|
Name |
Accession |
Description |
Interval |
E-value |
| HelD |
COG3973 |
DNA helicase IV [Replication, recombination and repair]; |
1-746 |
0e+00 |
|
DNA helicase IV [Replication, recombination and repair];
Pssm-ID: 443173 [Multi-domain] Cd Length: 699 Bit Score: 703.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 1 MLYQRLDAMRDHAAKRLARALRET-GGTPQARSQRDTATAMYREQVAQFDAVENGLCFGRLDFDDDRTA-----HVGRIG 74
Cdd:COG3973 17 EVYARLDELRAEAEERLAEARKEGwGGTPQALSERDAFAAHAERRLARLDRLEDSPYFGRIDFQEEGEDdgetiYIGRIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 75 IFDEtHGHRPLLVDWRSDAARPFYLATAAA----------PHGVARRRHIRTSGRTVVHLDDEVLDLTAAdpagstGLAG 144
Cdd:COG3973 97 LTDE-DDGEPLVVDWRAPIASPFYDATPGPasyeapggtiPGGVVRRRQYRIRGGKLTGVFDEVLDPDAA------ALIG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 145 EATLFAALGAGRTGRMRDIVETIQAEQDQIIRSDVAGLLVVQGGPGTGKTAVALHRVAYLLYTHRRELSTRAVLVVGPNA 224
Cdd:COG3973 170 DEALQAALSRNRDGRMKDIVATIQAEQDRIIRADLRGVLVVQGGAGSGKTAVALHRAAYLLYTHRERLERGGVLIVGPNR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 225 TFLNYISQVLPSLAETGVLLCTPGDLFP---GVTARRDEPAEVAEIKGRPVMVDVLAAAVADRQR-LPDEPVEinVEQDT 300
Cdd:COG3973 250 LFLDYISQVLPSLGEEGVVQTTFGDLVPellGVEATAEEDPEVARLKGSLRMAEVLDRAVRDLEReVPFEDIR--VEGGE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 301 LLLDPAAIAAARTRARrSGKLHNLARPMFDTEIIHALAAQLAAKIGADplggdnllDEADIAEIRRELRREPEVLAVLDW 380
Cdd:COG3973 328 VILSAEEIAEAFYRAR-RSLPHNKRRERLRERLLDALKDQLAAELGKL--------WDEERDELRRELRRSKPVRAALNR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 381 LWPILTPQQLVAGLFASAARLAAAAPQLTAAERDLLRREPR----GGWSPADVPLLDEAAELLGEDatveavlaererqr 456
Cdd:COG3973 399 LWPFLDPAELYRDLFSDPELLARAAGWLSPEERALLLRPTRelkkGRWTVADVALLDELAELLGGP-------------- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 457 qieyaegaleiamgsrsidvedeaepellaatdlidadrladrhgygeqltaaqraavDRRWAFGHIVVDEAQELSPMAW 536
Cdd:COG3973 465 ----------------------------------------------------------DRTWTYGHVVVDEAQDLSPMQW 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 537 RLLMRRAPNRSMTVVGDVAQTGDL-GGTSSWAQVFEPYVADRWRLAELQVNYRTPAEIMSVAGRLLADIDPTLTPPRSVR 615
Cdd:COG3973 487 RVLKRRFPSASFTIVGDLAQAIHPyRGAESWEEVLEPLGGDRARLVELTKSYRSTAEIMEFANRVLRAAGPDLPPPESVR 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 616 ETGVPPWATRT-VPAELPARLVDAVsREAAAVADGRLGVIVPAAR-LAELGRAVATAVPDATAGDRS-DLVDRVVVLTVR 692
Cdd:COG3973 567 RHGEPPRVVRVpSEAELAAAVVEAV-RELLAEGEGTIAVICKTAReAEALYAALKAGLPVTLIDDESeELEAGVVVLPAY 645
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 2226886465 693 QAKGLEFDSVIVVEPAEIAAESPRGDSDLYVALTRATRRLGIVHGGELPAALAD 746
Cdd:COG3973 646 LAKGLEFDAVVVVDPDEIVYESPRGRRLLYVALTRATHRLTVLHTGELPPLLAG 699
|
|
| HelD_BACSU |
NF041464 |
RNA polymerase recycling motor HelD (Bacillota-type); |
159-239 |
1.91e-22 |
|
RNA polymerase recycling motor HelD (Bacillota-type);
Pssm-ID: 469352 [Multi-domain] Cd Length: 772 Bit Score: 102.97 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 159 RMRDIVETIQAEQDQIIRSDVAGLLVVQGGPGTGKTAVALHRVAYLLYTHRRELSTRAVLVVGPNATFLNYISQVLPSLA 238
Cdd:NF041464 205 QMKSIVATIQKEQNQIIRNERSKLLIVQGAAGSGKTSAALQRVAYLLYRYRETLSAENIVLFSPNPLFNSYVATVLPELG 284
|
.
