|
Name |
Accession |
Description |
Interval |
E-value |
| Mfd |
COG1197 |
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ... |
9-955 |
0e+00 |
|
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];
Pssm-ID: 440810 [Multi-domain] Cd Length: 1130 Bit Score: 962.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 9 FLNSLKKVNKQKILVL-PDGY----LYD----IDEEGEVFIYPDFDIFPFENLDISPNIKANRMKTLYALLTKKNATVLT 79
Cdd:COG1197 18 LLAALARALGRPLLVVtADEReaerLAEdlrfFLPDLPVLLFPAWETLPYDRFSPSPDIVSERLATLRRLASGKPGIVVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 80 TFSSLIKYTLPKKEFA--IKKIKVGDTFDLEyNVPYHL---GYNLTEEVTSPGEYSKRGFVRDFFVPIYEQPVRIELWDE 154
Cdd:COG1197 98 PVRALLQRLPPPELLAaaSLSLKVGDELDLE-ELRERLvaaGYERVDQVEEPGEFAVRGGILDIFPPGSEHPVRIEFFGD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 155 VIDRISFFDIYSQRSIENLKEIEIIPGSEIMKFDHNLEIYEERLKKYTIGTNEEEPL--TLDQFNTLPGI------FYKD 226
Cdd:COG1197 177 EIESIRTFDPETQRSLEKVDEVELLPAREFPLDEEAIERFRERLRELFGLDPKLDELyeALSEGIAFAGIeyylplFYEE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 227 KNTILSYLNEDRDIYLINKEEIINSYREKVKENYEMCDN----------------------------------------- 265
Cdd:COG1197 257 LATLFDYLPEDALVVLDEPERIEEAAEEFWEEIEERYEArrhdrgrpllppeelfldpeelfaalkrrprvtlspfaalp 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 266 -------------------------ELKR-------------------KIYKMFSGHNLEILNKIKYEEVK--------- 292
Cdd:COG1197 337 egagvvnlgarplpsfagqlealleELKRllkdggrvllaaesegrreRLLELLRDHGIPARLVESLAELSpggvaitvg 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 293 -------LTLEKIYFI-------------KPKKEDKRLEYIplLDWEDLNEGDLVVHEDYGIGIYHGVNKIETPLGLREF 352
Cdd:COG1197 417 plehgfeLPDAKLAVIteselfgervkrrRRKKKRSADAFI--RDLSELKPGDYVVHVDHGIGRYLGLETLEVGGAERDY 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 353 VTLEYSDNSKVYVPVGRLDKLSKYIG-DPETVKISSLNSKSWKNTKQKVKEEIKlKI-RELQKIYALRENQRGIQLFGDP 430
Cdd:COG1197 495 LVLEYAGGDKLYVPVDQLDLISRYVGsEGEAPKLDKLGGSDWQKAKAKAKKAVR-DIaAELLKLYAERAARKGFAFSPDT 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 431 ELEEKFKETFPYVETPDQEKSINEVMRDLESERPMDRLLSGDSGFGKTEVAMRASFRTVVSNYQVLLLAPTTILAKQHYE 510
Cdd:COG1197 574 PWQREFEAAFPYEETPDQLRAIEEVKADMESPRPMDRLVCGDVGFGKTEVALRAAFKAVMDGKQVAVLVPTTLLAQQHYE 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 511 NFKQRMDPFGIKIALVTRHKTQKEKKDLFESIKKGQTDIVIGTHALLSDLLQVKKLGLVIVDEEQRFGVLQKEKFKKLSE 590
Cdd:COG1197 654 TFKERFAGFPVRVEVLSRFRTAKEQKETLEGLADGKVDIVIGTHRLLSKDVKFKDLGLLIIDEEQRFGVRHKEKLKALRA 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 591 GVNFLMMSATPIPRTLYMSISGLRDISTISTPPVGRLPIQTFVGKYSDKLIRTAILREKSRGGQTIYIHNRVQELNELYK 670
Cdd:COG1197 734 NVDVLTLTATPIPRTLQMSLSGIRDLSIIATPPEDRLPVKTFVGEYDDALIREAILRELLRGGQVFYVHNRVEDIEKVAA 813
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 671 KLQSLVPEVKITMVHGGTSKKEFINSINNLYDGNIDLLLSTTIIENGIDIPNVNTLILDDPERYGISQLYQIKGRVGRSN 750
Cdd:COG1197 814 RLQELVPEARIAVAHGQMSERELERVMLDFYEGEFDVLVCTTIIETGIDIPNANTIIIERADRFGLAQLYQLRGRVGRSH 893
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 751 RRAFVYFLFK--KEVTPQTKKRLEAIKKYNEPGSGLKLALRDLEIRGYGDILGIEQKGHINAIGYHLYHEMLNKILFEyg 828
Cdd:COG1197 894 RRAYAYLLYPpdKVLTEDAEKRLEAIQEFTELGAGFKLAMHDLEIRGAGNLLGEEQSGHIAEVGFDLYLQMLEEAVAA-- 971
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 829 IKKEEEIQKPQTyTEIKgIKGSLVIPESYIPNSIERMRIYRSISVAKTVDDVEDIKSEIRDKYGKLPQEVERLFQYALIK 908
Cdd:COG1197 972 LKGGKEPEEEWE-PEIN-LGVPALIPEDYIPDVRQRLELYKRIASAESEEELDELQEELIDRFGPLPEEVENLLAVARLK 1049
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|.
gi 1341788692 909 VKANMEGIKEIEIGDTYISFKFEND--VNP--VIEKYDKYSRKITFYPETK 955
Cdd:COG1197 1050 LLARRLGIEKIDAGGKGIRIEFSPNtpLDPekLIRLIQKQPGRYKLDGDDK 1100
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
115-920 |
0e+00 |
|
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: 759.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 115 LGYNLTEEVTSPGEYSKRGFVRDFFVPIYEQPVRIELWDEVIDRISFFDIYSQRSIENLKEIEIIPGSEIM----KFDHN 190
Cdd:TIGR00580 4 LGYERVDLVEEEGEFSVRGEILDIFPPGSELPVRIEFFGDEIESIREFDVDSQRSLEELLEITILPAKEFIlleeETIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 191 LEIYE------------ERLKKYTIGTNEEEPLTL---------DQFNTLPGIFYKDKNTILSYLNEDRDIY------LI 243
Cdd:TIGR00580 84 LKDNAarvedakhletiEALSEGTLPAGEEMFLPLffedlsslfDYLPDNTPILLDDPERFHSAARFLQRELeefynaLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 244 NKEEIINSYRE----------------------------KVKENYEMCDN--------------ELKRKI----YKMFSG 277
Cdd:TIGR00580 164 EAKKLINPPRLdldpselafeasaislsrvqlenehlslKASEAIEGAQKhsrlefgeilafkeELFRWLkagfKITVAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 278 HNLEILNKIKY-------------------------------EEVKLTLEKIYFI----------KPKKEDKRLEYIPLL 316
Cdd:TIGR00580 244 ESESQAERLKSllaehdiaaqvidesciiipavryvmigalsSGFILPTAGLAVIteselfgsrvLRRPKKSRLKSKPIE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 317 DWEDLNEGDLVVHEDYGIGIYHGVNKIETPLGLREFVTLEYSDNSKVYVPVGRLDKLSKYIG-DPETVKISSLNSKSWKN 395
Cdd:TIGR00580 324 SLNELNPGDYVVHLDHGIGRFLGLETLEVGGIERDYLVLEYAGEDKLYVPVEQLHLISRYVGgSGKNPALDKLGGKSWEK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 396 TKQKVKEEIKLKIRELQKIYALRENQRGIQLFGDPELEEKFKETFPYVETPDQEKSINEVMRDLESERPMDRLLSGDSGF 475
Cdd:TIGR00580 404 TKAKVKKSVREIAAKLIELYAKRKAIKGHAFPPDLEWQQEFEDSFPFEETPDQLKAIEEIKADMESPRPMDRLVCGDVGF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 476 GKTEVAMRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRMDPFGIKIALVTRHKTQKEKKDLFESIKKGQTDIVIGTHA 555
Cdd:TIGR00580 484 GKTEVAMRAAFKAVLDGKQVAVLVPTTLLAQQHFETFKERFANFPVTIELLSRFRSAKEQNEILKELASGKIDILIGTHK 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 556 LLSDLLQVKKLGLVIVDEEQRFGVLQKEKFKKLSEGVNFLMMSATPIPRTLYMSISGLRDISTISTPPVGRLPIQTFVGK 635
