: 2.44e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 1 MIPQNFIDDLLYRLDIADVVGRYVQLKSAGANLQGLCPFHKEKSPSFSVSPSKQFYHCFGCGASGNAIGFVMEHLGMTFP 80
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 81 EAVEQLAGQLGMEVPYEKGMDLPEEVRSERDQIVELLTRSANYYKAQLKQSP---RAVQYLKNRGLTGQIAARYGLGYAP 157
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKKEQKSKRKKLYELLELAAKFFKNQLKHTPenrAALDYLQSRGLSDETIDRFELGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 158 ENYQNLESVV---DDYASNVLLDtAGLTKLSEqNSRRYDRFRDRVMFPIRNAKGQVIGFGGRVIEKAEPKYLNSPETPVF 234
Cdd:TIGR01391 161 NNWDFLFDFLqnkKGFDLELLAE-AGLLVKKE-NGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 235 HKGHEVYGLFEARQAIHKKGYVLITEGYMDVVALAQWGFENAVATLGTAVTPDHVQKLFKQTDRLVFAFDGDGAGQKAAW 314
Cdd:TIGR01391 239 KKSELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 315 RALQACLSHVNEVKradFIFLPTEHDPDSYVRTEGPDGFEALVAKALSLSDYLLRQVGSQFQVRQVEGSSAAVAFLKPLV 394
Cdd:TIGR01391 319 RAIELLLPLGINVK---VIKLPGGKDPDEYLRKEGVEALKKLLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLI 395
|
410 420
....*....|....*....|
gi 2526761200 395 AQVQPSVFRSALVRSLADLL 414
Cdd:TIGR01391 396 KKIPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
123-247 |
2.06e-50 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 170.01 E-value: 2.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 123 YYKAQLKQSP--RAVQYLKNRGLTGQIAARYGLGYAPENYQNLESVV--DDYASNVLLDtAGLTKLSEQNsRRYDRFRDR 198
Cdd:pfam08275 1 FYQELLKTNEgaAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLkkKGFSEEELLE-AGLLSKNEDG-RYYDRFRNR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2526761200 199 VMFPIRNAKGQVIGFGGRVIEKAEP-KYLNSPETPVFHKGHEVYGLFEAR 247
Cdd:pfam08275 79 IMFPIKDARGRVVGFGGRALDDDKPpKYLNSPETPLFKKSKLLYGLDEAK 128
|
|
| zf-CHC2 |
pfam01807 |
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases. |
3-97 |
8.23e-50 |
|
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
Pssm-ID: 426447 [Multi-domain] Cd Length: 95 Bit Score: 167.43 E-value: 8.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 3 PQNFIDDLLYRLDIADVVGRYVQLKSAGANLQGLCPFHKEKSPSFSVSPSKQFYHCFGCGASGNAIGFVMEHLGMTFPEA 82
Cdd:pfam01807 1 PPEFIDDLKNRIDIVDVVGQYVKLKKRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIKFLMKIEKLSFVEA 80
|
90
....*....|....*
gi 2526761200 83 VEQLAGQLGMEVPYE 97
Cdd:pfam01807 81 VEKLADRYGIEIPYE 95
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
256-332 |
5.91e-31 |
|
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: 115.30 E-value: 5.91e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526761200 256 VLITEGYMDVVALAQWGFENAVATLGTAVTPDHVQKLFKQTDRLVFAFDGDGAGQKAAWRALQACLSHVNEVKRADF 332
Cdd:cd03364 3 VILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKLGLNVRVLTL 79
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
33-87 |
6.31e-29 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 108.92 E-value: 6.31e-29
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2526761200 33 LQGLCPFHKEKSPSFSVSPSKQFYHCFGCGASGNAIGFVMEHLGMTFPEAVEQLA 87
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| TOPRIM_primases |
cd01029 |
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
256-332 |
1.31e-25 |
|
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: 100.42 E-value: 1.31e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526761200 256 VLITEGYMDVVALAQWGFENAVATLGTAVTPDHVQKLFKQTDRLVFAFDGDGAGQKAAWRALQACLSHVNEVKRADF 332
Cdd:cd01029 3 VIIVEGYMDVLALHQAGIKNVVAALGTANTEEQLRLLKRFARTVILAFDNDEAGKKAAARALELLLALGGRVRVPPL 79
|
|
| Toprim_4 |
pfam13662 |
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ... |
254-330 |
1.39e-18 |
|
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: 80.41 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 254 GYVLITEGYMDVVALAQWGFENAVATLGTAV-TPDHVQKL------FKQTDRLVFAFDGDGAGQKAAWRALQACLSHVNE 326
Cdd:pfam13662 1 SEIIVVEGYADVIALEKAGYKGAVAVLGGALsPLDGIGPEdlnidsLGGIKEVILALDGDVAGEKTALYLAEALLEEGVK 80
|
....
