|
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: 703.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 4 RIPRVFINDLLARTDIVDLIDARVKLKKQGKNYHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAVDFLMNYDKLEFV 83
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 84 ETVEELAAMHNLEVPYEAGSGPSQIERHQRQTLYQLMDGLNSFYQQSLKHS-AAEPARQYLNKRGLSDDVIARFAIGYAP 162
Cdd:COG0358 81 EAVEELAERAGIELPEEEGSPEEREEASERERLYEALELAAKFYQEQLKNTpEGKAARDYLKKRGLSDETIERFGLGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 163 PGWDNVLKRFGGNSEDRKSLIDAGMLVTNDQGRSYDRFRERVMFPIRDKRGRVIGFGGRVLGDALPKYLNSPETDIFHKG 242
Cdd:COG0358 161 DGWDALLKHLKKKGFSEEELVEAGLVIEREDGGYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFHKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 243 RQLYGLYEAQQDNAEPPRLLVVEGYMDVVALAQYDINYAVASLGTSTTADHIQLLFRVTNNVICCYDGDRAGRDAAWRAL 322
Cdd:COG0358 241 RVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALRAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 323 ETALpymTDGRQLRFMFLPDGEDPDTLVRKEGKAAFEARMEQAQPLSTFLFNSLMPQVDLSTPDGRAQLSTLALPLISQV 402
Cdd:COG0358 321 ELLL---KDGLQVRVLFLPDGEDPDELIRKEGAEAFRELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLAKI 397
|
410 420
....*....|....*....|...
gi 1730591779 403 PGETLRIYLRQELGNKLGILDDS 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: 571.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 4 RIPRVFINDLLARTDIVDLIDARVKLKKQGKNYHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAVDFLMNYDKLEFV 83
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 84 ETVEELAAMHNLEVPYEAGSGPSQIERHQRQTLYQLMDGLNSFYQQSLKHSAAEP-ARQYLNKRGLSDDVIARFAIGYAP 162
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKKEQKSKRKKLYELLELAAKFFKNQLKHTPENRaALDYLQSRGLSDETIDRFELGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 163 PGWDNVLKRFGGNSE-DRKSLIDAGMLVTNDQGRSYDRFRERVMFPIRDKRGRVIGFGGRVLGDALPKYLNSPETDIFHK 241
Cdd:TIGR01391 161 NNWDFLFDFLQNKKGfDLELLAEAGLLVKKENGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 242 GRQLYGLYEAQQDNAEPPRLLVVEGYMDVVALAQYDINYAVASLGTSTTADHIQLLFRVTNNVICCYDGDRAGRDAAWRA 321
Cdd:TIGR01391 241 SELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAALRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 322 LETALPYmtdGRQLRFMFLPDGEDPDTLVRKEGKAAFEARMEQAQPLSTFLFNSLMPQVDLSTPDGRAQLSTLALPLISQ 401
Cdd:TIGR01391 321 IELLLPL---GINVKVIKLPGGKDPDEYLRKEGVEALKKLLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLIKK 397
|
410
....*....|....*...
