|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
4-425 |
0e+00 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 702.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 4 RIPRVFINDLLARTDIVDLIDARVKLKKQGKNFHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFV 83
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 84 ETVEELAAMHNLDVPYEAGSGPSQIERHQRQNLYQLMDGLNTFYQQSLMQ-PAAGPARQYLEKRGLSSEVITRFAIGYAP 162
Cdd:COG0358 81 EAVEELAERAGIELPEEEGSPEEREEASERERLYEALELAAKFYQEQLKNtPEGKAARDYLKKRGLSDETIERFGLGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 163 PGWDNVLKRFGGNQENRQSLIDAGMLVTNDQGRSYDRFRERVMFPIRDKRGRVIGFGGRVLGDAMPKYLNSPETDIFHKG 242
Cdd:COG0358 161 DGWDALLKHLKKKGFSEEELVEAGLVIEREDGGYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFHKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 243 RQLYGLYEAQQDNAEPPRLLVVEGYMDVVALAQFGINYAVASLGTSTTADHIQLLFRVTNQVVCCYDGDRAGRDAAWRAL 322
Cdd:COG0358 241 RVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALRAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 323 ETALpymTDGRQLRFMFLPDGEDPDTLVRKEGKAAFEGRMEQAQPLSTFLFNSLLPQVDLSTPDGRAQLSTLALPLITQV 402
Cdd:COG0358 321 ELLL---KDGLQVRVLFLPDGEDPDELIRKEGAEAFRELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLAKI 397
|
410 420
....*....|....*....|...
gi 497337635 403 PGETLRIYLRQELGNKLGILDDA 425
Cdd:COG0358 398 PDPILRELYLRELAERLGLDEEA 420
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
4-419 |
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: 575.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 4 RIPRVFINDLLARTDIVDLIDARVKLKKQGKNFHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFV 83
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 84 ETVEELAAMHNLDVPYEAGSGPSQIERHQRQNLYQLMDGLNTFYQQSLM-QPAAGPARQYLEKRGLSSEVITRFAIGYAP 162
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKKEQKSKRKKLYELLELAAKFFKNQLKhTPENRAALDYLQSRGLSDETIDRFELGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 163 PGWDNVLKRFGGNQENRQS-LIDAGMLVTNDQGRSYDRFRERVMFPIRDKRGRVIGFGGRVLGDAMPKYLNSPETDIFHK 241
Cdd:TIGR01391 161 NNWDFLFDFLQNKKGFDLElLAEAGLLVKKENGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 242 GRQLYGLYEAQQDNAEPPRLLVVEGYMDVVALAQFGINYAVASLGTSTTADHIQLLFRVTNQVVCCYDGDRAGRDAAWRA 321
Cdd:TIGR01391 241 SELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAALRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 322 LETALPYmtdGRQLRFMFLPDGEDPDTLVRKEGKAAFEGRMEQAQPLSTFLFNSLLPQVDLSTPDGRAQLSTLALPLITQ 401
Cdd:TIGR01391 321 IELLLPL---GINVKVIKLPGGKDPDEYLRKEGVEALKKLLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLIKK 397
|
410
....*....|....*...
gi 497337635 402 VPGETLRIYLRQELGNKL 419
Cdd:TIGR01391 398 IPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
126-252 |
2.86e-58 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 190.81 E-value: 2.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 126 FYQQSLMQPAAGPARQYLEKRGLSSEVITRFAIGYAPPGWDNVLKRFGGNQENRQSLIDAGMLVTNDQGRSYDRFRERVM 205
Cdd:pfam08275 1 FYQELLKTNEGAAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLKKKGFSEEELLEAGLLSKNEDGRYYDRFRNRIM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 497337635 206 FPIRDKRGRVIGFGGRVL-GDAMPKYLNSPETDIFHKGRQLYGLYEAQ 252
Cdd:pfam08275 81 FPIKDARGRVVGFGGRALdDDKPPKYLNSPETPLFKKSKLLYGLDEAK 128
|
|
| DnaG_DnaB_bind |
smart00766 |
DNA primase DnaG DnaB-binding; DnaG_DnaB_bind defines a domain of primase required for ... |
451-574 |
1.70e-42 |
|
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: 148.56 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 451 MRILIGLLVQNPDLAPLVPPLEGLDPRKMPGLGLFNELVKTCLAQPGLTTGLLLEQYRGTNEAATLEKLSMWDDIADKDI 530
Cdd:smart00766 1 MRELIRLLLQNPELASLVPDLLPLELFTHPGLALLAELLALCRGAPGLTTGQLLEHWRDTPYRELLSELAVWDHLIDEEN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 497337635 531 AEKTFTDSLNHMFDSLLELRQEELIARDRTHGLSSEERRELWTI 574
Cdd:smart00766 81 LEEEFQDALARLRKQLLERRIEELIAKLRRSGLTVEEKKELQAL 124
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
260-340 |
4.75e-34 |
|
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: 123.78 E-value: 4.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 260 RLLVVEGYMDVVALAQFGINYAVASLGTSTTADHIQLLFRVTNQVVCCYDGDRAGRDAAWRALETALPYmtdGRQLRFMF 339
Cdd:cd03364 2 KVILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKL---GLNVRVLT 78
|
.
