|
Name |
Accession |
Description |
Interval |
E-value |
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
1-726 |
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: 1016.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 1 MRFVEVAIKVPLPRTFDYKIDEQLispsAPIVPGMRVLVPFGNQKKVAVVLALKTHTDVPENKIKAVTEVIDQTPILSSQ 80
Cdd:COG1198 1 MKIAEVALPVPLDRPFDYLVPEGL----ELVQPGSRVLVPFGRRQVVGIVVGLKEESDVDPAKLKPILAVLDDEPLLPEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 81 HLELLSFTARYYCYPLGETIHIALPGALRQGENPDKTSINMISLTEKGAkvPSLKAKTQLNLLKQLAQSGKS-SITEL-K 158
Cdd:COG1198 77 LLELLRWVADYYLCPLGEVLRLALPAGLRQGYPARIKTERYVRLTLGEE--LPKRAPKQRRVLEALREHGGPlTLSELaK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 159 ALGFSKKTIDALIDKELVT-QSIEHDNQWQSVAPTVGTKPVLNKEQAVACTTINQSV-GFKSFLLEGVTGSGKTEVYLQC 236
Cdd:COG1198 155 EAGVSRSVLKALVKKGLLEiEEREVDRDPFAPDVPAEPPPTLNEEQQAAVEAIRAAAgGFSVFLLHGVTGSGKTEVYLQA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 237 LEEVLKRGEQALVLVPEIGLTPQTVNRFRRRFPDtPIMLWHSALTDNERLQTWRFCEKGSCAIVIGTRSSIFLPFLKLGM 316
Cdd:COG1198 235 IAEVLAQGKQALVLVPEIALTPQTVERFRARFGA-RVAVLHSGLSDGERLDEWRRARRGEARIVIGTRSALFAPFPNLGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 317 IVVDEEHDSSFKQQDTLRYHARDLAAYRAFQHKIPLILGSATPALETLHKAINNKYQLLSLTERAQTATDNQFMLLDMKG 396
Cdd:COG1198 314 IIVDEEHDSSYKQEDGPRYHARDVAVVRAKLEGAPVVLGSATPSLESLYNAQKGRYRLLELPERAGGAPLPEVELVDMRE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 397 QPDQAG--IAHASLATMRQHLNRGKQVMVFLNRRGFSPTLICHECGWLSECNRCSTSATFHKAIGQMICHHCGEQHPVPH 474
Cdd:COG1198 394 EPLEGGriLSPPLLEAIEETLERGEQVLLFLNRRGYAPFLLCRDCGWVAKCPNCDVSLTYHRSRRRLRCHYCGYEEPVPK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 475 QCPDCGSTQIFPNGKGTEQIEEFLSSEFPDTPVTRIDRDSTRRKGSLEKALEEINQGGARILVGTQMLAKGHHFADVSLV 554
Cdd:COG1198 474 QCPECGSDSLRPFGPGTERVEEELAELFPDARVLRMDRDTTRRKGALEKLLEAFARGEADILVGTQMLAKGHDFPNVTLV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 555 LILDVDSGLYSCDFRATEHLAQLVTQVAGRAGRSGEPGQVLLQTHFPEHPLLQDLVNNGYQDFARFALSERDDADLPPIT 634
Cdd:COG1198 554 GVLDADLGLNSPDFRAAERTFQLLTQVAGRAGRAEKPGEVLIQTYNPEHPVIQALLNHDYEAFYEEELAERKAAGYPPFG 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 635 NMAIVRAQGHSIKLVVDFLTDLV----PVNGVSGIQLLGPIPAPLERVAGMYRFQLHIQAQDRKVLHQYLAQMVDYLSTs 710
Cdd:COG1198 634 RLALLRASGKDEEAAEEFAQALAralrALLSADGVEVLGPAPAPIARLRGRYRWQLLLKAPSRAALQQLLRALLALLEK- 712
|
730
....*....|....*.
