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Conserved domains on  [gi|446698615|ref|WP_000775961|]
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MULTISPECIES: exodeoxyribonuclease V subunit alpha [Enterobacteriaceae]

Protein Classification

exodeoxyribonuclease V subunit alpha( domain architecture ID 11485051)

exodeoxyribonuclease V subunit alpha is the RecD subunit of the RecBCD complex, which is involved in homologous double-strand break repair

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
recD PRK10875
exodeoxyribonuclease V subunit alpha;
3-608 0e+00

exodeoxyribonuclease V subunit alpha;


:

Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 1126.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615   3 LQKQLLEAVEHKQLRPLDVQFALTVAGDEHPAVTLAAALLSHDAGEGHVCLPLSRLENN---EASHPLLATCVSEI-GEL 78
Cdd:PRK10875   1 MQKLLLQAVEQKLLRPLDVQFALMVAGDEDPALTLAAALLSADAGEGHVCLPLSRLQPEylfEGRHPELAQALWEAaGEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  79 QNWEECLLASQAVSRGDEPTPMILCGDRLYLNRMWCNERTVARFFNEVNHAIEVDEALLAQTLDKLF-PVSDEINWQKVA 157
Cdd:PRK10875  81 QDWQEALLASPAVSDGDQPTPLVLCGDRLYLQRMWQNERTVARFFNEVNHAIEVDEALLRQTLDALFgPVTDEVDWQKVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 158 AAVALTRRISVISGGPGTGKTTTVAKLLAALIQMADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEDA 237
Cdd:PRK10875 161 AAVALTRRISVISGGPGTGKTTTVAKLLAALIQLADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEEA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 238 STLHRLLGAQPGSQRLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASVEAGAVLGDICAYA 317
Cdd:PRK10875 241 STLHRLLGAQPGSQRLRYHAGNPLHLDVLVVDEASMVDLPMMARLIDALPPHARVIFLGDRDQLASVEAGAVLGDICRFA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 318 NAGFTAERARQLSRLTGTHVPAGTGTEAASLRDSLCLLQKSYRFGSDSGIGQLAAAINSGDKTAVKTVFQQDFTDIEKRL 397
Cdd:PRK10875 321 EAGYSAERAQQLSRLTGCHLPAGTGTEAASVRDSLCLLRKSYRFGSDSGIGQLAAAVNRGDKRAAKAVFQQGFSDIEKRP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 398 LQSGEDYIAMLEEALAGYGRYLDLLQARAEPDLIIQAFNEYQLLCALREGPFGVAGLNERIEQFMQQKRKIHRH--PHSR 475
Cdd:PRK10875 401 LQSGEDYQAMLEEALAGYGRYLDLLAARAEPEAILAAFNRYQLLCALREGPFGVAGLNERIEQALQQKRLIRRPsgPHSR 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 476 WYEGRPVMIARNDSALGLFNGDIGIALDRGQGT-RVWFAMPDGNIKSVQPSRLPEHETTWAMTVHKSQGSEFDHAALILP 554
Cdd:PRK10875 481 WYEGRPVMIARNDSALGLFNGDIGIALDRGQGElRVWFQLPDGNIKSVQPSRLPEHETAWAMTVHKSQGSEFDHTALVLP 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446698615 555 SQRTPVVTRELVYTAVTRARRRLSLYADERILSAAIATRTERRSGLAALFSSRE 608
Cdd:PRK10875 561 NQFTPVVTRELVYTAITRARRRLSLYADERVLSAAIATRTERRSGLAARLSSRA 614
 
Name Accession Description Interval E-value
recD PRK10875
exodeoxyribonuclease V subunit alpha;
3-608 0e+00