gi 2226886465 239 E 239
Cdd:NF041464 285 E 285
|
|
| UvrD_C_2 |
pfam13538 |
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ... |
686-735 |
7.80e-08 |
|
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.
Pssm-ID: 463913 [Multi-domain] Cd Length: 52 Bit Score: 49.11 E-value: 7.80e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2226886465 686 VVVLTVRQAKGLEFDSVIVVEPAEIAAESPRGDSD-LYVALTRATRRLGIV 735
Cdd:pfam13538 2 AYALTVHKAQGSEFPAVFLVDPDLTAHYHSMLRRRlLYTAVTRARKKLVLV 52
|
|
| SF1_C_UvrD |
cd18807 |
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ... |
685-735 |
2.11e-05 |
|
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350194 [Multi-domain] Cd Length: 150 Bit Score: 45.30 E-value: 2.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2226886465 685 RVVVLTVRQAKGLEFDSVIVV--------EPAEIAAESPRGDSD------LYVALTRATRRLGIV 735
Cdd:cd18807 85 RVTLMTIHASKGLEFPVVFIVglgegfipSDASYHAAKEDEERLeeerrlLYVALTRAKKELYLV 149
|
|
| PRK14866 |
PRK14866 |
hypothetical protein; Provisional |
511-706 |
6.92e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237840 Cd Length: 451 Bit Score: 39.60 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 511 RAAVDRRWAFGHIVVDEAqeLSPMAWRLLMRRAPNRSMTVVGDVAQTGDLGGtsswaqvfepyvaDRWRLAEL--QVNYR 588
Cdd:PRK14866 202 RIVLETDWAFGHIAADWQ--LGALGDPAVLRAAFEASGADAAYIDRKAMSSG-------------DRPRLEALleELGLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 589 --TPAEIMSVAGR----------LLADIDPTLtPPRSVRETGVPPWATRTVPAELPARlVDAVSREAAAVADGRLGVIVP 656
Cdd:PRK14866 267 vlSETWLRETGGVplslvraledLAGTIDPGL-RFGEPARLGDGDPVVVDLPGELLDE-AQGVDREAVRAALDEHPVAFL 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2226886465 657 AARLAELgRAVATAVPDATAGDRSDLVDRVV-VLTVRQAKGLEFDSVIVVE 706
Cdd:PRK14866 345 TTGGGTR-LGGFIAFEAADSDIREDLVDLCVkVLKEKYDSVYRGDNELVIR 394
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HelD |
COG3973 |
DNA helicase IV [Replication, recombination and repair]; |
1-746 |
0e+00 |
|
DNA helicase IV [Replication, recombination and repair];
Pssm-ID: 443173 [Multi-domain] Cd Length: 699 Bit Score: 703.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 1 MLYQRLDAMRDHAAKRLARALRET-GGTPQARSQRDTATAMYREQVAQFDAVENGLCFGRLDFDDDRTA-----HVGRIG 74
Cdd:COG3973 17 EVYARLDELRAEAEERLAEARKEGwGGTPQALSERDAFAAHAERRLARLDRLEDSPYFGRIDFQEEGEDdgetiYIGRIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 75 IFDEtHGHRPLLVDWRSDAARPFYLATAAA----------PHGVARRRHIRTSGRTVVHLDDEVLDLTAAdpagstGLAG 144