gi 497337635 340 L 340
Cdd:cd03364 79 L 79
|
|
| DnaG_DnaB_bind |
pfam08278 |
DNA primase DnaG DnaB-binding; Eubacterial DnaG primases interact with several factors to from ... |
451-572 |
8.02e-33 |
|
DNA primase DnaG DnaB-binding; Eubacterial DnaG primases interact with several factors to from the replisome. One of these factors in DnaB, a helicase. This domain has been demonstrated to be responsible for the interaction between DnaG and DnaB.
Pssm-ID: 429895 Cd Length: 122 Bit Score: 121.97 E-value: 8.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 451 MRILIGLLVQNPDLAPLVPPLEGLDPRKMPGLGLFNELVKTCLAQPGLTTGLLLEQYRGTNEAATLEKLSMWD-DIADKD 529
Cdd:pfam08278 1 EREALKLLLQHPELAGPVPDALPLEAFTHPGLALLRELIEAAGARPGLSTAQLLEHWRDTPYEALLAELAVEPlQVDEEE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 497337635 530 IAEKTFTDSLNHMFDSLLELRQEELIARDRtHGLSSEERRELW 572
Cdd:pfam08278 81 NLEREFDDALARLQEQAVERRIAELKAKLR-QGLTVEEKEELR 122
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
36-90 |
1.20e-32 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 119.32 E-value: 1.20e-32
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 497337635 36 FHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFVETVEELA 90
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
183-362 |
1.90e-09 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 58.67 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 183 IDAGMLvTNDQGRSYDRFRERVMFPIRDkrgrviGFGGRVLGDAMPKYL--NSPETDIFHkgrqlyglyeAQQDNAEPPR 260
Cdd:PHA02031 99 IDPNMM-EPGLPLEYSERQGRLIFRTDA------GWLGRATADQQPKWVgyGYPAPDYVG----------WPPELSMPRP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 261 LLVVEGYMDVVALaQFGIN----YAVASLGTSTTADHIQLLFRVT-NQVVCCYDGDRAGRDAAWRALETALPYMTDGrql 335
Cdd:PHA02031 162 VVLTEDYLSALKV-RWACNkpevFAVALLGTRLRDRLAAILLQQTcPRVLIFLDGDPAGVDGSAGAMRRLRPLLIEG--- 237
|
170 180
....*....|....*....|....*..
gi 497337635 336 RFMFLPDGEDPDTLVRKEGKAAFEGRM 362
Cdd:PHA02031 238 QVIITPDGFDPKDLEREQIRELLIGRI 264
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
4-425 |
0e+00 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 702.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 4 RIPRVFINDLLARTDIVDLIDARVKLKKQGKNFHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFV 83
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 84 ETVEELAAMHNLDVPYEAGSGPSQIERHQRQNLYQLMDGLNTFYQQSLMQ-PAAGPARQYLEKRGLSSEVITRFAIGYAP 162
Cdd:COG0358 81 EAVEELAERAGIELPEEEGSPEEREEASERERLYEALELAAKFYQEQLKNtPEGKAARDYLKKRGLSDETIERFGLGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 163 PGWDNVLKRFGGNQENRQSLIDAGMLVTNDQGRSYDRFRERVMFPIRDKRGRVIGFGGRVLGDAMPKYLNSPETDIFHKG 242
Cdd:COG0358 161 DGWDALLKHLKKKGFSEEELVEAGLVIEREDGGYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFHKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 243 RQLYGLYEAQQDNAEPPRLLVVEGYMDVVALAQFGINYAVASLGTSTTADHIQLLFRVTNQVVCCYDGDRAGRDAAWRAL 322
Cdd:COG0358 241 RVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALRAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 323 ETALpymTDGRQLRFMFLPDGEDPDTLVRKEGKAAFEGRMEQAQPLSTFLFNSLLPQVDLSTPDGRAQLSTLALPLITQV 402
Cdd:COG0358 321 ELLL---KDGLQVRVLFLPDGEDPDELIRKEGAEAFRELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLAKI 397
|
410 420
....*....|....*....|...
