|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
4-428 |
0e+00 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 666.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 4 RIPEETIETIRRTVDIVDVISDYVQLKKQGRNYFGLCPFHGEKTPSFSVSPEKQIFHCFGCGAGGNVFSFLMDIEGISFL 83
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 84 EAVKRLAVKANIDLShlQLDDADKSRTNTGETKMMVEAHELLKKFYHHLLVNTNEGQKALDYLQDRGWTREIIDQFEIGY 163
Cdd:COG0358 81 EAVEELAERAGIELP--EEEGSPEEREEASERERLYEALELAAKFYQEQLKNTPEGKAARDYLKKRGLSDETIERFGLGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 164 APNSWDFAVKLLSGRGFSLELMEKAGLIIRKENGDYFDRFRHRIMFPILNHHGDTVGFSGRLLGEGQPKYLNSPETAIFH 243
Cdd:COG0358 159 APDGWDALLKHLKKKGFSEEELVEAGLVIEREDGGYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 244 KGKILYNFHQARLHIRKHQEVILLEGFADVISAVQAGVAHSVATMGTALTEEHARILRRNVDTVIICYDGDASGIEATFR 323
Cdd:COG0358 239 KGRVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 324 AAEVLTEAGCHVKIATIPDGLDPDEYIRKYGPDRFrRDIIDAGSSLMAFKMMYFRKGKNLQDENDKIRYIEEVLREISKL 403
Cdd:COG0358 319 ALELLLKDGLQVRVLFLPDGEDPDELIRKEGAEAF-RELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLAKI 397
|
410 420
....*....|....*....|....*
gi 489341928 404 PNPIEWDYYLRQLADEFSLSLSALQ 428
Cdd:COG0358 398 PDPILRELYLRELAERLGLDEEALD 422
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
4-420 |
0e+00 |
|
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: 581.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 4 RIPEETIETIRRTVDIVDVISDYVQLKKQGRNYFGLCPFHGEKTPSFSVSPEKQIFHCFGCGAGGNVFSFLMDIEGISFL 83
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 84 EAVKRLAVKANIDLSHLQLDDadKSRTNTGETKMMVEAHELLKKFYHHLLVNTNEGQKALDYLQDRGWTREIIDQFEIGY 163
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQ--EKKEQKSKRKKLYELLELAAKFFKNQLKHTPENRAALDYLQSRGLSDETIDRFELGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 164 APNSWDFAVKLLSGR-GFSLELMEKAGLIIRKENGDYFDRFRHRIMFPILNHHGDTVGFSGRLLGEGQPKYLNSPETAIF 242
Cdd:TIGR01391 159 APNNWDFLFDFLQNKkGFDLELLAEAGLLVKKENGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 243 HKGKILYNFHQARLHIRKHQEVILLEGFADVISAVQAGVAHSVATMGTALTEEHARILRRNVDTVIICYDGDASGIEATF 322
Cdd:TIGR01391 239 KKSELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 323 RAAEVLTEAGCHVKIATIPDGLDPDEYIRKYGPDRFRRdIIDAGSSLMAFKMMYFRKGKNLQDENDKIRYIEEVLREISK 402
Cdd:TIGR01391 319 RAIELLLPLGINVKVIKLPGGKDPDEYLRKEGVEALKK-LLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLIKK 397
|
410
....*....|....*...