Cdd:COG3973 97 LTDE-DDGEPLVVDWRAPIASPFYDATPGPasyeapggtiPGGVVRRRQYRIRGGKLTGVFDEVLDPDAA------ALIG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 145 EATLFAALGAGRTGRMRDIVETIQAEQDQIIRSDVAGLLVVQGGPGTGKTAVALHRVAYLLYTHRRELSTRAVLVVGPNA 224
Cdd:COG3973 170 DEALQAALSRNRDGRMKDIVATIQAEQDRIIRADLRGVLVVQGGAGSGKTAVALHRAAYLLYTHRERLERGGVLIVGPNR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 225 TFLNYISQVLPSLAETGVLLCTPGDLFP---GVTARRDEPAEVAEIKGRPVMVDVLAAAVADRQR-LPDEPVEinVEQDT 300
Cdd:COG3973 250 LFLDYISQVLPSLGEEGVVQTTFGDLVPellGVEATAEEDPEVARLKGSLRMAEVLDRAVRDLEReVPFEDIR--VEGGE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 301 LLLDPAAIAAARTRARrSGKLHNLARPMFDTEIIHALAAQLAAKIGADplggdnllDEADIAEIRRELRREPEVLAVLDW 380
Cdd:COG3973 328 VILSAEEIAEAFYRAR-RSLPHNKRRERLRERLLDALKDQLAAELGKL--------WDEERDELRRELRRSKPVRAALNR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 381 LWPILTPQQLVAGLFASAARLAAAAPQLTAAERDLLRREPR----GGWSPADVPLLDEAAELLGEDatveavlaererqr 456
Cdd:COG3973 399 LWPFLDPAELYRDLFSDPELLARAAGWLSPEERALLLRPTRelkkGRWTVADVALLDELAELLGGP-------------- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 457 qieyaegaleiamgsrsidvedeaepellaatdlidadrladrhgygeqltaaqraavDRRWAFGHIVVDEAQELSPMAW 536
Cdd:COG3973 465 ----------------------------------------------------------DRTWTYGHVVVDEAQDLSPMQW 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 537 RLLMRRAPNRSMTVVGDVAQTGDL-GGTSSWAQVFEPYVADRWRLAELQVNYRTPAEIMSVAGRLLADIDPTLTPPRSVR 615
Cdd:COG3973 487 RVLKRRFPSASFTIVGDLAQAIHPyRGAESWEEVLEPLGGDRARLVELTKSYRSTAEIMEFANRVLRAAGPDLPPPESVR 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 616 ETGVPPWATRT-VPAELPARLVDAVsREAAAVADGRLGVIVPAAR-LAELGRAVATAVPDATAGDRS-DLVDRVVVLTVR 692
Cdd:COG3973 567 RHGEPPRVVRVpSEAELAAAVVEAV-RELLAEGEGTIAVICKTAReAEALYAALKAGLPVTLIDDESeELEAGVVVLPAY 645
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 2226886465 693 QAKGLEFDSVIVVEPAEIAAESPRGDSDLYVALTRATRRLGIVHGGELPAALAD 746
Cdd:COG3973 646 LAKGLEFDAVVVVDPDEIVYESPRGRRLLYVALTRATHRLTVLHTGELPPLLAG 699
|
|
| HelD_BACSU |
NF041464 |
RNA polymerase recycling motor HelD (Bacillota-type); |
159-239 |
1.91e-22 |
|
RNA polymerase recycling motor HelD (Bacillota-type);
Pssm-ID: 469352 [Multi-domain] Cd Length: 772 Bit Score: 102.97 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 159 RMRDIVETIQAEQDQIIRSDVAGLLVVQGGPGTGKTAVALHRVAYLLYTHRRELSTRAVLVVGPNATFLNYISQVLPSLA 238
Cdd:NF041464 205 QMKSIVATIQKEQNQIIRNERSKLLIVQGAAGSGKTSAALQRVAYLLYRYRETLSAENIVLFSPNPLFNSYVATVLPELG 284
|
.