gi 2527404910 711 KLAQKVRWSLDVDPID 726
Cdd:COG1198 713 PLPRKVRWSIDVDPQS 728
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
1-727 |
0e+00 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 916.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 1 MRFVEVAIKVPLPRTFDYKIDEQLispsaPIVPGMRVLVPFGNQKKVAVVLALKTHTDVPENKIKAVTEVIDQTPILSSQ 80
Cdd:PRK05580 2 MKIARVLLPVPLPRPFDYLIPEGL-----EVQPGDRVRVPFGNRKLIGVVVGVEEGSEVPADKLKPILEVLDLEPLLPPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 81 HLELLSFTARYYCYPLGETIHIALPGALrqgenpdktsinmisltekgakvpslkaktqlnllkqlaqsgkssitelkAL 160
Cdd:PRK05580 77 LLRLLDWAADYYLSPLGEVLRLALLAEL--------------------------------------------------AL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 161 GFSKKTIDALIDKELVTQSIEHDNQWQSVAPTVGTKPVLNKEQAVACTTINQSVGFKSFLLEGVTGSGKTEVYLQCLEEV 240
Cdd:PRK05580 107 AASSAVLKGLVKKGLIELEEVEVLRLRPPPDPAFEPPTLNPEQAAAVEAIRAAAGFSPFLLDGVTGSGKTEVYLQAIAEV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 241 LKRGEQALVLVPEIGLTPQTVNRFRRRFPDtPIMLWHSALTDNERLQTWRFCEKGSCAIVIGTRSSIFLPFLKLGMIVVD 320
Cdd:PRK05580 187 LAQGKQALVLVPEIALTPQMLARFRARFGA-PVAVLHSGLSDGERLDEWRKAKRGEAKVVIGARSALFLPFKNLGLIIVD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 321 EEHDSSFKQQDTLRYHARDLAAYRAFQHKIPLILGSATPALETLHKAINNKYQLLSLTERAQTATDNQFMLLDMK---GQ 397
Cdd:PRK05580 266 EEHDSSYKQQEGPRYHARDLAVVRAKLENIPVVLGSATPSLESLANAQQGRYRLLRLTKRAGGARLPEVEIIDMRellRG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 398 PDQAGIAHASLATMRQHLNRGKQVMVFLNRRGFSPTLICHECGWLSECNRCSTSATFHKAIGQMICHHCGEQHPVPHQCP 477
Cdd:PRK05580 346 ENGSFLSPPLLEAIKQRLERGEQVLLFLNRRGYAPFLLCRDCGWVAECPHCDASLTLHRFQRRLRCHHCGYQEPIPKACP 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 478 DCGSTQIFPNGKGTEQIEEFLSSEFPDTPVTRIDRDSTRRKGSLEKALEEINQGGARILVGTQMLAKGHHFADVSLVLIL 557
Cdd:PRK05580 426 ECGSTDLVPVGPGTERLEEELAELFPEARILRIDRDTTRRKGALEQLLAQFARGEADILIGTQMLAKGHDFPNVTLVGVL 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 558 DVDSGLYSCDFRATEHLAQLVTQVAGRAGRSGEPGQVLLQTHFPEHPLLQDLVNNGYQDFARFALSERDDADLPPITNMA 637
Cdd:PRK05580 506 DADLGLFSPDFRASERTFQLLTQVAGRAGRAEKPGEVLIQTYHPEHPVIQALLAQDYDAFAEQELEERRAAGYPPFGRLA 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 638 IVRAQGHSIKLVVDFLTDLV----PVNGVSGIQLLGPIPAPLERVAGMYRFQLHIQAQDRKVLHQYLAQMVDYLSTSKLA 713
Cdd:PRK05580 586 LLRASAKDEEKAEKFAQQLAallpNLLPLLDVEVLGPAPAPIAKIAGRYRYQLLLKSPSRADLQKLLRAWLALLQKLPQA 665
|
730
....*....|....
gi 2527404910 714 QKVRWSLDVDPIDM 727
Cdd:PRK05580 666 RKVRWSIDVDPQSF 679
|
|
| priA |
TIGR00595 |
primosomal protein N'; All proteins in this family for which functions are known are ... |
220-725 |
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: 611.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 220 LLEGVTGSGKTEVYLQCLEEVLKRGEQALVLVPEIGLTPQTVNRFRRRFpDTPIMLWHSALTDNERLQTWRFCEKGSCAI 299
Cdd:TIGR00595 1 LLFGVTGSGKTEVYLQAIEKVLALGKSVLVLVPEIALTPQMIQRFKYRF-GSQVAVLHSGLSDSEKLQAWRKVKNGEILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 300 VIGTRSSIFLPFLKLGMIVVDEEHDSSFKQQDTLRYHARDLAAYRAFQHKIPLILGSATPALETLHKAINNKYQLLSLTE 379
Cdd:TIGR00595 80 VIGTRSALFLPFKNLGLIIVDEEHDSSYKQEEGPRYHARDVAVYRAKKFNCPVVLGSATPSLESYHNAKQKAYRLLVLTR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 380 RAQTATDNQFMLLDMKGQPDQAGIAHASLATMRQHLNRGKQVMVFLNRRGFSPTLICHECGWLSECNRCSTSATFHKAIG 459
Cdd:TIGR00595 160 RVSGRKPPEVKLIDMRKEPRQSFLSPELITAIEQTLAAGEQSILFLNRRGYSKNLLCRSCGYILCCPNCDVSLTYHKKEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 460 QMICHHCGEQHPVPHQCPDCGSTQIFPNGKGTEQIEEFLSSEFPDTPVTRIDRDSTRRKGSLEKALEEINQGGARILVGT 539
Cdd:TIGR00595 240 KLRCHYCGYQEPIPKTCPQCGSEDLVYKGYGTEQVEEELAKLFPGARIARIDSDTTSRKGAHEALLNQFANGKADILIGT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 540 QMLAKGHHFADVSLVLILDVDSGLYSCDFRATEHLAQLVTQVAGRAGRSGEPGQVLLQTHFPEHPLLQDLVNNGYQDFAR 619
Cdd:TIGR00595 320 QMIAKGHHFPNVTLVGVLDADSGLHSPDFRAAERGFQLLTQVAGRAGRAEDPGQVIIQTYNPNHPAIQAALTGDYEAFYE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 620 FALSERDDADLPPITNMAIVRAQGH---SIKLVVDFLTDLVPVNGVSGIQLLGPIPAPLERVAGMYRFQLHIQAQDRKVL 696
Cdd:TIGR00595 400 QELAQRRALNYPPFTRLIRLIFRGKneeKAQQTAQAAHELLKQNLDEKLEVLGPSPAPIAKIAGRYRYQILLKSKSFLVL 479
|
490 500
....*....|....*....|....*....
