|
Name |
Accession |
Description |
Interval |
E-value |
| recD_rel |
TIGR01448 |
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ... |
12-745 |
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: 1110.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 12 IKGTVEAILFQNSDNFYTVLKVDTIETNEDfdTMPTVVGFLPNIVEGDVYTFKGQVVDHPRYGKQLKAETFEKEMPQTKE 91
Cdd:TIGR01448 1 FSGTVEKILFENSTNFYVVLAVLRDETGED--TDATVVGVLPPLDEGDTYTFEGQWEEHAKYGYQFRAERMELEAPTSKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 92 AIISYLSSDLFKGVGKKTAQNIVNTLGDNAINDILDDHSVLEKVSGLSKKKQKQIAEQISANQESEKIMIRLHDLGFGPK 171
Cdd:TIGR01448 79 GIVAYLSSRSIKGVGKKLAQRIVKTFGEAAFDVLDDDPEKLLEVPGISKANLEKFVSQWSQQGDERRLLAGLQGLGIGIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 172 LSMAIYQFYLGDTLTILDRNPYQLIYDIKGIGFNKADQLARNIGIAYNDNERLKAALLYTLEEECIKQGHTYLPINVVID 251
Cdd:TIGR01448 159 LAQRIYKFYQADTLDRVEKDPYLLAEDVKGIGFLTADQLAQALGIALNDPRRITAGLVYSLQQACTEEGHTYLPRNRFIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 252 LTVDVLNYQ-DEEVIEPEKLDEMLQYLNEEKRLIIDNEQVAIPSLYYSEIKSVQNLFRIKTHTNKLTEIEQsdlQMHIGE 330
Cdd:TIGR01448 239 QVVHLLNVQpQERLLVPEAVELERLYLDEEPKLAAEDGRIYLPSLFRAEKQIASHIRRLLATSPAIGAIND---QEHIWE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 331 IEDANQVNYAASQKEALQTAINSKVMLLTGGPGTGKTTVIKGIVELYAEIHGLsldyddyvnddYPVVLAAPTGRASKRL 410
Cdd:TIGR01448 316 VEKKLRKGLSEEQKQALDTAIQHKVVILTGGPGTGKTTITRAIIELAEELGGL-----------LPVGLAAPTGRAAKRL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 411 QESTGLEAMTIHRLIGWNQDTKPEDILENEINARLIIIDEMSMVDTWLFHQFLSAVPLDAQLIFVGDEDQLPSVGPGQVF 490
Cdd:TIGR01448 385 GEVTGLTASTIHRLLGYGPDTFRHNHLEDPIDCDLLIVDESSMMDTWLALSLLAALPDHARLLLVGDTDQLPSVGPGQVL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 491 KDLIESKAIPRVNLTEVYRQQDGSSIIELAHRMKLGQ---KIDITQRFHDRSFINCQANQIPTVVEKVVTSAVNKGYTMA 567
Cdd:TIGR01448 465 KDLILSQAIPVTRLTKVYRQAAGSPIITLAHGILHGEapaWGDFKFLNLTRSEPEGAARHIPLMVEKIVGMARVGGIPGA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 568 DIQVLAPMYKGNAGIKRLNQVLQDILNPKKKDTREIEFGDVVFRKGDKVLQLVNRPNDNIFNGDIGVIVGIFWAKENalN 647
Cdd:TIGR01448 545 DIQVLAPMYKGPLGIDALNQHLQALLNPYQKGQGGIEIAEGEYRKGDRVMQTKNDYNNEIFNGDLGMIVKIEGAKQG--K 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 648 KDVLVVDFEGNEITFTKQDMMELTHAYCTSIHKSQGSEFPIVIMPIVKQYFRMLQRPILYTGLTRAKTSLVLLGDPEAFD 727
Cdd:TIGR01448 623 KDQVVVDFDGNEVELTRAELFNLTLAYATSIHKSQGSEFPTVILPIHTAHMRMLYRNLLYTALTRAKKRVILVGSAEAFD 702
|
730
....*....|....*...