gi 2226886465 239 E 239
Cdd:NF041464 285 E 285
|
|
| COG3972 |
COG3972 |
Superfamily I DNA and RNA helicases [Replication, recombination and repair]; |
504-750 |
1.94e-20 |
|
Superfamily I DNA and RNA helicases [Replication, recombination and repair];
Pssm-ID: 443172 [Multi-domain] Cd Length: 565 Bit Score: 95.67 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 504 EQLTAAQRAAVDRrWAFGHIVVDEAQELSPMAWRLL--MRRAPNRSMTVVGDVAQtgDLGGTSSWAQVFEPyvADRWRLA 581
Cdd:COG3972 274 KALLEAIQGEIIP-PIYDAILIDEAQDFEPEFLRLLyqLLKPPKKRLIWAYDEAQ--NIYGRKIPSAGGIP--AGIGRDT 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 582 ELQVNYRTPAEIMSVA----------------------GRLLADIDPTLTPPRSVRETGVPP-WATRTVPAELPARLVDA 638
Cdd:COG3972 349 ILKKNYRNTRPILTFAhafgmgllrppgllqgdaedyeVERPGDKVTLIRPPEPAGRKGPLPeFKKYDDRAEELEAIAEE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 639 VSR--EAAAVADGRLGVIVPAAR-LAELGRAVATA-------VPDATAGDRSDLV---DRVVVLTVRQAKGLEFDSVIVV 705
Cdd:COG3972 429 IKKnlRDEGLRPSDIAVIYLGNNeAKELGDRLAAAlerqgidSYIAGARSDPNFFwkdGGVTISTIHRAKGLEAPVVIIV 508
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2226886465 706 EPAEIAAESPRGDSD--LYVALTRATRRLGIVHGGELPAALADLADR 750
Cdd:COG3972 509 GLDQLAKGESLERLRnlLYVAMTRARGWLVVSGSGESMAELYDELRE 555
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
199-733 |
7.08e-08 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 56.42 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 199 HRVAYLLYTHRRELSTRAVLVVGPNATFLNYISQVLPSLAETGVLLctpgdlfpGVTARRDEPAEVAEIKGRPVMVDVLA 278
Cdd:COG3321 859 RRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAAL--------AAALLALAAAAAAALALAAAALAALL 930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 279 AAVADRQRLPDEPVEINVEQDTLLLDPAAIAAARTRARRSGKLHNLARPMFDTEIIHALAAQLAAKIGADPLGGDNLLDE 358
Cdd:COG3321 931 ALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAAL 1010
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 359 ADIAEIRRELRREPEVLAVLDWLWPILTPQQLVAGLFASAARLAAAAPQLTAAERDLLRREPRGGWSPADVPLLDEAAEL 438
Cdd:COG3321 1011 LLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAAL 1090
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 439 LGEDATVEAVLAERERQRQIEYAEGALEIAMGSRSIDVEDEAEPELLAATDLIDADRLADRHGYGEQLTAAQRAAVDRRW 518
Cdd:COG3321 1091 AAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAA 1170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 519 AfgHIVVDEAQELSPMAWRLLMRRAPNRSMTVVGDVAQTGDLGGTSSWAQVFEPYVADRWRLAELQVNYRTPAEIMSVAG 598
Cdd:COG3321 1171 A--ALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAAL 1248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 599 RLLADIDPTLTPPRSVRETGVPPWATRTVPAELPARLVDAVSREAAAVADGRLGVIVPAARLAELGRAVATAVPDATAGD 678
Cdd:COG3321 1249 AAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAA 1328
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2226886465 679 RSDLVDRVVVLTVRQAKGLEFDSVIVVEPAEIAAESPRGDSDLYVALTRATRRLG 733
Cdd:COG3321 1329 ALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAA 1383
|
|
| UvrD_C_2 |
pfam13538 |
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ... |
686-735 |
7.80e-08 |
|
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.
