|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
2-424 |
0e+00 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 563.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 2 RIDQSIINEIKDKTDILDLVSEYVKLEKRGRNYIGLCPFHDEKTPSFTVSEDKQICHCFGCKKGGNVFQFTQEIKDISFV 81
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 82 EAVKELGDRVNVAVDIEaTQSNSNVQIASDDLQMIEMHELIQEFYYYALTKTVEGEQALTYLQERGFTDALIKERGIGFA 161
Cdd:COG0358 81 EAVEELAERAGIELPEE-EGSPEEREEASERERLYEALELAAKFYQEQLKNTPEGKAARDYLKKRGLSDETIERFGLGYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 162 PDSSHFCHDFLQKKGYDIELAYEAGLLSRNEENfSYYDRFRNRIMFPLKNAQGRIVGYSGRTYTGQEPKYLNSPETPIFQ 241
Cdd:COG0358 160 PDGWDALLKHLKKKGFSEEELVEAGLVIEREDG-GYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 242 KRKLLYNLDKARKSIRKLDEIVLLEGFMDVIKSDTAGLKNVVATMGTQLSDEHITFIRKLTSNITLMFDGDFAGSEATLK 321
Cdd:COG0358 239 KGRVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 322 TGQNLLQQGLNVFVIQLPSGMDPDEYIGKYGNDAFTAFVKNdKKSFAHYKVSILKDEIAHNDLS-YERYLKELSHDISLM 400
Cdd:COG0358 319 ALELLLKDGLQVRVLFLPDGEDPDELIRKEGAEAFRELLEN-AKPLIEFLIERLLEGYDLDTPEgRAALLREALPLLAKI 397
|
410 420
....*....|....*....|....
gi 581500402 401 KSSILQQKALNDVAPFFNVSPEQL 424
Cdd:COG0358 398 PDPILRELYLRELAERLGLDEEAL 421
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
2-417 |
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: 557.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 2 RIDQSIINEIKDKTDILDLVSEYVKLEKRGRNYIGLCPFHDEKTPSFTVSEDKQICHCFGCKKGGNVFQFTQEIKDISFV 81
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 82 EAVKELGDRVNVAVDIEATQSNSNvQIASDDLQMIEMHELIQEFYYYALTKTVEGEQALTYLQERGFTDALIKERGIGFA 161
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKK-EQKSKRKKLYELLELAAKFFKNQLKHTPENRAALDYLQSRGLSDETIDRFELGYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 162 PDSSHFCHDFLQ-KKGYDIELAYEAGLLSRNEENfSYYDRFRNRIMFPLKNAQGRIVGYSGRTYTGQEPKYLNSPETPIF 240
Cdd:TIGR01391 160 PNNWDFLFDFLQnKKGFDLELLAEAGLLVKKENG-KYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 241 QKRKLLYNLDKARKSIRKLDEIVLLEGFMDVIKSDTAGLKNVVATMGTQLSDEHITFIRKLTSNITLMFDGDFAGSEATL 320
Cdd:TIGR01391 239 KKSELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 321 KTGQNLLQQGLNVFVIQLPSGMDPDEYIGKYGNDAFTAFVKNdKKSFAHYKVSILKDEI-AHNDLSYERYLKELSHDISL 399
Cdd:TIGR01391 319 RAIELLLPLGINVKVIKLPGGKDPDEYLRKEGVEALKKLLEN-SKSLIEFLIARLLSNYnLDTPEEKAKLVEELLPLIKK 397
|
410
....*....|....*...
