|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
2-460 |
0e+00 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 626.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 2 YYSDEIIEEVRSRNDIVDVISTYVKLQKKGSSYFGLCPFHNEKSPSFSVSRQKQMYYCFGCGAGGNVFTFLMEYENYTFV 81
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 82 EALKYLADRAGVELPEEEYSKEAKERADTRAILLEINKAAAQYYYVQLKSS-QGAVGLGYFKKRQLSDETIKAFGLGYSN 160
Cdd:COG0358 81 EAVEELAERAGIELPEEEGSPEEREEASERERLYEALELAAKFYQEQLKNTpEGKAARDYLKKRGLSDETIERFGLGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 161 KYSDDLYRYLKSKGYKDDMIAKAGLISIDEKNGVYDKFWNRVMFPIMDVNSRVIGFGGRVMGDAKPKYLNSPETMVFDKS 240
Cdd:COG0358 161 DGWDALLKHLKKKGFSEEELVEAGLVIEREDGGYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFHKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 241 RNLYGLNRARRT--KKPYFLLCEGYMDVISLHQAGFTNAVASLGTALTPGHAALIRRYVQEVYLTYDSDGAGTRAALRAM 318
Cdd:COG0358 241 RVLYGLDLARKAirKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALRAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 319 PILRDAGITAKIIRMEPYKDPDEFIKNLGAEKFEERIASARNVFMYSLEVLEKEYDMNSPEGKTEFMKETARRLTQFEEE 398
Cdd:COG0358 321 ELLLKDGLQVRVLFLPDGEDPDELIRKEGAEAFRELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLAKIPDP 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942060763 399 IERNNYIEAVAKAYHVGFE--DLRKLVGKMAVQAGLAKPVERPREIQNNRKNKKEDGILVSQKI 460
Cdd:COG0358 401 ILRELYLRELAERLGLDEEalDALARLKRRALEKRIEELKEELKEARGDEEEKKELRELLKKKL 464
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
2-409 |
1.46e-170 |
|
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: 490.58 E-value: 1.46e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 2 YYSDEIIEEVRSRNDIVDVISTYVKLQKKGSSYFGLCPFHNEKSPSFSVSRQKQMYYCFGCGAGGNVFTFLMEYENYTFV 81
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 82 EALKYLADRAGVELPEEEYSKEAKERADTRAILLEINKAAAQYYYVQLKS-SQGAVGLGYFKKRQLSDETIKAFGLGYSN 160
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKKEQKSKRKKLYELLELAAKFFKNQLKHtPENRAALDYLQSRGLSDETIDRFELGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 161 KYSDDLYRYLKS-KGYKDDMIAKAGLISIDEKNGVYDKFWNRVMFPIMDVNSRVIGFGGRVMGDAKPKYLNSPETMVFDK 239
Cdd:TIGR01391 161 NNWDFLFDFLQNkKGFDLELLAEAGLLVKKENGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 240 SRNLYGLNRARRT--KKPYFLLCEGYMDVISLHQAGFTNAVASLGTALTPGHAALIRRYVQEVYLTYDSDGAGTRAALRA 317
Cdd:TIGR01391 241 SELLYGLHKARKEirKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAALRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 318 MPILRDAGITAKIIRMEPYKDPDEFIKNLGAEKFEERIASARNVFMYSLEVLEKEYDMNSPEGKTEFMKETARRLTQFEE 397
Cdd:TIGR01391 321 IELLLPLGINVKVIKLPGGKDPDEYLRKEGVEALKKLLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLIKKIPD 400
|
410
....*....|..