Pssm-ID: 463913 [Multi-domain] Cd Length: 52 Bit Score: 49.11 E-value: 7.80e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2226886465 686 VVVLTVRQAKGLEFDSVIVVEPAEIAAESPRGDSD-LYVALTRATRRLGIV 735
Cdd:pfam13538 2 AYALTVHKAQGSEFPAVFLVDPDLTAHYHSMLRRRlLYTAVTRARKKLVLV 52
|
|
| UvrD_C |
pfam13361 |
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ... |
678-734 |
9.70e-07 |
|
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.
Pssm-ID: 433145 [Multi-domain] Cd Length: 377 Bit Score: 51.64 E-value: 9.70e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2226886465 678 DRSDLVDRVVVLTVRQAKGLEFDSVIVVE------PAEIAAESPRGDSD----LYVALTRATRRLGI 734
Cdd:pfam13361 306 EGSDIKERIPIMTIHQAKGLEFDTVFLAGleegifPSYRSIKDEGNLEEerrlFYVAITRAKKRLYI 372
|
|
| SF1_C_UvrD |
cd18807 |
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ... |
685-735 |
2.11e-05 |
|
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350194 [Multi-domain] Cd Length: 150 Bit Score: 45.30 E-value: 2.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2226886465 685 RVVVLTVRQAKGLEFDSVIVV--------EPAEIAAESPRGDSD------LYVALTRATRRLGIV 735
Cdd:cd18807 85 RVTLMTIHASKGLEFPVVFIVglgegfipSDASYHAAKEDEERLeeerrlLYVALTRAKKELYLV 149
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
681-735 |
3.12e-05 |
|
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 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: 350173 [Multi-domain] Cd Length: 89 Bit Score: 43.19 E-value: 3.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2226886465 681 DLVDRVVVLTVRQAKGLEFDSVIVVEPAEIAAESPRgdsdLYVALTRATRRLGIV 735
Cdd:cd18786 38 FDLQLVGAITIDSSQGLTFDVVTLYLPTANSLTPRR----LYVALTRARKRLVIY 88
|
|
| UvrD |
COG0210 |
Superfamily I DNA or RNA helicase [Replication, recombination and repair]; |
635-732 |
3.44e-05 |
|
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
Pssm-ID: 439980 [Multi-domain] Cd Length: 721 Bit Score: 47.24 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 635 LVDAVSREAAAVADGRLgvivpaARLAELGRAVATAVPDATAGDRSDLV----------------DRVVVLTVRQAKGLE 698
Cdd:COG0210 489 YEEELREEAGEEAERRL------ENLEELVDAAARFEERNPGASLEAFLeelallsdldaadedeDAVTLMTLHAAKGLE 562
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2226886465 699 FDSVIVV---E---PAEIAAESPRGDSD----LYVALTRATRRL 732
Cdd:COG0210 563 FPVVFLVgleEglfPHQRSLDDEEELEEerrlFYVAITRARERL 606
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|
| Viral_helicase1 |
pfam01443 |
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ... |
685-735 |
4.78e-05 |
|
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated and NTPase activity. This helicase has multiple roles at different stages of viral RNA replication, as dissected by mutational analysis.