gi 581500402 400 MKSSILQQKALNDVAPFF 417
Cdd:TIGR01391 398 IPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
126-253 |
5.62e-57 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 187.73 E-value: 5.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 126 YYYALTKTVEGEQALTYLQERGFTDALIKERGIGFAPDSSHFCHDFLQKKGYDIELAYEAGLLSRNEENfSYYDRFRNRI 205
Cdd:pfam08275 1 FYQELLKTNEGAAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLKKKGFSEEELLEAGLLSKNEDG-RYYDRFRNRI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 581500402 206 MFPLKNAQGRIVGYSGRTYTGQEP-KYLNSPETPIFQKRKLLYNLDKAR 253
Cdd:pfam08275 80 MFPIKDARGRVVGFGGRALDDDKPpKYLNSPETPLFKKSKLLYGLDEAK 128
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
34-88 |
4.30e-30 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 112.00 E-value: 4.30e-30
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 581500402 34 YIGLCPFHDEKTPSFTVSEDKQICHCFGCKKGGNVFQFTQEIKDISFVEAVKELG 88
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
260-338 |
2.88e-29 |
|
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: 110.68 E-value: 2.88e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581500402 260 DEIVLLEGFMDVIKSDTAGLKNVVATMGTQLSDEHITFIRKLTSNITLMFDGDFAGSEATLKTGQNLLQQGLNVFVIQL 338
Cdd:cd03364 1 KKVILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKLGLNVRVLTL 79
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
163-344 |
8.32e-07 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 50.96 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 163 DSSHFCHDFLQKKGYDIELAYEAGLLsrneenfsYYDRFRNRIMFPLKNaqgrivGYSGRTYTGQEPKYlnspeTPIFQK 242
Cdd:PHA02031 85 DAYQSLYGLLLSKGIDPNMMEPGLPL--------EYSERQGRLIFRTDA------GWLGRATADQQPKW-----VGYGYP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 243 RKLLYNLdKARKSIRKLdeIVLLEGFMDVIK---SDTAGLKNVVATMGTQLSDEHITFIRKLTS-NITLMFDGDFAGSEA 318
Cdd:PHA02031 146 APDYVGW-PPELSMPRP--VVLTEDYLSALKvrwACNKPEVFAVALLGTRLRDRLAAILLQQTCpRVLIFLDGDPAGVDG 222
|
170 180
....*....|....*....|....*.
gi 581500402 319 TLKTGQNLLQQGLNVFVIQLPSGMDP 344
Cdd:PHA02031 223 SAGAMRRLRPLLIEGQVIITPDGFDP 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
2-424 |
0e+00 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 563.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 2 RIDQSIINEIKDKTDILDLVSEYVKLEKRGRNYIGLCPFHDEKTPSFTVSEDKQICHCFGCKKGGNVFQFTQEIKDISFV 81
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 82 EAVKELGDRVNVAVDIEaTQSNSNVQIASDDLQMIEMHELIQEFYYYALTKTVEGEQALTYLQERGFTDALIKERGIGFA 161
Cdd:COG0358 81 EAVEELAERAGIELPEE-EGSPEEREEASERERLYEALELAAKFYQEQLKNTPEGKAARDYLKKRGLSDETIERFGLGYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 162 PDSSHFCHDFLQKKGYDIELAYEAGLLSRNEENfSYYDRFRNRIMFPLKNAQGRIVGYSGRTYTGQEPKYLNSPETPIFQ 241
Cdd:COG0358 160 PDGWDALLKHLKKKGFSEEELVEAGLVIEREDG-GYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 242 KRKLLYNLDKARKSIRKLDEIVLLEGFMDVIKSDTAGLKNVVATMGTQLSDEHITFIRKLTSNITLMFDGDFAGSEATLK 321
Cdd:COG0358 239 KGRVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 322 TGQNLLQQGLNVFVIQLPSGMDPDEYIGKYGNDAFTAFVKNdKKSFAHYKVSILKDEIAHNDLS-YERYLKELSHDISLM 400
Cdd:COG0358 319 ALELLLKDGLQVRVLFLPDGEDPDELIRKEGAEAFRELLEN-AKPLIEFLIERLLEGYDLDTPEgRAALLREALPLLAKI 397
|
410 420
....*....|....*....|....
gi 581500402 401 KSSILQQKALNDVAPFFNVSPEQL 424
Cdd:COG0358 398 PDPILRELYLRELAERLGLDEEAL 421
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
2-417 |
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: 557.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 2 RIDQSIINEIKDKTDILDLVSEYVKLEKRGRNYIGLCPFHDEKTPSFTVSEDKQICHCFGCKKGGNVFQFTQEIKDISFV 81
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 82 EAVKELGDRVNVAVDIEATQSNSNvQIASDDLQMIEMHELIQEFYYYALTKTVEGEQALTYLQERGFTDALIKERGIGFA 161
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKK-EQKSKRKKLYELLELAAKFFKNQLKHTPENRAALDYLQSRGLSDETIDRFELGYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 162 PDSSHFCHDFLQ-KKGYDIELAYEAGLLSRNEENfSYYDRFRNRIMFPLKNAQGRIVGYSGRTYTGQEPKYLNSPETPIF 240
Cdd:TIGR01391 160 PNNWDFLFDFLQnKKGFDLELLAEAGLLVKKENG-KYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 241 QKRKLLYNLDKARKSIRKLDEIVLLEGFMDVIKSDTAGLKNVVATMGTQLSDEHITFIRKLTSNITLMFDGDFAGSEATL 320
Cdd:TIGR01391 239 KKSELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 321 KTGQNLLQQGLNVFVIQLPSGMDPDEYIGKYGNDAFTAFVKNdKKSFAHYKVSILKDEI-AHNDLSYERYLKELSHDISL 399
Cdd:TIGR01391 319 RAIELLLPLGINVKVIKLPGGKDPDEYLRKEGVEALKKLLEN-SKSLIEFLIARLLSNYnLDTPEEKAKLVEELLPLIKK 397
|
410
....*....|....*...