gi 616690900 728 IGLKTNGQARLTQLCTLL 745
Cdd:TIGR01448 703 IAAARQGQARNTGLLERI 720
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
185-746 |
5.15e-135 |
|
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: 411.29 E-value: 5.15e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 185 LTILDRNPYQLIYDIkGIgFnkADQLARnigiaynDNERLKAALLYTLEEEcikqGHTYLPINVVIDLTVDVlnyqdeev 264
Cdd:COG0507 2 LEIREAWAEQGIYRI-GI-F--ADFIAR-------DDPIRAAALLSRAAGE----GHTFPLEDLAAARLLGV-------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 265 iePEKLDEMLQYLNEEKRLIIDNEQvAIPSLYYSEIKSVQNLFRIKTHtnkltEIEQSDLQMHIGEIEDANQVNYAASQK 344
Cdd:COG0507 59 --AEDIEAALAALVESGPLVLDGRR-YLTRLLEAEQRLARRLRRLARP-----ALDEADVEAALAALEPRAGITLSDEQR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 345 EALQTAIN-SKVMLLtggpgtgkttVIKGIVELYAEIHGlsldyddyvnddyPVVLAAPTGRASKRLQESTGLEAMTIHR 423
Cdd:COG0507 131 EAVALALTtRRVSVLtggagtgkttTLRALLAALEALGL-------------RVALAAPTGKAAKRLSESTGIEARTIHR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 424 LIGWNQDT-KPEDILENEIN-ARLIIIDEMSMVDTWLFHQFLSAVPL-DAQLIFVGDEDQLPSVGPGQVFKDLIESKAIP 500
Cdd:COG0507 198 LLGLRPDSgRFRHNRDNPLTpADLLVVDEASMVDTRLMAALLEALPRaGARLILVGDPDQLPSVGAGAVLRDLIESGTVP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 501 RVNLTEVYRQQDGSSIIELAHRMKLGQ-KIDITQRFHDRSFINCQANQipTVVEKVVTSAVNKGYTMADIQVLAPMykgN 579
Cdd:COG0507 278 VVELTEVYRQADDSRIIELAHAIREGDaPEALNARYADVVFVEAEDAE--EAAEAIVELYADRPAGGEDIQVLAPT---N 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 580 AGIKRLNQVLQDILNPKKKDTRE-IEFGDVVFRKGDKVLQLVNRPNDNIFNGDIGVIVGIfwakenALNKDVLVVDFEGN 658
Cdd:COG0507 353 AGVDALNQAIREALNPAGELERElAEDGELELYVGDRVMFTRNDYDLGVFNGDIGTVLSI------DEDEGRLTVRFDGR 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 659 E-ITFTKQDMMELTHAYCTSIHKSQGSEFPIVIMPIVKQYFRMLQRPILYTGLTRAKTSLVLLGDPEAFDIGLKTNGQaR 737
Cdd:COG0507 427 EiVTYDPSELDQLELAYAITVHKSQGSTFDRVILVLPSEHSPLLSRELLYTALTRARELLTLVGDRDALARAVRRDTA-R 505
|
....*....
gi 616690900 738 LTQLCTLLK 746
Cdd:COG0507 506 ATGLAERLR 514
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
343-508 |
1.32e-50 |
|
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: 174.28 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 343 QKEALQTAINSKVMLLTggpgtgkttVIKGIVELYAEihglsldyddyvnDDYPVVLAAPTGRASKRLQESTGLEAMTIH 422
Cdd:cd17933 2 QKAAVRLVLRNRVSVLTggagtgkttTLKALLAALEA-------------EGKRVVLAAPTGKAAKRLSESTGIEASTIH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 423 RLIGWNQDTKPEDIL-ENEINARLIIIDEMSMVDTWLFHQFLSAVPLDAQLIFVGDEDQLPSVGPGQVFKDLIESKAIPR 501
Cdd:cd17933 69 RLLGINPGGGGFYYNeENPLDADLLIVDEASMVDTRLMAALLSAIPAGARLILVGDPDQLPSVGAGNVLRDLIASKGVPT 148
|
....*..
gi 616690900 502 VNLTEVY 508
Cdd:cd17933 149 VELTEVF 155
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
343-486 |
7.03e-43 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 151.99 E-value: 7.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 343 QKEALQTAINSKVMLLTGGPGTGKTTVIKGIVELYAEIHGLSldyddyvnddYPVVLAAPTGRASKRLQESTGLEAMTIH 422
Cdd:pfam13245 1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGVS----------FPILLAAPTGRAAKRLSERTGLPASTIH 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690900 423 RLIGWNQDTKPEDIL--ENEINARLIIIDEMSMVDTWLFHQFLSAVPLDAQLIFVGDEDQLPSVGP 486
Cdd:pfam13245 71 RLLGFDDLEAGGFLRdeEEPLDGDLLIVDEFSMVDLPLAYRLLKALPDGAQLLLVGDPDQLPSVGP 136
|
|
| recD |
PRK10875 |
exodeoxyribonuclease V subunit alpha; |
399-737 |
6.75e-20 |
|
exodeoxyribonuclease V subunit alpha;
Pssm-ID: 236783 [Multi-domain] Cd Length: 615 Bit Score: 94.62 E-value: 6.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 399 LAAPTGRASKRLQESTGL-----------------EAMTIHRLIGWNQDTKPediL----ENEINARLIIIDEMSMVDTW 457