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 1126.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615   3 LQKQLLEAVEHKQLRPLDVQFALTVAGDEHPAVTLAAALLSHDAGEGHVCLPLSRLENN---EASHPLLATCVSEI-GEL 78
Cdd:PRK10875   1 MQKLLLQAVEQKLLRPLDVQFALMVAGDEDPALTLAAALLSADAGEGHVCLPLSRLQPEylfEGRHPELAQALWEAaGEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  79 QNWEECLLASQAVSRGDEPTPMILCGDRLYLNRMWCNERTVARFFNEVNHAIEVDEALLAQTLDKLF-PVSDEINWQKVA 157
Cdd:PRK10875  81 QDWQEALLASPAVSDGDQPTPLVLCGDRLYLQRMWQNERTVARFFNEVNHAIEVDEALLRQTLDALFgPVTDEVDWQKVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 158 AAVALTRRISVISGGPGTGKTTTVAKLLAALIQMADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEDA 237
Cdd:PRK10875 161 AAVALTRRISVISGGPGTGKTTTVAKLLAALIQLADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEEA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 238 STLHRLLGAQPGSQRLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASVEAGAVLGDICAYA 317
Cdd:PRK10875 241 STLHRLLGAQPGSQRLRYHAGNPLHLDVLVVDEASMVDLPMMARLIDALPPHARVIFLGDRDQLASVEAGAVLGDICRFA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 318 NAGFTAERARQLSRLTGTHVPAGTGTEAASLRDSLCLLQKSYRFGSDSGIGQLAAAINSGDKTAVKTVFQQDFTDIEKRL 397
Cdd:PRK10875 321 EAGYSAERAQQLSRLTGCHLPAGTGTEAASVRDSLCLLRKSYRFGSDSGIGQLAAAVNRGDKRAAKAVFQQGFSDIEKRP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 398 LQSGEDYIAMLEEALAGYGRYLDLLQARAEPDLIIQAFNEYQLLCALREGPFGVAGLNERIEQFMQQKRKIHRH--PHSR 475
Cdd:PRK10875 401 LQSGEDYQAMLEEALAGYGRYLDLLAARAEPEAILAAFNRYQLLCALREGPFGVAGLNERIEQALQQKRLIRRPsgPHSR 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 476 WYEGRPVMIARNDSALGLFNGDIGIALDRGQGT-RVWFAMPDGNIKSVQPSRLPEHETTWAMTVHKSQGSEFDHAALILP 554
Cdd:PRK10875 481 WYEGRPVMIARNDSALGLFNGDIGIALDRGQGElRVWFQLPDGNIKSVQPSRLPEHETAWAMTVHKSQGSEFDHTALVLP 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446698615 555 SQRTPVVTRELVYTAVTRARRRLSLYADERILSAAIATRTERRSGLAALFSSRE 608
Cdd:PRK10875 561 NQFTPVVTRELVYTAITRARRRLSLYADERVLSAAIATRTERRSGLAARLSSRA 614
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
7-598 0e+00

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: 554.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615    7 LLEAVEHKQLRPLDVQFAL---TVAGDEHPAVTLAAALLSHDAGEGHVCLPLSRLENNeASHPLLATCVSEIGELQNWEE 83
Cdd:TIGR01447   1 LKKLVQQGVLRPLDVAFAQflqHLAQKSNEEVALFAAVASALLRRGHPCLDLEKAAKS-PGLTGISEPDLGEKLNFDWLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615   84 CLLASQAVSRGDEPTPMI-LCGDRLYLNRMWCNERTVARFFNEVNHAieVDEALLAQTLDKLFPVSDEINWQKVAAAVAL 162
Cdd:TIGR01447  80 ALPASVLVGLPGETAPPLvLCDGRLYLRRYWREEEKLAAKLRTLLEA--RKRTAPSAILENLFPLLNEQNWRKTAVALAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  163 TRRISVISGGPGTGKTTTVAKLLAALI-QMADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEDASTLH 241
Cdd:TIGR01447 158 KSNFSLITGGPGTGKTTTVARLLLALVkQSPKQGKLRIALAAPTGKAAARLAESLRKAVKNLAAAEALIAALPSEAVTIH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  242 RLLGAQPGSQRLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASVEAGAVLGDICAYANAGF 321
Cdd:TIGR01447 238 RLLGIKPDTKRFRHHERNPLPLDVLVVDEASMVDLPLMAKLLKALPPNTKLILLGDKNQLPSVEAGAVLGDLCELASIGK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  322 TAERARQLSRLTGTHVPagtgteaasLRDSLCLLQKSYRFGSDSGIGQLAAAINSGDKTAVKTVfQQDFTDIEKRLLQSG 401
Cdd:TIGR01447 318 SILYALCKKINSKTRNP---------LSDNVCFLKTSHRFGKDSGIGQLAKAINSGDIEAVLNN-LRSGQLIEFEFLNSK 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  402 EDYIAMLEEALAGYGRYLDLLQARAEPDLIIQAFNEYQLLCALREGPFGVAGLNERIEQFMQQKRKihrHPHSR-WYEGR 480
Cdd:TIGR01447 388 EDAIERLKNLYVKYRTFLQKLAALSDAKEILETFDRLRLLTALRDGPFGVLGLNRRIEQELQEKYF---DPDEEgWYIGR 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  481 PVMIARNDSALGLFNGDIGIAL-DRGQGTRVWFAMPDGNiKSVQPSRLPEHETTWAMTVHKSQGSEFDHAALILPSQRTP 559
Cdd:TIGR01447 465 PIMVTENDYTLGLFNGDIGVLLrDPDGILTVWFHFADGS-KAVLPSRLPNYETAFAMTVHKSQGSEFDHVILILPNGNSP 543
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 446698615  560 VVTRELVYTAVTRARRRLSLYADERILSAAIATRTERRS 598
Cdd:TIGR01447 544 VLTRELLYTGITRAKDQLSVWSDKETLNAAIKRKNKRLS 582
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
23-603 9.21e-138