gi 581500402 400 MKSSILQQKALNDVAPFF 417
Cdd:TIGR01391 398 IPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
126-253 |
5.62e-57 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 187.73 E-value: 5.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 126 YYYALTKTVEGEQALTYLQERGFTDALIKERGIGFAPDSSHFCHDFLQKKGYDIELAYEAGLLSRNEENfSYYDRFRNRI 205
Cdd:pfam08275 1 FYQELLKTNEGAAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLKKKGFSEEELLEAGLLSKNEDG-RYYDRFRNRI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 581500402 206 MFPLKNAQGRIVGYSGRTYTGQEP-KYLNSPETPIFQKRKLLYNLDKAR 253
Cdd:pfam08275 80 MFPIKDARGRVVGFGGRALDDDKPpKYLNSPETPLFKKSKLLYGLDEAK 128
|
|
| zf-CHC2 |
pfam01807 |
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases. |
4-98 |
1.07e-45 |
|
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
Pssm-ID: 426447 [Multi-domain] Cd Length: 95 Bit Score: 156.26 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 4 DQSIINEIKDKTDILDLVSEYVKLEKRGRNYIGLCPFHDEKTPSFTVSEDKQICHCFGCKKGGNVFQFTQEIKDISFVEA 83
Cdd:pfam01807 1 PPEFIDDLKNRIDIVDVVGQYVKLKKRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIKFLMKIEKLSFVEA 80
|
90
....*....|....*
gi 581500402 84 VKELGDRVNVAVDIE 98
Cdd:pfam01807 81 VEKLADRYGIEIPYE 95
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
34-88 |
4.30e-30 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 112.00 E-value: 4.30e-30
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 581500402 34 YIGLCPFHDEKTPSFTVSEDKQICHCFGCKKGGNVFQFTQEIKDISFVEAVKELG 88
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
260-338 |
2.88e-29 |
|
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: 110.68 E-value: 2.88e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581500402 260 DEIVLLEGFMDVIKSDTAGLKNVVATMGTQLSDEHITFIRKLTSNITLMFDGDFAGSEATLKTGQNLLQQGLNVFVIQL 338
Cdd:cd03364 1 KKVILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKLGLNVRVLTL 79
|
|
| TOPRIM_primases |
cd01029 |
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
260-338 |
4.18e-21 |
|
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: 87.71 E-value: 4.18e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581500402 260 DEIVLLEGFMDVIKSDTAGLKNVVATMGTQLSDEHITFIRKLTSNITLMFDGDFAGSEATLKTGQNLLQQGLNVFVIQL 338
Cdd:cd01029 1 DEVIIVEGYMDVLALHQAGIKNVVAALGTANTEEQLRLLKRFARTVILAFDNDEAGKKAAARALELLLALGGRVRVPPL 79
|
|
| Toprim_2 |
pfam13155 |
Toprim-like; This is a family or Toprim-like proteins. |
263-348 |
1.57e-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: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 263 VLLEGFMDVIKSDTAGLKNV--VATMGTQLSDEHITFIRKLTSNITLMFDGDFAGSEATLKTGQNLLQQGLNVFVIQLPS 340
Cdd:pfam13155 1 VVFEGYIDALSLAQAGIKNVlyVATLGTALTEAQIKLLKRYPKEVILAFDNDEAGRKAAKRLAELLKEAGVDVKIRLLPD 80
|
....*...
