|
Name |
Accession |
Description |
Interval |
E-value |
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
1-800 |
0e+00 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 1116.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 1 MNVAEVIVDVsskNIDRPFDYKIPDHLKgMIEVGMRVIVPFGPRKLQGFVTGLKDSSELNGGSMKEVEKLLDLTPVLTEE 80
Cdd:COG1198 1 MKIAEVALPV---PLDRPFDYLVPEGLE-LVQPGSRVLVPFGRRQVVGIVVGLKEESDVDPAKLKPILAVLDDEPLLPEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 81 LMQLSSWLSDKTLSFKITALQAMLPAALKAKYEKELKvvdeealtpdikqlfrnqksllysditdesilsslqkfvrkgs 160
Cdd:COG1198 77 LLELLRWVADYYLCPLGEVLRLALPAGLRQGYPARIK------------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 161 idvtykvaqktnkkMIRMIEAGADKEelarhadsLTKQASKQLAVLTYFIGGGAKISAAELCKKTDSSSATLKTLLKKGL 240
Cdd:COG1198 114 --------------TERYVRLTLGEE--------LPKRAPKQRRVLEALREHGGPLTLSELAKEAGVSRSVLKALVKKGL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 241 LTESFEEVYRDPYQdRMFKKTEPLSLTEEQQAAFEPIKQAvaDHVHHVFLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVL 320
Cdd:COG1198 172 LEIEEREVDRDPFA-PDVPAEPPPTLNEEQQAAVEAIRAA--AGGFSVFLLHGVTGSGKTEVYLQAIAEVLAQGKQALVL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 321 VPEISLTPQMVNRFKGRFGSQVAVMHSGLSTGEKYDEWRKIQRKEVRLVVGARSAIFAPFENLGMIIIDEEHESSYKQEE 400
Cdd:COG1198 249 VPEIALTPQTVERFRARFGARVAVLHSGLSDGERLDEWRRARRGEARIVIGTRSALFAPFPNLGLIIVDEEHDSSYKQED 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 401 MPRYHAKDVAIRRAEHHSCPVVLGSATPTLESFARAKKGVYELLPLKHRVNRQLMPDVSLVDMREELRNGNRsMFSRELM 480
Cdd:COG1198 329 GPRYHARDVAVVRAKLEGAPVVLGSATPSLESLYNAQKGRYRLLELPERAGGAPLPEVELVDMREEPLEGGR-ILSPPLL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 481 EQLEEKLAKKEQAVLFLNKRGYSSFVMCRDCGYVPQCPHCDISMTYHRYGQRLKCHYCGHEEPVPGTCPECGSEHIRFFG 560
Cdd:COG1198 408 EAIEETLERGEQVLLFLNRRGYAPFLLCRDCGWVAKCPNCDVSLTYHRSRRRLRCHYCGYEEPVPKQCPECGSDSLRPFG 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 561 TGTQRVEEELTKVLPKARVIRMDVDTTSRKGAHEKLLSAFGEGKADILLGTQMIAKGLDFPNVTLVGVLSADTTLHIPDF 640
Cdd:COG1198 488 PGTERVEEELAELFPDARVLRMDRDTTRRKGALEKLLEAFARGEADILVGTQMLAKGHDFPNVTLVGVLDADLGLNSPDF 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 641 RAAEKTFQLLTQVSGRAGRHEKPGTVVIQTYTPSHYSIQLTKTHDYETFFQQEMAHRRAQSYPPYYYVALVTVSHEEAAK 720
Cdd:COG1198 568 RAAERTFQLLTQVAGRAGRAEKPGEVLIQTYNPEHPVIQALLNHDYEAFYEEELAERKAAGYPPFGRLALLRASGKDEEA 647
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 721 AAVTAEKITNYLRAGC-GPDTKILGPAASPIARIKDRYRYQCVIKYRQENELQIQLKKILEHYKRDIAQKhVMISIDMNP 799
Cdd:COG1198 648 AEEFAQALARALRALLsADGVEVLGPAPAPIARLRGRYRWQLLLKAPSRAALQQLLRALLALLEKPLPRK-VRWSIDVDP 726
|
.
