|
Name |
Accession |
Description |
Interval |
E-value |
| recD_rel |
TIGR01448 |
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ... |
25-750 |
0e+00 |
|
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the exodeoxyribonuclease V alpha chain of TIGR01447. Members of this family, however, are not found in a context of RecB and RecC and are longer by about 200 amino acids at the amino end. Chlamydia muridarum has both a member of this family and a RecD. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273632 [Multi-domain] Cd Length: 720 Bit Score: 706.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 25 IFHNEENLYSVVSMKVIETNEtydEKKVMINGHFPRMHEDEVFTLTGHFKDHPKYGKQYMVETFKKELPQTKAGMVQYLA 104
Cdd:TIGR01448 9 LFENSTNFYVVLAVLRDETGE---DTDATVVGVLPPLDEGDTYTFEGQWEEHAKYGYQFRAERMELEAPTSKEGIVAYLS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 105 SDLFKGIGKRTAEKIVDHLGEHAISKIMDDPEALNGV--VNKQKAQEIYETIVEHQGLEKVMSFLNGYGFGTKLSIKIYQ 182
Cdd:TIGR01448 86 SRSIKGVGKKLAQRIVKTFGEAAFDVLDDDPEKLLEVpgISKANLEKFVSQWSQQGDERRLLAGLQGLGIGIKLAQRIYK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 183 QYKEMTLEVIRNNPYQLIEEVDGIGFGRADDIGRALGISGNHDDRVRAGCFYTLENVSLQLGHVYMRKDQLVRETMSLLN 262
Cdd:TIGR01448 166 FYQADTLDRVEKDPYLLAEDVKGIGFLTADQLAQALGIALNDPRRITAGLVYSLQQACTEEGHTYLPRNRFIKQVVHLLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 263 NQ--EGRVTEEDIIGCIETMQSEGKVIIEEERVYLATLFYSEKGVVKSIRRLMnqEETPSFPEAEVLKTLGEIEEQLNVQ 340
Cdd:TIGR01448 246 VQpqERLLVPEAVELERLYLDEEPKLAAEDGRIYLPSLFRAEKQIASHIRRLL--ATSPAIGAINDQEHIWEVEKKLRKG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 341 YAPFQQEAIQTALHKPMMLLTGGPGTGKTTVIKGIVEMYASLHGlslnpneysddnPFPILLTAPTGRAAKRMSESTGLP 420
Cdd:TIGR01448 324 LSEEQKQALDTAIQHKVVILTGGPGTGKTTITRAIIELAEELGG------------LLPVGLAAPTGRAAKRLGEVTGLT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 421 ACTIHRLLGWTPEGSFQRNETDPVQGKLLIIDEFSMVDIWLANQLFKSLPTNIQVIVVGDEDQLPSVGPGQVLKDLLNAG 500
Cdd:TIGR01448 392 ASTIHRLLGYGPDTFRHNHLEDPIDCDLLIVDESSMMDTWLALSLLAALPDHARLLLVGDTDQLPSVGPGQVLKDLILSQ 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 501 AVPTVKLTEIYRQAEGSSVIQLAHAIKDGTLPP--DLAQNKKDRSFISCTGAQIVEVVKKVCENAKTKGFSARDVQVLAP 578
Cdd:TIGR01448 472 AIPVTRLTKVYRQAAGSPIITLAHGILHGEAPAwgDFKFLNLTRSEPEGAARHIPLMVEKIVGMARVGGIPGADIQVLAP 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 579 MYRGPAGINVLNEALQQVFNPKREKSKEIQYGDVVYRRGDKVLQLVNQPESQVFNGDIGEIVSVFYAKENveQQDMIIVS 658
Cdd:TIGR01448 552 MYKGPLGIDALNQHLQALLNPYQKGQGGIEIAEGEYRKGDRVMQTKNDYNNEIFNGDLGMIVKIEGAKQG--KKDQVVVD 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 659 FDGIEVTYTKPDLNQITHAYCCSIHKSQGSEFPIVIMPIVKSYNRMLRRNLIYTGITRSKKFLIICGEEVAFQSGVNRLD 738
Cdd:TIGR01448 630 FDGNEVELTRAELFNLTLAYATSIHKSQGSEFPTVILPIHTAHMRMLYRNLLYTALTRAKKRVILVGSAEAFDIAAARQG 709
|
730
....*....|..