gi 1730591779 402 VPGETLRIYLRQELGNKL 419
Cdd:TIGR01391 398 IPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
126-252 |
3.61e-61 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 198.13 E-value: 3.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 126 FYQQSLKHSAAEPARQYLNKRGLSDDVIARFAIGYAPPGWDNVLKRFGGNSEDRKSLIDAGMLVTNDQGRSYDRFRERVM 205
Cdd:pfam08275 1 FYQELLKTNEGAAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLKKKGFSEEELLEAGLLSKNEDGRYYDRFRNRIM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1730591779 206 FPIRDKRGRVIGFGGRVL-GDALPKYLNSPETDIFHKGRQLYGLYEAQ 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 ... |
451-575 |
6.21e-43 |
|
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: 149.72 E-value: 6.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 451 MRILIGLLVQNPELAPQVPSLAGLNHEKLPGLGLFSELVNTCLSQPGLTTGQLLEHYRGTKEAATLEKLSMWDDIADKDI 530
Cdd:smart00766 1 MRELIRLLLQNPELASLVPDLLPLELFTHPGLALLAELLALCRGAPGLTTGQLLEHWRDTPYRELLSELAVWDHLIDEEN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1730591779 531 AEKTFTDSLNHMFDSMLELRQEELIARERTHGLSSEERRELWMIN 575
Cdd:smart00766 81 LEEEFQDALARLRKQLLERRIEELIAKLRRSGLTVEEKKELQALL 125
|
|
| DnaG_DnaB_bind |
pfam08278 |
DNA primase DnaG DnaB-binding; Eubacterial DnaG primases interact with several factors to from ... |
451-572 |
3.28e-35 |
|
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: 128.52 E-value: 3.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 451 MRILIGLLVQNPELAPQVPSLAGLNHEKLPGLGLFSELVNTCLSQPGLTTGQLLEHYRGTKEAATLEKLSMWD-DIADKD 529
Cdd:pfam08278 1 EREALKLLLQHPELAGPVPDALPLEAFTHPGLALLRELIEAAGARPGLSTAQLLEHWRDTPYEALLAELAVEPlQVDEEE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1730591779 530 IAEKTFTDSLNHMFDSMLELRQEELIARERtHGLSSEERRELW 572
Cdd:pfam08278 81 NLEREFDDALARLQEQAVERRIAELKAKLR-QGLTVEEKEELR 122
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
260-340 |
2.36e-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: 121.85 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 260 RLLVVEGYMDVVALAQYDINYAVASLGTSTTADHIQLLFRVTNNVICCYDGDRAGRDAAWRALETALPYmtdGRQLRFMF 339
Cdd:cd03364 2 KVILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKL---GLNVRVLT 78
|
.
gi 1730591779 340 L 340
Cdd:cd03364 79 L 79
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
36-90 |
2.41e-32 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 118.16 E-value: 2.41e-32
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1730591779 36 YHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAVDFLMNYDKLEFVETVEELA 90
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
183-353 |
4.67e-09 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 57.51 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 183 IDAGMLvTNDQGRSYDRFRERVMFPIRDkrgrviGFGGRVLGDALPKYL--NSPETDIFHkgrqlyglyeAQQDNAEPPR 260
Cdd:PHA02031 99 IDPNMM-EPGLPLEYSERQGRLIFRTDA------GWLGRATADQQPKWVgyGYPAPDYVG----------WPPELSMPRP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 261 LLVVEGYMDVVALaQYDIN----YAVASLGTSTTADHIQLLFRVT-NNVICCYDGDRAGRDAAWRALETALPYMTDGrql 335
Cdd:PHA02031 162 VVLTEDYLSALKV-RWACNkpevFAVALLGTRLRDRLAAILLQQTcPRVLIFLDGDPAGVDGSAGAMRRLRPLLIEG--- 237
|
170
....*....|....*...
gi 1730591779 336 RFMFLPDGEDPDTLVRKE 353
Cdd:PHA02031 238 QVIITPDGFDPKDLEREQ 255
|
|
| |
|
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: 703.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 4 RIPRVFINDLLARTDIVDLIDARVKLKKQGKNYHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAVDFLMNYDKLEFV 83
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 84 ETVEELAAMHNLEVPYEAGSGPSQIERHQRQTLYQLMDGLNSFYQQSLKHS-AAEPARQYLNKRGLSDDVIARFAIGYAP 162
Cdd:COG0358 81 EAVEELAERAGIELPEEEGSPEEREEASERERLYEALELAAKFYQEQLKNTpEGKAARDYLKKRGLSDETIERFGLGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 163 PGWDNVLKRFGGNSEDRKSLIDAGMLVTNDQGRSYDRFRERVMFPIRDKRGRVIGFGGRVLGDALPKYLNSPETDIFHKG 242
Cdd:COG0358 161 DGWDALLKHLKKKGFSEEELVEAGLVIEREDGGYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFHKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 243 RQLYGLYEAQQDNAEPPRLLVVEGYMDVVALAQYDINYAVASLGTSTTADHIQLLFRVTNNVICCYDGDRAGRDAAWRAL 322
Cdd:COG0358 241 RVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALRAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 323 ETALpymTDGRQLRFMFLPDGEDPDTLVRKEGKAAFEARMEQAQPLSTFLFNSLMPQVDLSTPDGRAQLSTLALPLISQV 402
Cdd:COG0358 321 ELLL---KDGLQVRVLFLPDGEDPDELIRKEGAEAFRELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLAKI 397
|
410 420
....*....|....*....|...