gi 494651802 800 Y 800
Cdd:COG1198 727 Q 727
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
1-802 |
0e+00 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 1046.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 1 MNVAEVIVDVsskNIDRPFDYKIPDHLKgmIEVGMRVIVPFGPRKLQGFVTGLKDSSELNGGSMKEVEKLLDLTPVLTEE 80
Cdd:PRK05580 2 MKIARVLLPV---PLPRPFDYLIPEGLE--VQPGDRVRVPFGNRKLIGVVVGVEEGSEVPADKLKPILEVLDLEPLLPPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 81 LMQLSSWLSDKTLSFKITALQAMLPAALKAkyekelkvvdeealtpdikqlfrnqksllysditdESILSSLQKFVRKGS 160
Cdd:PRK05580 77 LLRLLDWAADYYLSPLGEVLRLALLAELAL-----------------------------------AASSAVLKGLVKKGL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 161 IDVtykvaqktnkkmirmieagadkeelarhadsltkqaskqlavltyfigggakisaaelckktdsssatlktllkkgl 240
Cdd:PRK05580 122 IEL----------------------------------------------------------------------------- 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 241 ltesfEEVYRDPYQDRMFKKTEPLSLTEEQQAAFEPIKQAVAdhvHHVFLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVL 320
Cdd:PRK05580 125 -----EEVEVLRLRPPPDPAFEPPTLNPEQAAAVEAIRAAAG---FSPFLLDGVTGSGKTEVYLQAIAEVLAQGKQALVL 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 321 VPEISLTPQMVNRFKGRFGSQVAVMHSGLSTGEKYDEWRKIQRKEVRLVVGARSAIFAPFENLGMIIIDEEHESSYKQEE 400
Cdd:PRK05580 197 VPEIALTPQMLARFRARFGAPVAVLHSGLSDGERLDEWRKAKRGEAKVVIGARSALFLPFKNLGLIIVDEEHDSSYKQQE 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 401 MPRYHAKDVAIRRAEHHSCPVVLGSATPTLESFARAKKGVYELLPLKHRVNRQLMPDVSLVDMREELRNGNRSMFSRELM 480
Cdd:PRK05580 277 GPRYHARDLAVVRAKLENIPVVLGSATPSLESLANAQQGRYRLLRLTKRAGGARLPEVEIIDMRELLRGENGSFLSPPLL 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 481 EQLEEKLAKKEQAVLFLNKRGYSSFVMCRDCGYVPQCPHCDISMTYHRYGQRLKCHYCGHEEPVPGTCPECGSEHIRFFG 560
Cdd:PRK05580 357 EAIKQRLERGEQVLLFLNRRGYAPFLLCRDCGWVAECPHCDASLTLHRFQRRLRCHHCGYQEPIPKACPECGSTDLVPVG 436
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 561 TGTQRVEEELTKVLPKARVIRMDVDTTSRKGAHEKLLSAFGEGKADILLGTQMIAKGLDFPNVTLVGVLSADTTLHIPDF 640
Cdd:PRK05580 437 PGTERLEEELAELFPEARILRIDRDTTRRKGALEQLLAQFARGEADILIGTQMLAKGHDFPNVTLVGVLDADLGLFSPDF 516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 641 RAAEKTFQLLTQVSGRAGRHEKPGTVVIQTYTPSHYSIQLTKTHDYETFFQQEMAHRRAQSYPPYYYVALVTVSHEEAAK 720
Cdd:PRK05580 517 RASERTFQLLTQVAGRAGRAEKPGEVLIQTYHPEHPVIQALLAQDYDAFAEQELEERRAAGYPPFGRLALLRASAKDEEK 596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 721 AAVTAEKITNYLRAGCGPD-TKILGPAASPIARIKDRYRYQCVIKYRQENELQIQLKKILEHYKRDIAQKHVMISIDMNP 799
Cdd:PRK05580 597 AEKFAQQLAALLPNLLPLLdVEVLGPAPAPIAKIAGRYRYQLLLKSPSRADLQKLLRAWLALLQKLPQARKVRWSIDVDP 676
|
...
gi 494651802 800 YML 802
Cdd:PRK05580 677 QSF 679
|
|
| priA |
TIGR00595 |
primosomal protein N'; All proteins in this family for which functions are known are ... |
290-800 |
0e+00 |
|
primosomal protein N'; All proteins in this family for which functions are known are components of the primosome which is involved in replication, repair, and recombination.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273162 [Multi-domain] Cd Length: 505 Bit Score: 843.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 290 LLHGVTGSGKTEIYLQSIEKVLAKGQEAIVLVPEISLTPQMVNRFKGRFGSQVAVMHSGLSTGEKYDEWRKIQRKEVRLV 369
Cdd:TIGR00595 1 LLFGVTGSGKTEVYLQAIEKVLALGKSVLVLVPEIALTPQMIQRFKYRFGSQVAVLHSGLSDSEKLQAWRKVKNGEILVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 370 VGARSAIFAPFENLGMIIIDEEHESSYKQEEMPRYHAKDVAIRRAEHHSCPVVLGSATPTLESFARAKKGVYELLPLKHR 449
Cdd:TIGR00595 81 IGTRSALFLPFKNLGLIIVDEEHDSSYKQEEGPRYHARDVAVYRAKKFNCPVVLGSATPSLESYHNAKQKAYRLLVLTRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 450 VNRQLMPDVSLVDMREELRNgnrSMFSRELMEQLEEKLAKKEQAVLFLNKRGYSSFVMCRDCGYVPQCPHCDISMTYHRY 529
Cdd:TIGR00595 161 VSGRKPPEVKLIDMRKEPRQ---SFLSPELITAIEQTLAAGEQSILFLNRRGYSKNLLCRSCGYILCCPNCDVSLTYHKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 530 GQRLKCHYCGHEEPVPGTCPECGSEHIRFFGTGTQRVEEELTKVLPKARVIRMDVDTTSRKGAHEKLLSAFGEGKADILL 609
Cdd:TIGR00595 238 EGKLRCHYCGYQEPIPKTCPQCGSEDLVYKGYGTEQVEEELAKLFPGARIARIDSDTTSRKGAHEALLNQFANGKADILI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 610 GTQMIAKGLDFPNVTLVGVLSADTTLHIPDFRAAEKTFQLLTQVSGRAGRHEKPGTVVIQTYTPSHYSIQLTKTHDYETF 689
Cdd:TIGR00595 318 GTQMIAKGHHFPNVTLVGVLDADSGLHSPDFRAAERGFQLLTQVAGRAGRAEDPGQVIIQTYNPNHPAIQAALTGDYEAF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 690 FQQEMAHRRAQSYPPYYYVALVTVSHEEAAKAAVTAEKITNYLRAGCGPDTKILGPAASPIARIKDRYRYQCVIKYRQEN 769
Cdd:TIGR00595 398 YEQELAQRRALNYPPFTRLIRLIFRGKNEEKAQQTAQAAHELLKQNLDEKLEVLGPSPAPIAKIAGRYRYQILLKSKSFL 477
|
490 500 510
....*....|....*....|....*....|.