Cdd:TIGR00580 564 LLQKDVKFKDLGLLIIDEEQRFGVKQKEKLKELRTSVDVLTLSATPIPRTLHMSMSGIRDLSIIATPPEDRLPVRTFVME 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 636 YSDKLIRTAILREKSRGGQTIYIHNRVQELNELYKKLQSLVPEVKITMVHGGTSKKEFINSINNLYDGNIDLLLSTTIIE 715
Cdd:TIGR00580 644 YDPELVREAIRRELLRGGQVFYVHNRIESIEKLATQLRELVPEARIAIAHGQMTENELEEVMLEFYKGEFQVLVCTTIIE 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 716 NGIDIPNVNTLILDDPERYGISQLYQIKGRVGRSNRRAFVYFLF--KKEVTPQTKKRLEAIKKYNEPGSGLKLALRDLEI 793
Cdd:TIGR00580 724 TGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKKKAYAYLLYphQKALTEDAQKRLEAIQEFSELGAGFKIALHDLEI 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 794 RGYGDILGIEQKGHINAIGYHLYHEMLNKILFEYgikKEEEIQKPQTYTEIKgIKGSLVIPESYIPNSIERMRIYRSISV 873
Cdd:TIGR00580 804 RGAGNLLGEEQSGHIESIGFDLYMELLEEAIEEL---KGGKPPKLEEETDIE-LPYSAFIPDDYIADDSLRLEFYKRIAS 879
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1341788692 874 AKTVDDVEDIKSEIRDKYGKLPQEVERLFQYALIKVKANMEGIKEIE 920
Cdd:TIGR00580 880 AETEEELEKIRDELIDRFGPLPEEARTLLDVARLKLLARKLGIRKLK 926
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
38-937 |
5.75e-172 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 532.40 E-value: 5.75e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 38 VFIYPDFDIFPFENLDISPNIKANRMKTLYALLTKKNATVLTTFSSLIKYTLP-----------KKEFAIKKIKVGDTFD 106
Cdd:PRK10689 67 VMNLADWETLPYDSFSPHQDIISSRLSTLYQLPTMQRGVLILPVNTLMQRVCPhsflhghalvmKKGQRLSRDALRAQLE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 107 leynvpyHLGYNLTEEVTSPGEYSKRGFVRDFFVPIYEQPVRIELWDEVIDRISFFDIYSQRSIENLKEIEIIPGSEIMK 186
Cdd:PRK10689 147 -------QAGYRHVDQVMEHGEYATRGALLDLFPMGSEEPYRIDFFDDEIDSLRVFDVDSQRTLEEVEAINLLPAHEFPT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 187 FDHNLEIYEERLK-KYTIGTNEEEPLTLDQFNTLP-GI-------FYKDKNTILSYLNEDrdIYLINKEEIINS---YRE 254
Cdd:PRK10689 220 DKAAIELFRSQWRdTFEVKRDAEHIYQQVSKGTLPaGIeywqplfFSEPLPPLFSYFPAN--TLLVNTGDLETSaerFWA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 255 KVKENYE------------------MCDN---ELK------------------------------------------RKI 271
Cdd:PRK10689 298 DTLARFEnrgvdpmrpllppeslwlRVDElfsELKnwprvqlktehlptkaantnlgyqklpdlavqaqqkapldalRRF 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 272 YKMFSGHNL-------------EILNKIKYEEVKL------------------------TLEKIYFI----------KPK 304
Cdd:PRK10689 378 LESFDGPVVfsvesegrrealgELLARIKIAPKRImrldeasdrgrylmigaaehgfidTVRNLALIcesdllgervARR 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 305 KEDKRLEYIP---LLDWEDLNEGDLVVHEDYGIGIYHGVNKIETPLGLREFVTLEYSDNSKVYVPVGRLDKLSKYIGDP- 380
Cdd:PRK10689 458 RQDSRRTINPdtlIRNLAELHPGQPVVHLEHGVGRYAGMTTLEAGGIKGEYLMLTYANDAKLYVPVSSLHLISRYAGGAe 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 381 ETVKISSLNSKSWKNTKQKVKEEIKLKIRELQKIYALRENQRGIQLFGDPELEEKFKETFPYVETPDQEKSINEVMRDLE 460
Cdd:PRK10689 538 ENAPLHKLGGDAWSRARQKAAEKVRDVAAELLDIYAQRAAKEGFAFKHDREQYQLFCDSFPFETTPDQAQAINAVLSDMC 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 461 SERPMDRLLSGDSGFGKTEVAMRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRMDPFGIKIALVTRHKTQKEKKDLFE 540
Cdd:PRK10689 618 QPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDRFANWPVRIEMLSRFRSAKEQTQILA 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 541 SIKKGQTDIVIGTHALLSDLLQVKKLGLVIVDEEQRFGVLQKEKFKKLSEGVNFLMMSATPIPRTLYMSISGLRDISTIS 620
Cdd:PRK10689 698 EAAEGKIDILIGTHKLLQSDVKWKDLGLLIVDEEHRFGVRHKERIKAMRADVDILTLTATPIPRTLNMAMSGMRDLSIIA 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 621 TPPVGRLPIQTFVGKYSDKLIRTAILREKSRGGQTIYIHNRVQELNELYKKLQSLVPEVKITMVHGGTSKKEFINSINNL 700
Cdd:PRK10689 778 TPPARRLAVKTFVREYDSLVVREAILREILRGGQVYYLYNDVENIQKAAERLAELVPEARIAIGHGQMRERELERVMNDF 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 701 YDGNIDLLLSTTIIENGIDIPNVNTLILDDPERYGISQLYQIKGRVGRSNRRAFVYFL--FKKEVTPQTKKRLEAIKKYN 778
Cdd:PRK10689 858 HHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRGRVGRSHHQAYAWLLtpHPKAMTTDAQKRLEAIASLE 937
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 779 EPGSGLKLALRDLEIRGYGDILGIEQKGHINAIGYHLYHEMLNKILFEYGIKKE---EEIQKPQTYTEikgIKGSLVIPE 855
Cdd:PRK10689 938 DLGAGFALATHDLEIRGAGELLGEEQSGQMETIGFSLYMELLENAVDALKAGREpslEDLTSQQTEVE---LRMPSLLPD 1014
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 856 SYIPNSIERMRIYRSISVAKTVDDVEDIKSEIRDKYGKLPQEVERLFQYALIKVKANMEGIKEIEIGDT--YISFKFEND 933
Cdd:PRK10689 1015 DFIPDVNTRLSFYKRIASAKNENELEEIKVELIDRFGLLPDPARNLLDIARLRQQAQKLGIRKLEGNEKggFIEFAEKNH 1094
|
....
gi 1341788692 934 VNPV 937
Cdd:PRK10689 1095 VDPA 1098
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
411-806 |
2.75e-118 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 377.47 E-value: 2.75e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 411 LQKIYALRENQRGIQLFGDPELEEKFKETFPYVETPDQEKSINEVMRDLESERPMDRLLSGDSGFGKTEVAMRASFRTVV 490
Cdd:COG1200 227 LLLRRARRRKRKGPALPGDGELLEAFLAALPFELTGAQKRVIAEIAADLASPHPMNRLLQGDVGSGKTVVALLAMLAAVE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 491 SNYQVLLLAPTTILAKQHYENFKQRMDPFGIKIALVT-RHKTqKEKKDLFESIKKGQTDIVIGTHALLSDLLQVKKLGLV 569
Cdd:COG1200 307 AGYQAALMAPTEILAEQHYRSLSKLLEPLGIRVALLTgSTKA-KERREILAALASGEADIVVGTHALIQDDVEFKNLGLV 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 570 IVDEEQRFGVLQKEKFKKLSEGVNFLMMSATPIPRTLYMSISG-LrDISTISTPPVGRLPIQTFV--GKYSDKLIRtAIL 646
Cdd:COG1200 386 VIDEQHRFGVEQRLALREKGEAPHVLVMTATPIPRTLAMTLYGdL-DVSVIDELPPGRKPIKTRVvpEERRDEVYE-RIR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 647 REKSRGGQtIYI---------HNRVQELNELYKKLQSLVPEVKITMVHGGTSKKE-------FinsinnlYDGNIDLLLS 710
Cdd:COG1200 464 EEIAKGRQ-AYVvcplieeseKLDLQAAEETYEELREAFPGLRVGLLHGRMKPAEkdavmaaF-------KAGEIDVLVA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 711 TTIIENGIDIPNVNTLILDDPERYGISQLYQIKGRVGRSNRRAFVYFLFKKEVTPQTKKRLEAIKKYNepgSGLKLALRD 790
Cdd:COG1200 536 TTVIEVGVDVPNATVMVIENAERFGLSQLHQLRGRVGRGSAQSYCLLLYDAPLSETARERLEVMRETN---DGFEIAEED 612
|
410
....*....|....*.