gi 446450225 739 DAmRQTTLASRL 750
Cdd:TIGR01448 710 QA-RNTGLLERI 720
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
211-751 |
2.79e-151 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 451.74 E-value: 2.79e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 211 ADDIGRalgisgnhDDRVRAGcfYTLENVSLQlGHVYMRKDQLVREtmsLLNnqegrvTEEDIIGCIETMQSEGKVIIEE 290
Cdd:COG0507 20 ADFIAR--------DDPIRAA--ALLSRAAGE-GHTFPLEDLAAAR---LLG------VAEDIEAALAALVESGPLVLDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 291 ERvYLATLFYSEKGVVKSIRRLmnqeETPSFPEAEVLKTLGEIEEQLNVQYAPFQQEAIQTALHK-PMMLLtggpgtgkt 369
Cdd:COG0507 80 RR-YLTRLLEAEQRLARRLRRL----ARPALDEADVEAALAALEPRAGITLSDEQREAVALALTTrRVSVLtggagtgkt 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 370 tVIKGIVEMYASLHglslnpneysddnpFPILLTAPTGRAAKRMSESTGLPACTIHRLLGWTP-EGSFQRNETDPVQ-GK 447
Cdd:COG0507 155 tTLRALLAALEALG--------------LRVALAAPTGKAAKRLSESTGIEARTIHRLLGLRPdSGRFRHNRDNPLTpAD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 448 LLIIDEFSMVDIWLANQLFKSLP-TNIQVIVVGDEDQLPSVGPGQVLKDLLNAGAVPTVKLTEIYRQAEGSSVIQLAHAI 526
Cdd:COG0507 221 LLVVDEASMVDTRLMAALLEALPrAGARLILVGDPDQLPSVGAGAVLRDLIESGTVPVVELTEVYRQADDSRIIELAHAI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 527 KDGTLPPDLAQNKKDRSFISC-TGAQIVEVVKKVCENAKTKGfsaRDVQVLAPMyrgPAGINVLNEALQQVFNPKREKSK 605
Cdd:COG0507 301 REGDAPEALNARYADVVFVEAeDAEEAAEAIVELYADRPAGG---EDIQVLAPT---NAGVDALNQAIREALNPAGELER 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 606 E-IQYGDVVYRRGDKVLQLVNQPESQVFNGDIGEIVSVFyakenvEQQDMIIVSFDGIE-VTYTKPDLNQITHAYCCSIH 683
Cdd:COG0507 375 ElAEDGELELYVGDRVMFTRNDYDLGVFNGDIGTVLSID------EDEGRLTVRFDGREiVTYDPSELDQLELAYAITVH 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446450225 684 KSQGSEFPIVIMPIVKSYNRMLRRNLIYTGITRSKKFLIICGEEVAFQSGVNRldDAMRQTTLASRLQ 751
Cdd:COG0507 449 KSQGSTFDRVILVLPSEHSPLLSRELLYTALTRARELLTLVGDRDALARAVRR--DTARATGLAERLR 514
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
345-489 |
4.62e-49 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 168.94 E-value: 4.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 345 QQEAIQTALHKPMMLLTGGPGTGKTTVIKGIVEMYASLHGLslnpneysddnPFPILLTAPTGRAAKRMSESTGLPACTI 424
Cdd:pfam13245 1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGV-----------SFPILLAAPTGRAAKRLSERTGLPASTI 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446450225 425 HRLLGWTP--EGSFQRNETDPVQGKLLIIDEFSMVDIWLANQLFKSLPTNIQVIVVGDEDQLPSVGP 489
Cdd:pfam13245 70 HRLLGFDDleAGGFLRDEEEPLDGDLLIVDEFSMVDLPLAYRLLKALPDGAQLLLVGDPDQLPSVGP 136
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
391-511 |
1.40e-48 |
|
DEXS-box helicase domain of RecD and similar proteins; 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 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: 350691 [Multi-domain] Cd Length: 155 Bit Score: 168.50 E-value: 1.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 391 EYSDDNPFPILLTAPTGRAAKRMSESTGLPACTIHRLLGWTPEGS-FQRNETDPVQGKLLIIDEFSMVDIWLANQLFKSL 469
Cdd:cd17933 34 AALEAEGKRVVLAAPTGKAAKRLSESTGIEASTIHRLLGINPGGGgFYYNEENPLDADLLIVDEASMVDTRLMAALLSAI 113
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446450225 470 PTNIQVIVVGDEDQLPSVGPGQVLKDLLNAGAVPTVKLTEIY 511
Cdd:cd17933 114 PAGARLILVGDPDQLPSVGAGNVLRDLIASKGVPTVELTEVF 155
|
|
| recD |
PRK10875 |
exodeoxyribonuclease V subunit alpha; |
286-734 |
5.98e-28 |
|
exodeoxyribonuclease V subunit alpha;
Pssm-ID: 236783 [Multi-domain] Cd Length: 615 Bit Score: 119.66 E-value: 5.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 286 VIIEEERVYLATLFYSEKGVVKSIRRlmnQEETPSFPEAEVLKTL----GEIEEQLNvqyapFQQEAIQTALHKPMmllt 361
Cdd:PRK10875 102 LVLCGDRLYLQRMWQNERTVARFFNE---VNHAIEVDEALLRQTLdalfGPVTDEVD-----WQKVAAAVALTRRI---- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 362 ggpgtgktTVIKG---------IVEMYASLhgLSLNPNEysddnPFPILLTAPTGRAAKRMSESTG-----LP------- 420