gi 494651802 770 ELQIQLKKILEhykRDIAQKHVMISIDMNPY 800
Cdd:TIGR00595 478 VLQKLVNKTLL---KEIPSSSVYCEVDVDPI 505
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
458-698 |
2.14e-143 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 421.65 E-value: 2.14e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 458 VSLVDMREELrngNRSMFSRELMEQLEEKLAKKEQAVLFLNKRGYSSFVMCRDCGYVPQCPHCDISMTYHRYGQRLKCHY 537
Cdd:cd18804 1 IEIVDMKEEE---LKSGFSPKLLDAIKETLEKGEQVILFLNRRGYSPSVLCRDCGYVPECPNCDVSMTYHKSTNKLKCHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 538 CGHEEPVPGTCPECGSEHIRFFGTGTQRVEEELTKVLPKARVIRMDVDTTSRKGAHEKLLSAFGEGKADILLGTQMIAKG 617
Cdd:cd18804 78 CGYQEPIPKQCPECGSEDLVFKGIGTERVEEELKTLFPEARIARIDRDTTRKKGALEKLLDQFERGEIDILIGTQMIAKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 618 LDFPNVTLVGVLSADTTLHIPDFRAAEKTFQLLTQVSGRAGRHEKPGTVVIQTYTPSHYSIQLTKTHDYETFFQQEMAHR 697
Cdd:cd18804 158 LDFPNVTLVGILNADSGLNSPDFRASERAFQLLTQVSGRAGRGDKPGKVIIQTYNPEHPLIQAAKEEDYEAFYEEELAER 237
|
.
gi 494651802 698 R 698
Cdd:cd18804 238 K 238
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
270-449 |
4.34e-106 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350687 [Multi-domain] Cd Length: 178 Bit Score: 323.01 E-value: 4.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 270 QQAAFEPIKQAVADHvhHVFLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVLVPEISLTPQMVNRFKGRFGSQVAVMHSGL 349
Cdd:cd17929 1 QRKAYEAIVSSLGGF--KTFLLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTPQLIKRFKKRFGDKVAVLHSKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 350 STGEKYDEWRKIQRKEVRLVVGARSAIFAPFENLGMIIIDEEHESSYKQEEMPRYHAKDVAIRRAEHHSCPVVLGSATPT 429
Cdd:cd17929 79 SDKERADEWRKIKRGEAKVVIGARSALFAPFKNLGLIIVDEEHDSSYKQDSGPRYHARDVAIYRAKLENAPVVLGSATPS 158
|
170 180
....*....|....*....|
gi 494651802 430 LESFARAKKGVYELLPLKHR 449
Cdd:cd17929 159 LESYYNAQQGKYRLLQLTER 178
|
|
| PriA_3primeBD |
pfam17764 |
3'DNA-binding domain (3'BD); This domain represents the N-terminal DNA-binding domain found in ... |
5-105 |
8.17e-35 |
|
3'DNA-binding domain (3'BD); This domain represents the N-terminal DNA-binding domain found in the PriA protein. The 3'BD, which has been shown to bind the 3' end of the leading-strand arm of replication fork structures.
Pssm-ID: 465491 [Multi-domain] Cd Length: 96 Bit Score: 127.57 E-value: 8.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 5 EVIVDVSsknIDRPFDYKIPDHLKgmIEVGMRVIVPFGPRKLQGFVTGLKDSSELNGGSMKEVEKLLDLTPVLTEELMQL 84
Cdd:pfam17764 1 EVAVPLP---LDRPFDYRVPEELA--VKIGMRVLVPFGKRKVTGIVVGLSEESEVDPEKLKPILEVLDEEPLLTPELLEL 75
|
90 100
....*....|....*....|.
gi 494651802 85 SSWLSDKTLSFKITALQAMLP 105
Cdd:pfam17764 76 ARWMAEYYLCPLGEVLRAALP 96
|
|
| PRK14873 |
PRK14873 |
primosomal protein N'; |
309-745 |
1.01e-34 |
|
primosomal protein N';
Pssm-ID: 237844 [Multi-domain] Cd Length: 665 Bit Score: 141.23 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 309 KVLAKGQEAIVLVPEISLTPQMVNRFKGRFGS-QVAVMHSGLSTGEKYDEWRKIQRKEVRLVVGARSAIFAPFENLGMII 387
Cdd:PRK14873 183 ATLRAGRGALVVVPDQRDVDRLEAALRALLGAgDVAVLSAGLGPADRYRRWLAVLRGQARVVVGTRSAVFAPVEDLGLVA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 388 IDEEHESSYKQEEMPRYHAKDVAIRRAEHHSCPVVLGSATPTLESFARAKKG-VYELLPLKHRVnRQLMPDVSLVD---- 462
Cdd:PRK14873 263 IWDDGDDLLAEPRAPYPHAREVALLRAHQHGCALLIGGHARTAEAQALVESGwAHDLVAPRPVV-RARAPRVRALGdsgl 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 463 --MREELRNGNR--SMFSRELMEQLEEKlakkeqAVLF-LNKRGYSSFVMCRDCGYVPQCPHCDISMTYHRYGQRLKCHY 537
Cdd:PRK14873 342 alERDPAARAARlpSLAFRAARDALEHG------PVLVqVPRRGYVPSLACARCRTPARCRHCTGPLGLPSAGGTPRCRW 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 538 CGHEEPvPGTCPECGSEHIRFFGTGTQRVEEELTKVLPKARVI-------RMDVDTTSR-----KGAhEKLLSAfgeGKA 605
Cdd:PRK14873 416 CGRAAP-DWRCPRCGSDRLRAVVVGARRTAEELGRAFPGVPVVtsggdqvVDTVDAGPAlvvatPGA-EPRVEG---GYG 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 606 DILLgtqmiakgldfpnvtlvgvLSADTTLHIPDFRAAEKTFQLLTQVSGRAGRHEKPGTVVI--QTYTPshySIQLTKT 683
Cdd:PRK14873 491 AALL-------------------LDAWALLGRQDLRAAEDTLRRWMAAAALVRPRADGGQVVVvaESSLP---TVQALIR 548
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651802 684 HDYETFFQQEMAHRRAQSYPPYYYVALVTvsheeAAKAAVTAEkitnYLRAGCGPDTKILGP 745
Cdd:PRK14873 549 WDPVGHAERELAERAEVGFPPAVRMAAVD-----GRPAAVAAL----LEAAGLPDGAEVLGP 601
|
|
| PriA_C |
pfam18074 |
Primosomal protein N C-terminal domain; This is the C-terminal domain found in PriA DNA ... |
704-799 |
1.86e-26 |
|
Primosomal protein N C-terminal domain; This is the C-terminal domain found in PriA DNA helicase, a multifunctional enzyme that mediates the process of restarting prematurely terminated DNA replication reactions in bacteria. The C-terminal domain (CTD) bears similarity to the S10 subunit which binds branched rRNA within the bacterial ribosome. The C-terminal domain is part of the helicase domain of PriA proteins. It acts together with the 3' DNA-binding domain to form a site for binding ssDNA-binding protein (SSB).