gi 497337635 403 PGETLRIYLRQELGNKLGILDDA 425
Cdd:COG0358 398 PDPILRELYLRELAERLGLDEEA 420
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
4-419 |
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: 575.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 4 RIPRVFINDLLARTDIVDLIDARVKLKKQGKNFHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFV 83
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 84 ETVEELAAMHNLDVPYEAGSGPSQIERHQRQNLYQLMDGLNTFYQQSLM-QPAAGPARQYLEKRGLSSEVITRFAIGYAP 162
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKKEQKSKRKKLYELLELAAKFFKNQLKhTPENRAALDYLQSRGLSDETIDRFELGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 163 PGWDNVLKRFGGNQENRQS-LIDAGMLVTNDQGRSYDRFRERVMFPIRDKRGRVIGFGGRVLGDAMPKYLNSPETDIFHK 241
Cdd:TIGR01391 161 NNWDFLFDFLQNKKGFDLElLAEAGLLVKKENGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 242 GRQLYGLYEAQQDNAEPPRLLVVEGYMDVVALAQFGINYAVASLGTSTTADHIQLLFRVTNQVVCCYDGDRAGRDAAWRA 321
Cdd:TIGR01391 241 SELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAALRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 322 LETALPYmtdGRQLRFMFLPDGEDPDTLVRKEGKAAFEGRMEQAQPLSTFLFNSLLPQVDLSTPDGRAQLSTLALPLITQ 401
Cdd:TIGR01391 321 IELLLPL---GINVKVIKLPGGKDPDEYLRKEGVEALKKLLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLIKK 397
|
410
....*....|....*...
gi 497337635 402 VPGETLRIYLRQELGNKL 419
Cdd:TIGR01391 398 IPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
126-252 |
2.86e-58 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 190.81 E-value: 2.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 126 FYQQSLMQPAAGPARQYLEKRGLSSEVITRFAIGYAPPGWDNVLKRFGGNQENRQSLIDAGMLVTNDQGRSYDRFRERVM 205
Cdd:pfam08275 1 FYQELLKTNEGAAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLKKKGFSEEELLEAGLLSKNEDGRYYDRFRNRIM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 497337635 206 FPIRDKRGRVIGFGGRVL-GDAMPKYLNSPETDIFHKGRQLYGLYEAQ 252
Cdd:pfam08275 81 FPIKDARGRVVGFGGRALdDDKPPKYLNSPETPLFKKSKLLYGLDEAK 128
|
|
| zf-CHC2 |
pfam01807 |
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases. |
6-100 |
1.07e-56 |
|
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
Pssm-ID: 426447 [Multi-domain] Cd Length: 95 Bit Score: 185.15 E-value: 1.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 6 PRVFINDLLARTDIVDLIDARVKLKKQGKNFHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFVET 85
Cdd:pfam01807 1 PPEFIDDLKNRIDIVDVVGQYVKLKKRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIKFLMKIEKLSFVEA 80
|
90
....*....|....*
gi 497337635 86 VEELAAMHNLDVPYE 100
Cdd:pfam01807 81 VEKLADRYGIEIPYE 95
|
|
| DnaG_DnaB_bind |
smart00766 |
DNA primase DnaG DnaB-binding; DnaG_DnaB_bind defines a domain of primase required for ... |
451-574 |
1.70e-42 |
|
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: 148.56 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 451 MRILIGLLVQNPDLAPLVPPLEGLDPRKMPGLGLFNELVKTCLAQPGLTTGLLLEQYRGTNEAATLEKLSMWDDIADKDI 530
Cdd:smart00766 1 MRELIRLLLQNPELASLVPDLLPLELFTHPGLALLAELLALCRGAPGLTTGQLLEHWRDTPYRELLSELAVWDHLIDEEN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 497337635 531 AEKTFTDSLNHMFDSLLELRQEELIARDRTHGLSSEERRELWTI 574
Cdd:smart00766 81 LEEEFQDALARLRKQLLERRIEELIAKLRRSGLTVEEKKELQAL 124
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
260-340 |
4.75e-34 |
|
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: 123.78 E-value: 4.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 260 RLLVVEGYMDVVALAQFGINYAVASLGTSTTADHIQLLFRVTNQVVCCYDGDRAGRDAAWRALETALPYmtdGRQLRFMF 339
Cdd:cd03364 2 KVILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKL---GLNVRVLT 78
|
.