Cdd:PRK10875 170 --------SVISGgpgtgktttVAKLLAAL--IQLADGE-----RCRIRLAAPTGKAAARLTESLGkalrqLPltdeqkk 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 421 -----ACTIHRLLGWTPEGSFQRNETD-PVQGKLLIIDEFSMVDIWLANQLFKSLPTNIQVIVVGDEDQLPSVGPGQVLK 494
Cdd:PRK10875 235 ripeeASTLHRLLGAQPGSQRLRYHAGnPLHLDVLVVDEASMVDLPMMARLIDALPPHARVIFLGDRDQLASVEAGAVLG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 495 DL---LNAG-----------------------AVPTVK-----LTEIYRQAEGSSVIQLAHAIKDGTLPPDLAQNKKDRS 543
Cdd:PRK10875 315 DIcrfAEAGysaeraqqlsrltgchlpagtgtEAASVRdslclLRKSYRFGSDSGIGQLAAAVNRGDKRAAKAVFQQGFS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 544 FISCTGAQIVEVVKKVCENAkTKGFS---------ARDVQVLAPMYR---------GPAGINVLNEALQQVFNPKReksk 605
Cdd:PRK10875 395 DIEKRPLQSGEDYQAMLEEA-LAGYGryldllaarAEPEAILAAFNRyqllcalreGPFGVAGLNERIEQALQQKR---- 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 606 EIQYGDVVYRR---GDKVLQLVNQPESQVFNGDIGeivsvfYAKENVEQQdmIIVSF---DGiEVTYTKPD-LNQITHAY 678
Cdd:PRK10875 470 LIRRPSGPHSRwyeGRPVMIARNDSALGLFNGDIG------IALDRGQGE--LRVWFqlpDG-NIKSVQPSrLPEHETAW 540
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446450225 679 CCSIHKSQGSEF-------PIVIMPIVKsynrmlrRNLIYTGITRSKKFLIICGEEVAFQSGV 734
Cdd:PRK10875 541 AMTVHKSQGSEFdhtalvlPNQFTPVVT-------RELVYTAITRARRRLSLYADERVLSAAI 596
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recD_rel |
TIGR01448 |
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ... |
25-750 |
0e+00 |
|
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the exodeoxyribonuclease V alpha chain of TIGR01447. Members of this family, however, are not found in a context of RecB and RecC and are longer by about 200 amino acids at the amino end. Chlamydia muridarum has both a member of this family and a RecD. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273632 [Multi-domain] Cd Length: 720 Bit Score: 706.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 25 IFHNEENLYSVVSMKVIETNEtydEKKVMINGHFPRMHEDEVFTLTGHFKDHPKYGKQYMVETFKKELPQTKAGMVQYLA 104
Cdd:TIGR01448 9 LFENSTNFYVVLAVLRDETGE---DTDATVVGVLPPLDEGDTYTFEGQWEEHAKYGYQFRAERMELEAPTSKEGIVAYLS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 105 SDLFKGIGKRTAEKIVDHLGEHAISKIMDDPEALNGV--VNKQKAQEIYETIVEHQGLEKVMSFLNGYGFGTKLSIKIYQ 182
Cdd:TIGR01448 86 SRSIKGVGKKLAQRIVKTFGEAAFDVLDDDPEKLLEVpgISKANLEKFVSQWSQQGDERRLLAGLQGLGIGIKLAQRIYK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 183 QYKEMTLEVIRNNPYQLIEEVDGIGFGRADDIGRALGISGNHDDRVRAGCFYTLENVSLQLGHVYMRKDQLVRETMSLLN 262
Cdd:TIGR01448 166 FYQADTLDRVEKDPYLLAEDVKGIGFLTADQLAQALGIALNDPRRITAGLVYSLQQACTEEGHTYLPRNRFIKQVVHLLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 263 NQ--EGRVTEEDIIGCIETMQSEGKVIIEEERVYLATLFYSEKGVVKSIRRLMnqEETPSFPEAEVLKTLGEIEEQLNVQ 340
Cdd:TIGR01448 246 VQpqERLLVPEAVELERLYLDEEPKLAAEDGRIYLPSLFRAEKQIASHIRRLL--ATSPAIGAINDQEHIWEVEKKLRKG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 341 YAPFQQEAIQTALHKPMMLLTGGPGTGKTTVIKGIVEMYASLHGlslnpneysddnPFPILLTAPTGRAAKRMSESTGLP 420
Cdd:TIGR01448 324 LSEEQKQALDTAIQHKVVILTGGPGTGKTTITRAIIELAEELGG------------LLPVGLAAPTGRAAKRLGEVTGLT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 421 ACTIHRLLGWTPEGSFQRNETDPVQGKLLIIDEFSMVDIWLANQLFKSLPTNIQVIVVGDEDQLPSVGPGQVLKDLLNAG 500
Cdd:TIGR01448 392 ASTIHRLLGYGPDTFRHNHLEDPIDCDLLIVDESSMMDTWLALSLLAALPDHARLLLVGDTDQLPSVGPGQVLKDLILSQ 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 501 AVPTVKLTEIYRQAEGSSVIQLAHAIKDGTLPP--DLAQNKKDRSFISCTGAQIVEVVKKVCENAKTKGFSARDVQVLAP 578
Cdd:TIGR01448 472 AIPVTRLTKVYRQAAGSPIITLAHGILHGEAPAwgDFKFLNLTRSEPEGAARHIPLMVEKIVGMARVGGIPGADIQVLAP 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 579 MYRGPAGINVLNEALQQVFNPKREKSKEIQYGDVVYRRGDKVLQLVNQPESQVFNGDIGEIVSVFYAKENveQQDMIIVS 658
Cdd:TIGR01448 552 MYKGPLGIDALNQHLQALLNPYQKGQGGIEIAEGEYRKGDRVMQTKNDYNNEIFNGDLGMIVKIEGAKQG--KKDQVVVD 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 659 FDGIEVTYTKPDLNQITHAYCCSIHKSQGSEFPIVIMPIVKSYNRMLRRNLIYTGITRSKKFLIICGEEVAFQSGVNRLD 738
Cdd:TIGR01448 630 FDGNEVELTRAELFNLTLAYATSIHKSQGSEFPTVILPIHTAHMRMLYRNLLYTALTRAKKRVILVGSAEAFDIAAARQG 709
|
730
....*....|..