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: 9.21e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  23 FALTVAGDeHPAvtLAAALLSHDAGEGHVClPLSRLenneASHPLLatcvseiGELQNWEECLLAsqAVSRGdeptPMIL 102
Cdd:COG0507   19 FADFIARD-DPI--RAAALLSRAAGEGHTF-PLEDL----AAARLL-------GVAEDIEAALAA--LVESG----PLVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 103 CGDRlYLNRMWCNERTVARFFNEVNHAiEVDEALLAQTLDKLFPVS--DEINWQKVAAAVAL-TRRISVISggpgtgktt 179
Cdd:COG0507   78 DGRR-YLTRLLEAEQRLARRLRRLARP-ALDEADVEAALAALEPRAgiTLSDEQREAVALALtTRRVSVLT--------- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 180 tvAK-------LLAALIQMADGERCRIRLAAPTGKAAARLTESLGKalrqlpltdeqkkripeDASTLHRLLGAQPGSQR 252
Cdd:COG0507  147 --GGagtgkttTLRALLAALEALGLRVALAAPTGKAAKRLSESTGI-----------------EARTIHRLLGLRPDSGR 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 253 LRHHAGNPLH-LDVLVVDEASMIDLPMMSRLIDALP-DHARVIFLGDRDQLASVEAGAVLGDICAYANAGftaerarqls 330
Cdd:COG0507  208 FRHNRDNPLTpADLLVVDEASMVDTRLMAALLEALPrAGARLILVGDPDQLPSVGAGAVLRDLIESGTVP---------- 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 331 rltgthvpagtgteaaslrdsLCLLQKSYRFGSDSGIGQLAAAINSGDktaVKTVFQQDFTDIEKRLLQSGEDyiaMLEE 410
Cdd:COG0507  278 ---------------------VVELTEVYRQADDSRIIELAHAIREGD---APEALNARYADVVFVEAEDAEE---AAEA 330
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 411 ALAGYGRYLdllqaraepdliiQAFNEYQLLCALregPFGVAGLNERIEQFMQQ----KRKIHRHPHSRWYEGRPVMIAR 486
Cdd:COG0507  331 IVELYADRP-------------AGGEDIQVLAPT---NAGVDALNQAIREALNPagelERELAEDGELELYVGDRVMFTR 394
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 487 NDSALGLFNGDIGIALD-RGQGTRVWFAMPDGNIKSVQPSRLPEHETTWAMTVHKSQGSEFDHAALILPSQRTPVVTREL 565
Cdd:COG0507  395 NDYDLGVFNGDIGTVLSiDEDEGRLTVRFDGREIVTYDPSELDQLELAYAITVHKSQGSTFDRVILVLPSEHSPLLSREL 474
                        570       580       590
                 ....*....|....*....|....*....|....*...
gi 446698615 566 VYTAVTRARRRLSLYADERILSAAIATRTERRSGLAAL 603
Cdd:COG0507  475 LYTALTRARELLTLVGDRDALARAVRRDTARATGLAER 512
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
153-315 7.46e-45

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: 156.56  E-value: 7.46e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 153 WQKVAAAVALTRRISVISGGPGTGKTTTVAKLLAALIQMadgeRCRIRLAAPTGKAAARLTESLGKalrqlpltdeqkkr 232
Cdd:cd17933    1 EQKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALEAE----GKRVVLAAPTGKAAKRLSESTGI-------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 233 ipeDASTLHRLLGAQPGSQRLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASVEAGAVLGD 312
Cdd:cd17933   63 ---EASTIHRLLGINPGGGGFYYNEENPLDADLLIVDEASMVDTRLMAALLSAIPAGARLILVGDPDQLPSVGAGNVLRD 139

                 ...
gi 446698615 313 ICA 315
Cdd:cd17933  140 LIA 142
AAA_19 pfam13245
AAA domain;
154-304 4.68e-27

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 106.53  E-value: 4.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  154 QKVAAAVALTRRISVISGGPGTGKTTTVAKLLAALIQMADGERcRIRLAAPTGKAAARLTESLGKalrqlpltdeqkkri 233
Cdd:pfam13245   1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGVSF-PILLAAPTGRAAKRLSERTGL--------------- 64
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446698615  234 peDASTLHRLLGAQPGSQ-RLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASV 304
Cdd:pfam13245  65 --PASTIHRLLGFDDLEAgGFLRDEEEPLDGDLLIVDEFSMVDLPLAYRLLKALPDGAQLLLVGDPDQLPSV 134
 
Name Accession Description Interval E-value
recD PRK10875
exodeoxyribonuclease V subunit alpha;
3-608 0e+00

