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Conserved domains on  [gi|738493081|ref|WP_036442501|]
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ATP-dependent RecD-like DNA helicase [Metamycoplasma hominis]

Protein Classification

ATP-dependent DNA helicase( domain architecture ID 11423480)

ATP-dependent DNA helicase belonging to the DEAD/DEAH box superfamily, utilizes the energy from ATP hydrolysis to unwind double-stranded DNA

CATH:  3.40.50.300
EC:  3.6.4.12
Gene Ontology:  GO:0032508|GO:0003677|GO:0005524|GO:0046872|GO:0003678|GO:0016887
PubMed:  2563148|20206133|20225155

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 244-745 1.37e-93

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: 301.13  E-value: 1.37e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 244 LKYLYNSGNTrilkdYLYDQLInfASQDTEWPRDVEtfnNSVELLVQNKYLIeieYEDGTYLSAkdVFDMEKYIVKRLKH 323
Cdd:COG0507   35 LSRAAGEGHT-----FPLEDLA--AARLLGVAEDIE---AALAALVESGPLV---LDGRRYLTR--LLEAEQRLARRLRR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 324 IESSSNP-----KFINFMPSEMFHPL---QLQAIETAL-TSKLTLITGNPGTGKTLITNEIIKQLLSVYDEddLAIVTPT 394
Cdd:COG0507  100 LARPALDeadveAALAALEPRAGITLsdeQREAVALALtTRRVSVLTGGAGTGKTTTLRALLAALEALGLR--VALAAPT 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 395 GRATINInniQEKTN--AVTIHSFLEWDVDNDKFMINEKN-AKPIECLIIDEFSMVSVDLFYSLLKGIKKNSlKRIILVG 471
Cdd:COG0507  178 GKAAKRL---SESTGieARTIHRLLGLRPDSGRFRHNRDNpLTPADLLVVDEASMVDTRLMAALLEALPRAG-ARLILVG 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 472 DKDQLPAIGAGYLIRDFIESNIFQTIVLSKIFRQAENFDIIQDALDINKGKLPE-FKGNNSQFIETKQSDLKSMLlfkln 550
Cdd:COG0507  254 DPDQLPSVGAGAVLRDLIESGTVPVVELTEVYRQADDSRIIELAHAIREGDAPEaLNARYADVVFVEAEDAEEAA----- 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 551 DLLQQGYSKR-----DIAILSPIynyETGIDQIN----ETLNNffRKLDGNEQIKYRDHVLAIDDKVINLVNDPKTKVFN 621
Cdd:COG0507  329 EAIVELYADRpaggeDIQVLAPT---NAGVDALNqairEALNP--AGELERELAEDGELELYVGDRVMFTRNDYDLGVFN 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 622 GEIGYISHFGFENKKnsfekvlasISVDFEnDSKTVSYSRKDFfANTYPAYCTSVHKYQGSECKCVIVVLFSEAKKLLSK 701
Cdd:COG0507  404 GDIGTVLSIDEDEGR---------LTVRFD-GREIVTYDPSEL-DQLELAYAITVHKSQGSTFDRVILVLPSEHSPLLSR 472

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 738493081 702 KLIYTAITRAKKYCVVIGEKEALITGINNDDDsnRITNIKYLWR 745
Cdd:COG0507  473 ELLYTALTRARELLTLVGDRDALARAVRRDTA--RATGLAERLR 514
 
Name Accession Description Interval E-value
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 244-745 1.37e-93

