|
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: 684.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 4 RIPRVFINDLLARTDIVDLIDVRVKLKKQGKNYHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFV 83
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 84 ETVEELAAMHNLEIPYEAGTGLSQIERHQRQNLYQLMNGLNDFYQQSL-THPAAKPARDYLQKRGLSAEIIQRFAIGFAP 162
Cdd:COG0358 81 EAVEELAERAGIELPEEEGSPEEREEASERERLYEALELAAKFYQEQLkNTPEGKAARDYLKKRGLSDETIERFGLGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 163 PGWDNALKRFGNNSDNKALLLDAGMLVNNEQGSTYDRFRNRVMFPIRDKRGRVIGFGGRVLGNDTPKYLNSPETDIFHKG 242
Cdd:COG0358 161 DGWDALLKHLKKKGFSEEELVEAGLVIEREDGGYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFHKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 243 RQLYGLYEAQQYSAEPQRLLVVEGYMDVVALAQYDINYAVASLGTSTTADHMHMLFRATNNVICCYDGDRAGRDAAWRAL 322
Cdd:COG0358 241 RVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALRAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 323 ETAmpyMTDGRQVRFMFLPDGEDPDTLVRKEGKAAFEARMEQAQPLSTFLFNSLLPQVDLSSPDGSTQLAALALPLINQV 402
Cdd:COG0358 321 ELL---LKDGLQVRVLFLPDGEDPDELIRKEGAEAFRELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLAKI 397
|
410 420
....*....|....*....|....*.
gi 446841609 403 PGDAHRIQLRQTLGLKLGIfDDSQLD 428
Cdd:COG0358 398 PDPILRELYLRELAERLGL-DEEALD 422
|
|
| 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: 568.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 4 RIPRVFINDLLARTDIVDLIDVRVKLKKQGKNYHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFV 83
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 84 ETVEELAAMHNLEIPYEAGTGLSQIERHQRQNLYQLMNGLNDFYQQSLTH-PAAKPARDYLQKRGLSAEIIQRFAIGFAP 162
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKKEQKSKRKKLYELLELAAKFFKNQLKHtPENRAALDYLQSRGLSDETIDRFELGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 163 PGWDNALKRFGNN-SDNKALLLDAGMLVNNEQGSTYDRFRNRVMFPIRDKRGRVIGFGGRVLGNDTPKYLNSPETDIFHK 241
Cdd:TIGR01391 161 NNWDFLFDFLQNKkGFDLELLAEAGLLVKKENGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 242 GRQLYGLYEAQQYSAEPQRLLVVEGYMDVVALAQYDINYAVASLGTSTTADHMHMLFRATNNVICCYDGDRAGRDAAWRA 321
Cdd:TIGR01391 241 SELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAALRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 322 LETAMPYmtdGRQVRFMFLPDGEDPDTLVRKEGKAAFEARMEQAQPLSTFLFNSLLPQVDLSSPDGSTQLAALALPLINQ 401
Cdd:TIGR01391 321 IELLLPL---GINVKVIKLPGGKDPDEYLRKEGVEALKKLLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLIKK 397
|
410
....*....|....*...