Cdd:PRK10875 204 LAAPTGKAAARLTESLGKalrqlpltdeqkkripeEASTLHRLLGAQPGSQR---LryhaGNPLHLDVLVVDEASMVDLP 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 458 LFHQFLSAVPLDAQLIFVGDEDQLPSVGPGQVFKDLI--------------------------ESKAIPRVN-----LTE 506
Cdd:PRK10875 281 MMARLIDALPPHARVIFLGDRDQLASVEAGAVLGDICrfaeagysaeraqqlsrltgchlpagTGTEAASVRdslclLRK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 507 VYRQQDGSSIIELAHRMKLGQKIDITQRFHDR-SFINC----QANQIPTVVEKVVT------SAVNKGYTMADI------ 569
Cdd:PRK10875 361 SYRFGSDSGIGQLAAAVNRGDKRAAKAVFQQGfSDIEKrplqSGEDYQAMLEEALAgygrylDLLAARAEPEAIlaafnr 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 570 -QVLAPMYKGNAGIKRLNQVLQDILNPKKKDTREIEfgdvVFRKGdkvlqLVNRP-----NDNI---FNGDIGVivgifw 640
Cdd:PRK10875 441 yQLLCALREGPFGVAGLNERIEQALQQKRLIRRPSG----PHSRW-----YEGRPvmiarNDSAlglFNGDIGI------ 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 641 akenALNKD--VLVVDF---EGNEITFTKQDMMELTHAYCTSIHKSQGSEF--PIVIMPivKQYFRMLQRPILYTGLTRA 713
Cdd:PRK10875 506 ----ALDRGqgELRVWFqlpDGNIKSVQPSRLPEHETAWAMTVHKSQGSEFdhTALVLP--NQFTPVVTRELVYTAITRA 579
|
410 420
....*....|....*....|....
gi 616690900 714 KTSLVLLGDPEAFDIGLKTNGQAR 737
Cdd:PRK10875 580 RRRLSLYADERVLSAAIATRTERR 603
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recD_rel |
TIGR01448 |
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ... |
12-745 |
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: 1110.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 12 IKGTVEAILFQNSDNFYTVLKVDTIETNEDfdTMPTVVGFLPNIVEGDVYTFKGQVVDHPRYGKQLKAETFEKEMPQTKE 91
Cdd:TIGR01448 1 FSGTVEKILFENSTNFYVVLAVLRDETGED--TDATVVGVLPPLDEGDTYTFEGQWEEHAKYGYQFRAERMELEAPTSKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 92 AIISYLSSDLFKGVGKKTAQNIVNTLGDNAINDILDDHSVLEKVSGLSKKKQKQIAEQISANQESEKIMIRLHDLGFGPK 171
Cdd:TIGR01448 79 GIVAYLSSRSIKGVGKKLAQRIVKTFGEAAFDVLDDDPEKLLEVPGISKANLEKFVSQWSQQGDERRLLAGLQGLGIGIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 172 LSMAIYQFYLGDTLTILDRNPYQLIYDIKGIGFNKADQLARNIGIAYNDNERLKAALLYTLEEECIKQGHTYLPINVVID 251
Cdd:TIGR01448 159 LAQRIYKFYQADTLDRVEKDPYLLAEDVKGIGFLTADQLAQALGIALNDPRRITAGLVYSLQQACTEEGHTYLPRNRFIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 252 LTVDVLNYQ-DEEVIEPEKLDEMLQYLNEEKRLIIDNEQVAIPSLYYSEIKSVQNLFRIKTHTNKLTEIEQsdlQMHIGE 330
Cdd:TIGR01448 239 QVVHLLNVQpQERLLVPEAVELERLYLDEEPKLAAEDGRIYLPSLFRAEKQIASHIRRLLATSPAIGAIND---QEHIWE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 331 IEDANQVNYAASQKEALQTAINSKVMLLTGGPGTGKTTVIKGIVELYAEIHGLsldyddyvnddYPVVLAAPTGRASKRL 410
Cdd:TIGR01448 316 VEKKLRKGLSEEQKQALDTAIQHKVVILTGGPGTGKTTITRAIIELAEELGGL-----------LPVGLAAPTGRAAKRL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 411 QESTGLEAMTIHRLIGWNQDTKPEDILENEINARLIIIDEMSMVDTWLFHQFLSAVPLDAQLIFVGDEDQLPSVGPGQVF 490
Cdd:TIGR01448 385 GEVTGLTASTIHRLLGYGPDTFRHNHLEDPIDCDLLIVDESSMMDTWLALSLLAALPDHARLLLVGDTDQLPSVGPGQVL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 491 KDLIESKAIPRVNLTEVYRQQDGSSIIELAHRMKLGQ---KIDITQRFHDRSFINCQANQIPTVVEKVVTSAVNKGYTMA 567
Cdd:TIGR01448 465 KDLILSQAIPVTRLTKVYRQAAGSPIITLAHGILHGEapaWGDFKFLNLTRSEPEGAARHIPLMVEKIVGMARVGGIPGA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 568 DIQVLAPMYKGNAGIKRLNQVLQDILNPKKKDTREIEFGDVVFRKGDKVLQLVNRPNDNIFNGDIGVIVGIFWAKENalN 647
Cdd:TIGR01448 545 DIQVLAPMYKGPLGIDALNQHLQALLNPYQKGQGGIEIAEGEYRKGDRVMQTKNDYNNEIFNGDLGMIVKIEGAKQG--K 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 648 KDVLVVDFEGNEITFTKQDMMELTHAYCTSIHKSQGSEFPIVIMPIVKQYFRMLQRPILYTGLTRAKTSLVLLGDPEAFD 727
Cdd:TIGR01448 623 KDQVVVDFDGNEVELTRAELFNLTLAYATSIHKSQGSEFPTVILPIHTAHMRMLYRNLLYTALTRAKKRVILVGSAEAFD 702
|
730
....*....|....*...