gi 1341788692 791 LEIRGYGDILGIEQKG 806
Cdd:COG1200 613 LELRGPGEFLGTRQSG 628
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
411-806 |
2.95e-118 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 377.18 E-value: 2.95e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 411 LQKIYALRENQRGIQLFGDPELEEKFKETFPYVETPDQEKSINEVMRDLESERPMDRLLSGDSGFGKTEVAMRASFRTVV 490
Cdd:PRK10917 229 LLLLRAGRRSKKAGPLPYDGELLKKFLASLPFELTGAQKRVVAEILADLASPKPMNRLLQGDVGSGKTVVAALAALAAIE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 491 SNYQVLLLAPTTILAKQHYENFKQRMDPFGIKIALVTRHKTQKEKKDLFESIKKGQTDIVIGTHALLSDLLQVKKLGLVI 570
Cdd:PRK10917 309 AGYQAALMAPTEILAEQHYENLKKLLEPLGIRVALLTGSLKGKERREILEAIASGEADIVIGTHALIQDDVEFHNLGLVI 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 571 VDEEQRFGVLQKEKFKKLSEGVNFLMMSATPIPRTLYMSISGLRDISTISTPPVGRLPIQTFVGKYSDK-----LIRTAI 645
Cdd:PRK10917 389 IDEQHRFGVEQRLALREKGENPHVLVMTATPIPRTLAMTAYGDLDVSVIDELPPGRKPITTVVIPDSRRdevyeRIREEI 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 646 lrekSRGGQTIYIHNRVQE--------LNELYKKLQSLVPEVKITMVHG--GTSKKEFInsINNLYDGNIDLLLSTTIIE 715
Cdd:PRK10917 469 ----AKGRQAYVVCPLIEEsekldlqsAEETYEELQEAFPELRVGLLHGrmKPAEKDAV--MAAFKAGEIDILVATTVIE 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 716 NGIDIPNVNTLILDDPERYGISQLYQIKGRVGRSNRRAFVYFLFKKEVTPQTKKRLEAIKKYNepgSGLKLALRDLEIRG 795
Cdd:PRK10917 543 VGVDVPNATVMVIENAERFGLAQLHQLRGRVGRGAAQSYCVLLYKDPLSETARERLKIMRETN---DGFVIAEKDLELRG 619
|
410
....*....|.
gi 1341788692 796 YGDILGIEQKG 806
Cdd:PRK10917 620 PGELLGTRQSG 630
|
|
| recG |
TIGR00643 |
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair] |
411-806 |
7.61e-112 |
|
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273192 [Multi-domain] Cd Length: 630 Bit Score: 358.58 E-value: 7.61e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 411 LQKIYALRENQRGIQLFGDPELEEKFKETFPYVETPDQEKSINEVMRDLESERPMDRLLSGDSGFGKTEVAMRASFRTVV 490
Cdd:TIGR00643 203 LARRLGEKQQFSAPPANPSEELLTKFLASLPFKLTRAQKRVVKEILQDLKSDVPMNRLLQGDVGSGKTLVAALAMLAAIE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 491 SNYQVLLLAPTTILAKQHYENFKQRMDPFGIKIALVTRHKTQKEKKDLFESIKKGQTDIVIGTHALLSDLLQVKKLGLVI 570
Cdd:TIGR00643 283 AGYQVALMAPTEILAEQHYNSLRNLLAPLGIEVALLTGSLKGKRRKELLETIASGQIHLVVGTHALIQEKVEFKRLALVI 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 571 VDEEQRFGVLQKEKF-KKLSEGVN--FLMMSATPIPRTLYMSISGLRDISTISTPPVGRLPIQTFVGKYSDK-LIRTAIL 646
Cdd:TIGR00643 363 IDEQHRFGVEQRKKLrEKGQGGFTphVLVMSATPIPRTLALTVYGDLDTSIIDELPPGRKPITTVLIKHDEKdIVYEFIE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 647 REKSRGGQTIYIHNRVQE--------LNELYKKLQSLVPEVKITMVHGGTSKKEFINSINNLYDGNIDLLLSTTIIENGI 718
Cdd:TIGR00643 443 EEIAKGRQAYVVYPLIEEsekldlkaAEALYERLKKAFPKYNVGLLHGRMKSDEKEAVMEEFREGEVDILVATTVIEVGV 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 719 DIPNVNTLILDDPERYGISQLYQIKGRVGRSNRRAFVYFLFKKEVTPQTKKRLEAIKKYNEpgsGLKLALRDLEIRGYGD 798
Cdd:TIGR00643 523 DVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKNPKSESAKKRLRVMADTLD---GFVIAEEDLELRGPGD 599
|
....*...
gi 1341788692 799 ILGIEQKG 806
Cdd:TIGR00643 600 LLGTKQSG 607
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
429-621 |
1.30e-107 |
|
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: 331.46 E-value: 1.30e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 429 DPELEEKFKETFPYVETPDQEKSINEVMRDLESERPMDRLLSGDSGFGKTEVAMRASFRTVVSNYQVLLLAPTTILAKQH 508
Cdd:cd17991 1 DGEEQEEFEASFPYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 509 YENFKQRMDPFGIKIALVTRHKTQKEKKDLFESIKKGQTDIVIGTHALLSDLLQVKKLGLVIVDEEQRFGVLQKEKFKKL 588
Cdd:cd17991 81 YETFKERFANFPVNVELLSRFTTAAEQREILEGLKEGKVDIVIGTHRLLSKDVEFKNLGLLIIDEEQRFGVKQKEKLKEL 160
|
170 180 190
....*....|....*....|....*....|...
gi 1341788692 589 SEGVNFLMMSATPIPRTLYMSISGLRDISTIST 621
Cdd:cd17991 161 RPNVDVLTLSATPIPRTLHMALSGIRDLSVIAT 193
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
411-623 |
6.34e-75 |
|
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: 245.52 E-value: 6.34e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 411 LQKIYALRENQRGIQLFGDPELEEKFKETFPYVETPDQEKSINEVMRDLESERPMDRLLSGDSGFGKTEVAMRASFRTVV 490
Cdd:cd17992 13 LLLRRRKIEELKGIILEISGELLKKFLEALPFELTGAQKRVIDEILRDLASEKPMNRLLQGDVGSGKTVVAALAMLAAVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 491 SNYQVLLLAPTTILAKQHYENFKQRMDPFGIKIALVTRHKTQKEKKDLFESIKKGQTDIVIGTHALLSDLLQVKKLGLVI 570
Cdd:cd17992 93 NGYQVALMAPTEILAEQHYDSLKKLLEPLGIRVALLTGSTKAKEKREILEKIASGEIDIVIGTHALIQEDVEFHNLGLVI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1341788692 571 VDEEQRFGVLQKEKFKKLSEGVNFLMMSATPIPRTLYMSISGLRDISTISTPP 623
Cdd:cd17992 173 IDEQHRFGVEQRLKLREKGETPHVLVMTATPIPRTLALTLYGDLDVSIIDELP 225
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
429-619 |
1.82e-59 |
|
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: 201.11 E-value: 1.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 429 DPELEEKFKETFPYVETPDQEKSINEVMRDLESERPMDRLLSGDSGFGKTEVAMRASFRTVVSNYQVLLLAPTTILAKQH 508
Cdd:cd17918 1 DRALIQELCKSLPFSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 509 YENFKQRMDPfgIKIALVTRHKTQKEKKdlfesikkgQTDIVIGTHALLSDLLQVKKLGLVIVDEEQRFGVLQKEKFKKL 588
Cdd:cd17918 81 YEEARKFLPF--INVELVTGGTKAQILS---------GISLLVGTHALLHLDVKFKNLDLVIVDEQHRFGVAQREALYNL 149
|
170 180 190
....*....|....*....|....*....|.