gi 446450225 739 DAmRQTTLASRL 750
Cdd:TIGR01448 710 QA-RNTGLLERI 720
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
211-751 |
2.79e-151 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 451.74 E-value: 2.79e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 211 ADDIGRalgisgnhDDRVRAGcfYTLENVSLQlGHVYMRKDQLVREtmsLLNnqegrvTEEDIIGCIETMQSEGKVIIEE 290
Cdd:COG0507 20 ADFIAR--------DDPIRAA--ALLSRAAGE-GHTFPLEDLAAAR---LLG------VAEDIEAALAALVESGPLVLDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 291 ERvYLATLFYSEKGVVKSIRRLmnqeETPSFPEAEVLKTLGEIEEQLNVQYAPFQQEAIQTALHK-PMMLLtggpgtgkt 369
Cdd:COG0507 80 RR-YLTRLLEAEQRLARRLRRL----ARPALDEADVEAALAALEPRAGITLSDEQREAVALALTTrRVSVLtggagtgkt 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 370 tVIKGIVEMYASLHglslnpneysddnpFPILLTAPTGRAAKRMSESTGLPACTIHRLLGWTP-EGSFQRNETDPVQ-GK 447
Cdd:COG0507 155 tTLRALLAALEALG--------------LRVALAAPTGKAAKRLSESTGIEARTIHRLLGLRPdSGRFRHNRDNPLTpAD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 448 LLIIDEFSMVDIWLANQLFKSLP-TNIQVIVVGDEDQLPSVGPGQVLKDLLNAGAVPTVKLTEIYRQAEGSSVIQLAHAI 526
Cdd:COG0507 221 LLVVDEASMVDTRLMAALLEALPrAGARLILVGDPDQLPSVGAGAVLRDLIESGTVPVVELTEVYRQADDSRIIELAHAI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 527 KDGTLPPDLAQNKKDRSFISC-TGAQIVEVVKKVCENAKTKGfsaRDVQVLAPMyrgPAGINVLNEALQQVFNPKREKSK 605
Cdd:COG0507 301 REGDAPEALNARYADVVFVEAeDAEEAAEAIVELYADRPAGG---EDIQVLAPT---NAGVDALNQAIREALNPAGELER 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 606 E-IQYGDVVYRRGDKVLQLVNQPESQVFNGDIGEIVSVFyakenvEQQDMIIVSFDGIE-VTYTKPDLNQITHAYCCSIH 683
Cdd:COG0507 375 ElAEDGELELYVGDRVMFTRNDYDLGVFNGDIGTVLSID------EDEGRLTVRFDGREiVTYDPSELDQLELAYAITVH 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446450225 684 KSQGSEFPIVIMPIVKSYNRMLRRNLIYTGITRSKKFLIICGEEVAFQSGVNRldDAMRQTTLASRLQ 751
Cdd:COG0507 449 KSQGSTFDRVILVLPSEHSPLLSRELLYTALTRARELLTLVGDRDALARAVRR--DTARATGLAERLR 514
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
345-489 |
4.62e-49 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 168.94 E-value: 4.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 345 QQEAIQTALHKPMMLLTGGPGTGKTTVIKGIVEMYASLHGLslnpneysddnPFPILLTAPTGRAAKRMSESTGLPACTI 424
Cdd:pfam13245 1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGV-----------SFPILLAAPTGRAAKRLSERTGLPASTI 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446450225 425 HRLLGWTP--EGSFQRNETDPVQGKLLIIDEFSMVDIWLANQLFKSLPTNIQVIVVGDEDQLPSVGP 489
Cdd:pfam13245 70 HRLLGFDDleAGGFLRDEEEPLDGDLLIVDEFSMVDLPLAYRLLKALPDGAQLLLVGDPDQLPSVGP 136
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
391-511 |
1.40e-48 |
|
DEXS-box helicase domain of RecD and similar proteins; 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 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: 350691 [Multi-domain] Cd Length: 155 Bit Score: 168.50 E-value: 1.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 391 EYSDDNPFPILLTAPTGRAAKRMSESTGLPACTIHRLLGWTPEGS-FQRNETDPVQGKLLIIDEFSMVDIWLANQLFKSL 469
Cdd:cd17933 34 AALEAEGKRVVLAAPTGKAAKRLSESTGIEASTIHRLLGINPGGGgFYYNEENPLDADLLIVDEASMVDTRLMAALLSAI 113