gi 616690900 728 IGLKTNGQARLTQLCTLL 745
Cdd:TIGR01448 703 IAAARQGQARNTGLLERI 720
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
185-746 |
5.15e-135 |
|
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: 411.29 E-value: 5.15e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 185 LTILDRNPYQLIYDIkGIgFnkADQLARnigiaynDNERLKAALLYTLEEEcikqGHTYLPINVVIDLTVDVlnyqdeev 264
Cdd:COG0507 2 LEIREAWAEQGIYRI-GI-F--ADFIAR-------DDPIRAAALLSRAAGE----GHTFPLEDLAAARLLGV-------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 265 iePEKLDEMLQYLNEEKRLIIDNEQvAIPSLYYSEIKSVQNLFRIKTHtnkltEIEQSDLQMHIGEIEDANQVNYAASQK 344
Cdd:COG0507 59 --AEDIEAALAALVESGPLVLDGRR-YLTRLLEAEQRLARRLRRLARP-----ALDEADVEAALAALEPRAGITLSDEQR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 345 EALQTAIN-SKVMLLtggpgtgkttVIKGIVELYAEIHGlsldyddyvnddyPVVLAAPTGRASKRLQESTGLEAMTIHR 423
Cdd:COG0507 131 EAVALALTtRRVSVLtggagtgkttTLRALLAALEALGL-------------RVALAAPTGKAAKRLSESTGIEARTIHR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 424 LIGWNQDT-KPEDILENEIN-ARLIIIDEMSMVDTWLFHQFLSAVPL-DAQLIFVGDEDQLPSVGPGQVFKDLIESKAIP 500
Cdd:COG0507 198 LLGLRPDSgRFRHNRDNPLTpADLLVVDEASMVDTRLMAALLEALPRaGARLILVGDPDQLPSVGAGAVLRDLIESGTVP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 501 RVNLTEVYRQQDGSSIIELAHRMKLGQ-KIDITQRFHDRSFINCQANQipTVVEKVVTSAVNKGYTMADIQVLAPMykgN 579
Cdd:COG0507 278 VVELTEVYRQADDSRIIELAHAIREGDaPEALNARYADVVFVEAEDAE--EAAEAIVELYADRPAGGEDIQVLAPT---N 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 580 AGIKRLNQVLQDILNPKKKDTRE-IEFGDVVFRKGDKVLQLVNRPNDNIFNGDIGVIVGIfwakenALNKDVLVVDFEGN 658
Cdd:COG0507 353 AGVDALNQAIREALNPAGELERElAEDGELELYVGDRVMFTRNDYDLGVFNGDIGTVLSI------DEDEGRLTVRFDGR 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 659 E-ITFTKQDMMELTHAYCTSIHKSQGSEFPIVIMPIVKQYFRMLQRPILYTGLTRAKTSLVLLGDPEAFDIGLKTNGQaR 737
Cdd:COG0507 427 EiVTYDPSELDQLELAYAITVHKSQGSTFDRVILVLPSEHSPLLSRELLYTALTRARELLTLVGDRDALARAVRRDTA-R 505
|
....*....
gi 616690900 738 LTQLCTLLK 746
Cdd:COG0507 506 ATGLAERLR 514
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
343-508 |
1.32e-50 |
|
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: 174.28 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 343 QKEALQTAINSKVMLLTggpgtgkttVIKGIVELYAEihglsldyddyvnDDYPVVLAAPTGRASKRLQESTGLEAMTIH 422
Cdd:cd17933 2 QKAAVRLVLRNRVSVLTggagtgkttTLKALLAALEA-------------EGKRVVLAAPTGKAAKRLSESTGIEASTIH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 423 RLIGWNQDTKPEDIL-ENEINARLIIIDEMSMVDTWLFHQFLSAVPLDAQLIFVGDEDQLPSVGPGQVFKDLIESKAIPR 501
Cdd:cd17933 69 RLLGINPGGGGFYYNeENPLDADLLIVDEASMVDTRLMAALLSAIPAGARLILVGDPDQLPSVGAGNVLRDLIASKGVPT 148
|
....*..