gi 942060763 398 EIERNNYIEAVA 409
Cdd:TIGR01391 401 PILRDYYLQKLA 412
|
|
| zf-CHC2 |
pfam01807 |
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases. |
4-98 |
4.23e-52 |
|
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
Pssm-ID: 426447 [Multi-domain] Cd Length: 95 Bit Score: 173.20 E-value: 4.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 4 SDEIIEEVRSRNDIVDVISTYVKLQKKGSSYFGLCPFHNEKSPSFSVSRQKQMYYCFGCGAGGNVFTFLMEYENYTFVEA 83
Cdd:pfam01807 1 PPEFIDDLKNRIDIVDVVGQYVKLKKRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIKFLMKIEKLSFVEA 80
|
90
....*....|....*
gi 942060763 84 LKYLADRAGVELPEE 98
Cdd:pfam01807 81 VEKLADRYGIEIPYE 95
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
258-333 |
6.74e-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: 120.70 E-value: 6.74e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942060763 258 LLCEGYMDVISLHQAGFTNAVASLGTALTPGHAALIRRYVQEVYLTYDSDGAGTRAALRAMPILRDAGITAKIIRM 333
Cdd:cd03364 4 ILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKLGLNVRVLTL 79
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
34-88 |
3.04e-30 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 112.39 E-value: 3.04e-30
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 942060763 34 YFGLCPFHNEKSPSFSVSRQKQMYYCFGCGAGGNVFTFLMEYENYTFVEALKYLA 88
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
166-355 |
1.52e-06 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 49.81 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 166 LYRYLKSKGYKDDMIAKAGLISIDEKNGvydkfwnRVMFPIMDvnsrviGFGGRVMGDAKPKYL--NSPETMVFdksrNL 243
Cdd:PHA02031 90 LYGLLLSKGIDPNMMEPGLPLEYSERQG-------RLIFRTDA------GWLGRATADQQPKWVgyGYPAPDYV----GW 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 244 YGLNRARRTkkpyFLLCEGYMDVISLHQA---GFTNAVASLGTALTPGHAA-LIRRYVQEVYLTYDSDGAGTRAALRAMP 319
Cdd:PHA02031 153 PPELSMPRP----VVLTEDYLSALKVRWAcnkPEVFAVALLGTRLRDRLAAiLLQQTCPRVLIFLDGDPAGVDGSAGAMR 228
|
170 180 190
....*....|....*....|....*....|....*.
gi 942060763 320 ILRDAGITAKIIRMEPYKDPdefiKNLGAEKFEERI 355
Cdd:PHA02031 229 RLRPLLIEGQVIITPDGFDP----KDLEREQIRELL 260
|
|
| DnaG_DnaB_bind |
smart00766 |
DNA primase DnaG DnaB-binding; DnaG_DnaB_bind defines a domain of primase required for ... |
458-584 |
6.83e-04 |
|
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: 39.94 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 458 QKILLTWLIESEDIFRQIEKYITPEDFSEGLFRQVAELLyEQYEKH-EVNPAQIMNHFTDEEEHRQVAGLFHTKIkeLTT 536
Cdd:smart00766 1 MRELIRLLLQNPELASLVPDLLPLELFTHPGLALLAELL-ALCRGApGLTTGQLLEHWRDTPYRELLSELAVWDH--LID 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 942060763 537 VKEQEKALQETILRVKDHSIEEATKNLdptdIQGLQRLM---NEKRKMQDL 584
Cdd:smart00766 78 EENLEEEFQDALARLRKQLLERRIEEL----IAKLRRSGltvEEKKELQAL 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DnaG |
COG0358 |
DNA primase (bacterial type) [Replication, recombination and repair]; |
2-460 |
0e+00 |
|
DNA primase (bacterial type) [Replication, recombination and repair];
Pssm-ID: 440127 [Multi-domain] Cd Length: 465 Bit Score: 626.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 2 YYSDEIIEEVRSRNDIVDVISTYVKLQKKGSSYFGLCPFHNEKSPSFSVSRQKQMYYCFGCGAGGNVFTFLMEYENYTFV 81