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446450225 470 PTNIQVIVVGDEDQLPSVGPGQVLKDLLNAGAVPTVKLTEIY 511
Cdd:cd17933 114 PAGARLILVGDPDQLPSVGAGNVLRDLIASKGVPTVELTEVF 155
|
|
| recD |
TIGR01447 |
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ... |
400-736 |
1.30e-45 |
|
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273631 [Multi-domain] Cd Length: 582 Bit Score: 172.64 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 400 ILLTAPTGRAAKRMSESTG---------------LP--ACTIHRLLGWTP-EGSFQRNETDPVQGKLLIIDEFSMVDIWL 461
Cdd:TIGR01447 195 IALAAPTGKAAARLAESLRkavknlaaaealiaaLPseAVTIHRLLGIKPdTKRFRHHERNPLPLDVLVVDEASMVDLPL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 462 ANQLFKSLPTNIQVIVVGDEDQLPSVGPGQVLKDLL---NAGAVPTVK-------------------LTEIYRQAEGSSV 519
Cdd:TIGR01447 275 MAKLLKALPPNTKLILLGDKNQLPSVEAGAVLGDLCelaSIGKSILYAlckkinsktrnplsdnvcfLKTSHRFGKDSGI 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 520 IQLAHAI--KDGTLPPDLAQNKKDRSFISC-TGAQIVEVVKKVC-------------ENAKTKGFSARDVQVLAPMYRGP 583
Cdd:TIGR01447 355 GQLAKAInsGDIEAVLNNLRSGQLIEFEFLnSKEDAIERLKNLYvkyrtflqklaalSDAKEILETFDRLRLLTALRDGP 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 584 AGINVLNEALQQvfnpkREKSKEIQYGDVVYRRGDKVLQLVNQPESQVFNGDIGEIvsvfyakeNVEQQDMIIVSF---D 660
Cdd:TIGR01447 435 FGVLGLNRRIEQ-----ELQEKYFDPDEEGWYIGRPIMVTENDYTLGLFNGDIGVL--------LRDPDGILTVWFhfaD 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446450225 661 GIEVTYTKpDLNQITHAYCCSIHKSQGSEFP--IVIMPivKSYNRMLRRNLIYTGITRSKKFLIICGEEVAFQSGVNR 736
Cdd:TIGR01447 502 GSKAVLPS-RLPNYETAFAMTVHKSQGSEFDhvILILP--NGNSPVLTRELLYTGITRAKDQLSVWSDKETLNAAIKR 576
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
340-549 |
7.96e-42 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 150.79 E-value: 7.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 340 QYAPFQQEAIQTALHKP--MMLLTGGPGTGKTTVIKGIVEMYASLhglslnpneysddnPFPILLTAPTGRAAKRMSEST 417
Cdd:pfam13604 1 TLNAEQAAAVRALLTSGdrVAVLVGPAGTGKTTALKALREAWEAA--------------GYRVIGLAPTGRAAKVLGEEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 418 GLPACTIHRLLGWTPEGsfqrneTDPVQGKLLIIDEFSMVDIWLANQLFKSLP-TNIQVIVVGDEDQLPSVGPGQVLKDL 496
Cdd:pfam13604 67 GIPADTIAKLLHRLGGR------AGLDPGTLLIVDEAGMVGTRQMARLLKLAEdAGARVILVGDPRQLPSVEAGGAFRDL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446450225 497 LNAGAvPTVKLTEIYRQAEgSSVIQLAHAIKDGTlPPDLAQNKKDRSFISCTG 549
Cdd:pfam13604 141 LAAGI-GTAELTEIVRQRD-PWQRAASLALRDGD-PAEALDALADRGRIHEGD 190
|
|
| HHH_4 |
pfam14490 |
Helix-hairpin-helix containing domain; This presumed domain contains at least one ... |
156-247 |
3.85e-36 |
|
Helix-hairpin-helix containing domain; This presumed domain contains at least one helix-hairpin-helix motif. This domain is often found in RecD helicases.
Pssm-ID: 464187 [Multi-domain] Cd Length: 91 Bit Score: 131.08 E-value: 3.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 156 EHQGLEKVMSFLNGYGFGTKLSIKIYQQYKEMTLEVIRNNPYQLIEEVDGIGFGRADDIGRALGISGNHDDRVRAGCFYT 235
Cdd:pfam14490 1 EQRGLREVMIFLQQYGISPALAVKIYKKYGEDALEILKENPYRLAEDIEGIGFKTADKIARKLGIAPDSPERIRAGILYV 80
|
90
....*....|..