gi 2526761200 327 VKRA 330
Cdd:pfam13662 81 VSRL 84
|
|
| Toprim_2 |
pfam13155 |
Toprim-like; This is a family or Toprim-like proteins. |
258-345 |
4.62e-18 |
|
Toprim-like; This is a family or Toprim-like proteins.
Pssm-ID: 463793 [Multi-domain] Cd Length: 88 Bit Score: 79.14 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 258 ITEGYMDVVALAQWGFENA--VATLGTAVTPDHVQKLFKQTDRLVFAFDGDGAGQKAAWRAlqacLSHVNEVKRADFIF- 334
Cdd:pfam13155 2 VFEGYIDALSLAQAGIKNVlyVATLGTALTEAQIKLLKRYPKEVILAFDNDEAGRKAAKRL----AELLKEAGVDVKIRl 77
|
90
....*....|.
gi 2526761200 335 LPTEHDPDSYV 345
Cdd:pfam13155 78 LPDGKDWNEYL 88
|
|
| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
255-332 |
6.95e-15 |
|
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: 70.15 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 255 YVLITEGYMDVVALAQWGFE--NAVATLGTAV--TPDHVQKLFKQTDRLVFAFDGDGAGQKAAWRALQACLSHVNEVKRA 330
Cdd:cd00188 2 KLIIVEGPSDALALAQAGGYggAVVALGGHALnkTRELLKRLLGEAKEVIIATDADREGEAIALRLLELLKSLGKKVRRL 81
|
..
gi 2526761200 331 DF 332
Cdd:cd00188 82 LL 83
|
|
| TOPRIM |
smart00493 |
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins; |
256-324 |
2.30e-14 |
|
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
Pssm-ID: 214695 [Multi-domain] Cd Length: 75 Bit Score: 68.06 E-value: 2.30e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526761200 256 VLITEGYMDVVALAQWGFE--NAVATLGTAVTPDHVQKLFKQTDR--LVFAFDGDGAGQKAAWRALQACLSHV 324
Cdd:smart00493 3 LIIVEGPADAIALEKAGGKrgNVVALGGHLLSKEQIKLLKKLAKKaeVILATDPDREGEAIAWELAELLKPAG 75
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
256-335 |
4.32e-13 |
|
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: 65.07 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 256 VLITEGYMDVVALAQ---WGFENAVATLGTAVTPDH---------VQKLFKQTDRLVFAFDGDGAGQKAAWRALQACLSH 323
Cdd:pfam01751 2 LIIVEGPSDAIALEKalgGGFQAVVAVLGHLLSLEKgpkkkalkaLKELALKAKEVILATDPDREGEAIALKLLELKELL 81
|
90
....*....|..
gi 2526761200 324 VNEVKRADFIFL 335
Cdd:pfam01751 82 ENAGGRVEFSEL 93
|
|
| DnaB_bind |
pfam10410 |
DnaB-helicase binding domain of primase; This domain is the C-terminal region three-helical ... |
364-417 |
5.76e-07 |
|
DnaB-helicase binding domain of primase; This domain is the C-terminal region three-helical domain of primase. Primases synthesize short RNA strands on single-stranded DNA templates, thereby generating the hybrid duplexes required for the initiation of synthesis by DNA polymerases. Primases are recruited to single-stranded DNA by helicases, and this domain is the region of the primase which binds DnaB-helicase. It is associated with the Toprim domain (pfam01751) which is the central catalytic core.
