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Conserved domains on  [gi|499194732|ref|WP_010892272|]
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exodeoxyribonuclease V subunit alpha [Chlamydia pneumoniae]

Protein Classification

exodeoxyribonuclease V subunit alpha( domain architecture ID 11492530)

exodeoxyribonuclease V subunit alpha, recD is part of the RecBCD complex.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
9-493 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: 548.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732    9 LEDLVHQQVISPLDIAFAS--KHIS-SDFEESFVFLAVSSALWRYGHPFLSLEENRIRPSLGGISETDL-----YRGFHN 80
Cdd:TIGR01447   1 LKKLVQQGVLRPLDVAFAQflQHLAqKSNEEVALFAAVASALLRRGHPCLDLEKAAKSPGLTGISEPDLgeklnFDWLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732   81 LPKEVRDKLF-------VVVSGRLYLRSLYTIRSKLLDKLSLLCSATPNYF--PPSIDSSILSEEQN---FIFNKITQGC 148
Cdd:TIGR01447  81 LPASVLVGLPgetapplVLCDGRLYLRRYWREEEKLAAKLRTLLEARKRTApsAILENLFPLLNEQNwrkTAVALALKSN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  149 FSIVSGGPGTGKTFLAAQLILSLVKQQP---KLRIAIVSPTGKATSHIRQILMKYN---------IFDDMVLMQTVHHFL 216
Cdd:TIGR01447 161 FSLITGGPGTGKTTTVARLLLALVKQSPkqgKLRIALAAPTGKAAARLAESLRKAVknlaaaealIAALPSEAVTIHRLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  217 QEYA--------YRRYNSIDVLLVDEGSMVTFDLLYSLVQTLQGYEKdkklytssLIILGDTNQLPPIGIG-VGNPLQDL 287
Cdd:TIGR01447 241 GIKPdtkrfrhhERNPLPLDVLVVDEASMVDLPLMAKLLKALPPNTK--------LILLGDKNQLPSVEAGaVLGDLCEL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  288 IG-------------------YFHENTFFLKTSHRAKTG-VVDQLTQSVL------------RGEMISFSPLPSISSAIE 335
Cdd:TIGR01447 313 ASigksilyalckkinsktrnPLSDNVCFLKTSHRFGKDsGIGQLAKAINsgdieavlnnlrSGQLIEFEFLNSKEDAIE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  336 VLKNRFVKSL--RQSEA-------------RLCVLTPMRHGPWGVLNLNTMIHQRLAR--SDPD-----LRIPIMVTSRY 393
Cdd:TIGR01447 393 RLKNLYVKYRtfLQKLAalsdakeiletfdRLRLLTALRDGPFGVLGLNRRIEQELQEkyFDPDeegwyIGRPIMVTEND 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  394 ETWGLFNGDTGLLCL-----KTQKLHFPQ-HEPIDSRALSQYVYNYVMSVHKSQGSEYDEVIVIIPKG-SEVFGVSILYT 466
Cdd:TIGR01447 473 YTLGLFNGDIGVLLRdpdgiLTVWFHFADgSKAVLPSRLPNYETAFAMTVHKSQGSEFDHVILILPNGnSPVLTRELLYT 552
                         570       580
                  ....*....|....*....|....*..
gi 499194732  467 AITRAKYRVSVWGDPETLHKIIKKSNY 493
Cdd:TIGR01447 553 GITRAKDQLSVWSDKETLNAAIKRKNK 579
 
Name Accession Description Interval E-value
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
9-493 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: 548.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732    9 LEDLVHQQVISPLDIAFAS--KHIS-SDFEESFVFLAVSSALWRYGHPFLSLEENRIRPSLGGISETDL-----YRGFHN 80
Cdd:TIGR01447   1 LKKLVQQGVLRPLDVAFAQflQHLAqKSNEEVALFAAVASALLRRGHPCLDLEKAAKSPGLTGISEPDLgeklnFDWLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732   81 LPKEVRDKLF-------VVVSGRLYLRSLYTIRSKLLDKLSLLCSATPNYF--PPSIDSSILSEEQN---FIFNKITQGC 148
Cdd:TIGR01447  81 LPASVLVGLPgetapplVLCDGRLYLRRYWREEEKLAAKLRTLLEARKRTApsAILENLFPLLNEQNwrkTAVALALKSN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  149 FSIVSGGPGTGKTFLAAQLILSLVKQQP---KLRIAIVSPTGKATSHIRQILMKYN---------IFDDMVLMQTVHHFL 216
Cdd:TIGR01447 161 FSLITGGPGTGKTTTVARLLLALVKQSPkqgKLRIALAAPTGKAAARLAESLRKAVknlaaaealIAALPSEAVTIHRLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  217 QEYA--------YRRYNSIDVLLVDEGSMVTFDLLYSLVQTLQGYEKdkklytssLIILGDTNQLPPIGIG-VGNPLQDL 287
Cdd:TIGR01447 241 GIKPdtkrfrhhERNPLPLDVLVVDEASMVDLPLMAKLLKALPPNTK--------LILLGDKNQLPSVEAGaVLGDLCEL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  288 IG-------------------YFHENTFFLKTSHRAKTG-VVDQLTQSVL------------RGEMISFSPLPSISSAIE 335
Cdd:TIGR01447 313 ASigksilyalckkinsktrnPLSDNVCFLKTSHRFGKDsGIGQLAKAINsgdieavlnnlrSGQLIEFEFLNSKEDAIE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  336 VLKNRFVKSL--RQSEA-------------RLCVLTPMRHGPWGVLNLNTMIHQRLAR--SDPD-----LRIPIMVTSRY 393
Cdd:TIGR01447 393 RLKNLYVKYRtfLQKLAalsdakeiletfdRLRLLTALRDGPFGVLGLNRRIEQELQEkyFDPDeegwyIGRPIMVTEND 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  394 ETWGLFNGDTGLLCL-----KTQKLHFPQ-HEPIDSRALSQYVYNYVMSVHKSQGSEYDEVIVIIPKG-SEVFGVSILYT 466
Cdd:TIGR01447 473 YTLGLFNGDIGVLLRdpdgiLTVWFHFADgSKAVLPSRLPNYETAFAMTVHKSQGSEFDHVILILPNGnSPVLTRELLYT 552
                         570       580
                  ....*....|....*....|....*..
gi 499194732  467 AITRAKYRVSVWGDPETLHKIIKKSNY 493
Cdd:TIGR01447 553 GITRAKDQLSVWSDKETLNAAIKRKNK 579
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
91-490 1.59e-63