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 1126.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615   3 LQKQLLEAVEHKQLRPLDVQFALTVAGDEHPAVTLAAALLSHDAGEGHVCLPLSRLENN---EASHPLLATCVSEI-GEL 78
Cdd:PRK10875   1 MQKLLLQAVEQKLLRPLDVQFALMVAGDEDPALTLAAALLSADAGEGHVCLPLSRLQPEylfEGRHPELAQALWEAaGEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  79 QNWEECLLASQAVSRGDEPTPMILCGDRLYLNRMWCNERTVARFFNEVNHAIEVDEALLAQTLDKLF-PVSDEINWQKVA 157
Cdd:PRK10875  81 QDWQEALLASPAVSDGDQPTPLVLCGDRLYLQRMWQNERTVARFFNEVNHAIEVDEALLRQTLDALFgPVTDEVDWQKVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 158 AAVALTRRISVISGGPGTGKTTTVAKLLAALIQMADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEDA 237
Cdd:PRK10875 161 AAVALTRRISVISGGPGTGKTTTVAKLLAALIQLADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEEA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 238 STLHRLLGAQPGSQRLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASVEAGAVLGDICAYA 317
Cdd:PRK10875 241 STLHRLLGAQPGSQRLRYHAGNPLHLDVLVVDEASMVDLPMMARLIDALPPHARVIFLGDRDQLASVEAGAVLGDICRFA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 318 NAGFTAERARQLSRLTGTHVPAGTGTEAASLRDSLCLLQKSYRFGSDSGIGQLAAAINSGDKTAVKTVFQQDFTDIEKRL 397
Cdd:PRK10875 321 EAGYSAERAQQLSRLTGCHLPAGTGTEAASVRDSLCLLRKSYRFGSDSGIGQLAAAVNRGDKRAAKAVFQQGFSDIEKRP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 398 LQSGEDYIAMLEEALAGYGRYLDLLQARAEPDLIIQAFNEYQLLCALREGPFGVAGLNERIEQFMQQKRKIHRH--PHSR 475
Cdd:PRK10875 401 LQSGEDYQAMLEEALAGYGRYLDLLAARAEPEAILAAFNRYQLLCALREGPFGVAGLNERIEQALQQKRLIRRPsgPHSR 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 476 WYEGRPVMIARNDSALGLFNGDIGIALDRGQGT-RVWFAMPDGNIKSVQPSRLPEHETTWAMTVHKSQGSEFDHAALILP 554
Cdd:PRK10875 481 WYEGRPVMIARNDSALGLFNGDIGIALDRGQGElRVWFQLPDGNIKSVQPSRLPEHETAWAMTVHKSQGSEFDHTALVLP 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446698615 555 SQRTPVVTRELVYTAVTRARRRLSLYADERILSAAIATRTERRSGLAALFSSRE 608
Cdd:PRK10875 561 NQFTPVVTRELVYTAITRARRRLSLYADERVLSAAIATRTERRSGLAARLSSRA 614
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
7-598 0e+00

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: 554.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615    7 LLEAVEHKQLRPLDVQFAL---TVAGDEHPAVTLAAALLSHDAGEGHVCLPLSRLENNeASHPLLATCVSEIGELQNWEE 83
Cdd:TIGR01447   1 LKKLVQQGVLRPLDVAFAQflqHLAQKSNEEVALFAAVASALLRRGHPCLDLEKAAKS-PGLTGISEPDLGEKLNFDWLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615   84 CLLASQAVSRGDEPTPMI-LCGDRLYLNRMWCNERTVARFFNEVNHAieVDEALLAQTLDKLFPVSDEINWQKVAAAVAL 162
Cdd:TIGR01447  80 ALPASVLVGLPGETAPPLvLCDGRLYLRRYWREEEKLAAKLRTLLEA--RKRTAPSAILENLFPLLNEQNWRKTAVALAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  163 TRRISVISGGPGTGKTTTVAKLLAALI-QMADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEDASTLH 241
Cdd:TIGR01447 158 KSNFSLITGGPGTGKTTTVARLLLALVkQSPKQGKLRIALAAPTGKAAARLAESLRKAVKNLAAAEALIAALPSEAVTIH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  242 RLLGAQPGSQRLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASVEAGAVLGDICAYANAGF 321
Cdd:TIGR01447 238 RLLGIKPDTKRFRHHERNPLPLDVLVVDEASMVDLPLMAKLLKALPPNTKLILLGDKNQLPSVEAGAVLGDLCELASIGK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  322 TAERARQLSRLTGTHVPagtgteaasLRDSLCLLQKSYRFGSDSGIGQLAAAINSGDKTAVKTVfQQDFTDIEKRLLQSG 401
Cdd:TIGR01447 318 SILYALCKKINSKTRNP---------LSDNVCFLKTSHRFGKDSGIGQLAKAINSGDIEAVLNN-LRSGQLIEFEFLNSK 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  402 EDYIAMLEEALAGYGRYLDLLQARAEPDLIIQAFNEYQLLCALREGPFGVAGLNERIEQFMQQKRKihrHPHSR-WYEGR 480
Cdd:TIGR01447 388 EDAIERLKNLYVKYRTFLQKLAALSDAKEILETFDRLRLLTALRDGPFGVLGLNRRIEQELQEKYF---DPDEEgWYIGR 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  481 PVMIARNDSALGLFNGDIGIAL-DRGQGTRVWFAMPDGNiKSVQPSRLPEHETTWAMTVHKSQGSEFDHAALILPSQRTP 559
Cdd:TIGR01447 465 PIMVTENDYTLGLFNGDIGVLLrDPDGILTVWFHFADGS-KAVLPSRLPNYETAFAMTVHKSQGSEFDHVILILPNGNSP 543
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 446698615  560 VVTRELVYTAVTRARRRLSLYADERILSAAIATRTERRS 598
Cdd:TIGR01447 544 VLTRELLYTGITRAKDQLSVWSDKETLNAAIKRKNKRLS 582
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
23-603 9.21e-138