Pssm-ID: 463082 Cd Length: 54 Bit Score: 46.68 E-value: 5.76e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2526761200 364 SDYLLRQVGSQFQVRQVEGSSAAVAFLKPLVAQVQPSVFRSALVRSLADLLGMT 417
Cdd:pfam10410 1 SEFLIRRLLKGYDLDTPEGRAAALREAAPLLAKIPDPVERDLYLRRLAEELGIS 54
|
|
| Toprim_3 |
pfam13362 |
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ... |
255-351 |
2.78e-05 |
|
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: 43.16 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 255 YVLITEGYMDVVALAQWgfENAVATLGTAVTP-DHVQKLF--KQTDRLVFAFDGDGA--GQKAAWRALQAClshvnevKR 329
Cdd:pfam13362 1 RLIIGEGIETALSLTQR--LNPPGTPVIALLSaANLKAVAwpERVKRVYIAADNDAAndGQAAAEKLAERL-------EA 71
|
90 100
....*....|....*....|....*.
gi 2526761200 330 ADF---IFLPTEH-DPDSYVRTEGPD 351
Cdd:pfam13362 72 AGIeavLLEPEAGeDWNDDLQQTGAA 97
|
|
| PRK08624 |
PRK08624 |
hypothetical protein; Provisional |
192-294 |
5.06e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 236314 [Multi-domain] Cd Length: 373 Bit Score: 45.70 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 192 YDRFRDRVMFPIRNAKGQVIGFGGRVIEKAE-------PKYLNspETPVFH-KGHEVYGLFEARQAIHKKGYVLITEGYM 263
Cdd:PRK08624 177 LDVISQRIIIPHRDESGELIGIRGRLLDKELvdknkyfPIYVN--DTGYNHpKGKILYGLWQNKKYIKEKKKVIIVESEK 254
|
90 100 110
....*....|....*....|....*....|...
gi 2526761200 264 DVVALAQ-WGFEN-AVATLGTAVTPDHVQKLFK 294
Cdd:PRK08624 255 SVLFSDKfYGEGNfVVAICGSNISEVQAEKLLR 287
|
|
| DnaG_DnaB_bind |
smart00766 |
DNA primase DnaG DnaB-binding; DnaG_DnaB_bind defines a domain of primase required for ... |
460-567 |
2.44e-03 |
|
DNA primase DnaG DnaB-binding; DnaG_DnaB_bind defines a domain of primase required for functional interaction with DnaB that attracts primase to the replication fork. DnaG_DnaB_bind is responsible for the interaction between DnaG and DnaB.
Pssm-ID: 197866 Cd Length: 125 Bit Score: 38.40 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526761200 460 LLGLaarLVRAPQCVGECFSLVELyeksDALPQEGHS-FIHLVEKIKENPNLLMARLPNAFNDQVHQSWVNGVVQEAQQL 538
Cdd:smart00766 4 LIRL---LLQNPELASLVPDLLPL----ELFTHPGLAlLAELLALCRGAPGLTTGQLLEHWRDTPYRELLSELAVWDHLI 76
|
90 100
....*....|....*....|....*....
gi 2526761200 539 DDEIDfETELKDAVYQCSEAWFKSELARL 567
Cdd:smart00766 77 DEENL-EEEFQDALARLRKQLLERRIEEL 104
|
|
| |