Cdd:COG0358 1 RIPDEFIDEIRARVDIVDVIGEYVKLKKAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVISFLMEYEGLSFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 82 EALKYLADRAGVELPEEEYSKEAKERADTRAILLEINKAAAQYYYVQLKSS-QGAVGLGYFKKRQLSDETIKAFGLGYSN 160
Cdd:COG0358 81 EAVEELAERAGIELPEEEGSPEEREEASERERLYEALELAAKFYQEQLKNTpEGKAARDYLKKRGLSDETIERFGLGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 161 KYSDDLYRYLKSKGYKDDMIAKAGLISIDEKNGVYDKFWNRVMFPIMDVNSRVIGFGGRVMGDAKPKYLNSPETMVFDKS 240
Cdd:COG0358 161 DGWDALLKHLKKKGFSEEELVEAGLVIEREDGGYYDRFRGRIMFPIRDLRGRVIGFGGRVLDDGEPKYLNSPETPLFHKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 241 RNLYGLNRARRT--KKPYFLLCEGYMDVISLHQAGFTNAVASLGTALTPGHAALIRRYVQEVYLTYDSDGAGTRAALRAM 318
Cdd:COG0358 241 RVLYGLDLARKAirKEDRVIVVEGYMDVIALHQAGIKNAVATLGTALTEEHIKLLKRYTDEVILCFDGDAAGQKAALRAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 319 PILRDAGITAKIIRMEPYKDPDEFIKNLGAEKFEERIASARNVFMYSLEVLEKEYDMNSPEGKTEFMKETARRLTQFEEE 398
Cdd:COG0358 321 ELLLKDGLQVRVLFLPDGEDPDELIRKEGAEAFRELLENAKPLIEFLIERLLEGYDLDTPEGRAALLREALPLLAKIPDP 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942060763 399 IERNNYIEAVAKAYHVGFE--DLRKLVGKMAVQAGLAKPVERPREIQNNRKNKKEDGILVSQKI 460
Cdd:COG0358 401 ILRELYLRELAERLGLDEEalDALARLKRRALEKRIEELKEELKEARGDEEEKKELRELLKKKL 464
|
|
| dnaG |
TIGR01391 |
DNA primase, catalytic core; Members of this family are DNA primase, a ubiquitous bacteria ... |
2-409 |
1.46e-170 |
|
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: 490.58 E-value: 1.46e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 2 YYSDEIIEEVRSRNDIVDVISTYVKLQKKGSSYFGLCPFHNEKSPSFSVSRQKQMYYCFGCGAGGNVFTFLMEYENYTFV 81
Cdd:TIGR01391 1 MIPEEFIDELKERVDIVDVISEYVKLKKKGRNYVGLCPFHHEKTPSFSVSPEKQFYHCFGCGAGGDAIKFLMEIEGISFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 82 EALKYLADRAGVELPEEEYSKEAKERADTRAILLEINKAAAQYYYVQLKS-SQGAVGLGYFKKRQLSDETIKAFGLGYSN 160
Cdd:TIGR01391 81 EAVEELAKRAGIDLPFEKDQQEKKEQKSKRKKLYELLELAAKFFKNQLKHtPENRAALDYLQSRGLSDETIDRFELGYAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 161 KYSDDLYRYLKS-KGYKDDMIAKAGLISIDEKNGVYDKFWNRVMFPIMDVNSRVIGFGGRVMGDAKPKYLNSPETMVFDK 239
Cdd:TIGR01391 161 NNWDFLFDFLQNkKGFDLELLAEAGLLVKKENGKYYDRFRNRIMFPIHDPKGRVVGFGGRALGDEKPKYLNSPETPLFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 240 SRNLYGLNRARRT--KKPYFLLCEGYMDVISLHQAGFTNAVASLGTALTPGHAALIRRYVQEVYLTYDSDGAGTRAALRA 317
Cdd:TIGR01391 241 SELLYGLHKARKEirKEKELILVEGYMDVIALHQAGIKNAVASLGTALTEEHIKLLKRYADEIILCFDGDKAGRKAALRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 318 MPILRDAGITAKIIRMEPYKDPDEFIKNLGAEKFEERIASARNVFMYSLEVLEKEYDMNSPEGKTEFMKETARRLTQFEE 397
Cdd:TIGR01391 321 IELLLPLGINVKVIKLPGGKDPDEYLRKEGVEALKKLLENSKSLIEFLIARLLSNYNLDTPEEKAKLVEELLPLIKKIPD 400
|
410
....*....|..
gi 942060763 398 EIERNNYIEAVA 409
Cdd:TIGR01391 401 PILRDYYLQKLA 412
|
|
| zf-CHC2 |
pfam01807 |
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases. |
4-98 |
4.23e-52 |
|
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
Pssm-ID: 426447 [Multi-domain] Cd Length: 95 Bit Score: 173.20 E-value: 4.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 4 SDEIIEEVRSRNDIVDVISTYVKLQKKGSSYFGLCPFHNEKSPSFSVSRQKQMYYCFGCGAGGNVFTFLMEYENYTFVEA 83
Cdd:pfam01807 1 PPEFIDDLKNRIDIVDVVGQYVKLKKRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIKFLMKIEKLSFVEA 80
|
90