gi 2527404910 697 HQYLAQmvdYLSTSKLAQKVRWSLDVDPI 725
Cdd:TIGR00595 480 QKLVNK---TLLKEIPSSSVYCEVDVDPI 505
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
391-625 |
1.38e-110 |
|
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: 334.60 E-value: 1.38e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 391 LLDMKGQPDQAGIAHASLATMRQHLNRGKQVMVFLNRRGFSPTLICHECGWLSECNRCSTSATFHKAIGQMICHHCGEQH 470
Cdd:cd18804 3 IVDMKEEELKSGFSPKLLDAIKETLEKGEQVILFLNRRGYSPSVLCRDCGYVPECPNCDVSMTYHKSTNKLKCHYCGYQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 471 PVPHQCPDCGSTQIFPNGKGTEQIEEFLSSEFPDTPVTRIDRDSTRRKGSLEKALEEINQGGARILVGTQMLAKGHHFAD 550
Cdd:cd18804 83 PIPKQCPECGSEDLVFKGIGTERVEEELKTLFPEARIARIDRDTTRKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527404910 551 VSLVLILDVDSGLYSCDFRATEHLAQLVTQVAGRAGRSGEPGQVLLQTHFPEHPLLQDLVNNGYQDFARFALSER 625
Cdd:cd18804 163 VTLVGILNADSGLNSPDFRASERAFQLLTQVSGRAGRGDKPGKVIIQTYNPEHPLIQAAKEEDYEAFYEEELAER 237
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
203-380 |
1.37e-91 |
|
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: 283.33 E-value: 1.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 203 QAVACTTINQSV-GFKSFLLEGVTGSGKTEVYLQCLEEVLKRGEQALVLVPEIGLTPQTVNRFRRRFPDtPIMLWHSALT 281
Cdd:cd17929 1 QRKAYEAIVSSLgGFKTFLLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTPQLIKRFKKRFGD-KVAVLHSKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 282 DNERLQTWRFCEKGSCAIVIGTRSSIFLPFLKLGMIVVDEEHDSSFKQQDTLRYHARDLAAYRAFQHKIPLILGSATPAL 361
Cdd:cd17929 80 DKERADEWRKIKRGEAKVVIGARSALFAPFKNLGLIIVDEEHDSSYKQDSGPRYHARDVAIYRAKLENAPVVLGSATPSL 159
|
170
....*....|....*....
gi 2527404910 362 ETLHKAINNKYQLLSLTER 380
Cdd:cd17929 160 ESYYNAQQGKYRLLQLTER 178
|
|
| PriA_3primeBD |
pfam17764 |
3'DNA-binding domain (3'BD); This domain represents the N-terminal DNA-binding domain found in ... |
5-105 |
4.50e-36 |
|
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: 131.04 E-value: 4.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 5 EVAIKVPLPRTFDYKIDEQLispsaPIVPGMRVLVPFGNQKKVAVVLALKTHTDVPENKIKAVTEVIDQTPILSSQHLEL 84
Cdd:pfam17764 1 EVAVPLPLDRPFDYRVPEEL-----AVKIGMRVLVPFGKRKVTGIVVGLSEESEVDPEKLKPILEVLDEEPLLTPELLEL 75
|
90 100
....*....|....*....|.