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: 9.21e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  23 FALTVAGDeHPAvtLAAALLSHDAGEGHVClPLSRLenneASHPLLatcvseiGELQNWEECLLAsqAVSRGdeptPMIL 102
Cdd:COG0507   19 FADFIARD-DPI--RAAALLSRAAGEGHTF-PLEDL----AAARLL-------GVAEDIEAALAA--LVESG----PLVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 103 CGDRlYLNRMWCNERTVARFFNEVNHAiEVDEALLAQTLDKLFPVS--DEINWQKVAAAVAL-TRRISVISggpgtgktt 179
Cdd:COG0507   78 DGRR-YLTRLLEAEQRLARRLRRLARP-ALDEADVEAALAALEPRAgiTLSDEQREAVALALtTRRVSVLT--------- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 180 tvAK-------LLAALIQMADGERCRIRLAAPTGKAAARLTESLGKalrqlpltdeqkkripeDASTLHRLLGAQPGSQR 252
Cdd:COG0507  147 --GGagtgkttTLRALLAALEALGLRVALAAPTGKAAKRLSESTGI-----------------EARTIHRLLGLRPDSGR 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 253 LRHHAGNPLH-LDVLVVDEASMIDLPMMSRLIDALP-DHARVIFLGDRDQLASVEAGAVLGDICAYANAGftaerarqls 330
Cdd:COG0507  208 FRHNRDNPLTpADLLVVDEASMVDTRLMAALLEALPrAGARLILVGDPDQLPSVGAGAVLRDLIESGTVP---------- 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 331 rltgthvpagtgteaaslrdsLCLLQKSYRFGSDSGIGQLAAAINSGDktaVKTVFQQDFTDIEKRLLQSGEDyiaMLEE 410
Cdd:COG0507  278 ---------------------VVELTEVYRQADDSRIIELAHAIREGD---APEALNARYADVVFVEAEDAEE---AAEA 330
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 411 ALAGYGRYLdllqaraepdliiQAFNEYQLLCALregPFGVAGLNERIEQFMQQ----KRKIHRHPHSRWYEGRPVMIAR 486
Cdd:COG0507  331 IVELYADRP-------------AGGEDIQVLAPT---NAGVDALNQAIREALNPagelERELAEDGELELYVGDRVMFTR 394
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 487 NDSALGLFNGDIGIALD-RGQGTRVWFAMPDGNIKSVQPSRLPEHETTWAMTVHKSQGSEFDHAALILPSQRTPVVTREL 565
Cdd:COG0507  395 NDYDLGVFNGDIGTVLSiDEDEGRLTVRFDGREIVTYDPSELDQLELAYAITVHKSQGSTFDRVILVLPSEHSPLLSREL 474
                        570       580       590
                 ....*....|....*....|....*....|....*...
gi 446698615 566 VYTAVTRARRRLSLYADERILSAAIATRTERRSGLAAL 603
Cdd:COG0507  475 LYTALTRARELLTLVGDRDALARAVRRDTARATGLAER 512
recD_rel TIGR01448
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ...
199-604 6.98e-51