gi 446841609 402 VPGDAHRIQLRQTLGLKL 419
Cdd:TIGR01391 398 IPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
126-252 |
1.60e-61 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 199.28 E-value: 1.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 126 FYQQSLTHPAAKPARDYLQKRGLSAEIIQRFAIGFAPPGWDNALKRFGNNSDNKALLLDAGMLVNNEQGSTYDRFRNRVM 205
Cdd:pfam08275 1 FYQELLKTNEGAAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLKKKGFSEEELLEAGLLSKNEDGRYYDRFRNRIM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446841609 206 FPIRDKRGRVIGFGGRVLGNDTP-KYLNSPETDIFHKGRQLYGLYEAQ 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 |
2.41e-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: 150.87 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 451 MRILIGLLVQNPDLAPLVPPLDALDQNKLPGLGLFKELVKTCLAQPGLTTGQLLELYRGTNDAATLEKLSMWDDIADKAI 530
Cdd:smart00766 1 MRELIRLLLQNPELASLVPDLLPLELFTHPGLALLAELLALCRGAPGLTTGQLLEHWRDTPYRELLSELAVWDHLIDEEN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446841609 531 AEKTFTDSLNHMFDSLLQLRQEELIARDRTHGLSSEERRELWTLN 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 |
1.85e-34 |
|
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: 126.59 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 451 MRILIGLLVQNPDLAPLVPPLDALDQNKLPGLGLFKELVKTCLAQPGLTTGQLLELYRGTNDAATLEKLSMWD-DIADKA 529
Cdd:pfam08278 1 EREALKLLLQHPELAGPVPDALPLEAFTHPGLALLRELIEAAGARPGLSTAQLLEHWRDTPYEALLAELAVEPlQVDEEE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446841609 530 IAEKTFTDSLNHMFDSLLQLRQEELIARDRtHGLSSEERRELW 572
Cdd:pfam08278 81 NLEREFDDALARLQEQAVERRIAELKAKLR-QGLTVEEKEELR 122
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
36-90 |
5.66e-33 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 120.09 E-value: 5.66e-33
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446841609 36 YHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFVETVEELA 90
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
260-340 |
8.12e-32 |
|
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: 117.62 E-value: 8.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 260 RLLVVEGYMDVVALAQYDINYAVASLGTSTTADHMHMLFRATNNVICCYDGDRAGRDAAWRALETAMPYmtdGRQVRFMF 339
Cdd:cd03364 2 KVILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKL---GLNVRVLT 78
|
.
gi 446841609 340 L 340
Cdd:cd03364 79 L 79
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
211-353 |
8.84e-10 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 59.82 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 211 KRGRVI-----GFGGRVLGNDTPKYL--NSPETDIFHkgrqlyglyeAQQYSAEPQRLLVVEGYMDVVALaQYDIN---- 279
Cdd:PHA02031 115 RQGRLIfrtdaGWLGRATADQQPKWVgyGYPAPDYVG----------WPPELSMPRPVVLTEDYLSALKV-RWACNkpev 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446841609 280 YAVASLGTSTTADHMHMLFRAT-NNVICCYDGDRAGRDAAWRALETAMPYMtdgRQVRFMFLPDGEDPDTLVRKE 353
Cdd:PHA02031 184 FAVALLGTRLRDRLAAILLQQTcPRVLIFLDGDPAGVDGSAGAMRRLRPLL---IEGQVIITPDGFDPKDLEREQ 255
|
|
| |
|
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: 684.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 4 RIPRVFINDLLARTDIVDLIDVRVKLKKQGKNYHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFV 83
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 84 ETVEELAAMHNLEIPYEAGTGLSQIERHQRQNLYQLMNGLNDFYQQSL-THPAAKPARDYLQKRGLSAEIIQRFAIGFAP 162
Cdd:COG0358 81 EAVEELAERAGIELPEEEGSPEEREEASERERLYEALELAAKFYQEQLkNTPEGKAARDYLKKRGLSDETIERFGLGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 163 PGWDNALKRFGNNSDNKALLLDAGMLVNNEQGSTYDRFRNRVMFPIRDKRGRVIGFGGRVLGNDTPKYLNSPETDIFHKG 242
Cdd:COG0358 161 DGWDALLKHLKKKGFSEEELVEAGLVIEREDGGYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFHKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 243 RQLYGLYEAQQYSAEPQRLLVVEGYMDVVALAQYDINYAVASLGTSTTADHMHMLFRATNNVICCYDGDRAGRDAAWRAL 322
Cdd:COG0358 241 RVLYGLDLARKAIRKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALRAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 323 ETAmpyMTDGRQVRFMFLPDGEDPDTLVRKEGKAAFEARMEQAQPLSTFLFNSLLPQVDLSSPDGSTQLAALALPLINQV 402
Cdd:COG0358 321 ELL---LKDGLQVRVLFLPDGEDPDELIRKEGAEAFRELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLAKI 397
|
410 420
....*....|....*....|....*.