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: 301.13  E-value: 1.37e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 244 LKYLYNSGNTrilkdYLYDQLInfASQDTEWPRDVEtfnNSVELLVQNKYLIeieYEDGTYLSAkdVFDMEKYIVKRLKH 323
Cdd:COG0507   35 LSRAAGEGHT-----FPLEDLA--AARLLGVAEDIE---AALAALVESGPLV---LDGRRYLTR--LLEAEQRLARRLRR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 324 IESSSNP-----KFINFMPSEMFHPL---QLQAIETAL-TSKLTLITGNPGTGKTLITNEIIKQLLSVYDEddLAIVTPT 394
Cdd:COG0507  100 LARPALDeadveAALAALEPRAGITLsdeQREAVALALtTRRVSVLTGGAGTGKTTTLRALLAALEALGLR--VALAAPT 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 395 GRATINInniQEKTN--AVTIHSFLEWDVDNDKFMINEKN-AKPIECLIIDEFSMVSVDLFYSLLKGIKKNSlKRIILVG 471
Cdd:COG0507  178 GKAAKRL---SESTGieARTIHRLLGLRPDSGRFRHNRDNpLTPADLLVVDEASMVDTRLMAALLEALPRAG-ARLILVG 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 472 DKDQLPAIGAGYLIRDFIESNIFQTIVLSKIFRQAENFDIIQDALDINKGKLPE-FKGNNSQFIETKQSDLKSMLlfkln 550
Cdd:COG0507  254 DPDQLPSVGAGAVLRDLIESGTVPVVELTEVYRQADDSRIIELAHAIREGDAPEaLNARYADVVFVEAEDAEEAA----- 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 551 DLLQQGYSKR-----DIAILSPIynyETGIDQIN----ETLNNffRKLDGNEQIKYRDHVLAIDDKVINLVNDPKTKVFN 621
Cdd:COG0507  329 EAIVELYADRpaggeDIQVLAPT---NAGVDALNqairEALNP--AGELERELAEDGELELYVGDRVMFTRNDYDLGVFN 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 622 GEIGYISHFGFENKKnsfekvlasISVDFEnDSKTVSYSRKDFfANTYPAYCTSVHKYQGSECKCVIVVLFSEAKKLLSK 701
Cdd:COG0507  404 GDIGTVLSIDEDEGR---------LTVRFD-GREIVTYDPSEL-DQLELAYAITVHKSQGSTFDRVILVLPSEHSPLLSR 472

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 738493081 702 KLIYTAITRAKKYCVVIGEKEALITGINNDDDsnRITNIKYLWR 745
Cdd:COG0507  473 ELLYTALTRARELLTLVGDRDALARAVRRDTA--RATGLAERLR 514
recD_rel TIGR01448
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ...
 103-731 9.99e-90

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: 296.70  E-value: 9.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  103 VIKFLKSSHFPGIGEEKAKLIVKDLGIDALKKMVEDNSIDYSKYSISELTWNYAVEFIKNNpTLIEDQMFFLTN-NLTPS 181
Cdd:TIGR01448  80 IVAYLSSRSIKGVGKKLAQRIVKTFGEAAFDVLDDDPEKLLEVPGISKANLEKFVSQWSQQ-GDERRLLAGLQGlGIGIK 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  182 LYEIVAKKFEhfKDFIDAYKDNFYLF----------------------YLDNERISLEDMDKLHNIFNKFEHPFKPATHL 239
Cdd:TIGR01448 159 LAQRIYKFYQ--ADTLDRVEKDPYLLaedvkgigfltadqlaqalgiaLNDPRRITAGLVYSLQQACTEEGHTYLPRNRF 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  240 YKSFLKYLYNSGNTRILkdylydqlinfasqdtewprdvetfnNSVELLVQNKYLIE--IEYEDGTYLSAKDVFDMEKYI 317
Cdd:TIGR01448 237 IKQVVHLLNVQPQERLL--------------------------VPEAVELERLYLDEepKLAAEDGRIYLPSLFRAEKQI 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  318 VKRL-------KHIESSSNPKFINFMPSEMFHPL---QLQAIETALTSKLTLITGNPGTGKTLITNEIIKQLLSVYDEDD 387
Cdd:TIGR01448 291 ASHIrrllatsPAIGAINDQEHIWEVEKKLRKGLseeQKQALDTAIQHKVVILTGGPGTGKTTITRAIIELAEELGGLLP 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  388 LAIVTPTGRATININNIQEKTnAVTIHSFLEWDVDNDKFMINEKnakPIEC--LIIDEFSMVSVDLFYSLLKGIKKNSlk 465
Cdd:TIGR01448 371 VGLAAPTGRAAKRLGEVTGLT-ASTIHRLLGYGPDTFRHNHLED---PIDCdlLIVDESSMMDTWLALSLLAALPDHA-- 444

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  466 RIILVGDKDQLPAIGAGYLIRDFIESNIFQTIVLSKIFRQAENFDIIQDALDINKGKLPE-----FKGNNSQFIETKQSD 540
Cdd:TIGR01448 445 RLLLVGDTDQLPSVGPGQVLKDLILSQAIPVTRLTKVYRQAAGSPIITLAHGILHGEAPAwgdfkFLNLTRSEPEGAARH 524