gi 1341788692 589 SEgVNFLMMSATPIPRTLYMSISGLRDISTI 619
Cdd:cd17918 150 GA-THFLEATATPIPRTLALALSGLLDLSVI 179
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
628-776 |
3.18e-52 |
|
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: 179.46 E-value: 3.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 628 PIQTFVGKYSDKLIRTAILREKSRGGQTIYIHNRVQELNELYKKLQSLVPEVKITMVHGGTSKKEFINSINNLYDGNIDL 707
Cdd:cd18810 1 PVRTYVMPYDDELIREAIERELLRGGQVFYVHNRIESIEKLATQLRQLVPEARIAIAHGQMTENELEEVMLEFAKGEYDI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1341788692 708 LLSTTIIENGIDIPNVNTLILDDPERYGISQLYQIKGRVGRSNRRAFVYFLF--KKEVTPQTKKRLEAIKK 776
Cdd:cd18810 81 LVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKERAYAYFLYpdQKKLTEDALKRLEAIQE 151
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
628-776 |
7.53e-46 |
|
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: 161.67 E-value: 7.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 628 PIQTFVGKYSDK-LIRTAILREKSRGGQTIYIHNRVQE--------LNELYKKLQSLVPEVKITMVHGGTSKKEFINSIN 698
Cdd:cd18792 1 PIRTYVIPHDDLdLVYEAIERELARGGQVYYVYPRIEEsekldlksIEALAEELKELVPEARVALLHGKMTEDEKEAVML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 699 NLYDGNIDLLLSTTIIENGIDIPNVNTLILDDPERYGISQLYQIKGRVGRSNRRAFVYFLF--KKEVTPQTKKRLEAIKK 776
Cdd:cd18792 81 EFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYpdPKKLTETAKKRLRAIAE 160
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
445-608 |
9.74e-30 |
|
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: 115.80 E-value: 9.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 445 TPDQEKSINEVM--RDLeserpmdrLLSGDSGFGKTEVAMRASFRTVVSN---YQVLLLAPTTILAKQHYENFKQRMDPF 519
Cdd:pfam00270 1 TPIQAEAIPAILegRDV--------LVQAPTGSGKTLAFLLPALEALDKLdngPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 520 GIKIALVTrhkTQKEKKDLFESIKKgqTDIVIGTHALLSDLLQ----VKKLGLVIVDEEQR-----FGVLQKEKFKKLSE 590
Cdd:pfam00270 73 GLKVASLL---GGDSRKEQLEKLKG--PDILVGTPGRLLDLLQerklLKNLKLLVLDEAHRlldmgFGPDLEEILRRLPK 147
|
170
....*....|....*...
gi 1341788692 591 GVNFLMMSATPiPRTLYM 608
Cdd:pfam00270 148 KRQILLLSATL-PRNLED 164
|
|
| CarD_TRCF |
smart01058 |
CarD-like/TRCF domain; CarD is a Myxococcus xanthus protein required for the activation of ... |
320-416 |
1.19e-28 |
|
CarD-like/TRCF domain; CarD is a Myxococcus xanthus protein required for the activation of light- and starvation-inducible genes. This family includes the presumed N-terminal domain. CarD interacts with the zinc-binding protein CarG, to form a complex that regulates multiple processes in Myxococcus xanthus. This family also includes a domain to the N-terminal side of the DEAD helicase of TRCF proteins. TRCF displaces RNA polymerase stalled at a lesion, binds to the damage recognition protein UvrA, and increases the template strand repair rate during transcription. This domain is involved in binding to the stalled RNA polymerase.
Pssm-ID: 215001 [Multi-domain] Cd Length: 99 Bit Score: 110.24 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 320 DLNEGDLVVHEDYGIGIYHGVNKIETPLGLREFVTLEYSDNSKVYVPVGRLDKLSKYIGDPETV--KISSLNSKSWKNTK 397
Cdd:smart01058 1 ELKIGDYVVHPDHGVGRYEGIETIEVGGEKREYLVLEYAGGDKLYVPVDNLDLGSRYVGSEGEVepVLDKLGGGSWSKRK 80
|
90
....*....|....*....
gi 1341788692 398 QKVKEEIKLKIRELQKIYA 416
Cdd:smart01058 81 RKAKSGIRDIAAELLRLYA 99
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
628-776 |
1.26e-26 |
|
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: 106.66 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 628 PIQTFVGKYSDK-LIRTAILREKSRGGQTIYIHNRVQE--------LNELYKKLQSLV-PEVKITMVHGGTSKKEFINSI 697
Cdd:cd18811 1 PITTYLIFHTRLdKVYEFVREEIAKGRQAYVIYPLIEEsekldlkaAVAMYEYLKERFrPELNVGLLHGRLKSDEKDAVM 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1341788692 698 NNLYDGNIDLLLSTTIIENGIDIPNVNTLILDDPERYGISQLYQIKGRVGRSNRRAFVYFLFKKEVTPQTKKRLEAIKK 776
Cdd:cd18811 81 AEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKDPLTETAKQRLRVMTE 159
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
436-623 |
1.57e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 105.27 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 436 FKETFPYVETPDQEKSINEVMrdlesERPMDRLLSGDSGFGKTEVAMRASFRTV--VSNYQVLLLAPTTILAKQHYENFK 513
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALL-----SGLRDVILAAPTGSGKTLAALLPALEALkrGKGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 514 QRMDPFGIKIALVTrhkTQKEKKDLFESIKKGQTDIVIGT-----HALLSDLLQVKKLGLVIVDEEQRFGVLQ-----KE 583
Cdd:smart00487 76 KLGPSLGLKVVGLY---GGDSKREQLRKLESGKTDILVTTpgrllDLLENDKLSLSNVDLVILDEAHRLLDGGfgdqlEK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1341788692 584 KFKKLSEGVNFLMMSATP---IPRTLYMSISGLRDISTISTPP 623
Cdd:smart00487 153 LLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPL 195
|
|
| CarD_CdnL_TRCF |
pfam02559 |
CarD-like/TRCF domain; CarD is a Myxococcus xanthus protein required for the activation of ... |
321-415 |
6.43e-23 |
|
CarD-like/TRCF domain; CarD is a Myxococcus xanthus protein required for the activation of light- and starvation-inducible genes. This family includes the presumed N-terminal domain, CdnL. CarD interacts with the zinc-binding protein CarG to form a complex that regulates multiple processes in Myxococcus xanthus. This family also includes a domain to the N-terminal side of the DEAD helicase of TRCF (transcription-repair-coupling factor) proteins. TRCF displaces RNA polymerase stalled at a lesion, binds to the damage recognition protein UvrA, and increases the template strand repair rate during transcription. This domain is involved in binding to the stalled RNA polymerase. The family includes members otherwise referred to as CdnL, for CarD N-terminal like, which differ functionally from CarD. The TRCF domain mentioned above is the RNA polymerase-interacting domain or RID.
Pssm-ID: 460590 [Multi-domain] Cd Length: 89 Bit Score: 93.66 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 321 LNEGDLVVHEDYGIGIYHGVNKIETplglREFVTLEYSDNSKVYVPVGRLDKLSKYIGDPETVKIssLNSKSWKNTKQKV 400
Cdd:pfam02559 1 LKVGDYVVHPDHGIGRIEGIEKLET----KDYYVLEYAGGDKLYVPVDNLDLIRKYISKGELDKL--GDGRRWRKYKEKL 74
|
90
....*....|....*
gi 1341788692 401 KEEIKLKIRELQKIY 415
Cdd:pfam02559 75 KSGDIEEAAELIKLY 89
|
|
| TRCF |
pfam03461 |
TRCF domain; |
853-940 |
6.92e-23 |
|
TRCF domain;
Pssm-ID: 460928 [Multi-domain] Cd Length: 95 Bit Score: 93.64 E-value: 6.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 853 IPESYIPNSIERMRIYRSISVAKTVDDVEDIKSEIRDKYGKLPQEVERLFQYALIKVKANMEGIKEIEIGDTYISFKFEN 932
Cdd:pfam03461 7 IPDDYIPDESQRLELYKRLASIETEEELDDLQEELIDRFGPLPEEVENLLEIARLKLLAKKLGIEKIDLKGGGIRITFSE 86
|
....*...
gi 1341788692 933 DVNPVIEK 940
Cdd:pfam03461 87 DAKIDPEK 94
|
|
| TRCF |
smart00982 |
This domain is found in proteins necessary for strand-specific repair in DNA such as TRCF in ... |
853-933 |
8.18e-22 |
|
This domain is found in proteins necessary for strand-specific repair in DNA such as TRCF in Escherichia coli; A lesion in the template strand blocks the RNA polymerase complex (RNAP). The RNAP-DNA-RNA complex is specifically recognised by the transcription-repair-coupling factor (TRCF) which releases RNAP and the truncated transcript.