gi 489341928 403 LPNPIEWDYYLRQLADEF 420
Cdd:TIGR01391 398 IPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
128-255 |
6.03e-63 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 203.14 E-value: 6.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 128 FYHHLLvNTNEGQKALDYLQDRGWTREIIDQFEIGYAPNSWDFAVKLLSGRGFSLELMEKAGLIIRKENGDYFDRFRHRI 207
Cdd:pfam08275 1 FYQELL-KTNEGAAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLKKKGFSEEELLEAGLLSKNEDGRYYDRFRNRI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489341928 208 MFPILNHHGDTVGFSGRLL-GEGQPKYLNSPETAIFHKGKILYNFHQAR 255
Cdd:pfam08275 80 MFPIKDARGRVVGFGGRALdDDKPPKYLNSPETPLFKKSKLLYGLDEAK 128
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
263-340 |
2.09e-33 |
|
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: 122.24 E-value: 2.09e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489341928 263 EVILLEGFADVISAVQAGVAHSVATMGTALTEEHARILRRNVDTVIICYDGDASGIEATFRAAEVLTEAGCHVKIATI 340
Cdd:cd03364 2 KVILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKLGLNVRVLTL 79
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
36-90 |
6.07e-33 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 120.09 E-value: 6.07e-33
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489341928 36 YFGLCPFHGEKTPSFSVSPEKQIFHCFGCGAGGNVFSFLMDIEGISFLEAVKRLA 90
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| PRK08624 |
PRK08624 |
hypothetical protein; Provisional |
54-312 |
8.32e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 236314 [Multi-domain] Cd Length: 373 Bit Score: 70.35 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 54 PEKQIFHCF-GCGAGGNVFSFL-----MDIEGISFLEAVKRLAVKANIdlshlqlddadksrtNTGETKMMVEAHELLKK 127
Cdd:PRK08624 55 IENDNFHCYtRCGDIFDVFELLckrlkMEGKALSFSKAIRKITKILGL---------------SYFYEPKQQGIKPSFLK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 128 FyhHLLVNTNEGQKALD-YLQDRGWTREIIDQFeIGYAPNSWdfavkllSGRGFSLELMEKAgliirkENGDYFDRFRHR 206
Cdd:PRK08624 120 I--LDWVWTGKKEKKEKiQPQLKSFNENILNQF-VKIPNRKW-------LDEGISEKTQKYW------EIKFYLDVISQR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 207 IMFPILNHHGDTVGFSGRLL-------GEGQPKYLNspETAIFH-KGKILYNFHQARLHIRKHQEVILLEGFADVISAVQ 278
Cdd:PRK08624 184 IIIPHRDESGELIGIRGRLLdkelvdkNKYFPIYVN--DTGYNHpKGKILYGLWQNKKYIKEKKKVIIVESEKSVLFSDK 261
|
250 260 270
....*....|....*....|....*....|....*..
gi 489341928 279 A-GVAH-SVATMGTALTEEHARI-LRRNVDTVIICYD 312
Cdd:PRK08624 262 FyGEGNfVVAICGSNISEVQAEKlLRLGVEEVTIALD 298
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
4-428 |
0e+00 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 666.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 4 RIPEETIETIRRTVDIVDVISDYVQLKKQGRNYFGLCPFHGEKTPSFSVSPEKQIFHCFGCGAGGNVFSFLMDIEGISFL 83
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 84 EAVKRLAVKANIDLShlQLDDADKSRTNTGETKMMVEAHELLKKFYHHLLVNTNEGQKALDYLQDRGWTREIIDQFEIGY 163
Cdd:COG0358 81 EAVEELAERAGIELP--EEEGSPEEREEASERERLYEALELAAKFYQEQLKNTPEGKAARDYLKKRGLSDETIERFGLGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 164 APNSWDFAVKLLSGRGFSLELMEKAGLIIRKENGDYFDRFRHRIMFPILNHHGDTVGFSGRLLGEGQPKYLNSPETAIFH 243
Cdd:COG0358 159 APDGWDALLKHLKKKGFSEEELVEAGLVIEREDGGYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 244 KGKILYNFHQARLHIRKHQEVILLEGFADVISAVQAGVAHSVATMGTALTEEHARILRRNVDTVIICYDGDASGIEATFR 323
Cdd:COG0358 239 KGRVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 324 AAEVLTEAGCHVKIATIPDGLDPDEYIRKYGPDRFrRDIIDAGSSLMAFKMMYFRKGKNLQDENDKIRYIEEVLREISKL 403