gi 497337635 340 L 340
Cdd:cd03364 79 L 79
|
|
| DnaG_DnaB_bind |
pfam08278 |
DNA primase DnaG DnaB-binding; Eubacterial DnaG primases interact with several factors to from ... |
451-572 |
8.02e-33 |
|
DNA primase DnaG DnaB-binding; Eubacterial DnaG primases interact with several factors to from the replisome. One of these factors in DnaB, a helicase. This domain has been demonstrated to be responsible for the interaction between DnaG and DnaB.
Pssm-ID: 429895 Cd Length: 122 Bit Score: 121.97 E-value: 8.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 451 MRILIGLLVQNPDLAPLVPPLEGLDPRKMPGLGLFNELVKTCLAQPGLTTGLLLEQYRGTNEAATLEKLSMWD-DIADKD 529
Cdd:pfam08278 1 EREALKLLLQHPELAGPVPDALPLEAFTHPGLALLRELIEAAGARPGLSTAQLLEHWRDTPYEALLAELAVEPlQVDEEE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 497337635 530 IAEKTFTDSLNHMFDSLLELRQEELIARDRtHGLSSEERRELW 572
Cdd:pfam08278 81 NLEREFDDALARLQEQAVERRIAELKAKLR-QGLTVEEKEELR 122
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
36-90 |
1.20e-32 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 119.32 E-value: 1.20e-32
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 497337635 36 FHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFVETVEELA 90
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| TOPRIM_primases |
cd01029 |
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
259-340 |
1.46e-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: 103.12 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 259 PRLLVVEGYMDVVALAQFGINYAVASLGTSTTADHIQLLFRVTNQVVCCYDGDRAGRDAAWRALETALPYmtdGRQLRFM 338
Cdd:cd01029 1 DEVIIVEGYMDVLALHQAGIKNVVAALGTANTEEQLRLLKRFARTVILAFDNDEAGKKAAARALELLLAL---GGRVRVP 77
|
..
gi 497337635 339 FL 340
Cdd:cd01029 78 PL 79
|
|
| Toprim_2 |
pfam13155 |
Toprim-like; This is a family or Toprim-like proteins. |
263-347 |
2.56e-22 |
|
Toprim-like; This is a family or Toprim-like proteins.
Pssm-ID: 463793 [Multi-domain] Cd Length: 88 Bit Score: 91.08 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 263 VVEGYMDVVALAQFGINYA--VASLGTSTTADHIQLLFRVTNQVVCCYDGDRAGRDAAWRALETALPymtDGRQLRFMFL 340
Cdd:pfam13155 2 VFEGYIDALSLAQAGIKNVlyVATLGTALTEAQIKLLKRYPKEVILAFDNDEAGRKAAKRLAELLKE---AGVDVKIRLL 78
|
....*..