Pssm-ID: 465633 [Multi-domain] Cd Length: 96 Bit Score: 103.84 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 704 PYYYVALVTVSHEEAAKAAVTAEKITNYLRAGC-GPDTKILGPAASPIARIKDRYRYQCVIKYRQENELQIQLKKILEHY 782
Cdd:pfam18074 1 PFSRLALIRVSGKDEEKAEKFAEELAELLKELLkLQGVEILGPAPAPIAKIKGRYRYQLLLKSKSRKALHQLLRELLEEL 80
|
90
....*....|....*..
gi 494651802 783 KRDIAQKhVMISIDMNP 799
Cdd:pfam18074 81 QKLPKRK-VRISIDVDP 96
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
258-431 |
7.91e-20 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 88.32 E-value: 7.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 258 FKKTEPLSLTEEQQAAFEPIKQAvadhvHHVFLLHGVTGSGKTEIYLQSIEKVLAKGQE--AIVLVPEISLTPQMVNRFK 335
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSG-----LRDVILAAPTGSGKTLAALLPALEALKRGKGgrVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 336 GRFGSQVAVMHSGLSTGEKYDEWRKIQRKEVRLVVGARSAIFAPFEN-------LGMIIIDEEHESSykqeemPRYHAKD 408
Cdd:smart00487 76 KLGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENdklslsnVDLVILDEAHRLL------DGGFGDQ 149
|
170 180
....*....|....*....|....
gi 494651802 409 VA-IRRAEHHSCPVVLGSATPTLE 431
Cdd:smart00487 150 LEkLLKLLPKNVQLLLLSATPPEE 173
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
267-429 |
1.90e-19 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 86.14 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 267 TEEQQAAFEPIKQAvadhvhHVFLLHGVTGSGKTEIY----LQSIEKVLAKGQeAIVLVPEISLTPQMVNRFKGRFGSQV 342
Cdd:pfam00270 1 TPIQAEAIPAILEG------RDVLVQAPTGSGKTLAFllpaLEALDKLDNGPQ-ALVLAPTRELAEQIYEELKKLGKGLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 343 AVMHSGLSTGEKYDEWRKIqrKEVRLVVGARSAIFA------PFENLGMIIIDEEHESSYKQeempryHAKDVA-IRRAE 415
Cdd:pfam00270 74 LKVASLLGGDSRKEQLEKL--KGPDILVGTPGRLLDllqerkLLKNLKLLVLDEAHRLLDMG------FGPDLEeILRRL 145
|
170
....*....|....
gi 494651802 416 HHSCPVVLGSATPT 429
Cdd:pfam00270 146 PKKRQILLLSATLP 159
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
264-428 |
2.68e-19 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 85.80 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 264 LSLTEEQQAAFEPIKQAVADHVHHvFLLHGVTGSGKTEIYLQSIEKVLAKG--QEAIVLVPEISLTPQMVNRFKGRFGSq 341
Cdd:pfam04851 2 LELRPYQIEAIENLLESIKNGQKR-GLIVMATGSGKTLTAAKLIARLFKKGpiKKVLFLVPRKDLLEQALEEFKKFLPN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 342 vAVMHSGLSTGEKYDEWrkiqRKEVRLVVGARSAIFAPFENL---------GMIIIDEEHESSYKqeempryhakdvAIR 412
Cdd:pfam04851 80 -YVEIGEIISGDKKDES----VDDNKIVVTTIQSLYKALELAslellpdffDVIIIDEAHRSGAS------------SYR 142
|
170
....*....|....*...