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: 214.84  E-value: 1.59e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  91 VVVSGRLYLRSLYTI----------RSKLLDKLSLLCSATPNYFPPsiDSSILSEEQNFIFNKI-TQGCFSIVSGGPGTG 159
Cdd:COG0507   75 LVLDGRRYLTRLLEAeqrlarrlrrLARPALDEADVEAALAALEPR--AGITLSDEQREAVALAlTTRRVSVLTGGAGTG 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 160 KTFLAAQLILSLVKQQpkLRIAIVSPTGKATSHIRQILMKYNifddmvlmQTVHHFL------QEYAYRRYNSI---DVL 230
Cdd:COG0507  153 KTTTLRALLAALEALG--LRVALAAPTGKAAKRLSESTGIEA--------RTIHRLLglrpdsGRFRHNRDNPLtpaDLL 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 231 LVDEGSMVTFDLLYSLVQTLqgYEKDKKLytsslIILGDTNQLPPIGigVGNPLQDLIGYFHENTFFLKTSHR-AKTGVV 309
Cdd:COG0507  223 VVDEASMVDTRLMAALLEAL--PRAGARL-----ILVGDPDQLPSVG--AGAVLRDLIESGTVPVVELTEVYRqADDSRI 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 310 DQLTQSVLRGEM----------ISFSPLPSISSAIEVLKNRfVKSLRQSEARLCVLTPMrhgPWGVLNLNTMIHQRLARS 379
Cdd:COG0507  294 IELAHAIREGDApealnaryadVVFVEAEDAEEAAEAIVEL-YADRPAGGEDIQVLAPT---NAGVDALNQAIREALNPA 369
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 380 ---------DPDLRI----PIMVTSRYETWGLFNGDTGLLC-----LKTQKLHFPQHEPI--DSRALSQYVYNYVMSVHK 439
Cdd:COG0507  370 gelerelaeDGELELyvgdRVMFTRNDYDLGVFNGDIGTVLsidedEGRLTVRFDGREIVtyDPSELDQLELAYAITVHK 449
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499194732 440 SQGSEYDEVIVIIPKG-SEVFGVSILYTAITRAKYRVSVWGDPETLHKIIKK 490
Cdd:COG0507  450 SQGSTFDRVILVLPSEhSPLLSRELLYTALTRARELLTLVGDRDALARAVRR 501
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
136-302 3.54e-40

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: 141.92  E-value: 3.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 136 EQNFIFNKITQGCFSIVSGGPGTGKTFLAAQLILSLvkQQPKLRIAIVSPTGKATSHIRQILmkynifddMVLMQTVHHF 215
Cdd:cd17933    1 EQKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAAL--EAEGKRVVLAAPTGKAAKRLSEST--------GIEASTIHRL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 216 LQEYAYR--------RYNSIDVLLVDEGSMVTFDLLYSLVQTLQgyekdkklYTSSLIILGDTNQLPPIGIgvGNPLQDL 287
Cdd:cd17933   71 LGINPGGggfyyneeNPLDADLLIVDEASMVDTRLMAALLSAIP--------AGARLILVGDPDQLPSVGA--GNVLRDL 140
                        170
                 ....*....|....*
gi 499194732 288 IGYFHENTFFLKTSH 302
Cdd:cd17933  141 IASKGVPTVELTEVF 155
recD PRK10875
exodeoxyribonuclease V subunit alpha;
150-489 1.25e-31