gi 2527404910 85 LSFTARYYCYPLGETIHIALP 105
Cdd:pfam17764 76 ARWMAEYYLCPLGEVLRAALP 96
|
|
| PRK14873 |
PRK14873 |
primosomal protein N'; |
6-728 |
5.10e-35 |
|
primosomal protein N';
Pssm-ID: 237844 [Multi-domain] Cd Length: 665 Bit Score: 141.61 E-value: 5.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 6 VAIKVPLP---RTFDYKIDEQLispSAPIVPGMRVLVPFGNQKKVAVVLALKTHTDvPENKIKAVTEVIDQTPILSSQHL 82
Cdd:PRK14873 16 VLPDLGLPhldRLFDYLVPEEL---SDDAQPGVRVRVRFGGRLVDGFVLERRSDSD-HEGKLRWLERVVSPEPVLTPEIR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 83 ELLSFTARYYCYPLGETIHIALPGalRQGEnpdktsinmislTEKGAKVPSLKAKT----QLNLLKQLAQsGKSSITELK 158
Cdd:PRK14873 92 RLARAVADRYAGTRADVLRLAVPP--RHAR------------VEKEPVATPPPPLTapppDPSGWAAYGR-GPRFLAALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 159 ALGFSKKTIDALIDKelvtqsiehdnQW-QSVAptvgtkpvlnkeQAVActtinqsvgfksfllegvtgsgktevylqcl 237
Cdd:PRK14873 157 AGRAARAVWQALPGE-----------DWaRRLA------------AAAA------------------------------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 238 eEVLKRGEQALVLVPEIGLTPQTVNRFRRRFPDTPIMLWHSALTDNERLQTWRFCEKGSCAIVIGTRSSIFLPFLKLGMI 317
Cdd:PRK14873 183 -ATLRAGRGALVVVPDQRDVDRLEAALRALLGAGDVAVLSAGLGPADRYRRWLAVLRGQARVVVGTRSAVFAPVEDLGLV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 318 VVDEEHDSSFKQQDTLRYHARDLAAYRAFQHKIPLILGSATPALET--------LHKAINNKYQLLSLTERAQTATDNQF 389
Cdd:PRK14873 262 AIWDDGDDLLAEPRAPYPHAREVALLRAHQHGCALLIGGHARTAEAqalvesgwAHDLVAPRPVVRARAPRVRALGDSGL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 390 MLLDMKGQPdQAGIAHASLATMRQHLNRGKqVMVFLNRRGFSPTLICHECGWLSECNRCSTSATFHKAIGQMICHHCGeQ 469
Cdd:PRK14873 342 ALERDPAAR-AARLPSLAFRAARDALEHGP-VLVQVPRRGYVPSLACARCRTPARCRHCTGPLGLPSAGGTPRCRWCG-R 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 470 HPVPHQCPDCGSTQIFPNGKGTEQIEEFLSSEFPDTPVtridRDSTRrkgslEKALEEINQGGAriLV----GTQMLAKG 545
Cdd:PRK14873 419 AAPDWRCPRCGSDRLRAVVVGARRTAEELGRAFPGVPV----VTSGG-----DQVVDTVDAGPA--LVvatpGAEPRVEG 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 546 HHFAdvslVLILDVDSGLYSCDFRATE----HLAQLVTQVAGRAgrsgEPGQVLLQTHfPEHPLLQDLVNNGYQDFARFA 621
Cdd:PRK14873 488 GYGA----ALLLDAWALLGRQDLRAAEdtlrRWMAAAALVRPRA----DGGQVVVVAE-SSLPTVQALIRWDPVGHAERE 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 622 LSERDDADLPPITNMAIVRAQGHSIKLVVDFLTdlvpvnGVSGIQLLGPIP-APLERVAGMYRFQLHIQ-------AQDR 693
Cdd:PRK14873 559 LAERAEVGFPPAVRMAAVDGRPAAVAALLEAAG------LPDGAEVLGPVPlPPGVRRPAGIDAREDRVralvrvpRARG 632
|
730 740 750
....*....|....*....|....*....|....*
gi 2527404910 694 KVLHQYLAQMVDYLSTSKLAQKVRwsLDVDPIDMI 728
Cdd:PRK14873 633 AELAAALRRAVAVRSARREPGPLR--VQIDPLDIG 665
|
|
| PriA_C |
pfam18074 |
Primosomal protein N C-terminal domain; This is the C-terminal domain found in PriA DNA ... |
632-724 |
3.19e-24 |
|
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: 97.29 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 632 PITNMAIVRAQGHSIKLVVDFLTD----LVPVNGVSGIQLLGPIPAPLERVAGMYRFQLHIQAQDRKVLHQYLAQMVDYL 707
Cdd:pfam18074 1 PFSRLALIRVSGKDEEKAEKFAEElaelLKELLKLQGVEILGPAPAPIAKIKGRYRYQLLLKSKSRKALHQLLRELLEEL 80
|
90
....*....|....*..