gi 616690900 502 VNLTEVY 508
Cdd:cd17933 149 VELTEVF 155
|
|
| recD |
TIGR01447 |
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ... |
397-735 |
3.81e-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: 171.48 E-value: 3.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 397 VVLAAPTGRASKRLQESTG-----------------LEAMTIHRLIGWNQDTK-PEDILENEINARLIIIDEMSMVDTWL 458
Cdd:TIGR01447 195 IALAAPTGKAAARLAESLRkavknlaaaealiaalpSEAVTIHRLLGIKPDTKrFRHHERNPLPLDVLVVDEASMVDLPL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 459 FHQFLSAVPLDAQLIFVGDEDQLPSVGPGQVFKDL---------IESKAIPRVN-------------LTEVYRQQDGSSI 516
Cdd:TIGR01447 275 MAKLLKALPPNTKLILLGDKNQLPSVEAGAVLGDLcelasigksILYALCKKINsktrnplsdnvcfLKTSHRFGKDSGI 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 517 IELAHRMKLG---QKIDITQRFHDRS--FINCQANQIPTVVEKVV------------TSAVNKGYTMADIQVLAPMYKGN 579
Cdd:TIGR01447 355 GQLAKAINSGdieAVLNNLRSGQLIEfeFLNSKEDAIERLKNLYVkyrtflqklaalSDAKEILETFDRLRLLTALRDGP 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 580 AGIKRLNQVLQDILNPKKKDTREIEfgdvvFRKGDKVLQLVNRPNDNIFNGDIGVIvgifwakeNALNKDVLVVDFEG-- 657
Cdd:TIGR01447 435 FGVLGLNRRIEQELQEKYFDPDEEG-----WYIGRPIMVTENDYTLGLFNGDIGVL--------LRDPDGILTVWFHFad 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 658 NEITFTKQDMMELTHAYCTSIHKSQGSEFP--IVIMPivKQYFRMLQRPILYTGLTRAKTSLVLLGDPEAFDIGLKTNGQ 735
Cdd:TIGR01447 502 GSKAVLPSRLPNYETAFAMTVHKSQGSEFDhvILILP--NGNSPVLTRELLYTGITRAKDQLSVWSDKETLNAAIKRKNK 579
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
343-486 |
7.03e-43 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 151.99 E-value: 7.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 343 QKEALQTAINSKVMLLTGGPGTGKTTVIKGIVELYAEIHGLSldyddyvnddYPVVLAAPTGRASKRLQESTGLEAMTIH 422
Cdd:pfam13245 1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGVS----------FPILLAAPTGRAAKRLSERTGLPASTIH 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690900 423 RLIGWNQDTKPEDIL--ENEINARLIIIDEMSMVDTWLFHQFLSAVPLDAQLIFVGDEDQLPSVGP 486
Cdd:pfam13245 71 RLLGFDDLEAGGFLRdeEEPLDGDLLIVDEFSMVDLPLAYRLLKALPDGAQLLLVGDPDQLPSVGP 136
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
339-543 |
1.31e-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: 153.49 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 339 YAASQKEALQTAINS--KVMLLTGGPGTGKTTVIKGIVELYAEIHGlsldyddyvnddyPVVLAAPTGRASKRLQESTGL 416
Cdd:pfam13604 2 LNAEQAAAVRALLTSgdRVAVLVGPAGTGKTTALKALREAWEAAGY-------------RVIGLAPTGRAAKVLGEELGI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 417 EAMTIHRLIGWNQDTKPEDileneiNARLIIIDEMSMVDTWLFHQFLSAVP-LDAQLIFVGDEDQLPSVGPGQVFKDLIe 495
Cdd:pfam13604 69 PADTIAKLLHRLGGRAGLD------PGTLLIVDEAGMVGTRQMARLLKLAEdAGARVILVGDPRQLPSVEAGGAFRDLL- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 616690900 496 SKAIPRVNLTEVYRQQDgSSIIELAHRMKLGQKIDITQRFHDRSFINC 543
Cdd:pfam13604 142 AAGIGTAELTEIVRQRD-PWQRAASLALRDGDPAEALDALADRGRIHE 188
|
|
| HHH_4 |
pfam14490 |
Helix-hairpin-helix containing domain; This presumed domain contains at least one ... |
152-243 |
5.36e-33 |
|
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: 122.22 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 152 ANQESEKIMIRLHDLGFGPKLSMAIYQFYLGDTLTILDRNPYQLIYDIKGIGFNKADQLARNIGIAYNDNERLKAALLYT 231
Cdd:pfam14490 1 EQRGLREVMIFLQQYGISPALAVKIYKKYGEDALEILKENPYRLAEDIEGIGFKTADKIARKLGIAPDSPERIRAGILYV 80
|
90
....*....|..