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 128.52  E-value: 1.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 150 SIVSGGPGTGKTFLAAQLILSLVK--QQPKLRIAIVSPTGKA----TSHIRQILMKYNIFDDMV-LM----QTVHHFL-- 216
Cdd:PRK10875 170 SVISGGPGTGKTTTVAKLLAALIQlaDGERCRIRLAAPTGKAaarlTESLGKALRQLPLTDEQKkRIpeeaSTLHRLLga 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 217 ----QEYAYRRYN--SIDVLLVDEGSMVTFDLLYSLVQTLQGYEKdkklytssLIILGDTNQLPpiGIGVGNPLQDlIGY 290
Cdd:PRK10875 250 qpgsQRLRYHAGNplHLDVLVVDEASMVDLPMMARLIDALPPHAR--------VIFLGDRDQLA--SVEAGAVLGD-ICR 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 291 FHENTF--------------------------------FLKTSHR--AKTGVvDQLTQSVLRGEM-------------IS 323
Cdd:PRK10875 319 FAEAGYsaeraqqlsrltgchlpagtgteaasvrdslcLLRKSYRfgSDSGI-GQLAAAVNRGDKraakavfqqgfsdIE 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 324 FSPLPSISSAIEVLKN------RFVKSLRQSEA------------RLCVLtpmRHGPWGVLNLNTMIHQRLARS------ 379
Cdd:PRK10875 398 KRPLQSGEDYQAMLEEalagygRYLDLLAARAEpeailaafnryqLLCAL---REGPFGVAGLNERIEQALQQKrlirrp 474
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 380 -DPDLRI----PIMVTSRYETWGLFNGDTGLLCLKTQ---KLHFP----QHEPIDSRALSQYVYNYVMSVHKSQGSEYDE 447
Cdd:PRK10875 475 sGPHSRWyegrPVMIARNDSALGLFNGDIGIALDRGQgelRVWFQlpdgNIKSVQPSRLPEHETAWAMTVHKSQGSEFDH 554
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 499194732 448 VIVIIP-KGSEVFGVSILYTAITRAKYRVSVWGDPETLHKIIK 489
Cdd:PRK10875 555 TALVLPnQFTPVVTRELVYTAITRARRRLSLYADERVLSAAIA 597
AAA_19 pfam13245
AAA domain;
150-277 4.59e-17

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 77.64  E-value: 4.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  150 SIVSGGPGTGKTFLAAQLILSLVKQ-QPKLRIAIVSPTGKATSHIRqilmkynifdDMVLM--QTVHHFLQ--------- 217
Cdd:pfam13245  14 VLLTGGPGTGKTTTIRHIVALLVALgGVSFPILLAAPTGRAAKRLS----------ERTGLpaSTIHRLLGfddleaggf 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  218 EYAYRRYNSIDVLLVDEGSMVTFDLLYSLVQTLqgyekdkkLYTSSLIILGDTNQLPPIG 277
Cdd:pfam13245  84 LRDEEEPLDGDLLIVDEFSMVDLPLAYRLLKAL--------PDGAQLLLVGDPDQLPSVG 135
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
151-277 5.08e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 46.21  E-value: 5.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732   151 IVSGGPGTGKTFLAAQLILSLvkQQPKLRIAIVSPTGKATSHIRQILMKYNIFDDMVLMQtVHHFLQEYAYRRYNSIDVL 230
Cdd:smart00382   6 LIVGPPGSGKTTLARALAREL--GPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSG-ELRLRLALALARKLKPDVL 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 499194732   231 LVDE-GSMVTFDLLYSLVQTLQGYEKDKKLYTSSLIILGDTNQLPPIG 277
Cdd:smart00382  83 ILDEiTSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
 
Name Accession Description Interval E-value
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
9-493 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: 548.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732    9 LEDLVHQQVISPLDIAFAS--KHIS-SDFEESFVFLAVSSALWRYGHPFLSLEENRIRPSLGGISETDL-----YRGFHN 80
Cdd:TIGR01447   1 LKKLVQQGVLRPLDVAFAQflQHLAqKSNEEVALFAAVASALLRRGHPCLDLEKAAKSPGLTGISEPDLgeklnFDWLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732   81 LPKEVRDKLF-------VVVSGRLYLRSLYTIRSKLLDKLSLLCSATPNYF--PPSIDSSILSEEQN---FIFNKITQGC 148
Cdd:TIGR01447  81 LPASVLVGLPgetapplVLCDGRLYLRRYWREEEKLAAKLRTLLEARKRTApsAILENLFPLLNEQNwrkTAVALALKSN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  149 FSIVSGGPGTGKTFLAAQLILSLVKQQP---KLRIAIVSPTGKATSHIRQILMKYN---------IFDDMVLMQTVHHFL 216
Cdd:TIGR01447 161 FSLITGGPGTGKTTTVARLLLALVKQSPkqgKLRIALAAPTGKAAARLAESLRKAVknlaaaealIAALPSEAVTIHRLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  217 QEYA--------YRRYNSIDVLLVDEGSMVTFDLLYSLVQTLQGYEKdkklytssLIILGDTNQLPPIGIG-VGNPLQDL 287
Cdd:TIGR01447 241 GIKPdtkrfrhhERNPLPLDVLVVDEASMVDLPLMAKLLKALPPNTK--------LILLGDKNQLPSVEAGaVLGDLCEL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  288 IG-------------------YFHENTFFLKTSHRAKTG-VVDQLTQSVL------------RGEMISFSPLPSISSAIE 335
Cdd:TIGR01447 313 ASigksilyalckkinsktrnPLSDNVCFLKTSHRFGKDsGIGQLAKAINsgdieavlnnlrSGQLIEFEFLNSKEDAIE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  336 VLKNRFVKSL--RQSEA-------------RLCVLTPMRHGPWGVLNLNTMIHQRLAR--SDPD-----LRIPIMVTSRY 393
Cdd:TIGR01447 393 RLKNLYVKYRtfLQKLAalsdakeiletfdRLRLLTALRDGPFGVLGLNRRIEQELQEkyFDPDeegwyIGRPIMVTEND 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  394 ETWGLFNGDTGLLCL-----KTQKLHFPQ-HEPIDSRALSQYVYNYVMSVHKSQGSEYDEVIVIIPKG-SEVFGVSILYT 466
Cdd:TIGR01447 473 YTLGLFNGDIGVLLRdpdgiLTVWFHFADgSKAVLPSRLPNYETAFAMTVHKSQGSEFDHVILILPNGnSPVLTRELLYT 552
                         570       580
                  ....*....|....*....|....*..
gi 499194732  467 AITRAKYRVSVWGDPETLHKIIKKSNY 493
Cdd:TIGR01447 553 GITRAKDQLSVWSDKETLNAAIKRKNK 579
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
91-490 1.59e-63