....*....|....*
gi 942060763 84 LKYLADRAGVELPEE 98
Cdd:pfam01807 81 VEKLADRYGIEIPYE 95
|
|
| Toprim_N |
pfam08275 |
DNA primase catalytic core, N-terminal domain; |
124-250 |
1.65e-51 |
|
DNA primase catalytic core, N-terminal domain;
Pssm-ID: 429892 [Multi-domain] Cd Length: 128 Bit Score: 173.09 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 124 YYYVQLKSSQGAVGLGYFKKRQLSDETIKAFGLGYSNKYSDDLYRYLKSKGYKDDMIAKAGLISIDEKNGVYDKFWNRVM 203
Cdd:pfam08275 1 FYQELLKTNEGAAALDYLKSRGLSDETIERFQIGYAPDGWDNLLKFLKKKGFSEEELLEAGLLSKNEDGRYYDRFRNRIM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 942060763 204 FPIMDVNSRVIGFGGRVMGDAKP-KYLNSPETMVFDKSRNLYGLNRAR 250
Cdd:pfam08275 81 FPIKDARGRVVGFGGRALDDDKPpKYLNSPETPLFKKSKLLYGLDEAK 128
|
|
| TOPRIM_DnaG_primases |
cd03364 |
TOPRIM_DnaG_primases: The topoisomerase-primase (TORPIM) nucleotidyl transferase/hydrolase ... |
258-333 |
6.74e-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: 120.70 E-value: 6.74e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942060763 258 LLCEGYMDVISLHQAGFTNAVASLGTALTPGHAALIRRYVQEVYLTYDSDGAGTRAALRAMPILRDAGITAKIIRM 333
Cdd:cd03364 4 ILVEGYMDVIALHQAGIKNVVASLGTALTEEQAELLKRLAKEVILAFDGDEAGQKAALRALELLLKLGLNVRVLTL 79
|
|
| ZnF_CHCC |
smart00400 |
zinc finger; |
34-88 |
3.04e-30 |
|
zinc finger;
Pssm-ID: 128681 [Multi-domain] Cd Length: 55 Bit Score: 112.39 E-value: 3.04e-30
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 942060763 34 YFGLCPFHNEKSPSFSVSRQKQMYYCFGCGAGGNVFTFLMEYENYTFVEALKYLA 88
Cdd:smart00400 1 YKGLCPFHGEKTPSFSVSPDKQFFHCFGCGAGGNVISFLMKYDKLSFVEAVKKLA 55
|
|
| Toprim_2 |
pfam13155 |
Toprim-like; This is a family or Toprim-like proteins. |
259-343 |
6.10e-30 |
|
Toprim-like; This is a family or Toprim-like proteins.
Pssm-ID: 463793 [Multi-domain] Cd Length: 88 Bit Score: 112.66 E-value: 6.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 259 LCEGYMDVISLHQAGFTNA--VASLGTALTPGHAALIRRYVQEVYLTYDSDGAGTRAALRAMPILRDAGITAKIIRMEPY 336
Cdd:pfam13155 2 VFEGYIDALSLAQAGIKNVlyVATLGTALTEAQIKLLKRYPKEVILAFDNDEAGRKAAKRLAELLKEAGVDVKIRLLPDG 81
|
....*..
gi 942060763 337 KDPDEFI 343
Cdd:pfam13155 82 KDWNEYL 88
|
|
| TOPRIM_primases |
cd01029 |
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
258-332 |
6.60e-26 |
|
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in the active site regions of bacterial DnaG-type primases and their homologs. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The prototypical bacterial primase. Escherichia coli DnaG is a single subunit enzyme.
Pssm-ID: 173779 [Multi-domain] Cd Length: 79 Bit Score: 101.19 E-value: 6.60e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942060763 258 LLCEGYMDVISLHQAGFTNAVASLGTALTPGHAALIRRYVQEVYLTYDSDGAGTRAALRAMPILRDAGITAKIIR 332
Cdd:cd01029 4 IIVEGYMDVLALHQAGIKNVVAALGTANTEEQLRLLKRFARTVILAFDNDEAGKKAAARALELLLALGGRVRVPP 78
|
|
| Toprim_4 |
pfam13662 |
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ... |
258-331 |
3.36e-20 |
|
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: 85.03 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 258 LLCEGYMDVISLHQAGFTNAVASLGTAL-TPGHAALIRRY------VQEVYLTYDSDGAGTRAALRAMPILRDAGITAKI 330
Cdd:pfam13662 4 IVVEGYADVIALEKAGYKGAVAVLGGALsPLDGIGPEDLNidslggIKEVILALDGDVAGEKTALYLAEALLEEGVKVSR 83
|
.