gi 494651802 413 R-AEHHSCPVVLG-SATP 428
Cdd:pfam04851 143 NiLEYFKPAFLLGlTATP 160
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
286-427 |
1.71e-16 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 77.06 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 286 HHVFLLHGVTGSGKTEIYLQSIEKVLA-KGQEAIVLVPEISLTPQMVNRFKGRF--GSQVAVMHSGLSTGEKYDEWrkiq 362
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLkKGKKVLVLVPTKALALQTAERLRELFgpGIRVAVLVGGSSAEEREKNK---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494651802 363 RKEVRLVVGARSAIFAP--------FENLGMIIIDEEHESSYKQEEMPRYhakDVAIRRAEHHSCPVVLGSAT 427
Cdd:cd00046 77 LGDADIIIATPDMLLNLllredrlfLKDLKLIIVDEAHALLIDSRGALIL---DLAVRKAGLKNAQVILLSAT 146
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
265-667 |
1.66e-15 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 79.92 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 265 SLTEEQQAAFEPIKQAVADHVHHvfLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVLVPE----ISLTPqmvnRFKGRF-G 339
Cdd:COG4098 110 TLTPAQQKASDELLEAIKKKEEH--LVWAVCGAGKTEMLFPAIAEALKQGGRVCIATPRvdvvLELAP----RLQQAFpG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 340 SQVAVMHsglstGEKYDEWRKIQrkevrLVVgA--------RSAifapFEnlgMIIIDEEHESSYKQEEMPRYhakdvAI 411
Cdd:COG4098 184 VDIAALY-----GGSEEKYRYAQ-----LVI-AtthqllrfYQA----FD---LLIIDEVDAFPYSGDPMLQY-----AV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 412 RRAEHHSCPVVLGSATPT--LESFARAKKGVYELLPLkhRVNRQLMPD---VSLVDMREELRNGNrsmFSRELMEQLEEK 486
Cdd:COG4098 241 KRARKPDGKLIYLTATPSkaLQRQVKRGKLKVVKLPA--RYHGHPLPVpkfKWLGNWKKRLRRGK---LPRKLLKWLKKR 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 487 LAKKEQAVLFlnkrgyssfvmcrdcgyvpqCPHcdISMtyhrygqrlkchycgheepvpgtcpecgsehirffgtgTQRV 566
Cdd:COG4098 316 LKEGRQLLIF--------------------VPT--IEL--------------------------------------LEQL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 567 EEELTKVLPKARvirmdVDTTS-----RKgahEKLLsAFGEGKADILLGTQMIAKGLDFPNVTlVGVLSADTTLhipdF- 640
Cdd:COG4098 336 VALLQKLFPEER-----IAGVHaedpeRK---EKVQ-AFRDGEIPILVTTTILERGVTFPNVD-VAVLGADHPV----Ft 401
|
410 420
....*....|....*....|....*....
gi 494651802 641 RAAektfqlLTQVSGRAGRH-EKP-GTVV 667
Cdd:COG4098 402 EAA------LVQIAGRVGRSaDYPtGEVI 424
|
|
| PriA_CRR |
pfam18319 |
PriA DNA helicase Cys-rich region (CRR) domain; This is a cys-rich region (CRR) domain found ... |
517-543 |
2.74e-14 |
|
PriA DNA helicase Cys-rich region (CRR) domain; This is a cys-rich region (CRR) domain found in PriA DNA helicases. In bacteria, the replication restart process is orchestrated by the PriA DNA helicase, which identifies replication forks via structure-specific DNA binding and interactions with fork-associated ssDNA-binding proteins (SSBs). The CRR region which is embedded within the C-terminal helicase lobe has been identified to bind two Zn2+ ions. This 50-residue insertion forms a structure on the surface of the helicase core in which two Zn2+ ions are coordinated by invariant Cys residues. Biochemical experiments have shown that sequence changes to Zn2+-binding Cys residues in the PriA CRR can eliminate helicase, but not ATPase, activity and can block assembly of PriB onto DNA-bound PriA, implicating the CRR in multiple functions in PriA.
Pssm-ID: 465708 [Multi-domain] Cd Length: 27 Bit Score: 67.17 E-value: 2.74e-14
10 20
....*....|....*....|....*..
gi 494651802 517 CPHCDISMTYHRYGQRLKCHYCGHEEP 543
Cdd:pfam18319 1 CPNCDVSLTYHKSRNRLRCHYCGYTEP 27
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
252-400 |
5.17e-13 |
|
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350749 [Multi-domain] Cd Length: 193 Bit Score: 68.37 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 252 PYQDRmFKKTEPLSLTEEQQAAFEPIKQAVADHVHHVFLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVLVPEISLTPQMV 331
Cdd:cd17991 3 EEQEE-FEASFPYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQHY 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494651802 332 NRFKGRF---GSQVAVMhSGLSTGEKYDEWRK-IQRKEVRLVVGARSAIF--APFENLGMIIIDEEHESSYKQEE 400
Cdd:cd17991 82 ETFKERFanfPVNVELL-SRFTTAAEQREILEgLKEGKVDIVIGTHRLLSkdVEFKNLGLLIIDEEQRFGVKQKE 155
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
251-664 |
4.92e-11 |
|
transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273152 [Multi-domain] Cd Length: 926 Bit Score: 66.61 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 251 DPYQDRmFKKTEPLSLTEEQQAAFEPIKQAVADHVHHVFLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVLVPEISLTPQM 330
Cdd:TIGR00580 438 LEWQQE-FEDSFPFEETPDQLKAIEEIKADMESPRPMDRLVCGDVGFGKTEVAMRAAFKAVLDGKQVAVLVPTTLLAQQH 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 331 VNRFKGRF---GSQVAVMHSGLSTGEKYDEWRKIQRKEVRLVVGARSAI--FAPFENLGMIIIDEEHESSYKQEEmpryH 405
Cdd:TIGR00580 517 FETFKERFanfPVTIELLSRFRSAKEQNEILKELASGKIDILIGTHKLLqkDVKFKDLGLLIIDEEQRFGVKQKE----K 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 406 AKDvaiRRAEHHscpVVLGSATP---TLE-SFARAKkgvyellplkhrvnrqlmpDVSLVDMREElrngNRSMFSRELME 481
Cdd:TIGR00580 593 LKE---LRTSVD---VLTLSATPiprTLHmSMSGIR-------------------DLSIIATPPE----DRLPVRTFVME 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 482 QLEEKLAkkeQAVLFLNKRGYSSFvmcrdcgYVpqcpHCDISmtyhrygqrlkchycgheepvpgtcpecgsehirffgt 561
Cdd:TIGR00580 644 YDPELVR---EAIRRELLRGGQVF-------YV----HNRIE-------------------------------------- 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 562 GTQRVEEELTKVLPKARVirmdvdttsrKGAH--------EKLLSAFGEGKADILLGTQMIAKGLDFPNVTLVGVLSADT 633
Cdd:TIGR00580 672 SIEKLATQLRELVPEARI----------AIAHgqmtenelEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIERADK 741
|
410 420 430
....*....|....*....|....*....|.