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: 214.84  E-value: 1.59e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  91 VVVSGRLYLRSLYTI----------RSKLLDKLSLLCSATPNYFPPsiDSSILSEEQNFIFNKI-TQGCFSIVSGGPGTG 159
Cdd:COG0507   75 LVLDGRRYLTRLLEAeqrlarrlrrLARPALDEADVEAALAALEPR--AGITLSDEQREAVALAlTTRRVSVLTGGAGTG 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 160 KTFLAAQLILSLVKQQpkLRIAIVSPTGKATSHIRQILMKYNifddmvlmQTVHHFL------QEYAYRRYNSI---DVL 230
Cdd:COG0507  153 KTTTLRALLAALEALG--LRVALAAPTGKAAKRLSESTGIEA--------RTIHRLLglrpdsGRFRHNRDNPLtpaDLL 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 231 LVDEGSMVTFDLLYSLVQTLqgYEKDKKLytsslIILGDTNQLPPIGigVGNPLQDLIGYFHENTFFLKTSHR-AKTGVV 309
Cdd:COG0507  223 VVDEASMVDTRLMAALLEAL--PRAGARL-----ILVGDPDQLPSVG--AGAVLRDLIESGTVPVVELTEVYRqADDSRI 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 310 DQLTQSVLRGEM----------ISFSPLPSISSAIEVLKNRfVKSLRQSEARLCVLTPMrhgPWGVLNLNTMIHQRLARS 379
Cdd:COG0507  294 IELAHAIREGDApealnaryadVVFVEAEDAEEAAEAIVEL-YADRPAGGEDIQVLAPT---NAGVDALNQAIREALNPA 369
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 380 ---------DPDLRI----PIMVTSRYETWGLFNGDTGLLC-----LKTQKLHFPQHEPI--DSRALSQYVYNYVMSVHK 439
Cdd:COG0507  370 gelerelaeDGELELyvgdRVMFTRNDYDLGVFNGDIGTVLsidedEGRLTVRFDGREIVtyDPSELDQLELAYAITVHK 449
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499194732 440 SQGSEYDEVIVIIPKG-SEVFGVSILYTAITRAKYRVSVWGDPETLHKIIKK 490
Cdd:COG0507  450 SQGSTFDRVILVLPSEhSPLLSRELLYTALTRARELLTLVGDRDALARAVRR 501
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
136-302 3.54e-40

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: 141.92  E-value: 3.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 136 EQNFIFNKITQGCFSIVSGGPGTGKTFLAAQLILSLvkQQPKLRIAIVSPTGKATSHIRQILmkynifddMVLMQTVHHF 215
Cdd:cd17933    1 EQKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAAL--EAEGKRVVLAAPTGKAAKRLSEST--------GIEASTIHRL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 216 LQEYAYR--------RYNSIDVLLVDEGSMVTFDLLYSLVQTLQgyekdkklYTSSLIILGDTNQLPPIGIgvGNPLQDL 287
Cdd:cd17933   71 LGINPGGggfyyneeNPLDADLLIVDEASMVDTRLMAALLSAIP--------AGARLILVGDPDQLPSVGA--GNVLRDL 140
                        170
                 ....*....|....*
gi 499194732 288 IGYFHENTFFLKTSH 302
Cdd:cd17933  141 IASKGVPTVELTEVF 155
recD_rel TIGR01448
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ...
88-484 1.23e-32