gi 446841609 403 PGDAHRIQLRQTLGLKLGIfDDSQLD 428
Cdd:COG0358 398 PDPILRELYLRELAERLGL-DEEALD 422
|
|
| 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: 568.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 4 RIPRVFINDLLARTDIVDLIDVRVKLKKQGKNYHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFV 83
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 84 ETVEELAAMHNLEIPYEAGTGLSQIERHQRQNLYQLMNGLNDFYQQSLTH-PAAKPARDYLQKRGLSAEIIQRFAIGFAP 162
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKKEQKSKRKKLYELLELAAKFFKNQLKHtPENRAALDYLQSRGLSDETIDRFELGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 163 PGWDNALKRFGNN-SDNKALLLDAGMLVNNEQGSTYDRFRNRVMFPIRDKRGRVIGFGGRVLGNDTPKYLNSPETDIFHK 241
Cdd:TIGR01391 161 NNWDFLFDFLQNKkGFDLELLAEAGLLVKKENGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 242 GRQLYGLYEAQQYSAEPQRLLVVEGYMDVVALAQYDINYAVASLGTSTTADHMHMLFRATNNVICCYDGDRAGRDAAWRA 321
Cdd:TIGR01391 241 SELLYGLHKARKEIRKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAALRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 322 LETAMPYmtdGRQVRFMFLPDGEDPDTLVRKEGKAAFEARMEQAQPLSTFLFNSLLPQVDLSSPDGSTQLAALALPLINQ 401
Cdd:TIGR01391 321 IELLLPL---GINVKVIKLPGGKDPDEYLRKEGVEALKKLLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLIKK 397
|
410
....*....|....*...
gi 446841609 402 VPGDAHRIQLRQTLGLKL 419
Cdd:TIGR01391 398 IPDPILRDYYLQKLAQLL 415
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
126-252 |
1.60e-61 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 199.28 E-value: 1.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 126 FYQQSLTHPAAKPARDYLQKRGLSAEIIQRFAIGFAPPGWDNALKRFGNNSDNKALLLDAGMLVNNEQGSTYDRFRNRVM 205
Cdd:pfam08275 1 FYQELLKTNEGAAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLKKKGFSEEELLEAGLLSKNEDGRYYDRFRNRIM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446841609 206 FPIRDKRGRVIGFGGRVLGNDTP-KYLNSPETDIFHKGRQLYGLYEAQ 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 |
9.34e-57 |
|
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
Pssm-ID: 426447 [Multi-domain] Cd Length: 95 Bit Score: 185.53 E-value: 9.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 6 PRVFINDLLARTDIVDLIDVRVKLKKQGKNYHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFVET 85
Cdd:pfam01807 1 PPEFIDDLKNRIDIVDVVGQYVKLKKRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIKFLMKIEKLSFVEA 80
|
90
....*....|....*
gi 446841609 86 VEELAAMHNLEIPYE 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 |
2.41e-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: 150.87 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 451 MRILIGLLVQNPDLAPLVPPLDALDQNKLPGLGLFKELVKTCLAQPGLTTGQLLELYRGTNDAATLEKLSMWDDIADKAI 530
Cdd:smart00766 1 MRELIRLLLQNPELASLVPDLLPLELFTHPGLALLAELLALCRGAPGLTTGQLLEHWRDTPYRELLSELAVWDHLIDEEN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446841609 531 AEKTFTDSLNHMFDSLLQLRQEELIARDRTHGLSSEERRELWTLN 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 |
1.85e-34 |
|
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: 126.59 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 451 MRILIGLLVQNPDLAPLVPPLDALDQNKLPGLGLFKELVKTCLAQPGLTTGQLLELYRGTNDAATLEKLSMWD-DIADKA 529
Cdd:pfam08278 1 EREALKLLLQHPELAGPVPDALPLEAFTHPGLALLRELIEAAGARPGLSTAQLLEHWRDTPYEALLAELAVEPlQVDEEE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446841609 530 IAEKTFTDSLNHMFDSLLQLRQEELIARDRtHGLSSEERRELW 572
Cdd:pfam08278 81 NLEREFDDALARLQEQAVERRIAELKAKLR-QGLTVEEKEELR 122
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
36-90 |
5.66e-33 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 120.09 E-value: 5.66e-33
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446841609 36 YHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFVETVEELA 90
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
260-340 |
8.12e-32 |
|
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: 117.62 E-value: 8.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 260 RLLVVEGYMDVVALAQYDINYAVASLGTSTTADHMHMLFRATNNVICCYDGDRAGRDAAWRALETAMPYmtdGRQVRFMF 339
Cdd:cd03364 2 KVILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKL---GLNVRVLT 78
|
.
gi 446841609 340 L 340
Cdd:cd03364 79 L 79
|
|
| TOPRIM_primases |
cd01029 |
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
259-340 |
7.94e-25 |
|
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in the active site regions of bacterial DnaG-type primases and their homologs. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The prototypical bacterial primase. Escherichia coli DnaG is a single subunit enzyme.