gi 1730591779 403 PGETLRIYLRQELGNKLGILDDS 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: 571.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 4 RIPRVFINDLLARTDIVDLIDARVKLKKQGKNYHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAVDFLMNYDKLEFV 83
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 84 ETVEELAAMHNLEVPYEAGSGPSQIERHQRQTLYQLMDGLNSFYQQSLKHSAAEP-ARQYLNKRGLSDDVIARFAIGYAP 162
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKKEQKSKRKKLYELLELAAKFFKNQLKHTPENRaALDYLQSRGLSDETIDRFELGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 163 PGWDNVLKRFGGNSE-DRKSLIDAGMLVTNDQGRSYDRFRERVMFPIRDKRGRVIGFGGRVLGDALPKYLNSPETDIFHK 241
Cdd:TIGR01391 161 NNWDFLFDFLQNKKGfDLELLAEAGLLVKKENGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 242 GRQLYGLYEAQQDNAEPPRLLVVEGYMDVVALAQYDINYAVASLGTSTTADHIQLLFRVTNNVICCYDGDRAGRDAAWRA 321
Cdd:TIGR01391 241 SELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAALRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 322 LETALPYmtdGRQLRFMFLPDGEDPDTLVRKEGKAAFEARMEQAQPLSTFLFNSLMPQVDLSTPDGRAQLSTLALPLISQ 401
Cdd:TIGR01391 321 IELLLPL---GINVKVIKLPGGKDPDEYLRKEGVEALKKLLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLIKK 397
|
410
....*....|....*...
gi 1730591779 402 VPGETLRIYLRQELGNKL 419
Cdd:TIGR01391 398 IPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
126-252 |
3.61e-61 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 198.13 E-value: 3.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 126 FYQQSLKHSAAEPARQYLNKRGLSDDVIARFAIGYAPPGWDNVLKRFGGNSEDRKSLIDAGMLVTNDQGRSYDRFRERVM 205
Cdd:pfam08275 1 FYQELLKTNEGAAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLKKKGFSEEELLEAGLLSKNEDGRYYDRFRNRIM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1730591779 206 FPIRDKRGRVIGFGGRVL-GDALPKYLNSPETDIFHKGRQLYGLYEAQ 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 |
3.16e-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: 183.99 E-value: 3.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 6 PRVFINDLLARTDIVDLIDARVKLKKQGKNYHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAVDFLMNYDKLEFVET 85
Cdd:pfam01807 1 PPEFIDDLKNRIDIVDVVGQYVKLKKRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIKFLMKIEKLSFVEA 80
|
90
....*....|....*
gi 1730591779 86 VEELAAMHNLEVPYE 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 ... |
451-575 |
6.21e-43 |
|
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: 149.72 E-value: 6.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 451 MRILIGLLVQNPELAPQVPSLAGLNHEKLPGLGLFSELVNTCLSQPGLTTGQLLEHYRGTKEAATLEKLSMWDDIADKDI 530