gi 616690900 232 LEEECiKQGHTY 243
Cdd:pfam14490 81 LKQAA-SNGHTY 91
|
|
| TraA_Ti |
TIGR02768 |
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a ... |
397-726 |
1.42e-22 |
|
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: 103.73 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 397 VVLAAPTGRASKRLQESTGLEAMTIHRL-IGWNQDtkpEDILENeinARLIIIDEMSMVDTWLFHQFLS-AVPLDAQLIF 474
Cdd:TIGR02768 399 VIGAALSGKAAEGLQAESGIESRTLASLeYAWANG---RDLLSD---KDVLVIDEAGMVGSRQMARVLKeAEEAGAKVVL 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 475 VGDEDQLPSVGPGQVFKDLIESkaIPRVNLTEVYRQQDG---SSIIELAhRMKLGQKIditQRFHDRSFINcQANQIPTV 551
Cdd:TIGR02768 473 VGDPEQLQPIEAGAAFRAIAER--IGYAELETIRRQREAwarQASLELA-RGDVEKAL---AAYRDHGHIT-IHDTREEA 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 552 VEKVVTS--AVNKGYTMADIQVLapMYKGNAGIKRLNQVLQDILNPKKKDTREIEF----GDVVFRKGDKVLQLVNRPND 625
Cdd:TIGR02768 546 IEQVVADwkQDLREANPAGSQIM--LAHTRKDVRALNEAAREALIERGELGESILFqtarGERKFAAGDRIVFLENNRDL 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 626 NIFNGDIGVIVGIfwakenalNKDVLVVDF-EGNEITFTKQDMMELTHAYCTSIHKSQGSefpivimpIVKQYF----RM 700
Cdd:TIGR02768 624 GVKNGMLGTVEEI--------EDGRLVVQLdSGELVIIPQAEYDALDHGYATTIHKSQGV--------TVDRAFvlasKS 687
|
330 340
....*....|....*....|....*.
gi 616690900 701 LQRPILYTGLTRAKTSLVLLGDPEAF 726
Cdd:TIGR02768 688 MDRHLAYVAMTRHRESVQLYAGKEDF 713
|
|
| SH3_13 |
pfam18335 |
ATP-dependent RecD-like DNA helicase SH3 domain; This is an SH3 (SRC homology domain 3) domain ... |
585-655 |
1.85e-22 |
|
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: 91.38 E-value: 1.85e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690900 585 LNQVLQDILNPKKKDTREIEFGDVVFRKGDKVLQLVNRPNDNIFNGDIGVIVGIfwakenALNKDVLVVDF 655
Cdd:pfam18335 1 LNQRLQEALNPPSPGKKEIKFGGRIFRVGDKVMQTKNNYDLGVFNGDIGIIVAI------DKEEKTLTVDF 65
|
|
| recD |
PRK10875 |
exodeoxyribonuclease V subunit alpha; |
399-737 |
6.75e-20 |
|
exodeoxyribonuclease V subunit alpha;
Pssm-ID: 236783 [Multi-domain] Cd Length: 615 Bit Score: 94.62 E-value: 6.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 399 LAAPTGRASKRLQESTGL-----------------EAMTIHRLIGWNQDTKPediL----ENEINARLIIIDEMSMVDTW 457
Cdd:PRK10875 204 LAAPTGKAAARLTESLGKalrqlpltdeqkkripeEASTLHRLLGAQPGSQR---LryhaGNPLHLDVLVVDEASMVDLP 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 458 LFHQFLSAVPLDAQLIFVGDEDQLPSVGPGQVFKDLI--------------------------ESKAIPRVN-----LTE 506
Cdd:PRK10875 281 MMARLIDALPPHARVIFLGDRDQLASVEAGAVLGDICrfaeagysaeraqqlsrltgchlpagTGTEAASVRdslclLRK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 507 VYRQQDGSSIIELAHRMKLGQKIDITQRFHDR-SFINC----QANQIPTVVEKVVT------SAVNKGYTMADI------ 569
Cdd:PRK10875 361 SYRFGSDSGIGQLAAAVNRGDKRAAKAVFQQGfSDIEKrplqSGEDYQAMLEEALAgygrylDLLAARAEPEAIlaafnr 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 570 -QVLAPMYKGNAGIKRLNQVLQDILNPKKKDTREIEfgdvVFRKGdkvlqLVNRP-----NDNI---FNGDIGVivgifw 640
Cdd:PRK10875 441 yQLLCALREGPFGVAGLNERIEQALQQKRLIRRPSG----PHSRW-----YEGRPvmiarNDSAlglFNGDIGI------ 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 641 akenALNKD--VLVVDF---EGNEITFTKQDMMELTHAYCTSIHKSQGSEF--PIVIMPivKQYFRMLQRPILYTGLTRA 713
Cdd:PRK10875 506 ----ALDRGqgELRVWFqlpDGNIKSVQPSRLPEHETAWAMTVHKSQGSEFdhTALVLP--NQFTPVVTRELVYTAITRA 579
|
410 420
....*....|....*....|....