Pssm-ID: 173779 [Multi-domain] Cd Length: 79 Bit Score: 98.11 E-value: 7.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 259 QRLLVVEGYMDVVALAQYDINYAVASLGTSTTADHMHMLFRATNNVICCYDGDRAGRDAAWRALETAMPYmtdGRQVRFM 338
Cdd:cd01029 1 DEVIIVEGYMDVLALHQAGIKNVVAALGTANTEEQLRLLKRFARTVILAFDNDEAGKKAAARALELLLAL---GGRVRVP 77
|
..
gi 446841609 339 FL 340
Cdd:cd01029 78 PL 79
|
|
| Toprim_2 |
pfam13155 |
Toprim-like; This is a family or Toprim-like proteins. |
263-347 |
5.54e-21 |
|
Toprim-like; This is a family or Toprim-like proteins.
Pssm-ID: 463793 [Multi-domain] Cd Length: 88 Bit Score: 87.62 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 263 VVEGYMDVVALAQYDINYA--VASLGTSTTADHMHMLFRATNNVICCYDGDRAGRDAAWRALETAMPymtDGRQVRFMFL 340
Cdd:pfam13155 2 VFEGYIDALSLAQAGIKNVlyVATLGTALTEAQIKLLKRYPKEVILAFDNDEAGRKAAKRLAELLKE---AGVDVKIRLL 78
|
....*..
gi 446841609 341 PDGEDPD 347
Cdd:pfam13155 79 PDGKDWN 85
|
|
| TOPRIM |
smart00493 |
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins; |
260-329 |
2.34e-15 |
|
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
Pssm-ID: 214695 [Multi-domain] Cd Length: 75 Bit Score: 71.14 E-value: 2.34e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446841609 260 RLLVVEGYMDVVALAQYDIN--YAVASLGTSTTADHMHMLFRATNN--VICCYDGDRAGRDAAWRALETAMPYM 329
Cdd:smart00493 2 VLIIVEGPADAIALEKAGGKrgNVVALGGHLLSKEQIKLLKKLAKKaeVILATDPDREGEAIAWELAELLKPAG 75
|
|
| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
260-340 |
6.27e-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: 64.37 E-value: 6.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 260 RLLVVEGYMDVVALAQYDINY--AVASLGTS--TTADHMHMLFRATNNVICCYDGDRAGRDAAWRALETAMPYmtdGRQV 335
Cdd:cd00188 2 KLIIVEGPSDALALAQAGGYGgaVVALGGHAlnKTRELLKRLLGEAKEVIIATDADREGEAIALRLLELLKSL---GKKV 78
|
....*
gi 446841609 336 RFMFL 340
Cdd:cd00188 79 RRLLL 83
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
260-323 |
1.41e-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: 1.41e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446841609 260 RLLVVEGYMDVVALAQY---DINYAVASLGTSTTADH---------MHMLFRATNNVICCYDGDRAGRDAAWRALE 323
Cdd:pfam01751 1 ELIIVEGPSDAIALEKAlggGFQAVVAVLGHLLSLEKgpkkkalkaLKELALKAKEVILATDPDREGEAIALKLLE 76
|
|
| Toprim_4 |
pfam13662 |
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ... |
260-324 |
4.14e-10 |
|
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: 56.52 E-value: 4.14e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446841609 260 RLLVVEGYMDVVALAQYDINYAVASLGTS-TTADHMHML------FRATNNVICCYDGDRAGRDAAWRALET 324
Cdd:pfam13662 2 EIIVVEGYADVIALEKAGYKGAVAVLGGAlSPLDGIGPEdlnidsLGGIKEVILALDGDVAGEKTALYLAEA 73
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
211-353 |
8.84e-10 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 59.82 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 211 KRGRVI-----GFGGRVLGNDTPKYL--NSPETDIFHkgrqlyglyeAQQYSAEPQRLLVVEGYMDVVALaQYDIN---- 279