gi 942060763 331 I 331
Cdd:pfam13662 84 L 84
|
|
| TOPRIM |
smart00493 |
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins; |
258-325 |
3.29e-11 |
|
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
Pssm-ID: 214695 [Multi-domain] Cd Length: 75 Bit Score: 59.20 E-value: 3.29e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942060763 258 LLCEGYMDVISLHQAGF--TNAVASLGTALTPGHAALIRRYVQ--EVYLTYDSDGAGTRAALRAMPILRDAG 325
Cdd:smart00493 4 IIVEGPADAIALEKAGGkrGNVVALGGHLLSKEQIKLLKKLAKkaEVILATDPDREGEAIAWELAELLKPAG 75
|
|
| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
258-333 |
2.05e-09 |
|
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: 54.36 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 258 LLCEGYMDVISLHQAGF--TNAVASLGTAL--TPGHAALIRRYVQEVYLTYDSDGAGTRAALRAMPILRDAGITAKIIRM 333
Cdd:cd00188 4 IIVEGPSDALALAQAGGygGAVVALGGHALnkTRELLKRLLGEAKEVIIATDADREGEAIALRLLELLKSLGKKVRRLLL 83
|
|
| DnaB_bind |
pfam10410 |
DnaB-helicase binding domain of primase; This domain is the C-terminal region three-helical ... |
362-415 |
5.98e-09 |
|
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: 52.07 E-value: 5.98e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 942060763 362 FMYSLEVLEKEYDMNSPEGKTEFMKETARRLTQFEEEIERNNYIEAVAKAYHVG 415
Cdd:pfam10410 1 SEFLIRRLLKGYDLDTPEGRAAALREAAPLLAKIPDPVERDLYLRRLAEELGIS 54
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|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
259-333 |
1.81e-08 |
|
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: 51.97 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 259 LCEGYMDVISLHQA---GFTNAVASLGTALTP---------GHAALIRRYVQEVYLTYDSDGAGTRAALRAM---PILRD 323
Cdd:pfam01751 4 IVEGPSDAIALEKAlggGFQAVVAVLGHLLSLekgpkkkalKALKELALKAKEVILATDPDREGEAIALKLLelkELLEN 83
|
90
....*....|
gi 942060763 324 AGITAKIIRM 333
Cdd:pfam01751 84 AGGRVEFSEL 93
|
|
| PHA02031 |
PHA02031 |
putative DnaG-like primase |
166-355 |
1.52e-06 |
|
putative DnaG-like primase
Pssm-ID: 222844 [Multi-domain] Cd Length: 266 Bit Score: 49.81 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 166 LYRYLKSKGYKDDMIAKAGLISIDEKNGvydkfwnRVMFPIMDvnsrviGFGGRVMGDAKPKYL--NSPETMVFdksrNL 243
Cdd:PHA02031 90 LYGLLLSKGIDPNMMEPGLPLEYSERQG-------RLIFRTDA------GWLGRATADQQPKWVgyGYPAPDYV----GW 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 244 YGLNRARRTkkpyFLLCEGYMDVISLHQA---GFTNAVASLGTALTPGHAA-LIRRYVQEVYLTYDSDGAGTRAALRAMP 319
Cdd:PHA02031 153 PPELSMPRP----VVLTEDYLSALKVRWAcnkPEVFAVALLGTRLRDRLAAiLLQQTCPRVLIFLDGDPAGVDGSAGAMR 228
|
170 180 190
....*....|....*....|....*....|....*.
gi 942060763 320 ILRDAGITAKIIRMEPYKDPdefiKNLGAEKFEERI 355
Cdd:PHA02031 229 RLRPLLIEGQVIITPDGFDP----KDLEREQIRELL 260
|
|
| Toprim_3 |
pfam13362 |
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ... |
256-349 |
1.58e-06 |
|
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic acid manipulation.
Pssm-ID: 433146 [Multi-domain] Cd Length: 97 Bit Score: 46.63 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 256 YFLLCEGYMDVISLHQAGF---TNAVASLGTA-LTPGHAAlirRYVQEVYLTYDSDGA--GTRAALRAMPILRDAGITAK 329
Cdd:pfam13362 1 RLIIGEGIETALSLTQRLNppgTPVIALLSAAnLKAVAWP---ERVKRVYIAADNDAAndGQAAAEKLAERLEAAGIEAV 77
|
90 100
....*....|....*....|
gi 942060763 330 IIRMEPYKDPDEFIKNLGAE 349
Cdd:pfam13362 78 LLEPEAGEDWNDDLQQTGAA 97
|
|
| DnaG_DnaB_bind |
smart00766 |
DNA primase DnaG DnaB-binding; DnaG_DnaB_bind defines a domain of primase required for ... |
458-584 |
6.83e-04 |
|
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: 39.94 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942060763 458 QKILLTWLIESEDIFRQIEKYITPEDFSEGLFRQVAELLyEQYEKH-EVNPAQIMNHFTDEEEHRQVAGLFHTKIkeLTT 536
Cdd:smart00766 1 MRELIRLLLQNPELASLVPDLLPLELFTHPGLALLAELL-ALCRGApGLTTGQLLEHWRDTPYRELLSELAVWDH--LID 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 942060763 537 VKEQEKALQETILRVKDHSIEEATKNLdptdIQGLQRLM---NEKRKMQDL 584
Cdd:smart00766 78 EENLEEEFQDALARLRKQLLERRIEEL----IAKLRRSGltvEEKKELQAL 124
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