Pssm-ID: 198050 [Multi-domain] Cd Length: 100 Bit Score: 90.99 E-value: 8.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 853 IPESYIPNSIERMRIYRSISVAKTVDDVEDIKSEIRDKYGKLPQEVERLFQYALIKVKANMEGIKEIEIGDTYISFKFEN 932
Cdd:smart00982 8 IPEDYIPDVRQRLELYKRIASAETEEELDEIQEELIDRFGPLPEEVKNLLEVARLKLLAKKLGIEKIDAGGKGIVIEFSP 87
|
.
gi 1341788692 933 D 933
Cdd:smart00982 88 D 88
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
646-750 |
8.32e-18 |
|
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: 79.95 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 646 LREKSRGGQTIYIHNRVQELNElyKKLQSLvPEVKITMVHGGTSKKEFINSINNLYDGNIDLLLSTTIIENGIDIPNVNT 725
Cdd:pfam00271 9 LLKKERGGKVLIFSQTKKTLEA--ELLLEK-EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDL 85
|
90 100
....*....|....*....|....*
gi 1341788692 726 LILDDPErYGISQLYQIKGRVGRSN 750
Cdd:pfam00271 86 VINYDLP-WNPASYIQRIGRAGRAG 109
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
465-600 |
4.43e-17 |
|
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: 78.98 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 465 MDRLLSGDSGFGKTEVAMRASFRTVVSNY-QVLLLAPTTILAKQHYENFKQRMDPfGIKIALVTRHKTQKEKkdlfESIK 543
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKGkKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEER----EKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 544 KGQTDIVIGTHALLSDLLQ------VKKLGLVIVDEEQRFGVLQKEK-------FKKLSEGVNFLMMSAT 600
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLredrlfLKDLKLIIVDEAHALLIDSRGAlildlavRKAGLKNAQVILLSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
667-748 |
1.90e-16 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 74.94 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 667 ELYKKLQSLvpEVKITMVHGGTSKKEFINSINNLYDGNIDLLLSTTIIENGIDIPNVNTLILDDPeRYGISQLYQIKGRV 746
Cdd:smart00490 2 ELAELLKEL--GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL-PWSPASYIQRIGRA 78
|
..
gi 1341788692 747 GR 748
Cdd:smart00490 79 GR 80
|
|
| UvrB_inter |
pfam17757 |
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the ... |
98-183 |
4.20e-16 |
|
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the UvrA protein.
Pssm-ID: 465486 [Multi-domain] Cd Length: 91 Bit Score: 74.35 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 98 KIKVGDTFDLEyNVPYHL---GYNLTEEVTSPGEYSKRGFVRDFFvPIY--EQPVRIELWDEVIDRISFFDIYSQRSIEN 172
Cdd:pfam17757 2 SLKVGQEIDRD-ELLRKLvelGYERNDIVFERGTFRVRGDIVDIF-PAYseDEAIRIEFFGDEIESIREFDPLTGRSLEK 79
|
90
....*....|.
gi 1341788692 173 LKEIEIIPGSE 183
Cdd:pfam17757 80 LDEVTIYPASH 90
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
448-574 |
8.52e-16 |
|
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: 76.48 E-value: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 448 QEKSINEVMRDLESERPMdrLLSGDSGFGKTEVAMRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRmdpFGIKIALVT 527
Cdd:cd17929 1 QRKAYEAIVSSLGGFKTF--LLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTPQLIKRFKKR---FGDKVAVLH 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1341788692 528 RHKTQKEKKDLFESIKKGQTDIVIGTHALLsdLLQVKKLGLVIVDEE 574
Cdd:cd17929 76 SKLSDKERADEWRKIKRGEAKVVIGARSAL--FAPFKNLGLIIVDEE 120
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
445-779 |
1.73e-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: 80.30 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 445 TPDQEKSINEVMRDLESERPMdrLLSGDSGFGKTEV-------AMR-------ASFRTVVsnyqVLLLAPttilakqhye 510
Cdd:COG4098 112 TPAQQKASDELLEAIKKKEEH--LVWAVCGAGKTEMlfpaiaeALKqggrvciATPRVDV----VLELAP---------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 511 NFKQrmdPF-GIKIALVtrHKTQKEKKdlfesikkGQTDIVIGT-HALLS-----DLlqvkklglVIVDE---------E 574
Cdd:COG4098 176 RLQQ---AFpGVDIAAL--YGGSEEKY--------RYAQLVIATtHQLLRfyqafDL--------LIIDEvdafpysgdP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 575 Q-RFGVlqkEKFKKlsEGVNFLMMSATPiPRTLYMSI-SGLRDISTISTPPVGR-LPIQTFV-----------GKYSDKL 640
Cdd:COG4098 235 MlQYAV---KRARK--PDGKLIYLTATP-SKALQRQVkRGKLKVVKLPARYHGHpLPVPKFKwlgnwkkrlrrGKLPRKL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 641 IRTaILREKSRGGQT-IYIHNrVQELNELYKKLQSLVPEVKITMVHGGTSKKEfiNSINNLYDGNIDLLLSTTIIENGID 719
Cdd:COG4098 309 LKW-LKKRLKEGRQLlIFVPT-IELLEQLVALLQKLFPEERIAGVHAEDPERK--EKVQAFRDGEIPILVTTTILERGVT 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1341788692 720 IPNVNTLILD-DPERYGISQLYQIKGRVGRSNRRAF--VYFlFKKEVTPQTKKRLEAIKKYNE 779
Cdd:COG4098 385 FPNVDVAVLGaDHPVFTEAALVQIAGRVGRSADYPTgeVIF-FHHGKTRAMKRAIREIKRMNR 446
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
397-906 |
1.23e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.14 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 397 KQKVKEEIKLKIRELQKIYALRENQRGIQLF--GDPELEEKFKetfPYvetPDQEKSINEVMRDLESERpmDR-LLSGDS 473
Cdd:COG1061 38 RRLAIKEGTREDGRRLPEEDTERELAEAEALeaGDEASGTSFE---LR---PYQQEALEALLAALERGG--GRgLVVAPT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 474 GFGKTEVAMRAsFRTVVSNYQVLLLAPTTILAKQHYENFKQRMDpfgikialvtrhktqkeKKDLFESIKKGQTDIVIGT 553
Cdd:COG1061 110 GTGKTVLALAL-AAELLRGKRVLVLVPRRELLEQWAEELRRFLG-----------------DPLAGGGKKDSDAPITVAT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 554 HALLSDLLQVKKL----GLVIVDEEQRFGVLQKEKFKKLSEGVNFLMMSATP-------IPRTLYMSIS---GLRDI--S 617
Cdd:COG1061 172 YQSLARRAHLDELgdrfGLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTATPfrsdgreILLFLFDGIVyeySLKEAieD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 618 TISTPPV----------GRLPIQTFVGKYSDKLIRTA---------ILREKSRGGQTIYIHNRVQELNELYKKLQSLvpE 678
Cdd:COG1061 252 GYLAPPEyygirvdltdERAEYDALSERLREALAADAerkdkilreLLREHPDDRKTLVFCSSVDHAEALAELLNEA--G 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 679 VKITMVHGGTSKKEFINSINNLYDGNIDLLLSTTIIENGIDIPNVNTLILDDPERYGIsQLYQIKGRV---GRSNRRAFV 755
Cdd:COG1061 330 IRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPR-EFIQRLGRGlrpAPGKEDALV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 756 YFLFKKEVTPQ----TKKRLEAIKKYNEPGSGLKLALRDLEIRGYGDILGIEQKGHINAIGYHLYHE---MLNKILFEYG 828
Cdd:COG1061 409 YDFVGNDVPVLeelaKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDAlllVLAELLLLEL 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1341788692 829 IKKEEEIQKPQTYTEIKGIKGSLVIPESYIPNSIERMRIYRSISVAKTVDDVEDIKSEIRDKYGKLPQEVERLFQYAL 906
Cdd:COG1061 489 LALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKELLRAALAA 566
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
445-574 |
1.55e-12 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 71.69 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 445 TPDQEKSINEVMRDLESERPMdrLLSGDSGFGKTEVAMRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRmdpFGIKIA 524
Cdd:COG1198 197 NEEQQAAVEAIRAAAGGFSVF--LLHGVTGSGKTEVYLQAIAEVLAQGKQALVLVPEIALTPQTVERFRAR---FGARVA 271
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1341788692 525 LVTRHKTQKEKKDLFESIKKGQTDIVIGTH-ALlsdLLQVKKLGLVIVDEE 574
Cdd:COG1198 272 VLHSGLSDGERLDEWRRARRGEARIVIGTRsAL---FAPFPNLGLIIVDEE 319
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
400-574 |
5.43e-12 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 69.80 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 400 VKEEIKLKIRELQKIYALRENQRGIQLFGDPELeekfketfpyveTPDQEKSInEVMRDLESERPMdrLLSGDSGFGKTE 479
Cdd:PRK05580 113 LKGLVKKGLIELEEVEVLRLRPPPDPAFEPPTL------------NPEQAAAV-EAIRAAAGFSPF--LLDGVTGSGKTE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 480 VAMRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRmdpFGIKIALVTRHKTQKEKKDLFESIKKGQTDIVIGTH-ALLs 558
Cdd:PRK05580 178 VYLQAIAEVLAQGKQALVLVPEIALTPQMLARFRAR---FGAPVAVLHSGLSDGERLDEWRKAKRGEAKVVIGARsALF- 253
|
170
....*....|....*.