gi 446450225 236 LENvSLQLGHVY 247
Cdd:pfam14490 81 LKQ-AASNGHTY 91
|
|
| recD |
PRK10875 |
exodeoxyribonuclease V subunit alpha; |
286-734 |
5.98e-28 |
|
exodeoxyribonuclease V subunit alpha;
Pssm-ID: 236783 [Multi-domain] Cd Length: 615 Bit Score: 119.66 E-value: 5.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 286 VIIEEERVYLATLFYSEKGVVKSIRRlmnQEETPSFPEAEVLKTL----GEIEEQLNvqyapFQQEAIQTALHKPMmllt 361
Cdd:PRK10875 102 LVLCGDRLYLQRMWQNERTVARFFNE---VNHAIEVDEALLRQTLdalfGPVTDEVD-----WQKVAAAVALTRRI---- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 362 ggpgtgktTVIKG---------IVEMYASLhgLSLNPNEysddnPFPILLTAPTGRAAKRMSESTG-----LP------- 420
Cdd:PRK10875 170 --------SVISGgpgtgktttVAKLLAAL--IQLADGE-----RCRIRLAAPTGKAAARLTESLGkalrqLPltdeqkk 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 421 -----ACTIHRLLGWTPEGSFQRNETD-PVQGKLLIIDEFSMVDIWLANQLFKSLPTNIQVIVVGDEDQLPSVGPGQVLK 494
Cdd:PRK10875 235 ripeeASTLHRLLGAQPGSQRLRYHAGnPLHLDVLVVDEASMVDLPMMARLIDALPPHARVIFLGDRDQLASVEAGAVLG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 495 DL---LNAG-----------------------AVPTVK-----LTEIYRQAEGSSVIQLAHAIKDGTLPPDLAQNKKDRS 543
Cdd:PRK10875 315 DIcrfAEAGysaeraqqlsrltgchlpagtgtEAASVRdslclLRKSYRFGSDSGIGQLAAAVNRGDKRAAKAVFQQGFS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 544 FISCTGAQIVEVVKKVCENAkTKGFS---------ARDVQVLAPMYR---------GPAGINVLNEALQQVFNPKReksk 605
Cdd:PRK10875 395 DIEKRPLQSGEDYQAMLEEA-LAGYGryldllaarAEPEAILAAFNRyqllcalreGPFGVAGLNERIEQALQQKR---- 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 606 EIQYGDVVYRR---GDKVLQLVNQPESQVFNGDIGeivsvfYAKENVEQQdmIIVSF---DGiEVTYTKPD-LNQITHAY 678
Cdd:PRK10875 470 LIRRPSGPHSRwyeGRPVMIARNDSALGLFNGDIG------IALDRGQGE--LRVWFqlpDG-NIKSVQPSrLPEHETAW 540
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446450225 679 CCSIHKSQGSEF-------PIVIMPIVKsynrmlrRNLIYTGITRSKKFLIICGEEVAFQSGV 734
Cdd:PRK10875 541 AMTVHKSQGSEFdhtalvlPNQFTPVVT-------RELVYTAITRARRRLSLYADERVLSAAI 596
|
|
| SH3_13 |
pfam18335 |
ATP-dependent RecD-like DNA helicase SH3 domain; This is an SH3 (SRC homology domain 3) domain ... |
589-659 |
1.73e-19 |
|
ATP-dependent RecD-like DNA helicase SH3 domain; This is an SH3 (SRC homology domain 3) domain found in RecD helicases (EC 3.6.4.12) that belong to the bacterial Superfamily 1B (SF1B). This superfamily of helicases translocate in a 5'-3' direction and are required for a range of cellular activities across all domains of life. Structural analysis indicate that the extension of the 5'-tail of the unwound DNA duplex induces a large conformational change in the RecD subunit, that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit. The process involves this SH3 domain that binds to a region of the RecB subunit. Studies of RecD in E. coli also revealed that the SH3 domain interacts with the ssDNA tail in a location different to that normally occupied by a peptide in canonical eukaryotic SH3 domains, thus retaining the potential to bind peptide at the same time as the ssDNA tail.
Pssm-ID: 465715 [Multi-domain] Cd Length: 65 Bit Score: 82.91 E-value: 1.73e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446450225 589 LNEALQQVFNPKREKSKEIQYGDVVYRRGDKVLQLVNQPESQVFNGDIGEIVSVfyakenVEQQDMIIVSF 659
Cdd:pfam18335 1 LNQRLQEALNPPSPGKKEIKFGGRIFRVGDKVMQTKNNYDLGVFNGDIGIIVAI------DKEEKTLTVDF 65
|
|
| SF1_C_RecD |
cd18809 |
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ... |
671-725 |
2.55e-17 |
|
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: 77.22 E-value: 2.55e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446450225 671 LNQITHAYCCSIHKSQGSEFPIVIMPIVKSyNRMLRRNLIYTGITRSKKFLIICG 725
Cdd:cd18809 27 LNERLQAYAMTIHKSQGSEFDRVIVVLPTS-HPMLSRGLLYTALTRARKLLTLVG 80
|
|
| UvrD_C_2 |
pfam13538 |
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ... |
676-724 |
1.74e-14 |
|
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: 67.98 E-value: 1.74e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446450225 676 HAYCCSIHKSQGSEFPIVIM---PIVKSYNRMLRRNLIYTGITRSKKFLIIC 724
Cdd:pfam13538 1 LAYALTVHKAQGSEFPAVFLvdpDLTAHYHSMLRRRLLYTAVTRARKKLVLV 52
|
|
| TraA_Ti |
TIGR02768 |
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a ... |
404-718 |
2.49e-13 |
|
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a single strand exonuclease (N-terminus, MobA/MobL, pfam03389) as well as a helicase domain (central region, homologous to the corresponding region of the F-type relaxase TraI, TIGR02760). This protein likely fills the same role as TraI(F), nicking (at the oriT site) and unwinding the coiled plasmid prior to conjugative transfer.