gi 494651802 634 tlhipdFRAAEktfqlLTQVSGRAGRHEKPG 664
Cdd:TIGR00580 742 ------FGLAQ-----LYQLRGRVGRSKKKA 761
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
256-400 |
2.60e-10 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 60.12 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 256 RMFKKTEPLSLTEEQQAAFEPIKQAVADHVHHVFLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVLVPEISLTPQMVNRFK 335
Cdd:cd17918 6 QELCKSLPFSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEAR 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494651802 336 GRFgsqvAVMHSGLSTGEKydewRKIQRKEVRLVVGARSAIF--APFENLGMIIIDEEHESSYKQEE 400
Cdd:cd17918 86 KFL----PFINVELVTGGT----KAQILSGISLLVGTHALLHldVKFKNLDLVIVDEQHRFGVAQRE 144
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
568-659 |
7.73e-10 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 56.07 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 568 EELTKVLPKA--RVIRMDVDTTSRKgaHEKLLSAFGEGKADILLGTQMIAKGLDFPNVTLVGVLSADttlhipdfraaeK 645
Cdd:smart00490 1 EELAELLKELgiKVARLHGGLSQEE--REEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP------------W 66
|
90
....*....|....
gi 494651802 646 TFQLLTQVSGRAGR 659
Cdd:smart00490 67 SPASYIQRIGRAGR 80
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
243-491 |
4.35e-09 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 59.71 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 243 ESFEEVYRDPYQDRMFKKTEPLSLTEE-QQAAFEPIKQAvADHVHHVFLLHGVTGSGKTEIYLQSIEKVLAKGQEA--IV 319
Cdd:COG1203 104 QALDHLLAERLERLLPKKSKPRTPINPlQNEALELALEA-AEEEPGLFILTAPTGGGKTEAALLFALRLAAKHGGRriIY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 320 LVPEISLTPQMVNRFKGRFGSQVAVMHSglSTGEKYDEWRKIQRKEVRLVVGARSAIFAP-------------FEN---- 382
Cdd:COG1203 183 ALPFTSIINQTYDRLRDLFGEDVLLHHS--LADLDLLEEEEEYESEARWLKLLKELWDAPvvvttidqlfeslFSNrkgq 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 383 ----LGM----IIIDEEHesSYKqeemPRYHAK-DVAIRRAEHHSCPVVLGSAT-PTLesFARAKKGVYELLP------- 445
Cdd:COG1203 261 errlHNLansvIILDEVQ--AYP----PYMLALlLRLLEWLKNLGGSVILMTATlPPL--LREELLEAYELIPdepeelp 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651802 446 ------LKHRVN--RQLMPDVSLVD-MREELRNGNRSMF-------SRELMEQLEEKLAKKE 491
Cdd:COG1203 333 eyfrafVRKRVElkEGPLSDEELAElILEALHKGKSVLVivntvkdAQELYEALKEKLPDEE 394
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
559-660 |
1.24e-08 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 53.37 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 559 FGTGTQRVEEELTKVLPKARVIRMDVDTTSRKgaHEKLLSAFGEGKADILLGTQMIAKGLDFPNVTLVGVLSADTTLhip 638
Cdd:pfam00271 21 FSQTKKTLEAELLLEKEGIKVARLHGDLSQEE--REEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWNP--- 95
|
90 100
....*....|....*....|..
gi 494651802 639 dfraaektfQLLTQVSGRAGRH 660
Cdd:pfam00271 96 ---------ASYIQRIGRAGRA 108
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
243-630 |
1.42e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 58.11 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 243 ESFEEVYRDPYQDRMFKKTEPLSLTEEQQAAFEPIKQAVADHvHHVFLLHGVTGSGKTEIYLQSIEKVLAKGQeAIVLVP 322
Cdd:COG1061 58 TERELAEAEALEAGDEASGTSFELRPYQQEALEALLAALERG-GGRGLVVAPTGTGKTVLALALAAELLRGKR-VLVLVP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 323 EISLTPQMVNRFKGRFGSQvavmhsgLSTGEKYDEWRKIqrkevrlVVG-----ARSAIFAPFENL-GMIIIDEEHessy 396
Cdd:COG1061 136 RRELLEQWAEELRRFLGDP-------LAGGGKKDSDAPI-------TVAtyqslARRAHLDELGDRfGLVIIDEAH---- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 397 kqeempryHAKDVAIRR-AEHHSCPVVLG-SATP--------TLESFARAkkgVYElLPLKHRVNRQLMPDVSLVDMREE 466
Cdd:COG1061 198 --------HAGAPSYRRiLEAFPAAYRLGlTATPfrsdgreiLLFLFDGI---VYE-YSLKEAIEDGYLAPPEYYGIRVD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 467 LRNGNRSMfsRELMEQLEEKLAKKEQAVL-----FLNKRGYSSFVMCRdCGYVPQCphcdismtyhrygqrlkchycghe 541
Cdd:COG1061 266 LTDERAEY--DALSERLREALAADAERKDkilreLLREHPDDRKTLVF-CSSVDHA------------------------ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 542 epvpgtcpecgsehirffgtgtQRVEEELTKVLPKARVIRMDVDTTSRkgahEKLLSAFGEGKADILLGTQMIAKGLDFP 621
Cdd:COG1061 319 ----------------------EALAELLNEAGIRAAVVTGDTPKKER----EEILEAFRDGELRILVTVDVLNEGVDVP 372
|
....*....