gi 1341788692 559 dlLQVKKLGLVIVDEE 574
Cdd:PRK05580 254 --LPFKNLGLIIVDEE 267
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
467-572 |
2.35e-10 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 60.80 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 467 RLLSGDS-------GFGKTEVAMRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRMDPFGIKIALVTRHK--TQKEKKD 537
Cdd:cd17924 28 RLLRGKSfaiiaptGVGKTTFGLATSLYLASKGKRSYLIFPTKSLVKQAYERLSKYAEKAGVEVKILVYHSrlKKKEKEE 107
|
90 100 110
....*....|....*....|....*....|....*...
gi 1341788692 538 LFESIKKGQTDIVIGTHALLS---DLLQVKKLGLVIVD 572
Cdd:cd17924 108 LLEKIEKGDFDILVTTNQFLSknfDLLSNKKFDFVFVD 145
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
468-600 |
5.58e-09 |
|
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: 56.50 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 468 LLSGDSGFGKTEVAMRASFRTVVSNYQ-VLLLAPTTILAKQHYENFKQRMDPFGIKIALVTRhktqkekkDLFESIKK-G 545
Cdd:cd17921 21 LVSAPTSSGKTLIAELAILRALATSGGkAVYIAPTRALVNQKEADLRERFGPLGKNVGLLTG--------DPSVNKLLlA 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1341788692 546 QTDIVIGT----HALLSDL--LQVKKLGLVIVDE------EQRFGVLQK--EKFKKLSEGVNFLMMSAT 600
Cdd:cd17921 93 EADILVATpeklDLLLRNGgeRLIQDVRLVVVDEahligdGERGVVLELllSRLLRINKNARFVGLSAT 161
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
445-777 |
6.62e-09 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 59.39 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 445 TPDQEKSINEVM--RDLeserpmdrLLSGDSGFGKTevamrASF-------------RTVvsnyQVLLLAPTTILAKQHY 509
Cdd:COG0513 26 TPIQAQAIPLILagRDV--------LGQAQTGTGKT-----AAFllpllqrldpsrpRAP----QALILAPTRELALQVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 510 ENFKQRMDPFGIKIALV---TRHKTQKEKkdlfesIKKGqTDIVIGTHALLSDLLQVKKLGL-----VIVDEEQR---FG 578
Cdd:COG0513 89 EELRKLAKYLGLRVATVyggVSIGRQIRA------LKRG-VDIVVATPGRLLDLIERGALDLsgvetLVLDEADRmldMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 579 VLQ--KEKFKKLSEGVNFLMMSATpIPRTLyMSISG--LRDISTIS----TPPVGRLPIQTFVGKYSDK---LIRtaILR 647
Cdd:COG0513 162 FIEdiERILKLLPKERQTLLFSAT-MPPEI-RKLAKryLKNPVRIEvapeNATAETIEQRYYLVDKRDKlelLRR--LLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 648 EKsRGGQTIYIHNRVQELNELYKKLQSLvpEVKITMVHGGTSKKEFINSINNLYDGNIDLLLSTTIIENGIDIPNVnTLI 727
Cdd:COG0513 238 DE-DPERAIVFCNTKRGADRLAEKLQKR--GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDV-SHV 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1341788692 728 L-----DDPERYgisqLYQIkGRVGRSNRRAFVYFLfkkeVTPQTKKRLEAIKKY 777
Cdd:COG0513 314 InydlpEDPEDY----VHRI-GRTGRAGAEGTAISL----VTPDERRLLRAIEKL 359
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
474-601 |
1.19e-07 |
|
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: 51.92 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 474 GFGKTEVAMRASFRTvvSNYQVLLLAPTTILAKQHYENFKQrmdpFGIKIALvtrHKTQKEKKDLFESIkkgqtDIVIGT 553
Cdd:cd17926 28 GSGKTLTALALIAYL--KELRTLIVVPTDALLDQWKERFED----FLGDSSI---GLIGGGKKKDFDDA-----NVVVAT 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1341788692 554 HALLSDLLQVKKL-----GLVIVDEEQRFGVLQKEKFKKLSEGVNFLMMSATP 601
Cdd:cd17926 94 YQSLSNLAEEEKDlfdqfGLLIVDEAHHLPAKTFSEILKELNAKYRLGLTATP 146
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
468-748 |
3.84e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 53.75 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 468 LLSGDS-------GFGKTEVAMRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRMDPFGIKIALVTRhktqkekkDLFE 540
Cdd:COG1204 35 LLEGKNlvvsaptASGKTLIAELAILKALLNGGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTG--------DYDS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 541 SIKK-GQTDIVIGT----HALLS---DLLqvKKLGLVIVDE------EQRFGVLQK--EKFKKLSEGVNFLMMSATpipr 604
Cdd:COG1204 107 DDEWlGRYDILVATpeklDSLLRngpSWL--RDVDLVVVDEahliddESRGPTLEVllARLRRLNPEAQIVALSAT---- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 605 tlymsISGLRDI----------STISTPP--VGRL--PIQTFVGKYSDKLIRT--AILREKSRGGQTIYIHNRVQELNEL 668
Cdd:COG1204 181 -----IGNAEEIaewldaelvkSDWRPVPlnEGVLydGVLRFDDGSRRSKDPTlaLALDLLEEGGQVLVFVSSRRDAESL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 669 YKKLQSLVPEVKITMV-----------------------------------HGGTSK-------KEFINsinnlydGNID 706
Cdd:COG1204 256 AKKLADELKRRLTPEEreeleelaeellevseethtnekladclekgvafhHAGLPSelrrlveDAFRE-------GLIK 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1341788692 707 LLLSTTIIENGIDIPnVNTLILDDPERYGISQL-----YQIKGRVGR 748
Cdd:COG1204 329 VLVATPTLAAGVNLP-ARRVIIRDTKRGGMVPIpvlefKQMAGRAGR 374
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
473-601 |
4.19e-07 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 50.98 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 473 SGFGKTEVA-MRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRMDpFGIKIALVTRHKTQKEKKDLFESIKkgqtdIVI 551
Cdd:cd18035 25 TGLGKTIIAiLVAADRLTKKGGKVLILAPSRPLVEQHAENLKRVLN-IPDKITSLTGEVKPEERAERWDASK-----IIV 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 552 GT-----HALLSDLLQVKKLGLVIVDEEQRFG-----VLQKEKFKKLSEGVNFLMMSATP 601
Cdd:cd18035 99 ATpqvieNDLLAGRITLDDVSLLIFDEAHHAVgnyayVYIAHRYKREANNPLILGLTASP 158
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
707-759 |
7.06e-07 |
|
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: 47.70 E-value: 7.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1341788692 707 LLLSTTIIENGIDIPNVNTLILDDPERYgISQLYQIKGRVGRSNRRAFVYFLF 759
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSS-AASYIQRVGRAGRGGKDEGEVILF 76
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
474-601 |
2.04e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 51.65 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 474 GFGKTEVA-MRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRMDPFGIKIALVTRHKTQKEKKDLFESIKkgqtdIVIG 552
Cdd:COG1111 27 GLGKTAVAlLVIAERLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKRKELWEKAR-----IIVA 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1341788692 553 T-HALLSDLL----QVKKLGLVIVDEEQR-FG----VLQKEKFKKLSEGVNFLMMSATP 601
Cdd:COG1111 102 TpQVIENDLIagriDLDDVSLLIFDEAHRaVGnyayVYIAERYHEDAKDPLILGMTASP 160
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
493-573 |
4.77e-06 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box 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: 350715 [Multi-domain] Cd Length: 198 Bit Score: 48.35 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 493 YQVLLLAPTTILAKQHYENFKQRMDPFGIKIALVTRHKTQKEKKDLfESIKKgqTDIVIGTHALLSDLLQVKKLGL---- 568
Cdd:cd17957 61 LRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGP-KSITK--YDILVSTPLRLVFLLKQGPIDLssve 137
|
....*.