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  541 LKSMLLFKLNDLLQQGYSKRDIAILSPIYNYETGIDQINETLNNFFR-KLDGNEQIKYRDHVLAIDDKVINLVNDPKTKV 619
Cdd:TIGR01448 525 IPLMVEKIVGMARVGGIPGADIQVLAPMYKGPLGIDALNQHLQALLNpYQKGQGGIEIAEGEYRKGDRVMQTKNDYNNEI 604

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  620 FNGEIGYISH--FGFENKKNSfekvlasISVDFenDSKTVSYSRKDFFaNTYPAYCTSVHKYQGSECKCVIVVLFSEAKK 697
Cdd:TIGR01448 605 FNGDLGMIVKieGAKQGKKDQ-------VVVDF--DGNEVELTRAELF-NLTLAYATSIHKSQGSEFPTVILPIHTAHMR 674

                         650       660       670
                  ....*....|....*....|....*....|....
gi 738493081  698 LLSKKLIYTAITRAKKYCVVIGEKEALITGINND 731
Cdd:TIGR01448 675 MLYRNLLYTALTRAKKRVILVGSAEAFDIAAARQ 708
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 345-503 3.73e-44

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: 155.79  E-value: 3.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 345 QLQAIETALTSKLTLITGNPGTGKTLITNEIIKQLLSVydEDDLAIVTPTGRATINInniQEKTN--AVTIHSFLEWDVD 422
Cdd:cd17933    2 QKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALEAE--GKRVVLAAPTGKAAKRL---SESTGieASTIHRLLGINPG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 423 NDKFMINEKNAKPIECLIIDEFSMVSVDLFYSLLKGIKKNSlkRIILVGDKDQLPAIGAGYLIRDFIESNIFQTIVLSKI 502
Cdd:cd17933   77 GGGFYYNEENPLDADLLIVDEASMVDTRLMAALLSAIPAGA--RLILVGDPDQLPSVGAGNVLRDLIASKGVPTVELTEV 154


                 .
gi 738493081 503 F 503
Cdd:cd17933  155 F 155
AAA_19 pfam13245
AAA domain;
345-481 5.03e-41

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 146.59  E-value: 5.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  345 QLQAIETALTSKLTLITGNPGTGKTLITNEIIKQLLSVYDEDD-LAIVTPTGRATININniqEKTN--AVTIHSFLEWD- 420
Cdd:pfam13245   1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGVSFpILLAAPTGRAAKRLS---ERTGlpASTIHRLLGFDd 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738493081  421 VDNDKFMINEKNAKPIECLIIDEFSMVSVDLFYSLLKGIKKNslKRIILVGDKDQLPAIGA 481
Cdd:pfam13245  78 LEAGGFLRDEEEPLDGDLLIVDEFSMVDLPLAYRLLKALPDG--AQLLLVGDPDQLPSVGP 136
recD PRK10875
exodeoxyribonuclease V subunit alpha;
352-482 4.56e-07

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 53.41  E-value: 4.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 352 ALTSKLTLITGNPGTGKTLITNEIIKQLLSVYDEDDLAI--VTPTGRAT-------------ININNIQEK---TNAVTI 413
Cdd:PRK10875 164 ALTRRISVISGGPGTGKTTTVAKLLAALIQLADGERCRIrlAAPTGKAAarlteslgkalrqLPLTDEQKKripEEASTL 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738493081 414 HSFLEWDVDNDKFMINEKNAKPIECLIIDEFSMVSVDLFYSLLKGIKKNSlkRIILVGDKDQLPAIGAG 482
Cdd:PRK10875 244 HRLLGAQPGSQRLRYHAGNPLHLDVLVVDEASMVDLPMMARLIDALPPHA--RVIFLGDRDQLASVEAG 310
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 354-494 4.28e-03

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: 38.51  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081   354 TSKLTLITGNPGTGKTLITNEIIKQLLsvYDEDDLAIVTPTGRATININNIQEKTNAVTIHSFLewDVDNDKFMINEKNA 433
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELG--PPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS--GELRLRLALALARK 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738493081   434 KPIECLIIDE-FSMVSVDLFYSLLKGIKKNSLKRIILvgdKDQLPAIGAGYLIRDFIESNIF 494
Cdd:smart00382  77 LKPDVLILDEiTSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGPALLR 135
 
Name Accession Description Interval E-value
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 244-745 1.37e-93