gi 494651802 622 NVTLVGVLS 630
Cdd:COG1061 373 RLDVAILLR 381
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
561-668 |
6.13e-08 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 53.02 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 561 TGTQRVEEELTKVLP----KARVIRMDVDTTSRKgaheKLLSAFGEGKADILLGTQMIAKGLDFPNVTLVGVLSADttlh 636
Cdd:cd18790 34 TLTKRMAEDLTEYLQelgvKVRYLHSEIDTLERV----EIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDAD---- 105
|
90 100 110
....*....|....*....|....*....|..
gi 494651802 637 IPDFRAAEKTfqlLTQVSGRAGRHEKpGTVVI 668
Cdd:cd18790 106 KEGFLRSETS---LIQTIGRAARNVN-GKVIL 133
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
258-392 |
1.92e-07 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 52.53 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 258 FKKTEPLSLTEEQQAAFEPIKQAVADHVHHVFLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVLVP-EIsLTPQMVNRFKG 336
Cdd:cd17992 38 FLEALPFELTGAQKRVIDEILRDLASEKPMNRLLQGDVGSGKTVVAALAMLAAVENGYQVALMAPtEI-LAEQHYDSLKK 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494651802 337 RFGS---QVAVMHSGLSTGEKYDEWRKIQRKEVRLVVGARSAIFAP--FENLGMIIIDEEH 392
Cdd:cd17992 117 LLEPlgiRVALLTGSTKAKEKREILEKIASGEIDIVIGTHALIQEDveFHNLGLVIIDEQH 177
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
258-392 |
2.37e-06 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 51.30 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 258 FKKTEPLSLTEEQQAAFEPIKQAVADHVHHVFLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVLVP-EIsLTPQMVNRFK- 335
Cdd:PRK10917 254 FLASLPFELTGAQKRVVAEILADLASPKPMNRLLQGDVGSGKTVVAALAALAAIEAGYQAALMAPtEI-LAEQHYENLKk 332
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494651802 336 --GRFGSQVAVMHSGLSTGEKYDEWRKIQRKEVRLVVGARsAIFAP---FENLGMIIIDEEH 392
Cdd:PRK10917 333 llEPLGIRVALLTGSLKGKERREILEAIASGEADIVIGTH-ALIQDdveFHNLGLVIIDEQH 393
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
266-428 |
3.17e-06 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 47.69 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 266 LTEEQQAAFEPIKQAVADHvHHVFLLHgvTGSGKTEIYLQSIEKVLAKGqeAIVLVPEISLTPQMVNRFKgRFGSQVAVm 345
Cdd:cd17926 1 LRPYQEEALEAWLAHKNNR-RGILVLP--TGSGKTLTALALIAYLKELR--TLIVVPTDALLDQWKERFE-DFLGDSSI- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 346 hsGLSTGEKYDEwrkiqrKEVRLVVGAR--------SAIFAPFENLGMIIIDEEHessykqeempryHAKDVAIRR-AEH 416
Cdd:cd17926 74 --GLIGGGKKKD------FDDANVVVATyqslsnlaEEEKDLFDQFGLLIVDEAH------------HLPAKTFSEiLKE 133
|
170
....*....|...
gi 494651802 417 HSCPVVLG-SATP 428
Cdd:cd17926 134 LNAKYRLGlTATP 146
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
564-664 |
9.07e-06 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 46.49 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 564 QRVEEELTKVLPKARVIRMDVDTTSRKgaHEKLLSAFGEGKADILLGTQMIAKGLDFPNVTLVGVLSADttlhipdfraa 643
Cdd:cd18792 48 EALAEELKELVPEARVALLHGKMTEDE--KEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDAD----------- 114
|
90 100
....*....|....*....|...
gi 494651802 644 ekTFQL--LTQVSGRAGRHEKPG 664
Cdd:cd18792 115 --RFGLsqLHQLRGRVGRGKHQS 135
|
|
| DEXDc_ComFA |
cd17925 |
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ... |
270-348 |
9.39e-06 |
|
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350683 [Multi-domain] Cd Length: 143 Bit Score: 46.14 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 270 QQAAFEPIKQAVADHVHHvfLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVLVPEISLTPQMVNRFKGRF-GSQVAVMHSG 348
Cdd:cd17925 2 QQKASNALVETIDAKEDL--LVWAVTGAGKTEMLFPAIAQALRQGGRVAIASPRIDVCLELAPRLKAAFpGAAIVLLHGG 79
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
272-392 |
6.23e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 44.83 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 272 AAFEPIKQAVADHV---HHVFLLHGvTGSGKTEIYlqSIEKVLAKGQeAIVLVPEISLTPQMVNRFKgRFGSQVAVMHSG 348
Cdd:cd17920 11 DEFRPGQLEAINAVlagRDVLVVMP-TGGGKSLCY--QLPALLLDGV-TLVVSPLISLMQDQVDRLQ-QLGIRAAALNST 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 494651802 349 LSTGEKYDEWRKIQRKEVRLV-VG----ARSAIFAPFEN------LGMIIIDEEH 392
Cdd:cd17920 86 LSPEEKREVLLRIKNGQYKLLyVTperlLSPDFLELLQRlperkrLALIVVDEAH 140
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
564-659 |
7.53e-05 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 43.49 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 564 QRVEEELTKVLPKARVIRMDVDTTSRKgaHEKLLSAFGEGKADILLGTQMIAKGLDFPNVTLVGVLSADTtlhipdFRAA 643
Cdd:cd18810 39 EKLATQLRQLVPEARIAIAHGQMTENE--LEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADK------FGLA 110
|
90
....*....|....*.