gi 497337635 341 PDGEDPD 347
Cdd:pfam13155 79 PDGKDWN 85
|
|
| TOPRIM |
smart00493 |
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins; |
260-329 |
1.04e-17 |
|
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
Pssm-ID: 214695 [Multi-domain] Cd Length: 75 Bit Score: 77.69 E-value: 1.04e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497337635 260 RLLVVEGYMDVVALAQFGIN--YAVASLGTSTTADHIQLLFRVT--NQVVCCYDGDRAGRDAAWRALETALPYM 329
Cdd:smart00493 2 VLIIVEGPADAIALEKAGGKrgNVVALGGHLLSKEQIKLLKKLAkkAEVILATDPDREGEAIAWELAELLKPAG 75
|
|
| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
260-340 |
6.35e-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: 6.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 260 RLLVVEGYMDVVALAQFGINY--AVASLGTS--TTADHIQLLFRVTNQVVCCYDGDRAGRDAAWRALETALPYmtdGRQL 335
Cdd:cd00188 2 KLIIVEGPSDALALAQAGGYGgaVVALGGHAlnKTRELLKRLLGEAKEVIIATDADREGEAIALRLLELLKSL---GKKV 78
|
....*
gi 497337635 336 RFMFL 340
Cdd:cd00188 79 RRLLL 83
|
|
| Toprim_4 |
pfam13662 |
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ... |
260-327 |
7.02e-13 |
|
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: 64.23 E-value: 7.02e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497337635 260 RLLVVEGYMDVVALAQFGINYAVASLGTS-TTADHIQLL------FRVTNQVVCCYDGDRAGRDAAWRALETALP 327
Cdd:pfam13662 2 EIIVVEGYADVIALEKAGYKGAVAVLGGAlSPLDGIGPEdlnidsLGGIKEVILALDGDVAGEKTALYLAEALLE 76
|
|
| DnaB_bind |
pfam10410 |
DnaB-helicase binding domain of primase; This domain is the C-terminal region three-helical ... |
369-421 |
6.49e-12 |
|
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: 60.55 E-value: 6.49e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 497337635 369 STFLFNSLLPQVDLSTPDGRAQLSTLALPLITQVPGETLRIYLRQELGNKLGI 421
Cdd:pfam10410 1 SEFLIRRLLKGYDLDTPEGRAAALREAAPLLAKIPDPVERDLYLRRLAEELGI 53
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
260-323 |
1.33e-11 |
|
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: 60.83 E-value: 1.33e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497337635 260 RLLVVEGYMDVVALAQF---GINYAVASLGTSTTADH---------IQLLFRVTNQVVCCYDGDRAGRDAAWRALE 323
Cdd:pfam01751 1 ELIIVEGPSDAIALEKAlggGFQAVVAVLGHLLSLEKgpkkkalkaLKELALKAKEVILATDPDREGEAIALKLLE 76
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
183-362 |
1.90e-09 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 58.67 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 183 IDAGMLvTNDQGRSYDRFRERVMFPIRDkrgrviGFGGRVLGDAMPKYL--NSPETDIFHkgrqlyglyeAQQDNAEPPR 260
Cdd:PHA02031 99 IDPNMM-EPGLPLEYSERQGRLIFRTDA------GWLGRATADQQPKWVgyGYPAPDYVG----------WPPELSMPRP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 261 LLVVEGYMDVVALaQFGIN----YAVASLGTSTTADHIQLLFRVT-NQVVCCYDGDRAGRDAAWRALETALPYMTDGrql 335
Cdd:PHA02031 162 VVLTEDYLSALKV-RWACNkpevFAVALLGTRLRDRLAAILLQQTcPRVLIFLDGDPAGVDGSAGAMRRLRPLLIEG--- 237
|
170 180
....*....|....*....|....*..
gi 497337635 336 RFMFLPDGEDPDTLVRKEGKAAFEGRM 362
Cdd:PHA02031 238 QVIITPDGFDPKDLEREQIRELLIGRI 264
|
|
| PRK08624 |
PRK08624 |
hypothetical protein; Provisional |
55-300 |
2.72e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 236314 [Multi-domain] Cd Length: 373 Bit Score: 53.01 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 55 EKQFYHCF-GCGAHGNAIDFL-----MNYDKLEFVETVEELAAMHNLDV---PYEAGSGPSQIERH------QRQNLYQL 119
Cdd:PRK08624 56 ENDNFHCYtRCGDIFDVFELLckrlkMEGKALSFSKAIRKITKILGLSYfyePKQQGIKPSFLKILdwvwtgKKEKKEKI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 120 MDGLNTFYQQSLMQPAAGPARQYLEKrGLSSEVITRFAIGYAPpgwdnvlkrfggnqenrqslidagmlvtndqgrsyDR 199
Cdd:PRK08624 136 QPQLKSFNENILNQFVKIPNRKWLDE-GISEKTQKYWEIKFYL-----------------------------------DV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497337635 200 FRERVMFPIRDKRGRVIGFGGRVLGDA-------MPKYLNSPETDiFHKGRQLYGLYEAQQDNAEPPRLLVVEGYMDVVA 272
Cdd:PRK08624 180 ISQRIIIPHRDESGELIGIRGRLLDKElvdknkyFPIYVNDTGYN-HPKGKILYGLWQNKKYIKEKKKVIIVESEKSVLF 258
|
250 260 270
....*....|....*....|....*....|
gi 497337635 273 LAQF-GI-NYAVASLGTSTTADHIQLLFRV 300
Cdd:PRK08624 259 SDKFyGEgNFVVAICGSNISEVQAEKLLRL 288
|
|
| |