Pssm-ID: 274289 [Multi-domain] Cd Length: 744 Bit Score: 73.69 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 404 APTGRAAKRMSESTGLPACTIHRLlgwtpEGSFQRNETDPVQGKLLIIDEFSMVDiwlANQLFKSLPTNIQ----VIVVG 479
Cdd:TIGR02768 403 ALSGKAAEGLQAESGIESRTLASL-----EYAWANGRDLLSDKDVLVIDEAGMVG---SRQMARVLKEAEEagakVVLVG 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 480 DEDQLPSVGPGQVLKDLlnAGAVPTVKLTEIYRQAEG----SSVIQLAHAIKDGTlppdlaQNKKDRSFISCTGAQIVEV 555
Cdd:TIGR02768 475 DPEQLQPIEAGAAFRAI--AERIGYAELETIRRQREAwarqASLELARGDVEKAL------AAYRDHGHITIHDTREEAI 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 556 VKKVCENAKTKGFSARDVQVLAPMYRGpAGINVLNEALQQVFNPKREKSKEIQY----GDVVYRRGDKVLQLVNQPESQV 631
Cdd:TIGR02768 547 EQVVADWKQDLREANPAGSQIMLAHTR-KDVRALNEAAREALIERGELGESILFqtarGERKFAAGDRIVFLENNRDLGV 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 632 FNGDIGEIvsvfyakENVEQQDMIIVSFDGIEVTYTKPDLNQITHAYCCSIHKSQGsefpiviMPIVKSY---NRMLRRN 708
Cdd:TIGR02768 626 KNGMLGTV-------EEIEDGRLVVQLDSGELVIIPQAEYDALDHGYATTIHKSQG-------VTVDRAFvlaSKSMDRH 691
|
330
....*....|
gi 446450225 709 LIYTGITRSK 718
Cdd:TIGR02768 692 LAYVAMTRHR 701
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
681-723 |
2.11e-07 |
|
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: 49.36 E-value: 2.11e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446450225 681 SIHKSQGSEFPIVIMPIVKsyNRMLRRNLIYTGITRSKKFLII 723
Cdd:cd18786 47 TIDSSQGLTFDVVTLYLPT--ANSLTPRRLYVALTRARKRLVI 87
|
|
| RecB |
COG1074 |
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, ... |
681-725 |
2.58e-06 |
|
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: 51.12 E-value: 2.58e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446450225 681 SIHKSQGSEFPIVIMPIVKSYNRMLR----RNLIYTGITRSKKFLIICG 725
Cdd:COG1074 649 TIHKSKGLEFPVVFLPALRERARAEElaeeLRLLYVALTRARDRLVLSG 697
|
|
| PRK13889 |
PRK13889 |
conjugal transfer relaxase TraA; Provisional |
610-687 |
5.42e-06 |
|
conjugal transfer relaxase TraA; Provisional
Pssm-ID: 237546 [Multi-domain] Cd Length: 988 Bit Score: 50.07 E-value: 5.42e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446450225 610 GDVVYRRGDKVLQLVNQPESQVFNGDIGEIvsvfyakENVEQQDMIIVSFDGIEVTYTKPDLNQITHAYCCSIHKSQG 687
Cdd:PRK13889 597 GERSFASGDRVMFLQNERGLGVKNGTLGTI-------EQVSAQSMSVRLDDGRSVAFDLKDYDRIDHGYAATIHKAQG 667
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
397-498 |
2.26e-05 |
|
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: 44.40 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 397 PFPILLTAPTGRAAKRMSEstglpactihrllgwtpegsfqrnetdpvqgklLIIDEFSMVDIWLANQLFKSLPTNIQVI 476
Cdd:cd17914 31 PGRILLVTPTNKAAAQLDN---------------------------------ILVDEAAQILEPETSRLIDLALDQGRVI 77
|
90 100
....*....|....*....|..