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: 187.30  E-value: 6.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  199 IRLAAPTGKAAARLTESLGKAlrqlpltdeqkkripedASTLHRLLGAQPGSQRLRHHAgNPLHLDVLVVDEASMIDLPM 278
Cdd:TIGR01448 371 VGLAAPTGRAAKRLGEVTGLT-----------------ASTIHRLLGYGPDTFRHNHLE-DPIDCDLLIVDESSMMDTWL 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  279 MSRLIDALPDHARVIFLGDRDQLASVEAGAVLGDIcAYANAgftAERARqlsrltgthvpagtgteaaslrdslclLQKS 358
Cdd:TIGR01448 433 ALSLLAALPDHARLLLVGDTDQLPSVGPGQVLKDL-ILSQA---IPVTR---------------------------LTKV 481
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  359 YRFGSDSGIGQLAAAINSGDKTAVK--TVFQQDFTDIEkrllqSGEDYIAMLEEALAGYGRYLDLLQAraepdliiqafn 436
Cdd:TIGR01448 482 YRQAAGSPIITLAHGILHGEAPAWGdfKFLNLTRSEPE-----GAARHIPLMVEKIVGMARVGGIPGA------------ 544
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  437 EYQLLCALREGPFGVAGLNERIEQFMQQKRKIHRHPHSRWYEGRP---VMIARNDSALGLFNGDIG----IALDRGQGTR 509
Cdd:TIGR01448 545 DIQVLAPMYKGPLGIDALNQHLQALLNPYQKGQGGIEIAEGEYRKgdrVMQTKNDYNNEIFNGDLGmivkIEGAKQGKKD 624
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  510 VWFAMPDGNIKSVQPSRLPEHETTWAMTVHKSQGSEFDHAALILPSQRTPVVTRELVYTAVTRARRRLSLYADERILSAA 589
Cdd:TIGR01448 625 QVVVDFDGNEVELTRAELFNLTLAYATSIHKSQGSEFPTVILPIHTAHMRMLYRNLLYTALTRAKKRVILVGSAEAFDIA 704
                         410
                  ....*....|....*.
gi 446698615  590 IAT-RTERRSGLAALF 604
Cdd:TIGR01448 705 AARqGQARNTGLLERI 720
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
153-315 7.46e-45

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: 156.56  E-value: 7.46e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 153 WQKVAAAVALTRRISVISGGPGTGKTTTVAKLLAALIQMadgeRCRIRLAAPTGKAAARLTESLGKalrqlpltdeqkkr 232
Cdd:cd17933    1 EQKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALEAE----GKRVVLAAPTGKAAKRLSESTGI-------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 233 ipeDASTLHRLLGAQPGSQRLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASVEAGAVLGD 312
Cdd:cd17933   63 ---EASTIHRLLGINPGGGGFYYNEENPLDADLLIVDEASMVDTRLMAALLSAIPAGARLILVGDPDQLPSVGAGNVLRD 139

                 ...
gi 446698615 313 ICA 315
Cdd:cd17933  140 LIA 142
AAA_19 pfam13245
AAA domain;
154-304 4.68e-27

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 106.53  E-value: 4.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  154 QKVAAAVALTRRISVISGGPGTGKTTTVAKLLAALIQMADGERcRIRLAAPTGKAAARLTESLGKalrqlpltdeqkkri 233
Cdd:pfam13245   1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGVSF-PILLAAPTGRAAKRLSERTGL--------------- 64
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446698615  234 peDASTLHRLLGAQPGSQ-RLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASV 304
Cdd:pfam13245  65 --PASTIHRLLGFDDLEAgGFLRDEEEPLDGDLLIVDEFSMVDLPLAYRLLKALPDGAQLLLVGDPDQLPSV 134
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
181-359 3.84e-25

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: 100.64  E-value: 3.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 181 VAKLLAALIQMADGERCRIRLAAPTGKAAARLteslgkalrqlpltdeqkkripedastlhrllgaqpgsqrlrhhagnp 260
Cdd:cd17914   16 LVKIVAALMQNKNGEPGRILLVTPTNKAAAQL------------------------------------------------ 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 261 lhlDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASVEAGAVLGDICAyanagftaerarqlsrltgthvPAG 340
Cdd:cd17914   48 ---DNILVDEAAQILEPETSRLIDLALDQGRVILVGDHDQLGPVWRGAVLAKICN----------------------EQS 102
                        170
                 ....*....|....*....
gi 446698615 341 TGTEAASLRDSLCLLQKSY 359
Cdd:cd17914  103 LFTRLVRLGVSLIRLQVQY 121
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
184-382 4.03e-23

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: 97.25  E-value: 4.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  184 LLAALIQMADGERCRIRLAAPTGKAAARLTESLGkalrqlpltdeqkkripEDASTLHRLLGAQPGSQRLRHHagnplhl 263
Cdd:pfam13604  34 ALKALREAWEAAGYRVIGLAPTGRAAKVLGEELG-----------------IPADTIAKLLHRLGGRAGLDPG------- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  264 DVLVVDEASMIDLPMMSRLIDALPDH-ARVIFLGDRDQLASVEAGAVLGDICAyanagftaerarqlsrltgthvpagTG 342
Cdd:pfam13604  90 TLLIVDEAGMVGTRQMARLLKLAEDAgARVILVGDPRQLPSVEAGGAFRDLLA-------------------------AG 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 446698615  343 TEAASLRDslcllqkSYRFGsDSGIGQLAAAINSGDKTAV 382
Cdd:pfam13604 145 IGTAELTE-------IVRQR-DPWQRAASLALRDGDPAEA 176
Helicase_RecD pfam05127
Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase ...
181-354 3.67e-21

Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase activity, and a Walker B motif. In tRNA(Met) cytidine acetyltransferase (TmcA) it may function as an RNA helicase motor (driven by ATP hydrolysis) which delivers the wobble base to the active centre of the GCN5-related N-acetyltransferase (GNAT) domain. It is found in the bacterial exodeoxyribonuclease V alpha chain (RecD), which has 5'-3' helicase activity. It is structurally similar to the motor domain 1A in other SF1 helicases.