gi 581500402 341 GMDPDEYI 348
Cdd:pfam13155 81 GKDWNEYL 88
|
|
| Toprim_4 |
pfam13662 |
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ... |
260-336 |
1.22e-14 |
|
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: 69.24 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 260 DEIVLLEGFMDVIKSDTAGLKNVVATMGTQLS-DEHI------TFIRKLTSNITLMFDGDFAGSEATLKTGQNLLQQGLN 332
Cdd:pfam13662 1 SEIIVVEGYADVIALEKAGYKGAVAVLGGALSpLDGIgpedlnIDSLGGIKEVILALDGDVAGEKTALYLAEALLEEGVK 80
|
....
gi 581500402 333 VFVI 336
Cdd:pfam13662 81 VSRL 84
|
|
| TOPRIM |
smart00493 |
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins; |
260-330 |
9.29e-11 |
|
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
Pssm-ID: 214695 [Multi-domain] Cd Length: 75 Bit Score: 58.04 E-value: 9.29e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581500402 260 DEIVLLEGFMDVIKSDTAGLK--NVVATMGTQLSDEHITFIRKLTSN--ITLMFDGDFAGSEATLKTGQNLLQQG 330
Cdd:smart00493 1 KVLIIVEGPADAIALEKAGGKrgNVVALGGHLLSKEQIKLLKKLAKKaeVILATDPDREGEAIAWELAELLKPAG 75
|
|
| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
260-338 |
2.61e-07 |
|
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: 48.58 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 260 DEIVLLEGFMDVIKSDTAGLK--NVVATMGTqLSDEHITFIRKL---TSNITLMFDGDFAGSEATLKTGQNLLQQGLNVF 334
Cdd:cd00188 1 KKLIIVEGPSDALALAQAGGYggAVVALGGH-ALNKTRELLKRLlgeAKEVIIATDADREGEAIALRLLELLKSLGKKVR 79
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....
gi 581500402 335 VIQL 338
Cdd:cd00188 80 RLLL 83
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| PHA02031 |
PHA02031 |
putative DnaG-like primase |
163-344 |
8.32e-07 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 50.96 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 163 DSSHFCHDFLQKKGYDIELAYEAGLLsrneenfsYYDRFRNRIMFPLKNaqgrivGYSGRTYTGQEPKYlnspeTPIFQK 242
Cdd:PHA02031 85 DAYQSLYGLLLSKGIDPNMMEPGLPL--------EYSERQGRLIFRTDA------GWLGRATADQQPKW-----VGYGYP 145
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 243 RKLLYNLdKARKSIRKLdeIVLLEGFMDVIK---SDTAGLKNVVATMGTQLSDEHITFIRKLTS-NITLMFDGDFAGSEA 318
Cdd:PHA02031 146 APDYVGW-PPELSMPRP--VVLTEDYLSALKvrwACNKPEVFAVALLGTRLRDRLAAILLQQTCpRVLIFLDGDPAGVDG 222
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170 180
....*....|....*....|....*.
gi 581500402 319 TLKTGQNLLQQGLNVFVIQLPSGMDP 344
Cdd:PHA02031 223 SAGAMRRLRPLLIEGQVIITPDGFDP 248
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| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
261-338 |
7.55e-06 |
|
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: 44.65 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 261 EIVLLEGFMDVI---KSDTAGLKNVVATMGTQLSDEH------ITFIRKL---TSNITLMFDGDFAGSEATLKTGQN--- 325
Cdd:pfam01751 1 ELIIVEGPSDAIaleKALGGGFQAVVAVLGHLLSLEKgpkkkaLKALKELalkAKEVILATDPDREGEAIALKLLELkel 80
|
90
....*....|...
gi 581500402 326 LLQQGLNVFVIQL 338
Cdd:pfam01751 81 LENAGGRVEFSEL 93
|
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| PRK08624 |
PRK08624 |
hypothetical protein; Provisional |
183-294 |
4.00e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 236314 [Multi-domain] Cd Length: 373 Bit Score: 46.08 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581500402 183 YEAGLLSRNEENFS---YYDRFRNRIMFPLKNAQGRIVGYSGRTYTGQE-------PKYLNSPETPiFQKRKLLYNLDKA 252
Cdd:PRK08624 159 LDEGISEKTQKYWEikfYLDVISQRIIIPHRDESGELIGIRGRLLDKELvdknkyfPIYVNDTGYN-HPKGKILYGLWQN 237
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 581500402 253 RKSIRKLDEIVLLEGFMDVIKSDT--AGLKNVVATMGTQLSDEH 294
Cdd:PRK08624 238 KKYIKEKKKVIIVESEKSVLFSDKfyGEGNFVVAICGSNISEVQ 281
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