Cdd:COG0358 319 ALELLLKDGLQVRVLFLPDGEDPDELIRKEGAEAF-RELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLAKI 397
|
410 420
....*....|....*....|....*
gi 489341928 404 PNPIEWDYYLRQLADEFSLSLSALQ 428
Cdd:COG0358 398 PDPILRELYLRELAERLGLDEEALD 422
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
4-420 |
0e+00 |
|
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: 581.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 4 RIPEETIETIRRTVDIVDVISDYVQLKKQGRNYFGLCPFHGEKTPSFSVSPEKQIFHCFGCGAGGNVFSFLMDIEGISFL 83
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 84 EAVKRLAVKANIDLSHLQLDDadKSRTNTGETKMMVEAHELLKKFYHHLLVNTNEGQKALDYLQDRGWTREIIDQFEIGY 163
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQ--EKKEQKSKRKKLYELLELAAKFFKNQLKHTPENRAALDYLQSRGLSDETIDRFELGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 164 APNSWDFAVKLLSGR-GFSLELMEKAGLIIRKENGDYFDRFRHRIMFPILNHHGDTVGFSGRLLGEGQPKYLNSPETAIF 242
Cdd:TIGR01391 159 APNNWDFLFDFLQNKkGFDLELLAEAGLLVKKENGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 243 HKGKILYNFHQARLHIRKHQEVILLEGFADVISAVQAGVAHSVATMGTALTEEHARILRRNVDTVIICYDGDASGIEATF 322
Cdd:TIGR01391 239 KKSELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 323 RAAEVLTEAGCHVKIATIPDGLDPDEYIRKYGPDRFRRdIIDAGSSLMAFKMMYFRKGKNLQDENDKIRYIEEVLREISK 402
Cdd:TIGR01391 319 RAIELLLPLGINVKVIKLPGGKDPDEYLRKEGVEALKK-LLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLIKK 397
|
410
....*....|....*...
gi 489341928 403 LPNPIEWDYYLRQLADEF 420
Cdd:TIGR01391 398 IPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
128-255 |
6.03e-63 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 203.14 E-value: 6.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 128 FYHHLLvNTNEGQKALDYLQDRGWTREIIDQFEIGYAPNSWDFAVKLLSGRGFSLELMEKAGLIIRKENGDYFDRFRHRI 207
Cdd:pfam08275 1 FYQELL-KTNEGAAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLKKKGFSEEELLEAGLLSKNEDGRYYDRFRNRI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489341928 208 MFPILNHHGDTVGFSGRLL-GEGQPKYLNSPETAIFHKGKILYNFHQAR 255
Cdd:pfam08275 80 MFPIKDARGRVVGFGGRALdDDKPPKYLNSPETPLFKKSKLLYGLDEAK 128
|
|
| zf-CHC2 |
pfam01807 |
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases. |
6-100 |
1.55e-54 |
|
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
Pssm-ID: 426447 [Multi-domain] Cd Length: 95 Bit Score: 180.14 E-value: 1.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 6 PEETIETIRRTVDIVDVISDYVQLKKQGRNYFGLCPFHGEKTPSFSVSPEKQIFHCFGCGAGGNVFSFLMDIEGISFLEA 85
Cdd:pfam01807 1 PPEFIDDLKNRIDIVDVVGQYVKLKKRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIKFLMKIEKLSFVEA 80
|
90
....*....|....*
gi 489341928 86 VKRLAVKANIDLSHL 100
Cdd:pfam01807 81 VEKLADRYGIEIPYE 95
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
263-340 |
2.09e-33 |
|
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: 122.24 E-value: 2.09e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489341928 263 EVILLEGFADVISAVQAGVAHSVATMGTALTEEHARILRRNVDTVIICYDGDASGIEATFRAAEVLTEAGCHVKIATI 340
Cdd:cd03364 2 KVILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKLGLNVRVLTL 79
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
36-90 |
6.07e-33 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 120.09 E-value: 6.07e-33
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489341928 36 YFGLCPFHGEKTPSFSVSPEKQIFHCFGCGAGGNVFSFLMDIEGISFLEAVKRLA 90
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| Toprim_2 |
pfam13155 |
Toprim-like; This is a family or Toprim-like proteins. |
265-350 |
5.21e-32 |
|
Toprim-like; This is a family or Toprim-like proteins.