gi 2527404910 708 STSKLaQKVRWSLDVDP 724
Cdd:pfam18074 81 QKLPK-RKVRISIDVDP 96
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
217-358 |
3.57e-21 |
|
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: 90.16 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 217 KSFLLEGVTGSGKTEVYLQCLEEVL-KRGEQALVLVPEIGLTPQTVNRFRRRF-PDTPIMLWHSALTDNERLQTWRfcek 294
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLlKKGKKVLVLVPTKALALQTAERLRELFgPGIRVAVLVGGSSAEEREKNKL---- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527404910 295 GSCAIVIGTRSSIFLP--------FLKLGMIVVDEEHDSSFKQQDTLRYharDLAAYRAFQHKIPLILGSAT 358
Cdd:cd00046 78 GDADIIIATPDMLLNLllredrlfLKDLKLIIVDEAHALLIDSRGALIL---DLAVRKAGLKNAQVILLSAT 146
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
217-360 |
1.01e-18 |
|
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: 83.83 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 217 KSFLLEGVTGSGKTEVYLQCLEEVLKR---GEQALVLVPEIGLTPQTVNRFRRRFPDTPIMLwHSALTDNERLQTWRfcE 293
Cdd:pfam00270 15 RDVLVQAPTGSGKTLAFLLPALEALDKldnGPQALVLAPTRELAEQIYEELKKLGKGLGLKV-ASLLGGDSRKEQLE--K 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527404910 294 KGSCAIVIGTRSSIFLPFLK------LGMIVVDEEHD-SSFKQQDTLRYHARDLAAyrafqhKIPLILGSATPA 360
Cdd:pfam00270 92 LKGPDILVGTPGRLLDLLQErkllknLKLLVLDEAHRlLDMGFGPDLEEILRRLPK------KRQILLLSATLP 159
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
199-362 |
2.30e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 84.08 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 199 LNKEQAVACTTINQsvGFKSFLLEGVTGSGKTEVYLQCLEEVLKRGE--QALVLVPEIGLTPQTVNRFRRRFPDTPImLW 276
Cdd:smart00487 9 LRPYQKEAIEALLS--GLRDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELKKLGPSLGL-KV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 277 HSALTDNERLQTWRFCEKGSCAIVIGTRSSIF-------LPFLKLGMIVVDEEHD-SSFKQQDTLRYHARDLAayrafqH 348
Cdd:smart00487 86 VGLYGGDSKREQLRKLESGKTDILVTTPGRLLdllendkLSLSNVDLVILDEAHRlLDGGFGDQLEKLLKLLP------K 159
|
170
....*....|....
gi 2527404910 349 KIPLILGSATPALE 362
Cdd:smart00487 160 NVQLLLLSATPPEE 173
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
196-359 |
1.84e-13 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 68.85 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 196 KPVLNKEQAVACTTINQSV--GFKSFLLEGVTGSGKTEVYLQCLEEVLKRG--EQALVLVPEIGLTPQTVNRFRRRFPD- 270
Cdd:pfam04851 1 KLELRPYQIEAIENLLESIknGQKRGLIVMATGSGKTLTAAKLIARLFKKGpiKKVLFLVPRKDLLEQALEEFKKFLPNy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 271 TPIMLWHSALTDNERLQTWRfcekgscaIVIGTRSSIF---------LPFLKLGMIVVDEEHDSSFKqqdtlryHARDLA 341
Cdd:pfam04851 81 VEIGEIISGDKKDESVDDNK--------IVVTTIQSLYkalelasleLLPDFFDVIIIDEAHRSGAS-------SYRNIL 145
|
170
....*....|....*....
gi 2527404910 342 AYraFQHKIplILG-SATP 359
Cdd:pfam04851 146 EY--FKPAF--LLGlTATP 160
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
220-368 |
1.59e-12 |
|
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: 66.83 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 220 LLEGVTGSGKTEVYLQCLEEVLKRGEQALVLVPEIGLTPQTVNRFRRRFPDTP--IMLWHSALTDNERLQTWRFCEKGSC 297
Cdd:cd17991 40 LICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQHYETFKERFANFPvnVELLSRFTTAAEQREILEGLKEGKV 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527404910 298 AIVIGTRSSIF--LPFLKLGMIVVDEEHDSSFKQQDTLryhardlaayRAFQHKIPLILGSATPALETLHKAI 368
Cdd:cd17991 120 DIVIGTHRLLSkdVEFKNLGLLIIDEEQRFGVKQKEKL----------KELRPNVDVLTLSATPIPRTLHMAL 182
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
220-334 |
4.85e-12 |
|
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: 65.13 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 220 LLEGVTGSGKTEVYLQCLEEVLKRGEQALVLVPEIGLTPQTVNRFRRRFPDTPIMLwhsaLTDNERLQTwrfceKGSCAI 299
Cdd:cd17918 40 LLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKFLPFINVEL----VTGGTKAQI-----LSGISL 110
|
90 100 110
....*....|....*....|....*....|....*..