Pssm-ID: 366646 [Multi-domain] Cd Length: 227 Bit Score: 45.45 E-value: 4.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2226886465 685 RVVVLTVRQAKGLEFDSVIVVEPAEIAAESPRGDS-DLYVALTRATRRLGIV 735
Cdd:pfam01443 175 GVRVTTVHEVQGLTFDSVTLVLDTDTDLLIISDSPeHLYVALTRHRKSLHIL 226
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|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
182-222 |
1.05e-04 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. 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. SF1 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: 438706 [Multi-domain] Cd Length: 121 Bit Score: 42.47 E-value: 1.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2226886465 182 LLVVQGGPGTGKTAVALHRVAYLLytHRRELSTRAVLVVGP 222
Cdd:cd17914 1 LSLIQGPPGTGKTRVLVKIVAALM--QNKNGEPGRILLVTP 39
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|
| RecB |
COG1074 |
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, ... |
684-732 |
1.06e-04 |
|
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440692 [Multi-domain] Cd Length: 866 Bit Score: 45.72 E-value: 1.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2226886465 684 DRVVVLTVRQAKGLEFDSVIVVEPAEIAAESPRGDSD--LYVALTRATRRL 732
Cdd:COG1074 643 DAVRIMTIHKSKGLEFPVVFLPALRERARAEELAEELrlLYVALTRARDRL 693
|
|
| SF1_C_RecD |
cd18809 |
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ... |
689-735 |
1.85e-04 |
|
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350196 [Multi-domain] Cd Length: 80 Bit Score: 40.62 E-value: 1.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2226886465 689 LTVRQAKGLEFDSVIVVEPAEIAAESPRGdsdLYVALTRATRRLGIV 735
Cdd:cd18809 36 MTIHKSQGSEFDRVIVVLPTSHPMLSRGL---LYTALTRARKLLTLV 79
|
|
| DEXQc_UvrD |
cd17932 |
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ... |
169-228 |
3.07e-04 |
|
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD 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: 350690 [Multi-domain] Cd Length: 189 Bit Score: 42.50 E-value: 3.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 169 AEQDQIIRsDVAGLLVVQGGPGTGKTAVALHRVAYLLytHRRELSTRAVLVVgpnaTFLN 228
Cdd:cd17932 2 PEQREAVT-HPDGPLLVLAGAGSGKTRVLTHRIAYLI--LEGGVPPERILAV----TFTN 54
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
182-223 |
8.90e-04 |
|
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to 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: 438708 [Multi-domain] Cd Length: 121 Bit Score: 39.91 E-value: 8.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2226886465 182 LLVVQGGPGTGKTAVALHRVAYLLythrRELSTRAVLVVGPN 223
Cdd:cd17934 1 ISLIQGPPGTGKTTTIAAIVLQLL----KGLRGKRVLVTAQS 38
|
|
| UvrD-helicase |
pfam00580 |
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ... |
170-228 |
1.14e-03 |
|
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyze ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.
Pssm-ID: 395462 [Multi-domain] Cd Length: 267 Bit Score: 41.46 E-value: 1.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2226886465 170 EQDQIIRSdVAGLLVVQGGPGTGKTAVALHRVAYLLytHRRELSTRAVLVVgpnaTFLN 228
Cdd:pfam00580 4 EQRKAVTH-LGGPLLVLAGAGSGKTRVLTERIAYLI--LEGGIDPEEILAV----TFTN 55
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|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
182-220 |
3.18e-03 |
|
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain] Cd Length: 178 Bit Score: 39.06 E-value: 3.18e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2226886465 182 LLVVQGGPGTGKTAVALhRVAYLLYTHRRELSTRAVLVV 220
Cdd:cd17936 18 LALIQGPPGTGKTFLGV-KLVRALLQNQDLSITGPILVV 55
|
|
| PRK14866 |
PRK14866 |
hypothetical protein; Provisional |
511-706 |
6.92e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237840 Cd Length: 451 Bit Score: 39.60 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 511 RAAVDRRWAFGHIVVDEAqeLSPMAWRLLMRRAPNRSMTVVGDVAQTGDLGGtsswaqvfepyvaDRWRLAEL--QVNYR 588
Cdd:PRK14866 202 RIVLETDWAFGHIAADWQ--LGALGDPAVLRAAFEASGADAAYIDRKAMSSG-------------DRPRLEALleELGLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226886465 589 --TPAEIMSVAGR----------LLADIDPTLtPPRSVRETGVPPWATRTVPAELPARlVDAVSREAAAVADGRLGVIVP 656
Cdd:PRK14866 267 vlSETWLRETGGVplslvraledLAGTIDPGL-RFGEPARLGDGDPVVVDLPGELLDE-AQGVDREAVRAALDEHPVAFL 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2226886465 657 AARLAELgRAVATAVPDATAGDRSDLVDRVV-VLTVRQAKGLEFDSVIVVE 706
Cdd:PRK14866 345 TTGGGTR-LGGFIAFEAADSDIREDLVDLCVkVLKEKYDSVYRGDNELVIR 394
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