gi 616690900 714 KTSLVLLGDPEAFDIGLKTNGQAR 737
Cdd:PRK10875 580 RRRLSLYADERVLSAAIATRTERR 603
|
|
| SF1_C_RecD |
cd18809 |
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ... |
672-721 |
5.99e-15 |
|
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: 70.28 E-value: 5.99e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 616690900 672 HAYCTSIHKSQGSEFPIVIMPIVKQyFRMLQRPILYTGLTRAKTSLVLLG 721
Cdd:cd18809 32 QAYAMTIHKSQGSEFDRVIVVLPTS-HPMLSRGLLYTALTRARKLLTLVG 80
|
|
| UvrD_C_2 |
pfam13538 |
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ... |
672-720 |
1.79e-13 |
|
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: 65.29 E-value: 1.79e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 616690900 672 HAYCTSIHKSQGSEFPIVIM--PIVKQYFR-MLQRPILYTGLTRAKTSLVLL 720
Cdd:pfam13538 1 LAYALTVHKAQGSEFPAVFLvdPDLTAHYHsMLRRRLLYTAVTRARKKLVLV 52
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
619-721 |
2.11e-08 |
|
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: 52.05 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 619 LVNRPNDNIfngDIGVIVgifwakenALNKDVLVVDfegNEITFTKQDMMELTHAYCTSIHKSQGSEFPIVIMPIVKQyf 698
Cdd:cd18786 3 IVNAANGLY---KGVVLT--------PYHRDRAYLN---QYLQGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTA-- 66
|
90 100
....*....|....*....|...
gi 616690900 699 RMLQRPILYTGLTRAKTSLVLLG 721
Cdd:cd18786 67 NSLTPRRLYVALTRARKRLVIYD 89
|
|
| PRK13709 |
PRK13709 |
conjugal transfer nickase/helicase TraI; Provisional |
396-512 |
2.88e-07 |
|
conjugal transfer nickase/helicase TraI; Provisional
Pssm-ID: 237478 [Multi-domain] Cd Length: 1747 Bit Score: 54.41 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 396 PVVLA-APTGRASKRLQeSTGLEAMTIHRLI-GWNQDT----KPEdileneINARLIIIDEMSMV---DTWLFHQFLSAV 466
Cdd:PRK13709 1017 PRVVGlGPTHRAVGEMR-SAGVDAQTLASFLhDTQLQQrsgeTPD------FSNTLFLLDESSMVgntDMARAYALIAAG 1089
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 616690900 467 plDAQLIFVGDEDQLPSVGPGQVFKDLIESKAIPRVNLTEVYRQQD 512
Cdd:PRK13709 1090 --GGRAVSSGDTDQLQAIAPGQPFRLMQTRSAADVAIMKEIVRQTP 1133
|
|
| PRK13826 |
PRK13826 |
Dtr system oriT relaxase; Provisional |
397-719 |
3.13e-07 |
|
Dtr system oriT relaxase; Provisional
Pssm-ID: 237524 [Multi-domain] Cd Length: 1102 Bit Score: 54.40 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 397 VVLAAPTGRASKRLQESTGLEAMTIHRL-IGWNQDtkpEDILENEInarLIIIDEMSMVDTWLFHQFLSAVP-LDAQLIF 474
Cdd:PRK13826 428 VVGGALAGKAAEGLEKEAGIQSRTLSSWeLRWNQG---RDQLDNKT---VFVLDEAGMVASRQMALFVEAVTrAGAKLVL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 475 VGDEDQLPSVGPGQVFKDLIESkaIPRVNLTEVYRQQ-----DGSsiIELAhRMKLGQKIDiTQRFHDR---SFINCQAn 546
Cdd:PRK13826 502 VGDPEQLQPIEAGAAFRAIADR--IGYAELETIYRQReqwmrDAS--LDLA-RGNVGKALD-AYRANGRvigSRLKAEA- 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 547 qiptvVEKVVtSAVNKGYTMAD-IQVLAPMYKgnaGIKRLNQVLQDILNPK----KKDTREIEFGDVVFRKGDKVLQLVN 621
Cdd:PRK13826 575 -----VESLI-ADWNRDYDPTKtTLILAHLRR---DVRMLNEMARAKLVERgivgEGHAFRTADGERRFAAGDQIVFLKN 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 622 RPNDNIFNGDIGVIVgifwakENALNKDVLVVDfEGN---EITFTKQDMMELTHAYCTSIHKSQGSefpivIMPIVKQYF 698
Cdd:PRK13826 646 EGSLGVKNGMIGKVV------EAAPNRIVAEIG-EGEhrrQVTVEQRFYNNLDHGYATTIHKSQGA-----TVDRVKVLA 713
|
330 340
....*....|....*....|..