gi 2527404910 300 VIGTRSSIFL--PFLKLGMIVVDEEHDSSFKQQDTLR 334
Cdd:cd17918 111 LVGTHALLHLdvKFKNLDLVIVDEQHRFGVAQREALY 147
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
220-427 |
4.32e-09 |
|
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: 60.06 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 220 LLEGVTGSGKTEVYLQCLEEVLKRGEQALVLVPEIGLTPQTVNRFRRRFPDTP--IMLWHSALTDNERLQTWRFCEKGSC 297
Cdd:TIGR00580 476 LVCGDVGFGKTEVAMRAAFKAVLDGKQVAVLVPTTLLAQQHFETFKERFANFPvtIELLSRFRSAKEQNEILKELASGKI 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 298 AIVIGTRSSI--FLPFLKLGMIVVDEEHDSSFKQQDTLRyhardlaAYRAFQHKIPLilgSATPALETLHKAINNKYQLL 375
Cdd:TIGR00580 556 DILIGTHKLLqkDVKFKDLGLLIIDEEQRFGVKQKEKLK-------ELRTSVDVLTL---SATPIPRTLHMSMSGIRDLS 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2527404910 376 SLTeraqTATDNQFMLLDMKGQPDQAGIAHAslatMRQHLNRGKQVMVFLNR 427
Cdd:TIGR00580 626 IIA----TPPEDRLPVRTFVMEYDPELVREA----IRRELLRGGQVFYVHNR 669
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
492-589 |
2.40e-08 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 51.44 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 492 EQIEEFLSSEfpDTPVTRIDRDSTRRKgsLEKALEEINQGGARILVGTQMLAKGHHFADVSLVLILDVDSGLyscdfrat 571
Cdd:smart00490 1 EELAELLKEL--GIKVARLHGGLSQEE--REEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP-------- 68
|
90
....*....|....*...
gi 2527404910 572 ehlaQLVTQVAGRAGRSG 589
Cdd:smart00490 69 ----ASYIQRIGRAGRAG 82
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
199-595 |
7.84e-08 |
|
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: 55.27 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 199 LNKEQAVACTTINQSV-GFKSFLLEGVTGSGKTEVYLQCLEEVLKRGEQALVLVPEIG----LTPqtvnRFRRRFPDTPI 273
Cdd:COG4098 111 LTPAQQKASDELLEAIkKKEEHLVWAVCGAGKTEMLFPAIAEALKQGGRVCIATPRVDvvleLAP----RLQQAFPGVDI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 274 MLWHSALTDNERL---------QTWRFCEKgscaivigtrssiFlpflklGMIVVDE------EHDssfkqqDTLRYhar 338
Cdd:COG4098 187 AALYGGSEEKYRYaqlviatthQLLRFYQA-------------F------DLLIIDEvdafpySGD------PMLQY--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 339 dlAAYRAFQHKIPLILGSATPALETLHKAINNKYQLLSLTER--------AQTATDNQFMLLDMKGQ-PDQAgiahasLA 409
Cdd:COG4098 239 --AVKRARKPDGKLIYLTATPSKALQRQVKRGKLKVVKLPARyhghplpvPKFKWLGNWKKRLRRGKlPRKL------LK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 410 TMRQHLNRGKQVMVFLnrrgfsPTlichecgwlsecnrcstsatfhkaIGQMichhcgeqhpvphqcpdcgstqifpngk 489
Cdd:COG4098 311 WLKKRLKEGRQLLIFV------PT------------------------IELL---------------------------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 490 gtEQIEEFLSSEFPDTPVTRIDRDSTRRKgslEKaLEEINQGGARILVGTQMLAKGHHFADVSlVLILDVDSGLYscdfr 569
Cdd:COG4098 333 --EQLVALLQKLFPEERIAGVHAEDPERK---EK-VQAFRDGEIPILVTTTILERGVTFPNVD-VAVLGADHPVF----- 400
|
410 420
....*....|....*....|....*...
gi 2527404910 570 aTEhlAQLVtQVAGRAGRSGE-P-GQVL 595
Cdd:COG4098 401 -TE--AALV-QIAGRVGRSADyPtGEVI 424
|
|
| PriA_CRR |
pfam18319 |
PriA DNA helicase Cys-rich region (CRR) domain; This is a cys-rich region (CRR) domain found ... |
445-471 |
2.40e-07 |
|
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: 47.14 E-value: 2.40e-07
10 20
....*....|....*....|....*..