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: 131.83  E-value: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732   88 KLFVVVSGRLYLRSLYTIRSKLLDKLSLLCSATPNYFPPSIDSSI----------LSEEQNFIFNKITQGCFSIVSGGPG 157
Cdd:TIGR01448 269 PKLAAEDGRIYLPSLFRAEKQIASHIRRLLATSPAIGAINDQEHIwevekklrkgLSEEQKQALDTAIQHKVVILTGGPG 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  158 TGKTFLAAQLILSLVKQQPKLRIAIVSPTGKATSHIRQILMKynifddmvLMQTVHHFLQ-------EYAYRRYNSIDVL 230
Cdd:TIGR01448 349 TGKTTITRAIIELAEELGGLLPVGLAAPTGRAAKRLGEVTGL--------TASTIHRLLGygpdtfrHNHLEDPIDCDLL 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  231 LVDEGSMVTFDLLYSLVQTLQGYEKdkklytssLIILGDTNQLPPigIGVGNPLQDLIGYFHENTFFLKTSHR--AKTGV 308
Cdd:TIGR01448 421 IVDESSMMDTWLALSLLAALPDHAR--------LLLVGDTDQLPS--VGPGQVLKDLILSQAIPVTRLTKVYRqaAGSPI 490
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  309 VdQLTQSVLRGEM---ISFSPLPSISSAIEVLKNR-------FVKSLRQSE---ARLCVLTPMRHGPWGVLNLNTMIHQR 375
Cdd:TIGR01448 491 I-TLAHGILHGEApawGDFKFLNLTRSEPEGAARHiplmvekIVGMARVGGipgADIQVLAPMYKGPLGIDALNQHLQAL 569
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  376 L---ARSDPDLRIP---------IMVT-SRYETwGLFNGDTGLLC-----LKTQKLH----FPQHEPIDSRA-LSQYVYN 432
Cdd:TIGR01448 570 LnpyQKGQGGIEIAegeyrkgdrVMQTkNDYNN-EIFNGDLGMIVkiegaKQGKKDQvvvdFDGNEVELTRAeLFNLTLA 648
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499194732  433 YVMSVHKSQGSEYDEVIVIIPKGSEV-FGVSILYTAITRAKYRVSVWGDPETL 484
Cdd:TIGR01448 649 YATSIHKSQGSEFPTVILPIHTAHMRmLYRNLLYTALTRAKKRVILVGSAEAF 701
recD PRK10875
exodeoxyribonuclease V subunit alpha;
150-489 1.25e-31

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 128.52  E-value: 1.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 150 SIVSGGPGTGKTFLAAQLILSLVK--QQPKLRIAIVSPTGKA----TSHIRQILMKYNIFDDMV-LM----QTVHHFL-- 216
Cdd:PRK10875 170 SVISGGPGTGKTTTVAKLLAALIQlaDGERCRIRLAAPTGKAaarlTESLGKALRQLPLTDEQKkRIpeeaSTLHRLLga 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 217 ----QEYAYRRYN--SIDVLLVDEGSMVTFDLLYSLVQTLQGYEKdkklytssLIILGDTNQLPpiGIGVGNPLQDlIGY 290
Cdd:PRK10875 250 qpgsQRLRYHAGNplHLDVLVVDEASMVDLPMMARLIDALPPHAR--------VIFLGDRDQLA--SVEAGAVLGD-ICR 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 291 FHENTF--------------------------------FLKTSHR--AKTGVvDQLTQSVLRGEM-------------IS 323
Cdd:PRK10875 319 FAEAGYsaeraqqlsrltgchlpagtgteaasvrdslcLLRKSYRfgSDSGI-GQLAAAVNRGDKraakavfqqgfsdIE 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 324 FSPLPSISSAIEVLKN------RFVKSLRQSEA------------RLCVLtpmRHGPWGVLNLNTMIHQRLARS------ 379
Cdd:PRK10875 398 KRPLQSGEDYQAMLEEalagygRYLDLLAARAEpeailaafnryqLLCAL---REGPFGVAGLNERIEQALQQKrlirrp 474
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 380 -DPDLRI----PIMVTSRYETWGLFNGDTGLLCLKTQ---KLHFP----QHEPIDSRALSQYVYNYVMSVHKSQGSEYDE 447
Cdd:PRK10875 475 sGPHSRWyegrPVMIARNDSALGLFNGDIGIALDRGQgelRVWFQlpdgNIKSVQPSRLPEHETAWAMTVHKSQGSEFDH 554
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 499194732 448 VIVIIP-KGSEVFGVSILYTAITRAKYRVSVWGDPETLHKIIK 489
Cdd:PRK10875 555 TALVLPnQFTPVVTRELVYTAITRARRRLSLYADERVLSAAIA 597
SF1_C_RecD cd18809
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ...
422-479 9.61e-19

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: 80.68  E-value: 9.61e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499194732 422 DSRALSQYVYNYVMSVHKSQGSEYDEVIVIIPKGSEVFGVSILYTAITRAKYRVSVWG 479
Cdd:cd18809   23 GVDALNERLQAYAMTIHKSQGSEFDRVIVVLPTSHPMLSRGLLYTALTRARKLLTLVG 80
AAA_19 pfam13245
AAA domain;
150-277 4.59e-17

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 77.64  E-value: 4.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  150 SIVSGGPGTGKTFLAAQLILSLVKQ-QPKLRIAIVSPTGKATSHIRqilmkynifdDMVLM--QTVHHFLQ--------- 217
Cdd:pfam13245  14 VLLTGGPGTGKTTTIRHIVALLVALgGVSFPILLAAPTGRAAKRLS----------ERTGLpaSTIHRLLGfddleaggf 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  218 EYAYRRYNSIDVLLVDEGSMVTFDLLYSLVQTLqgyekdkkLYTSSLIILGDTNQLPPIG 277
Cdd:pfam13245  84 LRDEEEPLDGDLLIVDEFSMVDLPLAYRLLKAL--------PDGAQLLLVGDPDQLPSVG 135
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
149-303 8.31e-13

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: 64.95  E-value: 8.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 149 FSIVSGGPGTGKTFLAAQLILSLVKQQPKLRIAIVSPTGKATshirqilmkynifddmvlmqtvhhflqeyayrryNSID 228
Cdd:cd17934    1 ISLIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAV----------------------------------DNVD 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 229 VLLVDEGSMVTfdlLYSLVQTLQGYEKdkklytssLIILGDTNQLPPI---------GIGVGNPLQDLIG--YFHENTFF 297
Cdd:cd17934   47 VVIIDEASQIT---EPELLIALIRAKK--------VVLVGDPKQLPPVvqedhaallGLSFILSLLLLFRllLPGSPKVM 115