gi 446450225 477 VVGDEDQLPSVGPGQVLKDLLN 498
Cdd:cd17914 78 LVGDHDQLGPVWRGAVLAKICN 99
|
|
| SF1_C_UvrD |
cd18807 |
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ... |
622-725 |
2.28e-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: 44.91 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 622 QLVNQPESQVF-NGDIGEIVSVFYAKENVEQQDMII-----------VSFDGIEVTY-TKPDLNQITHA---YCCSIHKS 685
Cdd:cd18807 15 QNKNRPKKPLKaGNKSGGPVELLLAKDEADEAKAIAdeikrliesgpVQYSDIAILVrTNRQARVIEEAlrvTLMTIHAS 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446450225 686 QGSEFPIVIM--------PIVKSYNRMLR--------RNLIYTGITRSKKFLIICG 725
Cdd:cd18807 95 KGLEFPVVFIvglgegfiPSDASYHAAKEdeerleeeRRLLYVALTRAKKELYLVG 150
|
|
| PRK13709 |
PRK13709 |
conjugal transfer nickase/helicase TraI; Provisional |
404-513 |
1.07e-04 |
|
conjugal transfer nickase/helicase TraI; Provisional
Pssm-ID: 237478 [Multi-domain] Cd Length: 1747 Bit Score: 45.94 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 404 APTGRAAKRMSeSTGLPACTIHRLLGWTPEGsfQRN-ETDPVQGKLLIIDEFSMV---DIWLANQLFKSlpTNIQVIVVG 479
Cdd:PRK13709 1023 GPTHRAVGEMR-SAGVDAQTLASFLHDTQLQ--QRSgETPDFSNTLFLLDESSMVgntDMARAYALIAA--GGGRAVSSG 1097
|
90 100 110
....*....|....*....|....*....|....
gi 446450225 480 DEDQLPSVGPGQVLKDLLNAGAVPTVKLTEIYRQ 513
Cdd:PRK13709 1098 DTDQLQAIAPGQPFRLMQTRSAADVAIMKEIVRQ 1131
|
|
| DEXSc_Pif1_like |
cd18037 |
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ... |
345-512 |
1.07e-04 |
|
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 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: 350795 [Multi-domain] Cd Length: 183 Bit Score: 43.78 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 345 QQEAIQTALHKPMMLLTGGPGTGKTTVIKGIVemyaslhglslnpnEYSDDNPFPILLTAPTGRAAkrmsesTGLPACTI 424
Cdd:cd18037 2 QRRVLDLVLDGKNVFFTGSAGTGKSYLLRRII--------------RALPSRPKRVAVTASTGIAA------CNIGGTTL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 425 HRLLGWTPEGSF---------QRNETDP--VQGKLLIIDEFSMVDIWLANQL---FKSLPTN------IQVIVVGDEDQL 484
Cdd:cd18037 62 HSFAGIGLGSEPaedllervkRSPYLVQrwRKCDVLIIDEISMLDADLFDKLdrvAREVRGSdkpfggIQLILCGDFLQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446450225 485 PSVGPGQ---------VLKDLLNAGA-----VPTVKLTEIYR 512
Cdd:cd18037 142 PPVTKNSerqafffrgDQQFCFEAKSwerciFLTVELTKVFR 183
|
|
| TraI_TIGR |
TIGR02760 |
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome ... |
396-513 |
3.09e-04 |
|
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome complex. In the process of conjugative plasmid transfer the realaxosome binds to the plasmid at the oriT (origin of transfer) site. The relaxase protein TraI mediates the single-strand nicking and ATP-dependent unwinding (relaxation, helicase activity) of the plasmid molecule. These two activities reside in separate domains of the protein.
Pssm-ID: 274285 [Multi-domain] Cd Length: 1960 Bit Score: 44.51 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 396 NPFPILLTAPTGRAAKRMsESTGLPACTIHRLLGWTpegSFQRNETDPVQGKLLIIDEFSMVDIWLANQLF-KSLPTNIQ 474
Cdd:TIGR02760 1067 EQLQVIGLAPTHEAVGEL-KSAGVQAQTLDSFLTDI---SLYRNSGGDFRNTLFILDESSMVSNFQLTHATeLVQKSGSR 1142
|
90 100 110
....*....|....*....|....*....|....*....
gi 446450225 475 VIVVGDEDQLPSVGPGQVLKDLLNAGAVPTVKLTEIYRQ 513
Cdd:TIGR02760 1143 AVSLGDIAQLQSLAAGKPFELAITFDIIDTAIMKEIVRQ 1181
|
|
| PRK14712 |
PRK14712 |
conjugal transfer nickase/helicase TraI; Provisional |
404-513 |
8.34e-03 |
|
conjugal transfer nickase/helicase TraI; Provisional
Pssm-ID: 237796 [Multi-domain] Cd Length: 1623 Bit Score: 39.84 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446450225 404 APTGRAAKRMsESTGLPACTIHRLLGWTpEGSFQRNETDPVQGKLLIIDEFSMV---DIWLANQLFKSlpTNIQVIVVGD 480
Cdd:PRK14712 891 GPTHRAVGEM-RSAGVDAQTLASFLHDT-QLQQRSGETPDFSNTLFLLDESSMVgntDMARAYALIAA--GGGRAVASGD 966
|
90 100 110
....*....|....*....|....*....|...
gi 446450225 481 EDQLPSVGPGQVLKDLLNAGAVPTVKLTEIYRQ 513
Cdd:PRK14712 967 TDQLQAIAPGQPFRLQQTRSAADVVIMKEIVRQ 999
|
|
| |