gi 2527404910 445 CNRCSTSATFHKAIGQMICHHCGEQHP 471
Cdd:pfam18319 1 CPNCDVSLTYHKSRNRLRCHYCGYTEP 27
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
220-334 |
1.07e-06 |
|
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: 50.22 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 220 LLEGVTGSGKTEVYLQCLEEVLKRGEQALVLVP-EIgLTPQTVNRFRRRFPDTPI--MLWHSALTDNERLQTWRFCEKGS 296
Cdd:cd17992 70 LLQGDVGSGKTVVAALAMLAAVENGYQVALMAPtEI-LAEQHYDSLKKLLEPLGIrvALLTGSTKAKEKREILEKIASGE 148
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2527404910 297 CAIVIGTRSSIF--LPFLKLGMIVVDEEHDSSFKQQDTLR 334
Cdd:cd17992 149 IDIVIGTHALIQedVEFHNLGLVIIDEQHRFGVEQRLKLR 188
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
133-359 |
3.60e-06 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 50.41 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 133 SLKAKTQLNLLKQLAQSGKSSITELKALGFSKKTIDALIDKELVTQSIEHDNQWQSVAPTVGTKPVLNKEQAVACTTINQ 212
Cdd:COG1061 15 RSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALEALLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 213 --SVGFKSFLLEGVTGSGKTEVYLQCLEEvLKRGEQALVLVPEIGLTPQTVNRFRRRFPDTPIMLWHSALTDNerlqtwr 290
Cdd:COG1061 95 alERGGGRGLVVAPTGTGKTVLALALAAE-LLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAGGGKKDSDAP------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 291 fcekgscaIVIGTRSSI-FLPFLKL-----GMIVVDEEHdssfkqqdtlryHA-----RDLAayRAFQHKIplILG-SAT 358
Cdd:COG1061 167 --------ITVATYQSLaRRAHLDElgdrfGLVIIDEAH------------HAgapsyRRIL--EAFPAAY--RLGlTAT 222
|
.
gi 2527404910 359 P 359
Cdd:COG1061 223 P 223
|
|
| DEXDc_ComFA |
cd17925 |
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ... |
206-285 |
4.97e-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: 46.91 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 206 ACTTINQSvgfKSFLLEGVTGSGKTEVYLQCLEEVLKRGEQALVLVPEIGLTPQTVNRFRRRFPDTPIMLWHSALTDNER 285
Cdd:cd17925 9 LVETIDAK---EDLLVWAVTGAGKTEMLFPAIAQALRQGGRVAIASPRIDVCLELAPRLKAAFPGAAIVLLHGGSEDQYQ 85
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
220-370 |
6.48e-06 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 49.74 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 220 LLEGVTGSGKTEVYLQCLEEVLKRGEQALVLVPEIGLTPQTVNRFRRRFPDTPI---ML--WHSAltdNERLQTWRFCEK 294
Cdd:PRK10689 625 LVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDRFANWPVrieMLsrFRSA---KEQTQILAEAAE 701
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527404910 295 GSCAIVIGTRSSIF--LPFLKLGMIVVDEEHdssfkqqdtlRYHARDLAAYRAFQHKIPLILGSATPALETLHKAINN 370
Cdd:PRK10689 702 GKIDILIGTHKLLQsdVKWKDLGLLIVDEEH----------RFGVRHKERIKAMRADVDILTLTATPIPRTLNMAMSG 769
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
225-359 |
1.38e-05 |
|
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: 45.37 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 225 TGSGKTEVYLQCLEEVLKRGeqALVLVPEIGLTPQTVNRFRRRFPDTPIMlwhsaltdneRLQTWRFCEKGSCAIVIGTR 304
Cdd:cd17926 27 TGSGKTLTALALIAYLKELR--TLIVVPTDALLDQWKERFEDFLGDSSIG----------LIGGGKKKDFDDANVVVATY 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527404910 305 SSIF-------LPFLKLGMIVVDEEH---DSSFKqqdtlRYHARDLAAYRafqhkipliLG-SATP 359
Cdd:cd17926 95 QSLSnlaeeekDLFDQFGLLIVDEAHhlpAKTFS-----EILKELNAKYR---------LGlTATP 146
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
484-589 |
3.38e-05 |
|
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: 43.35 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 484 IFPNGKGTEQIEEFLSSEfpDTPVTRIDrdSTRRKGSLEKALEEINQGGARILVGTQMLAKGHHFADVSLVLILDVDSGl 563
Cdd:pfam00271 20 IFSQTKKTLEAELLLEKE--GIKVARLH--GDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWN- 94
|
90 100
....*....|....*....|....*.