Pssm-ID: 463793 [Multi-domain] Cd Length: 88 Bit Score: 118.43 E-value: 5.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 265 ILLEGFADVISAVQAGV--AHSVATMGTALTEEHARILRRNVDTVIICYDGDASGIEATFRAAEVLTEAGCHVKIATIPD 342
Cdd:pfam13155 1 VVFEGYIDALSLAQAGIknVLYVATLGTALTEAQIKLLKRYPKEVILAFDNDEAGRKAAKRLAELLKEAGVDVKIRLLPD 80
|
....*...
gi 489341928 343 GLDPDEYI 350
Cdd:pfam13155 81 GKDWNEYL 88
|
|
| TOPRIM_primases |
cd01029 |
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
262-339 |
7.12e-26 |
|
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: 101.19 E-value: 7.12e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489341928 262 QEVILLEGFADVISAVQAGVAHSVATMGTALTEEHARILRRNVDTVIICYDGDASGIEATFRAAEVLTEAGCHVKIAT 339
Cdd:cd01029 1 DEVIIVEGYMDVLALHQAGIKNVVAALGTANTEEQLRLLKRFARTVILAFDNDEAGKKAAARALELLLALGGRVRVPP 78
|
|
| Toprim_4 |
pfam13662 |
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ... |
263-339 |
5.07e-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: 78.87 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 263 EVILLEGFADVISAVQAGVAHSVATMGTAL-TEEHARILRRNVDT------VIICYDGDASGIEATFRAAEVLTEAGCHV 335
Cdd:pfam13662 2 EIIVVEGYADVIALEKAGYKGAVAVLGGALsPLDGIGPEDLNIDSlggikeVILALDGDVAGEKTALYLAEALLEEGVKV 81
|
....
gi 489341928 336 KIAT 339
Cdd:pfam13662 82 SRLA 85
|
|
| TOPRIM |
smart00493 |
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins; |
263-332 |
1.31e-13 |
|
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
Pssm-ID: 214695 [Multi-domain] Cd Length: 75 Bit Score: 66.13 E-value: 1.31e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489341928 263 EVILLEGFADVISAVQAGVAH--SVATMGTALTEEHARILRRNVD--TVIICYDGDASGIEATFRAAEVLTEAG 332
Cdd:smart00493 2 VLIIVEGPADAIALEKAGGKRgnVVALGGHLLSKEQIKLLKKLAKkaEVILATDPDREGEAIAWELAELLKPAG 75
|
|
| DnaB_bind |
pfam10410 |
DnaB-helicase binding domain of primase; This domain is the C-terminal region three-helical ... |
370-423 |
1.71e-13 |
|
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: 65.17 E-value: 1.71e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 489341928 370 MAFKMMYFRKGKNLQDENDKIRYIEEVLREISKLPNPIEWDYYLRQLADEFSLS 423
Cdd:pfam10410 1 SEFLIRRLLKGYDLDTPEGRAAALREAAPLLAKIPDPVERDLYLRRLAEELGIS 54
|
|
| PRK08624 |
PRK08624 |
hypothetical protein; Provisional |
54-312 |
8.32e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 236314 [Multi-domain] Cd Length: 373 Bit Score: 70.35 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 54 PEKQIFHCF-GCGAGGNVFSFL-----MDIEGISFLEAVKRLAVKANIdlshlqlddadksrtNTGETKMMVEAHELLKK 127
Cdd:PRK08624 55 IENDNFHCYtRCGDIFDVFELLckrlkMEGKALSFSKAIRKITKILGL---------------SYFYEPKQQGIKPSFLK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 128 FyhHLLVNTNEGQKALD-YLQDRGWTREIIDQFeIGYAPNSWdfavkllSGRGFSLELMEKAgliirkENGDYFDRFRHR 206
Cdd:PRK08624 120 I--LDWVWTGKKEKKEKiQPQLKSFNENILNQF-VKIPNRKW-------LDEGISEKTQKYW------EIKFYLDVISQR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 207 IMFPILNHHGDTVGFSGRLL-------GEGQPKYLNspETAIFH-KGKILYNFHQARLHIRKHQEVILLEGFADVISAVQ 278
Cdd:PRK08624 184 IIIPHRDESGELIGIRGRLLdkelvdkNKYFPIYVN--DTGYNHpKGKILYGLWQNKKYIKEKKKVIIVESEKSVLFSDK 261
|
250 260 270
....*....|....*....|....*....|....*..