gi 494651802 644 EktfqlLTQVSGRAGR 659
Cdd:cd18810 111 Q-----LYQLRGRVGR 121
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
295-392 |
9.97e-05 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 43.79 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 295 TGSGKTEIYLQSIEKVLAK-GQEAIVLVPEISLTPQMVNRFKGRFGSQVAVmhSGLSTGEKYDEWRKIQRKEV------R 367
Cdd:cd17921 26 TSSGKTLIAELAILRALATsGGKAVYIAPTRALVNQKEADLRERFGPLGKN--VGLLTGDPSVNKLLLAEADIlvatpeK 103
|
90 100
....*....|....*....|....*
gi 494651802 368 LVVGARSAIFAPFENLGMIIIDEEH 392
Cdd:cd17921 104 LDLLLRNGGERLIQDVRLVVVDEAH 128
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
594-668 |
1.15e-04 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 42.49 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 594 EKLLSAFGEGKADILLGTQMIAKGLDFPNVTLVgV-----LSADTTLHipdfRAaektfqlltqvsGRAGRHEKPGTVVI 668
Cdd:cd18787 67 ERALKKFRSGKVRVLVATDVAARGLDIPGVDHV-InydlpRDAEDYVH----RI------------GRTGRAGRKGTAIT 129
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
568-663 |
5.28e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 41.18 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 568 EELTKVL-PKARVIRMDvdttSRKGAHEKL--LSAFGEGKADILLGTQMIAKGLDFPNVTLVGVLSAD----TTLHipdf 640
Cdd:cd18811 52 EYLKERFrPELNVGLLH----GRLKSDEKDavMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAErfglSQLH---- 123
|
90 100
....*....|....*....|...
gi 494651802 641 raaektfqlltQVSGRAGRHEKP 663
Cdd:cd18811 124 -----------QLRGRVGRGDHQ 135
|
|
| COG2888 |
COG2888 |
Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 ... |
517-554 |
1.09e-03 |
|
Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 family [General function prediction only];
Pssm-ID: 442134 [Multi-domain] Cd Length: 52 Bit Score: 37.79 E-value: 1.09e-03
10 20 30
....*....|....*....|....*....|....*...
gi 494651802 517 CPHCdismtyhRYGQRLKCHYCGHEEPVPGTCPECGSE 554
Cdd:COG2888 20 CPNC-------GEALIIRCPKCRKQSNALYFCPKCGFE 50
|
|
| PRK07219 |
PRK07219 |
DNA topoisomerase I; Validated |
483-557 |
1.15e-03 |
|
DNA topoisomerase I; Validated
Pssm-ID: 235971 [Multi-domain] Cd Length: 822 Bit Score: 42.68 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 483 LEEKLAKKEQAVLFLNKRGYSSFVMCRDCGY----------VPQCPHCDISMTYH--RYGQRLKC-HY--CGHEEPVP-- 545
Cdd:PRK07219 647 LDEVCEKCGLPVIKILRGKQTFVVGCPDCEAekeeedpdevIGPCPKCGGELAIKqlKYGSFLGCtNYpkCKYTLPLPrr 726
|
90
....*....|....*....
gi 494651802 546 -------GTCPECGSEHIR 557
Cdd:PRK07219 727 gkitvtdEKCPECGLPLLR 745
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
289-392 |
3.20e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 39.24 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 289 FLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVLVPEISLTPQMVNRFKGRFGSQVAVmhsGLSTGeKYDEwrkiqrKEVRL 368
Cdd:cd18028 20 LLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKLEEIGLKV---GISTG-DYDE------DDEWL 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 494651802 369 vvGARSAIFAPFE--------------NLGMIIIDEEH 392
Cdd:cd18028 90 --GDYDIIVATYEkfdsllrhspswlrDVGVVVVDEIH 125
|
|
| DEXHc_UvrB |
cd17916 |
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ... |
258-338 |
3.40e-03 |
|
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II) and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA, but its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a member of the DEAD-like helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350674 [Multi-domain] Cd Length: 299 Bit Score: 40.27 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 258 FKKTEPLSLTEEQQAAFEPIKQAVADHVHHVFLLhGVTGSGKTEIYLQSIEKVlakGQEAIVLVPEISLTPQMVNRFKGR 337
Cdd:cd17916 1 FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLL-GVTGSGKTFTIANVIAQV---NKPTLVIAHNKTLAAQLYSEFKEF 76
|
.
gi 494651802 338 F 338
Cdd:cd17916 77 F 77
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
251-411 |
4.83e-03 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 40.50 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 251 DPYQDRMFKKTEPLSLTEEQQAAFEPIKQAVADHVHHVFLLHGVTGSGKTEIYLQSIEKVLAKGQEAIVLVPEISLTPQM 330
Cdd:PRK10689 586 DREQYQLFCDSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQH 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494651802 331 VNRFKGRFGS---QVAVMHSGLSTGEKYDEWRKIQRKEVRLVVGARSAIFAP--FENLGMIIIDEEHESSYKQEEMPRYH 405
Cdd:PRK10689 666 YDNFRDRFANwpvRIEMLSRFRSAKEQTQILAEAAEGKIDILIGTHKLLQSDvkWKDLGLLIVDEEHRFGVRHKERIKAM 745
|
....*.
gi 494651802 406 AKDVAI 411
Cdd:PRK10689 746 RADVDI 751
|
|
| |