gi 616690900 699 RM-LQRPILYTGLTRAKTSLVL 719
Cdd:PRK13826 714 SLsLDRHLTYVAMTRHREDLQL 735
|
|
| DEXSc_Pif1_like |
cd18037 |
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ... |
343-509 |
1.29e-05 |
|
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: 46.47 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 343 QKEALQTAINSKVMLLTGGPGTGKTTVIKGIVELYAEihglsldyddyvnDDYPVVLAAPTGRAskrlqeSTGLEAMTIH 422
Cdd:cd18037 2 QRRVLDLVLDGKNVFFTGSAGTGKSYLLRRIIRALPS-------------RPKRVAVTASTGIA------ACNIGGTTLH 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 423 RLIGWN-QDTKPEDILENE----------INARLIIIDEMSMVDTWLF---HQFLSAVPLDA------QLIFVGDEDQLP 482
Cdd:cd18037 63 SFAGIGlGSEPAEDLLERVkrspylvqrwRKCDVLIIDEISMLDADLFdklDRVAREVRGSDkpfggiQLILCGDFLQLP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 616690900 483 SVGPGQ---------VFKDLIESKAIPRVN-----LTEVYR 509
Cdd:cd18037 143 PVTKNSerqafffrgDQQFCFEAKSWERCIfltveLTKVFR 183
|
|
| RecB |
COG1074 |
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, ... |
677-721 |
4.13e-05 |
|
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: 47.26 E-value: 4.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 616690900 677 SIHKSQGSEFPIVIMPIVKQYFRMLQ-----RpILYTGLTRAKTSLVLLG 721
Cdd:COG1074 649 TIHKSKGLEFPVVFLPALRERARAEElaeelR-LLYVALTRARDRLVLSG 697
|
|
| TraI_TIGR |
TIGR02760 |
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome ... |
401-511 |
5.17e-05 |
|
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: 47.21 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690900 401 APTGRASKRLqESTGLEAMTIHRLIGWNQDTK--PEDilenEINArLIIIDEMSMVDTWLFHQF--LSAVPlDAQLIFVG 476
Cdd:TIGR02760 1075 APTHEAVGEL-KSAGVQAQTLDSFLTDISLYRnsGGD----FRNT-LFILDESSMVSNFQLTHAteLVQKS-GSRAVSLG 1147
|
90 100 110
....*....|....*....|....*....|....*
gi 616690900 477 DEDQLPSVGPGQVFKDLIESKAIPRVNLTEVYRQQ 511
Cdd:TIGR02760 1148 DIAQLQSLAAGKPFELAITFDIIDTAIMKEIVRQN 1182
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| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
444-492 |
7.95e-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: 40.16 E-value: 7.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 616690900 444 RLIIIDEMSMVDTWLFHQFLSAVPLDAQLIFVGDEDQLPSVGPGQVFKD 492
Cdd:cd17914 48 DNILVDEAAQILEPETSRLIDLALDQGRVILVGDHDQLGPVWRGAVLAK 96
|
|
| COG3972 |
COG3972 |
Superfamily I DNA and RNA helicases [Replication, recombination and repair]; |
676-728 |
2.06e-03 |
|
Superfamily I DNA and RNA helicases [Replication, recombination and repair];
Pssm-ID: 443172 [Multi-domain] Cd Length: 565 Bit Score: 41.74 E-value: 2.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 616690900 676 TSIHKSQGSEFPIVIMP----IVKQYFRMLQRPILYTGLTRAKTSLVLLGDPEAFDI 728
Cdd:COG3972 492 STIHRAKGLEAPVVIIVgldqLAKGESLERLRNLLYVAMTRARGWLVVSGSGESMAE 548
|
|
| SF1_C_UvrD |
cd18807 |
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ... |
677-721 |
2.39e-03 |
|
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: 39.14 E-value: 2.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690900 677 SIHKSQGSEFPIVIMPIVKQYFRMLQ----------------RPILYTGLTRAKTSLVLLG 721
Cdd:cd18807 90 TIHASKGLEFPVVFIVGLGEGFIPSDasyhaakedeerleeeRRLLYVALTRAKKELYLVG 150
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