                 ....*.
gi 499194732 298 LKTSHR 303
Cdd:cd17934  116 LDTQYR 121
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
136-315 1.55e-10

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: 60.34  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 136 EQNFIFNKITQGCFSIVSGGPGTGKTFLAAQLILSLvKQQPKlRIAIVSPTGKATSHIRQilmkynifddmvlmQTVHHF 215
Cdd:cd18037    1 EQRRVLDLVLDGKNVFFTGSAGTGKSYLLRRIIRAL-PSRPK-RVAVTASTGIAACNIGG--------------TTLHSF 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 216 L-----QEYAYRRYNSI-------------DVLLVDEGSMVTFDLLYSLVQTLQGYEKDKKLYTS-SLIILGDTNQLPPI 276
Cdd:cd18037   65 AgiglgSEPAEDLLERVkrspylvqrwrkcDVLIIDEISMLDADLFDKLDRVAREVRGSDKPFGGiQLILCGDFLQLPPV 144
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499194732 277 GiGVGNPLQDLIGYFHENTFFLKTSHRAKTGVVdQLTQS 315
Cdd:cd18037  145 T-KNSERQAFFFRGDQQFCFEAKSWERCIFLTV-ELTKV 181
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
150-306 3.86e-10

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: 57.50  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 150 SIVSGGPGTGKTFLAAQLILSLVKQQ--PKLRIAIVSPTGKATshirqilmkynifDDMvlmqtvhhflqeyayrrynsi 227
Cdd:cd17914    2 SLIQGPPGTGKTRVLVKIVAALMQNKngEPGRILLVTPTNKAA-------------AQL--------------------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 228 DVLLVDEGSMVTfDLLYSLVQTLQGYEKdkklytsSLIILGDTNQLPPIGIGvgnplQDLIGYFHEN-TFFLKTSHRAKT 306
Cdd:cd17914   48 DNILVDEAAQIL-EPETSRLIDLALDQG-------RVILVGDHDQLGPVWRG-----AVLAKICNEQsLFTRLVRLGVSL 114
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
149-288 2.49e-09

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: 56.80  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  149 FSIVSGGPGTGKTFlaaqlILSLVKQ---QPKLRIAIVSPTGKATShirqilmkynifddmVLMQ-------TVHHFLQE 218
Cdd:pfam13604  20 VAVLVGPAGTGKTT-----ALKALREaweAAGYRVIGLAPTGRAAK---------------VLGEelgipadTIAKLLHR 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499194732  219 YAYR-RYNSIDVLLVDEGSMVTFDLLYSLVQTLQGYekdkklyTSSLIILGDTNQLPPigIGVGNPLQDLI 288
Cdd:pfam13604  80 LGGRaGLDPGTLLIVDEAGMVGTRQMARLLKLAEDA-------GARVILVGDPRQLPS--VEAGGAFRDLL 141
UvrD_C_2 pfam13538
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ...
433-477 2.72e-09

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: 52.96  E-value: 2.72e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 499194732  433 YVMSVHKSQGSEYDEVIVIIPKGSEVFGVS----ILYTAITRAKYRVSV 477
Cdd:pfam13538   3 YALTVHKAQGSEFPAVFLVDPDLTAHYHSMlrrrLLYTAVTRARKKLVL 51
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
414-479 1.93e-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: 51.67  E-value: 1.93e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499194732 414 HFPQHEPIDSRALSQYVYNYVMSVHKSQGSEYDEVIVIIPKGSEvFGVSILYTAITRAKYRVSVWG 479
Cdd:cd18786   25 YLNQYLQGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTANS-LTPRRLYVALTRARKRLVIYD 89
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
173-484 1.85e-06

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 50.51  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 173 KQQPKLRIAIVSPTGKAtSHIRQILMKyNIFDDM-VLMQTVHHFLQEYAYRRyNSIDVLLVDEGSMVTF-DLLYSLVqtl 250
Cdd:COG1112  504 REAARLRRALRRELKKR-RELRKLLWD-ALLELApVVGMTPASVARLLPLGE-GSFDLVIIDEASQATLaEALGALA--- 577
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 251 qgyeKDKKLytsslIILGDTNQLPPI----------GIGVGNPLQD-LIGYFHENTFFLKTSHRaktgvvdqltqsvLRG 319
Cdd:COG1112  578 ----RAKRV-----VLVGDPKQLPPVvfgeeaeevaEEGLDESLLDrLLARLPERGVMLREHYR-------------MHP 635
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 320 EMISFS----------PLPSISSaievlknrfvKSLRQSEARLCVL-TPMRHGPWGVLNLNT--------MIHQRLARSD 380
Cdd:COG1112  636 EIIAFSnrlfydgklvPLPSPKA----------RRLADPDSPLVFIdVDGVYERRGGSRTNPeeaeavveLVRELLEDGP 705
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 381 PDLRIPImVTsryetwgLFNGDTGLLCLKTQKLHFPQHEPIdsralsqyvynYVMSVHKSQGSEYDEVIVII---PKGSE 457
Cdd:COG1112  706 DGESIGV-IT-------PYRAQVALIRELLREALGDGLEPV-----------FVGTVDRFQGDERDVIIFSLvysNDEDV 766
                        330       340       350
                 ....*....|....*....|....*....|....
gi 499194732 458 VFGVSILYT-------AITRAKYRVSVWGDPETL 484
Cdd:COG1112  767 PRNFGFLNGgprrlnvAVSRARRKLIVVGSRELL 800
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
151-277 5.08e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 46.21  E-value: 5.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732   151 IVSGGPGTGKTFLAAQLILSLvkQQPKLRIAIVSPTGKATSHIRQILMKYNIFDDMVLMQtVHHFLQEYAYRRYNSIDVL 230
Cdd:smart00382   6 LIVGPPGSGKTTLARALAREL--GPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSG-ELRLRLALALARKLKPDVL 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 499194732   231 LVDE-GSMVTFDLLYSLVQTLQGYEKDKKLYTSSLIILGDTNQLPPIG 277
Cdd:smart00382  83 ILDEiTSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
133-208 1.47e-05

DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members 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: 350796 [Multi-domain]  Cd Length: 229  Bit Score: 46.07  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 133 LSEEQNFIFNKITQG-CFS---IVSGGPGTGKTFLAAQLILSLVKQQPKLRIAIVSPTGKATSHIRQILMKYNIFDDMVL 208
Cdd:cd18038    2 LNDEQKLAVRNIVTGtSRPppyIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNALVTKREIL 81
phage_term_2 TIGR01547
phage terminase, large subunit, PBSX family; This model detects members of a highly divergent ...
151-296 1.92e-05

phage terminase, large subunit, PBSX family; This model detects members of a highly divergent family of the large subunit of phage terminase. All members are encoded by phage genomes or within prophage regions of bacterial genomes. This is a distinct family from pfam03354. [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273684 [Multi-domain]  Cd Length: 394  Bit Score: 47.02  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  151 IVSGGPGTGKTFLAAQLILSLVKQQPKLRIAIVSPTGKAT-----SHIRQILMKYNIFDDMVL----MQTVHHFLQEYAY 221
Cdd:TIGR01547   5 IAKGGRGSGKTFAIALKLVEKAARNKPQNILCARKVQNSIrdsvfKDIEDLLSIEGLNYEFKKskssMEIKILNTGKKFI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  222 -----------RRYNSIDVLLVDEGSMVTFDLLYSLVQTLQgYEKDKklytssLIILGDTNqlPPigigvgNPLQDLIGY 290
Cdd:TIGR01547  85 fkglndkpnklKSGAGIAIIWFEEASQLTKEDIKELIPRLR-EPGGK------RFIIFSSN--PE------SPLHWVYKR 149

                  ....*.
gi 499194732  291 FHENTF 296
Cdd:TIGR01547 150 FIENME 155
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
145-276 2.76e-05

EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It 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: 350693 [Multi-domain]  Cd Length: 207  Bit Score: 45.11  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 145 TQGCFSIVSGGPGTGKTFLAAQLILSLVKQQPKLRIAIVSPTGKATSHIRQILMKYNIFDDMVL----------MQTVHH 214
Cdd:cd17935   18 MQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEKIMALDIDERHLLrlghgakiiaMTCTHA 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499194732 215 FLQEYAYRRYN-SIDVLLVDEGSMV----TFDLLySLVQTLQGYEKDKKlytssLIILGDTNQLPPI 276
Cdd:cd17935   98 ALKRGELVELGfKYDNILMEEAAQIleieTFIPL-LLQNPEDGPNRLKR-----LIMIGDHHQLPPV 158
UvrD-helicase pfam00580
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ...
133-234 6.62e-05

UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyze ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.


Pssm-ID: 395462 [Multi-domain]  Cd Length: 267  Bit Score: 44.54  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  133 LSEEQNFIFNKITQGCFsiVSGGPGTGKTFLAAQLILSLVKQ---QPKlRIAIVSPTGKATSH----IRQILMKYNIFDD 205
Cdd:pfam00580   1 LNPEQRKAVTHLGGPLL--VLAGAGSGKTRVLTERIAYLILEggiDPE-EILAVTFTNKAAREmkerILKLLGKAELSEL 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 499194732  206 MVlmQTVHHF----LQEYAYRRYNSIDVLLVDE 234
Cdd:pfam00580  78 NI--STFHSFclriLRKYANRIGLLPNFSILDE 108
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
151-215 1.55e-04

DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain]  Cd Length: 230  Bit Score: 43.13  E-value: 1.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499194732 151 IVSGGPGTGKTFLAAQLILSLVKQQPKLRIAIVSPTGKATSHIRQILMKYNIFD--DMVLMQTVHHF 215
Cdd:cd18078   24 ILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKpgDMVRLNAVNRF 90
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
152-272 3.05e-04

DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350690 [Multi-domain]  Cd Length: 189  Bit Score: 41.73  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 152 VSGGPGTGKTFLAAQLILSLVKQQ--PKLRIAIVSPTGKATSHIRQ-------------------------ILMKYNIFD 204
Cdd:cd17932   17 VLAGAGSGKTRVLTHRIAYLILEGgvPPERILAVTFTNKAAKEMRErlrkllgeqlasgvwigtfhsfalrILRRYGDFD 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499194732 205 DMV-----LMQTVHHFLQEYAYRrynsIDVLLVDEgsmvtF----DLLYSLVQTLQGYEKdkklytsSLIILGDTNQ 272
Cdd:cd17932   97 DLLlyaleLLEENPDVREKLQSR----FRYILVDE-----YqdtnPLQYELLKLLAGDGK-------NLFVVGDDDQ 157
DEXDc smart00487
DEAD-like helicases superfamily;
133-186 4.38e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 41.32  E-value: 4.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 499194732   133 LSEEQNFIFNKITQGCFS-IVSGGPGTGKTFLAAQLILSLVKQQPKLRIAIVSPT 186
Cdd:smart00487   9 LRPYQKEAIEALLSGLRDvILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPT 63
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
145-243 6.75e-04

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 41.31  E-value: 6.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732 145 TQGCFSIVSGGPGTGKTFLAAQLILSLvkqQPKLRIA-IVSPTGKATSHIRQILMKYNI----FDDMVLMQTVHHFLQEY 219
Cdd:COG3267   41 QGGGFVVLTGEVGTGKTTLLRRLLERL---PDDVKVAyIPNPQLSPAELLRAIADELGLepkgASKADLLRQLQEFLLEL 117
                         90       100
                 ....*....|....*....|....
gi 499194732 220 AYRRYNSidVLLVDEGSMVTFDLL 243
Cdd:COG3267  118 AAAGRRV--VLIIDEAQNLPPETL 139
AAA_22 pfam13401
AAA domain;
149-247 1.00e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  149 FSIVSGGPGTGKTFLAAQLILSLVKQQPKLRIAIVSPTGKATSHIRQILMKYNI-----FDDMVLMQTVHHFLQEYAyrr 223
Cdd:pfam13401   7 ILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALGLplsgrLSKEELLAALQQLLLALA--- 83
                          90       100
                  ....*....|....*....|....
gi 499194732  224 ynSIDVLLVDEGSMVTFDLLYSLV 247
Cdd:pfam13401  84 --VAVVLIIDEAQHLSLEALEELR 105
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
149-202 1.56e-03

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 39.45  E-value: 1.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499194732 149 FSIVSGGPGTGKTFLAAQLILSLV---KQQPKLRIAIVSPTGKATSHIRQILMKYNI 202
Cdd:cd17936   18 LALIQGPPGTGKTFLGVKLVRALLqnqDLSITGPILVVCYTNHALDQFLEGLLDFGP 74
DUF2075 pfam09848
Schlafen group 3, DNA/RNA helicase domain; This domain is found in at the C terminus of group ...
151-234 2.07e-03

Schlafen group 3, DNA/RNA helicase domain; This domain is found in at the C terminus of group 3 Schlafen proteins from mammals, and represents the DNA/RNA helicase domain. Schlafen proteins are involved in the control of cell proliferation, induction of immune responses, and in the regulation of viral replication. These proteins inhibit DNA replication and promote cell death in response to DNA damage. They play a role in genome surveillance to kill cells with defective replication. This domain is also found in various uncharacterized prokaryotic proteins fused to a DNA helicase, GIY-YIG or PD-(D/E)XK catalytic domain or HsdR-N(terminal) domain, which are similar to AAA DNA helicase, Type III restriction enzyme ATPase, RecD and RuvB helicase.


Pssm-ID: 430875 [Multi-domain]  Cd Length: 355  Bit Score: 40.34  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499194732  151 IVSGGPGTGKTFLAAQLILSLVKQQPKLRIAIVSPTGKATSHIRQIL---MKYNIFDDMV-----LMQTVHhflqeyayR 222
Cdd:pfam09848   5 LVTGGPGTGKTVIGLNLFAELEDSDLGRTAVYLSGNHPLVLVLYEALagdLRKKRKKSAFqrptsFINNLH--------K 76
                          90
                  ....*....|..
gi 499194732  223 RYNSIDVLLVDE 234
Cdd:pfam09848  77 THPHEDVVIFDE 88
RecB COG1074
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, ...
434-493 2.10e-03

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: 40.72  E-value: 2.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499194732 434 VMSVHKSQGSEYDevIVIIPKGSEVFGVS-------ILYTAITRAKYRVSVWGdPETLHKIIKKSNY 493
Cdd:COG1074  647 IMTIHKSKGLEFP--VVFLPALRERARAEelaeelrLLYVALTRARDRLVLSG-AVKKKDAEKESSW 710
PRK13833 PRK13833
conjugal transfer protein TrbB; Provisional
128-188 2.20e-03

conjugal transfer protein TrbB; Provisional


Pssm-ID: 172360 [Multi-domain]  Cd Length: 323  Bit Score: 40.17  E-value: 2.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499194732 128 IDSSILSEEQ-NFIFNKITQGCFSIVSGGPGTGKTFLAAQLILSLVKQQPKLRIAIVSPTGK 188
Cdd:PRK13833 124 VTSKIMTEAQaSVIRSAIDSRLNIVISGGTGSGKTTLANAVIAEIVASAPEDRLVILEDTAE 185
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
140-193 7.49e-03

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.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 38.09  E-value: 7.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499194732  140 IFNKITQGCFSIVSGGPGTGKTFLAAQLILSLVKQQ-----PKLRIAIVSPTGKATSHI 193
Cdd:pfam13086   6 IRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPatsaaAGPRILVCAPSNAAVDNI 64
 
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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