Cdd:smart00766 1 MRELIRLLLQNPELASLVPDLLPLELFTHPGLALLAELLALCRGAPGLTTGQLLEHWRDTPYRELLSELAVWDHLIDEEN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1730591779 531 AEKTFTDSLNHMFDSMLELRQEELIARERTHGLSSEERRELWMIN 575
Cdd:smart00766 81 LEEEFQDALARLRKQLLERRIEELIAKLRRSGLTVEEKKELQALL 125
|
|
| DnaG_DnaB_bind |
pfam08278 |
DNA primase DnaG DnaB-binding; Eubacterial DnaG primases interact with several factors to from ... |
451-572 |
3.28e-35 |
|
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: 128.52 E-value: 3.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 451 MRILIGLLVQNPELAPQVPSLAGLNHEKLPGLGLFSELVNTCLSQPGLTTGQLLEHYRGTKEAATLEKLSMWD-DIADKD 529
Cdd:pfam08278 1 EREALKLLLQHPELAGPVPDALPLEAFTHPGLALLRELIEAAGARPGLSTAQLLEHWRDTPYEALLAELAVEPlQVDEEE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1730591779 530 IAEKTFTDSLNHMFDSMLELRQEELIARERtHGLSSEERRELW 572
Cdd:pfam08278 81 NLEREFDDALARLQEQAVERRIAELKAKLR-QGLTVEEKEELR 122
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
260-340 |
2.36e-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: 121.85 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 260 RLLVVEGYMDVVALAQYDINYAVASLGTSTTADHIQLLFRVTNNVICCYDGDRAGRDAAWRALETALPYmtdGRQLRFMF 339
Cdd:cd03364 2 KVILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKL---GLNVRVLT 78
|
.
gi 1730591779 340 L 340
Cdd:cd03364 79 L 79
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
36-90 |
2.41e-32 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 118.16 E-value: 2.41e-32
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1730591779 36 YHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAVDFLMNYDKLEFVETVEELA 90
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| TOPRIM_primases |
cd01029 |
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
259-340 |
9.27e-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: 100.81 E-value: 9.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 259 PRLLVVEGYMDVVALAQYDINYAVASLGTSTTADHIQLLFRVTNNVICCYDGDRAGRDAAWRALETALPYmtdGRQLRFM 338
Cdd:cd01029 1 DEVIIVEGYMDVLALHQAGIKNVVAALGTANTEEQLRLLKRFARTVILAFDNDEAGKKAAARALELLLAL---GGRVRVP 77
|
..
gi 1730591779 339 FL 340
Cdd:cd01029 78 PL 79
|
|
| Toprim_2 |
pfam13155 |
Toprim-like; This is a family or Toprim-like proteins. |
263-347 |
3.57e-22 |
|
Toprim-like; This is a family or Toprim-like proteins.
Pssm-ID: 463793 [Multi-domain] Cd Length: 88 Bit Score: 90.70 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 263 VVEGYMDVVALAQYDINYA--VASLGTSTTADHIQLLFRVTNNVICCYDGDRAGRDAAWRALETALPymtDGRQLRFMFL 340
Cdd:pfam13155 2 VFEGYIDALSLAQAGIKNVlyVATLGTALTEAQIKLLKRYPKEVILAFDNDEAGRKAAKRLAELLKE---AGVDVKIRLL 78
|
....*..