Cdd:PHA02031 115 RQGRLIfrtdaGWLGRATADQQPKWVgyGYPAPDYVG----------WPPELSMPRPVVLTEDYLSALKV-RWACNkpev 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446841609 280 YAVASLGTSTTADHMHMLFRAT-NNVICCYDGDRAGRDAAWRALETAMPYMtdgRQVRFMFLPDGEDPDTLVRKE 353
Cdd:PHA02031 184 FAVALLGTRLRDRLAAILLQQTcPRVLIFLDGDPAGVDGSAGAMRRLRPLL---IEGQVIITPDGFDPKDLEREQ 255
|
|
| DnaB_bind |
pfam10410 |
DnaB-helicase binding domain of primase; This domain is the C-terminal region three-helical ... |
369-421 |
9.95e-08 |
|
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: 48.61 E-value: 9.95e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446841609 369 STFLFNSLLPQVDLSSPDGSTQLAALALPLINQVPGDAHRIQLRQTLGLKLGI 421
Cdd:pfam10410 1 SEFLIRRLLKGYDLDTPEGRAAALREAAPLLAKIPDPVERDLYLRRLAEELGI 53
|
|
| PRK08624 |
PRK08624 |
hypothetical protein; Provisional |
33-299 |
2.12e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 236314 [Multi-domain] Cd Length: 373 Bit Score: 50.32 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 33 GKNYHACCPFHnektpsftvngEKQFYHCF-GCGAHGNAIDFL-----MNYDKLEFVETVEELAAMHNLEIPYEAGTGLS 106
Cdd:PRK08624 45 GGGSTKLYYYI-----------ENDNFHCYtRCGDIFDVFELLckrlkMEGKALSFSKAIRKITKILGLSYFYEPKQQGI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 107 Q---------IERHQRQNLYQLMNGLNDFYQQSLTHPAAKPARDYLQKrGLSAEIIQRFAIGFAPpgwdnalkrfgnnsd 177
Cdd:PRK08624 114 KpsflkildwVWTGKKEKKEKIQPQLKSFNENILNQFVKIPNRKWLDE-GISEKTQKYWEIKFYL--------------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 178 nkallldagmlvnneqgstyDRFRNRVMFPIRDKRGRVIGFGGRVLGN---DTPKYLNSPETDIFH---KGRQLYGLYEA 251
Cdd:PRK08624 178 --------------------DVISQRIIIPHRDESGELIGIRGRLLDKelvDKNKYFPIYVNDTGYnhpKGKILYGLWQN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446841609 252 QQYSAEPQRLLVVEGYMDVVALAQY--DINYAVASLGTSTTADHMHMLFR 299
Cdd:PRK08624 238 KKYIKEKKKVIIVESEKSVLFSDKFygEGNFVVAICGSNISEVQAEKLLR 287
|
|
| 61 |
PHA02540 |
DNA primase; Provisional |
28-231 |
4.81e-06 |
|
DNA primase; Provisional
Pssm-ID: 222863 [Multi-domain] Cd Length: 337 Bit Score: 48.83 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 28 KLKKQGKNYHACCPF-------HNEKtpSFTVNGEKQF--YHCFGCGAHGNAIDFLMNYDklefvetvEELAAMHNLEIP 98
Cdd:PHA02540 18 KQVRRSSFYNFRCPIcgdsqkdKNKA--RGWIYEKKDGgvFKCHNCGYHRPFGNFLKDYE--------PDLYREYIMERF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841609 99 YEAGTGLSQIERHQRQNLYQLM---NGLNDFYQQSlTHPAAKPARDYLQKRGLSAEIIQRFaiGFApPGWDNalkrfgnn 175
Cdd:PHA02540 88 KERGTGKGRPVPKPKFEFKKEKkviEKLPFCERLD-TLPEDHPIIKYVENRCIPKDKWKLL--YFT-REWQK-------- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446841609 176 sdnkallldagmLVNNEQGSTYDRFR--NRVMFPIRDKRGRVIGFGGRVLGNDTP-KYL 231
Cdd:PHA02540 156 ------------LVNSIKPDTYKKEKpePRLVIPIFNKDGKIESFQGRALRKDAPqKYI 202
|
|
| |