gi 489341928 279 A-GVAH-SVATMGTALTEEHARI-LRRNVDTVIICYD 312
Cdd:PRK08624 262 FyGEGNfVVAICGSNISEVQAEKlLRLGVEEVTIALD 298
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
168-346 |
1.54e-12 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 67.91 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 168 WDFAVKLLSGRGFSLELMEKAGLIirkengdYFDRFRHRIMFPILNhhgdtvGFSGRLLGEGQPKYL--NSPETAIFHkg 245
Cdd:PHA02031 87 YQSLYGLLLSKGIDPNMMEPGLPL-------EYSERQGRLIFRTDA------GWLGRATADQQPKWVgyGYPAPDYVG-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 246 kilynfHQARLHIRKhqEVILLEgfaDVISA------VQAGVAHSVATMGTALTEEHARIL-RRNVDTVIICYDGDASGI 318
Cdd:PHA02031 152 ------WPPELSMPR--PVVLTE---DYLSAlkvrwaCNKPEVFAVALLGTRLRDRLAAILlQQTCPRVLIFLDGDPAGV 220
|
170 180
....*....|....*....|....*...
gi 489341928 319 EATFRAAEVLTEAGCHVKIATIPDGLDP 346
Cdd:PHA02031 221 DGSAGAMRRLRPLLIEGQVIITPDGFDP 248
|
|
| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
263-340 |
1.78e-12 |
|
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: 63.21 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 263 EVILLEGFADVISAVQAGVAHS--VATMGTAL--TEEHARILRRNVDTVIICYDGDASGIEATFRAAEVLTEAGCHVKIA 338
Cdd:cd00188 2 KLIIVEGPSDALALAQAGGYGGavVALGGHALnkTRELLKRLLGEAKEVIIATDADREGEAIALRLLELLKSLGKKVRRL 81
|
..
gi 489341928 339 TI 340
Cdd:cd00188 82 LL 83
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
263-340 |
2.90e-09 |
|
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: 54.28 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 263 EVILLEGFADVISAVQAGVAHS---VATMGTALTEEH---------ARILRRNVDTVIICYDGDASGIEATFRAAEV--- 327
Cdd:pfam01751 1 ELIIVEGPSDAIALEKALGGGFqavVAVLGHLLSLEKgpkkkalkaLKELALKAKEVILATDPDREGEAIALKLLELkel 80
|
90
....*....|...
gi 489341928 328 LTEAGCHVKIATI 340
Cdd:pfam01751 81 LENAGGRVEFSEL 93
|
|
| Toprim_3 |
pfam13362 |
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ... |
264-356 |
7.82e-07 |
|
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: 47.40 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489341928 264 VILLEGFADVISAVQAGVAhsVATMGTALTE-EHARILR--RNVDTVIICYDGDA--SGIEATFRAAEVLTEAGCHVKIA 338
Cdd:pfam13362 2 LIIGEGIETALSLTQRLNP--PGTPVIALLSaANLKAVAwpERVKRVYIAADNDAanDGQAAAEKLAERLEAAGIEAVLL 79
|
90
....*....|....*...
gi 489341928 339 TIPDGLDPDEYIRKYGPD 356
Cdd:pfam13362 80 EPEAGEDWNDDLQQTGAA 97
|
|
| |