gi 1730591779 341 PDGEDPD 347
Cdd:pfam13155 79 PDGKDWN 85
|
|
| TOPRIM |
smart00493 |
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins; |
260-329 |
1.47e-16 |
|
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
Pssm-ID: 214695 [Multi-domain] Cd Length: 75 Bit Score: 74.60 E-value: 1.47e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730591779 260 RLLVVEGYMDVVALAQYDIN--YAVASLGTSTTADHIQLLFRVTNN--VICCYDGDRAGRDAAWRALETALPYM 329
Cdd:smart00493 2 VLIIVEGPADAIALEKAGGKrgNVVALGGHLLSKEQIKLLKKLAKKaeVILATDPDREGEAIAWELAELLKPAG 75
|
|
| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
260-340 |
1.12e-13 |
|
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: 66.68 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 260 RLLVVEGYMDVVALAQYDINY--AVASLGTS--TTADHIQLLFRVTNNVICCYDGDRAGRDAAWRALETALPYmtdGRQL 335
Cdd:cd00188 2 KLIIVEGPSDALALAQAGGYGgaVVALGGHAlnKTRELLKRLLGEAKEVIIATDADREGEAIALRLLELLKSL---GKKV 78
|
....*
gi 1730591779 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 |
1.15e-12 |
|
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: 63.84 E-value: 1.15e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730591779 260 RLLVVEGYMDVVALAQYDINYAVASLGTS-TTADHIQLL------FRVTNNVICCYDGDRAGRDAAWRALETALP 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 |
3.18e-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: 61.32 E-value: 3.18e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1730591779 369 STFLFNSLMPQVDLSTPDGRAQLSTLALPLISQVPGETLRIYLRQELGNKLGI 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 |
8.58e-12 |
|
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: 61.60 E-value: 8.58e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730591779 260 RLLVVEGYMDVVALAQY---DINYAVASLGTSTTADH---------IQLLFRVTNNVICCYDGDRAGRDAAWRALE 323
Cdd:pfam01751 1 ELIIVEGPSDAIALEKAlggGFQAVVAVLGHLLSLEKgpkkkalkaLKELALKAKEVILATDPDREGEAIALKLLE 76
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
183-353 |
4.67e-09 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 57.51 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 183 IDAGMLvTNDQGRSYDRFRERVMFPIRDkrgrviGFGGRVLGDALPKYL--NSPETDIFHkgrqlyglyeAQQDNAEPPR 260
Cdd:PHA02031 99 IDPNMM-EPGLPLEYSERQGRLIFRTDA------GWLGRATADQQPKWVgyGYPAPDYVG----------WPPELSMPRP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 261 LLVVEGYMDVVALaQYDIN----YAVASLGTSTTADHIQLLFRVT-NNVICCYDGDRAGRDAAWRALETALPYMTDGrql 335
Cdd:PHA02031 162 VVLTEDYLSALKV-RWACNkpevFAVALLGTRLRDRLAAILLQQTcPRVLIFLDGDPAGVDGSAGAMRRLRPLLIEG--- 237
|
170
....*....|....*...
gi 1730591779 336 RFMFLPDGEDPDTLVRKE 353
Cdd:PHA02031 238 QVIITPDGFDPKDLEREQ 255
|
|
| PRK08624 |
PRK08624 |
hypothetical protein; Provisional |
33-300 |
8.26e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 236314 [Multi-domain] Cd Length: 373 Bit Score: 51.47 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 33 GKNYHACCPFHnektpsftvngEKQFYHCF-GCGAHGNAVDFL-----MNYDKLEFVETVEELAAMHNLEV---PYEAGS 103
Cdd:PRK08624 45 GGGSTKLYYYI-----------ENDNFHCYtRCGDIFDVFELLckrlkMEGKALSFSKAIRKITKILGLSYfyePKQQGI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 104 GPSQIERH------QRQTLYQLMDGLNSFYQQSLKHSAAEPARQYLNKrGLSDDVIARFAIGYAPpgwdnvlkrfggnse 177
Cdd:PRK08624 114 KPSFLKILdwvwtgKKEKKEKIQPQLKSFNENILNQFVKIPNRKWLDE-GISEKTQKYWEIKFYL--------------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730591779 178 drkslidagmlvtndqgrsyDRFRERVMFPIRDKRGRVIGFGGRVLGDAL-------PKYLNSPETDiFHKGRQLYGLYE 250
Cdd:PRK08624 178 --------------------DVISQRIIIPHRDESGELIGIRGRLLDKELvdknkyfPIYVNDTGYN-HPKGKILYGLWQ 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1730591779 251 AQQDNAEPPRLLVVEGYMDVVALAQY--DINYAVASLGTSTTADHIQLLFRV 300
Cdd:PRK08624 237 NKKYIKEKKKVIIVESEKSVLFSDKFygEGNFVVAICGSNISEVQAEKLLRL 288
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|
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