gi 2527404910 564 yscdfratehLAQLVtQVAGRAGRSG 589
Cdd:pfam00271 95 ----------PASYI-QRIGRAGRAG 109
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
212-323 |
9.42e-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: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 212 QSVGFKSFLLEGV-------TGSGKTEVYLQCLEEVLKRGEQ-ALVLVPEIGLTPQTVNRFRRRFpdTPIMLWHSALTDN 283
Cdd:cd17921 6 QREALRALYLSGDsvlvsapTSSGKTLIAELAILRALATSGGkAVYIAPTRALVNQKEADLRERF--GPLGKNVGLLTGD 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2527404910 284 ErlqTWRFCEKGSCAIVIGT--------RSSIFLPFLKLGMIVVDEEH 323
Cdd:cd17921 84 P---SVNKLLLAEADILVATpekldlllRNGGERLIQDVRLVVVDEAH 128
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
515-598 |
1.61e-04 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The 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: 350172 [Multi-domain] Cd Length: 77 Bit Score: 40.77 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 515 TRRKGSLEKALEEINqggarILVGTQMLAKGHHFADVSLVLILDVDSglyscdFRATEHlaqlvtQVAGRAGR-SGEPGQ 593
Cdd:cd18785 10 TNSIEHAEEIASSLE-----ILVATNVLGEGIDVPSLDTVIFFDPPS------SAASYI------QRVGRAGRgGKDEGE 72
|
....*
gi 2527404910 594 VLLQT 598
Cdd:cd18785 73 VILFV 77
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
225-358 |
1.73e-03 |
|
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: 40.21 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 225 TGSGKTEVYlQcLEEVLKRGeQALVLVPEIGLTPQTVNRFRRRfpDTPIMLWHSALTDNERLQTWRFCEKGSCAIVIGT- 303
Cdd:cd17920 36 TGGGKSLCY-Q-LPALLLDG-VTLVVSPLISLMQDQVDRLQQL--GIRAAALNSTLSPEEKREVLLRIKNGQYKLLYVTp 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527404910 304 ---RSSIFLPFL-------KLGMIVVDEEHDSSFKQQDtLRYHARDLAAYRAFQHKIPLILGSAT 358
Cdd:cd17920 111 erlLSPDFLELLqrlperkRLALIVVDEAHCVSQWGHD-FRPDYLRLGRLRRALPGVPILALTAT 174
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
225-359 |
3.51e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is 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: 350685 [Multi-domain] Cd Length: 201 Bit Score: 39.34 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 225 TGSGKTEVYLQCLEEVLK-----RGEQALVLVPEIGLTPQTVNRFRRRFPDTPIMLwhSALTDNERLQTWRFCEKGSCAI 299
Cdd:cd17927 26 TGSGKTFVAVLICEHHLKkfpagRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKV--TGLSGDTSENVSVEQIVESSDV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527404910 300 VIGTrSSIFLPFLKLG---------MIVVDEEHDSsfkQQDtlryHARDLAAYRAFQHKI------PLILG-SATP 359
Cdd:cd17927 104 IIVT-PQILVNDLKSGtivslsdfsLLVFDECHNT---TKN----HPYNEIMFRYLDQKLgssgplPQILGlTASP 171
|
|
| PRK14559 |
PRK14559 |
serine/threonine phosphatase; |
434-506 |
4.15e-03 |
|
serine/threonine phosphatase;
Pssm-ID: 237756 [Multi-domain] Cd Length: 645 Bit Score: 40.42 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 434 LICHECGWLSE-----CNRCSTSATfhkaigQMICHHCGEQHPVPH-QCPDCGS----------TQIFPNGKGTEQIEEF 497
Cdd:PRK14559 2 LICPQCQFENPnnnrfCQKCGTSLT------HKPCPQCGTEVPVDEaHCPNCGAetgtiwwaiiAQASPNSEVLESGEAT 75
|
....*....
gi 2527404910 498 LSSEFPDTP 506
Cdd:PRK14559 76 QQSESSLTP 84
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
219-359 |
4.59e-03 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is 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: 350769 [Multi-domain] Cd Length: 207 Bit Score: 39.19 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527404910 219 FLLEGVTGSGKTEVYLQCLEEVLKRGE--QALVLVPEiGLTPQTVNRFRRRFP-DTPIMLWHSALTdNERLQTWRFCEKG 295
Cdd:cd18011 20 LLLADEVGLGKTIEAGLIIKELLLRGDakRVLILCPA-SLVEQWQDELQDKFGlPFLILDRETAAQ-LRRLIGNPFEEFP 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527404910 296 scaIVI--------GTRSSIFLPFLKLGMIVVDEEHD--SSFKQQDTLRYH-ARDLAayRAFQHkipLILGSATP 359
Cdd:cd18011 98 ---IVIvsldllkrSEERRGLLLSEEWDLVVVDEAHKlrNSGGGKETKRYKlGRLLA--KRARH---VLLLTATP 164
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