gi 1341788692 569 -VIVDE 573
Cdd:cd17957 138 yLVLDE 143
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
632-751 |
7.90e-06 |
|
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: 46.35 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 632 FVGKYSDKLIRTAILREKSRGGQTIYIHNRVQELNELYKKLQSLvpEVKITMVHGGTSKKEFINSINNLYDGNIDLLLST 711
Cdd:cd18787 7 VVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEEL--GIKVAALHGDLSQEERERALKKFRSGKVRVLVAT 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1341788692 712 TIIENGIDIPNVNTLIL----DDPERYgisqLYQIkGRVGRSNR 751
Cdd:cd18787 85 DVAARGLDIPGVDHVINydlpRDAEDY----VHRI-GRTGRAGR 123
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
466-777 |
8.29e-06 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 49.44 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 466 DRLLSGDSGFGKTEVAMRASFRTV---VSNYQVLLLAPTTILAKQHYENFKQRMDPFGIKI-ALVTRHKTqkekKDLFES 541
Cdd:PTZ00424 67 DTIGQAQSGTGKTATFVIAALQLIdydLNACQALILAPTRELAQQIQKVVLALGDYLKVRChACVGGTVV----RDDINK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 542 IKKGQtDIVIGTHALLSDL-----LQVKKLGLVIVDEEQR-----FGVLQKEKFKKLSEGVNFLMMSATPIPRTLYMSIS 611
Cdd:PTZ00424 143 LKAGV-HMVVGTPGRVYDMidkrhLRVDDLKLFILDEADEmlsrgFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 612 GLRDISTI--STPPVGRLPIQTF---VGKYSDKLIRTAILREKSRGGQTIYIHNRVQELNELYKKLQSlvPEVKITMVHG 686
Cdd:PTZ00424 222 FMRDPKRIlvKKDELTLEGIRQFyvaVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHE--RDFTVSCMHG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 687 GTSKKEFINSINNLYDGNIDLLLSTTIIENGIDIPNVNTLILDD----PERYgisqLYQIkGRVGRSNRRAfVYFLFkke 762
Cdd:PTZ00424 300 DMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDlpasPENY----IHRI-GRSGRFGRKG-VAINF--- 370
|
330
....*....|....*
gi 1341788692 763 VTPQTKKRLEAIKKY 777
Cdd:PTZ00424 371 VTPDDIEQLKEIERH 385
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
445-573 |
1.19e-05 |
|
DEAD-box helicase domain of 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 47.05 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 445 TPDQEKSINEVM--RDLeserpmdrLLSGDSGFGKTevamrASF------------RTVVSNYQVLLLAPTTILAKQHYE 510
Cdd:cd00268 14 TPIQAQAIPLILsgRDV--------IGQAQTGSGKT-----LAFllpilekllpepKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1341788692 511 NFKQRMDPFGIKIALV---TRHKTQKEKkdlfesiKKGQTDIVIGTHALLSDLLQVKKLGL-----VIVDE 573
Cdd:cd00268 81 VARKLGKGTGLKVAAIyggAPIKKQIEA-------LKKGPDIVVGTPGRLLDLIERGKLDLsnvkyLVLDE 144
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
468-600 |
3.68e-05 |
|
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: 45.40 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 468 LLSGDSGFGKTEVAMRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRmDPFGIKIALVTRHKTQKEKkdlfesiKKGQT 547
Cdd:cd18028 21 LISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKL-EEIGLKVGISTGDYDEDDE-------WLGDY 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1341788692 548 DIVIGTHALLSDLLQVKK-----LGLVIVDE------EQRFGVLQK--EKFKKLSEGVNFLMMSAT 600
Cdd:cd18028 93 DIIVATYEKFDSLLRHSPswlrdVGVVVVDEihlisdEERGPTLESivARLRRLNPNTQIIGLSAT 158
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
474-602 |
5.33e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.59 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 474 GFGKTEVAMR--ASFRTVVSNYQVLLLAPTTILAKQHYENFKQRMDpfgikialvTRHKTQKEKKDLFESIKKGQTDIVI 551
Cdd:pfam04851 33 GSGKTLTAAKliARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLP---------NYVEIGEIISGDKKDESVDDNKIVV 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1341788692 552 GT-HALLSDLLQVKKL------GLVIVDEEQRFG------VLQKEKFKKLsegvnfLMMSATPI 602
Cdd:pfam04851 104 TTiQSLYKALELASLEllpdffDVIIIDEAHRSGassyrnILEYFKPAFL------LGLTATPE 161
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
611-752 |
6.93e-05 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases 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: 350183 [Multi-domain] Cd Length: 150 Bit Score: 44.18 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 611 SGLRDISTISTPPVGRLPIQTFVGKYsdklIRTAILREKSRGGQTIYIHN------RV-QELNELYKKLqslVPEVKItM 683
Cdd:cd18796 1 KKKLDIKVILPVAPEIFPWAGESGAD----AYAEVIFLLERHKSTLVFTNtrsqaeRLaQRLRELCPDR---VPPDFI-A 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1341788692 684 VHGGTSKKEFINSI-NNLYDGNIDLLLSTTIIENGIDIPNVNTLI-LDDPerYGISQLYQikgRVGRSNRR 752
Cdd:cd18796 73 LHHGSLSRELREEVeAALKRGDLKVVVATSSLELGIDIGDVDLVIqIGSP--KSVARLLQ---RLGRSGHR 138
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
568-754 |
7.73e-05 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 45.88 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 568 LVIVDEEQRFGVLQKEKFKKLSE-----GVNFLMMSATpIP---RTLYMSISGLRDISTISTPPVGRLPIQTFVGKY-SD 638
Cdd:cd09639 126 LLIFDEVHFYDEYTLALILAVLEvlkdnDVPILLMSAT-LPkflKEYAEKIGYVEENEPLDLKPNERAPFIKIESDKvGE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 639 KLIRTAILREKSRGGQTIYIHNRVQELNELYKKLQSLVPEVKITMVHGGTS-----KKEfINSINNLYDGNIDLLLSTTI 713
Cdd:cd09639 205 ISSLERLLEFIKKGGSVAIIVNTVDRAQEFYQQLKEKGPEEEIMLIHSRFTekdraKKE-AELLLEFKKSEKFVIVATQV 283
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1341788692 714 IENGIDIpNVNTLIlddPERYGISQLYQikgRVGRSNRRAF 754
Cdd:cd09639 284 IEASLDI-SVDVMI---TELAPIDSLIQ---RLGRLHRYGE 317
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
670-756 |
1.09e-04 |
|
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: 44.93 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 670 KKLQSLVPEVKITMVHGGTSKKEFINS--INNLYDGNIDLLLSTTIIENGIDIPNVNTL-ILD-D----------PERyG 735
Cdd:cd18804 108 EELKTLFPEARIARIDRDTTRKKGALEklLDQFERGEIDILIGTQMIAKGLDFPNVTLVgILNaDsglnspdfraSER-A 186
|
90 100
....*....|....*....|.
gi 1341788692 736 ISQLYQIKGRVGRSNRRAFVY 756
Cdd:cd18804 187 FQLLTQVSGRAGRGDKPGKVI 207
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
667-757 |
2.12e-04 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 45.35 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 667 ELYKK-LQSLVPEVKITMVHGgtsKKEFINSI-NNLYDG-NIDLLLSTTIIENGIDIPNVnTLILDD-----PERYGISQ 738
Cdd:PHA02653 409 EEYKKyLEKRLPIYDFYIIHG---KVPNIDEIlEKVYSSkNPSIIISTPYLESSVTIRNA-THVYDTgrvyvPEPFGGKE 484
|
90 100
....*....|....*....|....*.
gi 1341788692 739 LY-------QIKGRVGRSNRRAFVYF 757
Cdd:PHA02653 485 MFisksmrtQRKGRVGRVSPGTYVYF 510
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
424-730 |
2.69e-04 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 44.78 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 424 IQLFGDPELEEKFK---ETFPY-VETPDQEKSINEVM--RDLeserpmdrLLSGDSGFGKTE------VAMRASFRTVVS 491
Cdd:PLN00206 120 ILSFSSCGLPPKLLlnlETAGYeFPTPIQMQAIPAALsgRSL--------LVSADTGSGKTAsflvpiISRCCTIRSGHP 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 492 NYQ----VLLLAPTTILAKQHYENFKQRMDPFGIKIALVTRHKTQKEKkdlFESIKKGqTDIVIGTHALLSDLL-----Q 562
Cdd:PLN00206 192 SEQrnplAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQ---LYRIQQG-VELIVGTPGRLIDLLskhdiE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 563 VKKLGLVIVDE-----EQRF--GVLQKekFKKLSEGvNFLMMSATPIPRTLYMSISGLRDISTISTPPVGR-------LP 628
Cdd:PLN00206 268 LDNVSVLVLDEvdcmlERGFrdQVMQI--FQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRpnkavkqLA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 629 IQTFVGKYSDKLIRtaILREKS--RGGQTIYIHNRVQElnELYKKLQSLVPEVKITMVHGGTSKKEFINSINNLYDGNID 706
Cdd:PLN00206 345 IWVETKQKKQKLFD--ILKSKQhfKPPAVVFVSSRLGA--DLLANAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVP 420
|
330 340
....*....|....*....|....