Pssm-ID: 461555 [Multi-domain]  Cd Length: 171  Bit Score: 90.67  E-value: 3.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  181 VAKLLAALIQMAdgeRCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEDastlhrllgaqpGSQRLRHHAGNP 260
Cdd:pfam05127  14 LGLAAAALIAQG---YSRIIVTAPSPANVQTLFEFAIKGLDALGLTPKFRDGIIRG------------NGQRIRFIAPDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  261 LHL-----DVLVVDEASMIDLPMMSRLidaLPDHARVIFlgdrdqlasveAGAVLGdicaYANAG------FTAE----- 324
Cdd:pfam05127  79 LLKlpgqaDLLVVDEAAAIPLPLLKQL---LRGFPRVVF-----------ATTVHG----YEGTGrgfslkFLAQlkkql 140
                         170       180       190
                  ....*....|....*....|....*....|.
gi 446698615  325 -RARQLSRLTGTHVPAGTGTEAAsLRDSLCL 354
Cdd:pfam05127 141 pGLRELELTEPIRYAEGDPLEKW-LNDLLLL 170
SF1_C_RecD cd18809
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ...
534-581 2.38e-18

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: 79.91  E-value: 2.38e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446698615 534 WAMTVHKSQGSEFDHAALILPSQRtPVVTRELVYTAVTRARRRLSLYA 581
Cdd:cd18809   34 YAMTIHKSQGSEFDRVIVVLPTSH-PMLSRGLLYTALTRARKLLTLVG 80
TraA_Ti TIGR02768
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a ...
116-598 9.46e-14

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: 74.46  E-value: 9.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  116 ERTVARFFNEVNHAieVDEALLAQTLDKLFPVSDEinwQKVAAA-VALTRRISVISGGPGTGKTTTVAKLLAALIQmadg 194
Cdd:TIGR02768 324 ARSAEALSQSQGHG--VSPPIVDAAIDQHYRLSEE---QYEAVRhVTGSGDIAVVVGRAGTGKSTMLKAAREAWEA---- 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  195 ERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRipeDASTLHRLlgaqpgsqrlrhhagnplhlDVLVVDEASMI 274
Cdd:TIGR02768 395 AGYRVIGAALSGKAAEGLQAESGIESRTLASLEYAWAN---GRDLLSDK--------------------DVLVIDEAGMV 451
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  275 DLPMMSRLID-ALPDHARVIFLGDRDQLASVEAGAVLGDICA---YAN-AGFTAER---ARQLSRLTGTHvpagtGTEAA 346
Cdd:TIGR02768 452 GSRQMARVLKeAEEAGAKVVLVGDPEQLQPIEAGAAFRAIAErigYAElETIRRQReawARQASLELARG-----DVEKA 526
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  347 slrdslclLQKSYRFGSDSGIGQLAAAINsgdktavktvfqqdftdiekrllQSGEDYIAMLEEAlAGYGRYLDLLQARA 426
Cdd:TIGR02768 527 --------LAAYRDHGHITIHDTREEAIE-----------------------QVVADWKQDLREA-NPAGSQIMLAHTRK 574
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  427 EpdliIQAFNEyqllcALREGPFGVAGLNERIE-QFMQQKRKIHrhphsrwyEGRPVMIARNDSALGLFNGDIGIALDRG 505
Cdd:TIGR02768 575 D----VRALNE-----AAREALIERGELGESILfQTARGERKFA--------AGDRIVFLENNRDLGVKNGMLGTVEEIE 637
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615  506 QGtRVWFAMPDGNIKSVQPSRLPEHETTWAMTVHKSQGSEFDHAALIlpsqRTPVVTRELVYTAVTRARRRLSLYADERI 585
Cdd:TIGR02768 638 DG-RLVVQLDSGELVIIPQAEYDALDHGYATTIHKSQGVTVDRAFVL----ASKSMDRHLAYVAMTRHRESVQLYAGKED 712
                         490
                  ....*....|....*
gi 446698615  586 LS--AAIATRTERRS 598
Cdd:TIGR02768 713 FTdrGALVKTLSRSS 727
SH3_13 pfam18335
ATP-dependent RecD-like DNA helicase SH3 domain; This is an SH3 (SRC homology domain 3) domain ...
454-512 1.85e-11

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: 59.80  E-value: 1.85e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446698615  454 LNERIEQFM---QQKRKIHRHPHSRWYEGRPVMIARNDSALGLFNGDIGI--ALDRGQGT-RVWF 512
Cdd:pfam18335   1 LNQRLQEALnppSPGKKEIKFGGRIFRVGDKVMQTKNNYDLGVFNGDIGIivAIDKEEKTlTVDF 65
UvrD_C_2 pfam13538
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ...
534-580 4.37e-11