gi 1341788692 707 LLLSTTIIENGIDIPNVNTLILDD 730
Cdd:PLN00206 421 VIVATGVLGRGVDLLRVRQVIIFD 444
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
687-759 |
3.92e-04 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is 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. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain] Cd Length: 143 Bit Score: 41.57 E-value: 3.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1341788692 687 GTSKKEFINSINNLYDGNIDLLLSTTIIENGIDIPNVNTLILDDPERYGIsQLYQIKGRVGRsNRRAFVYFLF 759
Cdd:cd18801 73 GMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPI-RMIQRMGRTGR-KRQGRVVVLL 143
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
454-603 |
4.78e-04 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 42.34 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 454 EVMRDL-ESERPMdrLLSGDSGFGKT---EVAMRASFRTVVS----NYQVLLLAPTTILAKQHYENFKQRMDPFGIKIAL 525
Cdd:cd18023 8 EVFPDLlYSDKNF--VVSAPTGSGKTvlfELAILRLLKERNPlpwgNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 526 VTRHKTQKEKKDLFesikkgQTDIVIGT-------------HALLSDLLQvkklgLVIVDE-----EQRFGVLQ------ 581
Cdd:cd18023 86 LTGDTEMDDTFEIQ------DADIILTTpekwdsmtrrwrdNGNLVQLVA-----LVLIDEvhiikENRGATLEvvvsrm 154
|
170 180
....*....|....*....|....*...
gi 1341788692 582 ------KEKFKKLSEGVNFLMMSATpIP 603
Cdd:cd18023 155 ktlsssSELRGSTVRPMRFVAVSAT-IP 181
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
622-758 |
6.42e-04 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 43.67 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 622 PPVGRLPIQTFVGKYSDKLIRTAIlrekSRGGQTI-YIHNRVQ-ELneLYKKLQSLVPE----VKITMVHGGTSKKEFIN 695
Cdd:COG1205 262 PPLVDDGIRRSALAEAARLLADLV----REGLRTLvFTRSRRGaEL--LARYARRALREpdlaDRVAAYRAGYLPEERRE 335
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1341788692 696 SINNLYDGNIDLLLSTTIIENGIDIPNVNTLILDD-PerYGISQLYQIKGRVGRSNRRAFVYFL 758
Cdd:COG1205 336 IERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGyP--GTRASFWQQAGRAGRRGQDSLVVLV 397
|
|
| UvrB |
COG0556 |
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair]; |
115-182 |
6.87e-04 |
|
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
Pssm-ID: 440322 [Multi-domain] Cd Length: 657 Bit Score: 43.46 E-value: 6.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 115 LGYNLTEEVTSPGEYSKRGFVRDFFvPIY--EQPVRIELWDEVIDRISFFDIYSQRSIENLKEIEIIPGS 182
Cdd:COG0556 176 LQYERNDIDFTRGTFRVRGDVIEIF-PAYseERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTIYPAS 244
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
450-577 |
9.39e-04 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box 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: 350714 [Multi-domain] Cd Length: 231 Bit Score: 41.85 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 450 KSINEVMRDLESERPMDRLLSGDSGFGKTeVA-----MRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRMDPFGIKIA 524
Cdd:cd17956 22 PWLLPSSKSTPPYRPGDLCVSAPTGSGKT-LAyvlpiVQALSKRVVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKVV 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1341788692 525 LVT-RHKTQKEKKDLFESIKKGQ---TDIVIGTHALLSDLLQ------VKKLGLVIVDEEQRF 577
Cdd:cd17956 101 SLSgQKSFKKEQKLLLVDTSGRYlsrVDILVATPGRLVDHLNstpgftLKHLRFLVIDEADRL 163
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
455-602 |
9.98e-04 |
|
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: 41.51 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 455 VMRDLESERPmdRLLSGDS-GFGKT-EVAMrasfrtVVSNYQ-------VLLLAPTTILakqhyENFKQRM-DPFGIKIA 524
Cdd:cd18011 9 VLRALRKPPV--RLLLADEvGLGKTiEAGL------IIKELLlrgdakrVLILCPASLV-----EQWQDELqDKFGLPFL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 525 LVTR---HKTQKEKKDLFESIkkgqtDIVIGTHALL------SDLLQVKKLGLVIVDEEQRFGVLQKEKFKKLSEGV--- 592
Cdd:cd18011 76 ILDRetaAQLRRLIGNPFEEF-----PIVIVSLDLLkrseerRGLLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLGrll 150
|
170
....*....|....*
gi 1341788692 593 -----NFLMMSATPI 602
Cdd:cd18011 151 akrarHVLLLTATPH 165
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
465-609 |
1.53e-03 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box 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: 350701 [Multi-domain] Cd Length: 192 Bit Score: 40.71 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 465 MDRLLSGDSGFGKT---EVAMRASFRTVVSNYQVLLLAPTTILAKQHYENFKQrMDPF--GIKI-ALVTRHKTQKEKKDL 538
Cdd:cd17943 28 HDLIVQAKSGTGKTlvfVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK-IGKKleGLKCeVFIGGTPVKEDKKKL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 539 fesikkGQTDIVIGT-----HALLSDLLQVKKLGLVIVDEEQRF--GVLQKE---KFKKLSEGVNFLMMSATpIPRTL-- 606
Cdd:cd17943 107 ------KGCHIAVGTpgrikQLIELGALNVSHVRLFVLDEADKLmeGSFQKDvnwIFSSLPKNKQVIAFSAT-YPKNLdn 179
|
....*..
gi 1341788692 607 ----YMS 609
Cdd:cd17943 180 llarYMR 186
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
473-615 |
1.78e-03 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box 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: 350697 [Multi-domain] Cd Length: 199 Bit Score: 40.77 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 473 SGFGKT---EVAMRASFRTVVSNYQVLLLAPTTILAKQHYENFKQRMDPFGIKI-ALVTRHKTQKEKKDLfesiKKGqTD 548
Cdd:cd17939 43 SGTGKTatfSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVKVhACIGGTSVREDRRKL----QYG-PH 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1341788692 549 IVIGTHALLSDLLQ-----VKKLGLVIVDE-----EQRFGVLQKEKFKKLSEGVNFLMMSATPIPRTLYMSISGLRD 615
Cdd:cd17939 118 IVVGTPGRVFDMLQrrslrTDKIKMFVLDEademlSRGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRD 194
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
465-600 |
2.78e-03 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box 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: 350708 [Multi-domain] Cd Length: 208 Bit Score: 40.02 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 465 MDRLLSGDSGFGKTEV---AMRASFRTVVSNYQVLLLAPTTILAKQ---HYENFKQRMDpfGIKIALVtrHKTQKEKKDL 538
Cdd:cd17950 40 MDVLCQAKSGMGKTAVfvlSTLQQLEPVDGQVSVLVICHTRELAFQisnEYERFSKYMP--NVKTAVF--FGGVPIKKDI 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1341788692 539 fESIKKGQTDIVIGTHALLSDLLQVKKLGL-----VIVDE-----EQ---RFGVlqKEKFKKLSEGVNFLMMSAT 600
Cdd:cd17950 116 -EVLKNKCPHIVVGTPGRILALVREKKLKLshvkhFVLDEcdkmlEQldmRRDV--QEIFRATPHDKQVMMFSAT 187
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
645-758 |
3.61e-03 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350176 [Multi-domain] Cd Length: 153 Bit Score: 39.15 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 645 ILREKSRGGQTIYIHNRVQELNELYKKLqsLVPevkitMVHGGTSKKEFINSINNLYDGNIDLLLSTTIIENGIDIPNVN 724
Cdd:cd18789 42 LLKRHEQGDKIIVFTDNVEALYRYAKRL--LKP-----FITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEAN 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1341788692 725 TLILddperygISQLY-------QIKGRVGR----SNRRAFVYFL 758
Cdd:cd18789 115 VAIQ-------ISGHGgsrrqeaQRLGRILRpkkgGGKNAFFYSL 152
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
115-182 |
4.04e-03 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 40.80 E-value: 4.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341788692 115 LGYNLTEEVTSPGEYSKRGFVRDFFvPIY--EQPVRIELWDEVIDRISFFDIYSQRSIENLKEIEIIPGS 182
Cdd:PRK05298 179 LQYERNDIDFQRGTFRVRGDVIEIF-PAYyeERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTIYPAS 247
|
|
| |