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: 58.35  E-value: 4.37e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 446698615  534 WAMTVHKSQGSEFDHAALILPSQRTPVV---TRELVYTAVTRARRRLSLY 580
Cdd:pfam13538   3 YALTVHKAQGSEFPAVFLVDPDLTAHYHsmlRRRLLYTAVTRARKKLVLV 52
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
534-581 3.37e-09

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: 53.98  E-value: 3.37e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446698615 534 WAMTVHKSQGSEFDHAALILPsqRTPVVTRELVYTAVTRARRRLSLYA 581
Cdd:cd18786   44 GAITIDSSQGLTFDVVTLYLP--TANSLTPRRLYVALTRARKRLVIYD 89
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
184-304 4.76e-06

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: 47.24  E-value: 4.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 184 LLAALIQMADGERCRIRLAAPTGKAAARLteslgkalrqlpltdeqkkripeDASTLHRLLGAQPGSQ----------RL 253
Cdd:cd18037   28 LLRRIIRALPSRPKRVAVTASTGIAACNI-----------------------GGTTLHSFAGIGLGSEpaedllervkRS 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446698615 254 RHHAGNPLHLDVLVVDEASMIDLPMMSRLiDALPDHAR----------VIFLGDRDQLASV 304
Cdd:cd18037   85 PYLVQRWRKCDVLIIDEISMLDADLFDKL-DRVAREVRgsdkpfggiqLILCGDFLQLPPV 144
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
205-301 1.20e-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: 41.84  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 205 TGKaaarlTESLGKALRQLpLTDEQKKRIpedastlhrLLGAQpgsqrlRHHAGNplHLDVLVVDEASMIDLPMmsrLID 284
Cdd:cd17934   10 TGK-----TTTIAAIVLQL-LKGLRGKRV---------LVTAQ------SNVAVD--NVDVVIIDEASQITEPE---LLI 63
                         90
                 ....*....|....*..
gi 446698615 285 ALPDHARVIFLGDRDQL 301
Cdd:cd17934   64 ALIRAKKVVLVGDPKQL 80
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
535-581 1.49e-04

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: 43.52  E-value: 1.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 446698615  535 AMTVHKSQGSEFDHAALIL---PSQRTPVVTRELVYTAVTRARRRLSLYA 581
Cdd:pfam01443 178 VTTVHEVQGLTFDSVTLVLdtdTDLLIISDSPEHLYVALTRHRKSLHILT 227
PRK13889 PRK13889
conjugal transfer relaxase TraA; Provisional
264-308 3.48e-04

conjugal transfer relaxase TraA; Provisional


Pssm-ID: 237546 [Multi-domain]  Cd Length: 988  Bit Score: 43.91  E-value: 3.48e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446698615 264 DVLVVDEASMIDLPMMSRLIDALPDH-ARVIFLGDRDQLASVEAGA 308
Cdd:PRK13889 435 DVLVIDEAGMVGTRQLERVLSHAADAgAKVVLVGDPQQLQAIEAGA 480
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
536-584 4.48e-04

Superfamily I DNA or RNA helicase [Replication, recombination and repair];


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 43.39  E-value: 4.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446698615 536 MTVHKSQGSEFDHAAL------ILPSQR---TPVVTRE---LVYTAVTRARRRLSL-YADER 584
Cdd:COG0210  553 MTLHAAKGLEFPVVFLvgleegLFPHQRsldDEEELEEerrLFYVAITRARERLYLtYAASR 614
UvrD_C pfam13361
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ...
536-577 2.16e-03

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: 40.85  E-value: 2.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446698615  536 MTVHKSQGSEFDHAAL------ILPSQRTPVVT------RELVYTAVTRARRRL 577
Cdd:pfam13361 317 MTIHQAKGLEFDTVFLagleegIFPSYRSIKDEgnleeeRRLFYVAITRAKKRL 370
COG3972 COG3972
Superfamily I DNA and RNA helicases [Replication, recombination and repair];
536-584 2.92e-03

Superfamily I DNA and RNA helicases [Replication, recombination and repair];


Pssm-ID: 443172 [Multi-domain]  Cd Length: 565  Bit Score: 40.59  E-value: 2.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446698615 536 MTVHKSQGSEFDHAALI----LPSQRTPVVTRELVYTAVTRARRRLSLYADER 584
Cdd:COG3972  492 STIHRAKGLEAPVVIIVgldqLAKGESLERLRNLLYVAMTRARGWLVVSGSGE 544
SF1_C_UvrD cd18807
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ...
536-579 3.11e-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: 38.37  E-value: 3.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698615 536 MTVHKSQGSEFDHAAL------ILPSQRTPVVT----------RELVYTAVTRARRRLSL 579
Cdd:cd18807   89 MTIHASKGLEFPVVFIvglgegFIPSDASYHAAkedeerleeeRRLLYVALTRAKKELYL 148
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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