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: 301.13  E-value: 1.37e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 244 LKYLYNSGNTrilkdYLYDQLInfASQDTEWPRDVEtfnNSVELLVQNKYLIeieYEDGTYLSAkdVFDMEKYIVKRLKH 323
Cdd:COG0507   35 LSRAAGEGHT-----FPLEDLA--AARLLGVAEDIE---AALAALVESGPLV---LDGRRYLTR--LLEAEQRLARRLRR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 324 IESSSNP-----KFINFMPSEMFHPL---QLQAIETAL-TSKLTLITGNPGTGKTLITNEIIKQLLSVYDEddLAIVTPT 394
Cdd:COG0507  100 LARPALDeadveAALAALEPRAGITLsdeQREAVALALtTRRVSVLTGGAGTGKTTTLRALLAALEALGLR--VALAAPT 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 395 GRATINInniQEKTN--AVTIHSFLEWDVDNDKFMINEKN-AKPIECLIIDEFSMVSVDLFYSLLKGIKKNSlKRIILVG 471
Cdd:COG0507  178 GKAAKRL---SESTGieARTIHRLLGLRPDSGRFRHNRDNpLTPADLLVVDEASMVDTRLMAALLEALPRAG-ARLILVG 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 472 DKDQLPAIGAGYLIRDFIESNIFQTIVLSKIFRQAENFDIIQDALDINKGKLPE-FKGNNSQFIETKQSDLKSMLlfkln 550
Cdd:COG0507  254 DPDQLPSVGAGAVLRDLIESGTVPVVELTEVYRQADDSRIIELAHAIREGDAPEaLNARYADVVFVEAEDAEEAA----- 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 551 DLLQQGYSKR-----DIAILSPIynyETGIDQIN----ETLNNffRKLDGNEQIKYRDHVLAIDDKVINLVNDPKTKVFN 621
Cdd:COG0507  329 EAIVELYADRpaggeDIQVLAPT---NAGVDALNqairEALNP--AGELERELAEDGELELYVGDRVMFTRNDYDLGVFN 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 622 GEIGYISHFGFENKKnsfekvlasISVDFEnDSKTVSYSRKDFfANTYPAYCTSVHKYQGSECKCVIVVLFSEAKKLLSK 701
Cdd:COG0507  404 GDIGTVLSIDEDEGR---------LTVRFD-GREIVTYDPSEL-DQLELAYAITVHKSQGSTFDRVILVLPSEHSPLLSR 472

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 738493081 702 KLIYTAITRAKKYCVVIGEKEALITGINNDDDsnRITNIKYLWR 745
Cdd:COG0507  473 ELLYTALTRARELLTLVGDRDALARAVRRDTA--RATGLAERLR 514
recD_rel TIGR01448
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ...
 103-731 9.99e-90

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: 296.70  E-value: 9.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  103 VIKFLKSSHFPGIGEEKAKLIVKDLGIDALKKMVEDNSIDYSKYSISELTWNYAVEFIKNNpTLIEDQMFFLTN-NLTPS 181
Cdd:TIGR01448  80 IVAYLSSRSIKGVGKKLAQRIVKTFGEAAFDVLDDDPEKLLEVPGISKANLEKFVSQWSQQ-GDERRLLAGLQGlGIGIK 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  182 LYEIVAKKFEhfKDFIDAYKDNFYLF----------------------YLDNERISLEDMDKLHNIFNKFEHPFKPATHL 239
Cdd:TIGR01448 159 LAQRIYKFYQ--ADTLDRVEKDPYLLaedvkgigfltadqlaqalgiaLNDPRRITAGLVYSLQQACTEEGHTYLPRNRF 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  240 YKSFLKYLYNSGNTRILkdylydqlinfasqdtewprdvetfnNSVELLVQNKYLIE--IEYEDGTYLSAKDVFDMEKYI 317
Cdd:TIGR01448 237 IKQVVHLLNVQPQERLL--------------------------VPEAVELERLYLDEepKLAAEDGRIYLPSLFRAEKQI 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  318 VKRL-------KHIESSSNPKFINFMPSEMFHPL---QLQAIETALTSKLTLITGNPGTGKTLITNEIIKQLLSVYDEDD 387
Cdd:TIGR01448 291 ASHIrrllatsPAIGAINDQEHIWEVEKKLRKGLseeQKQALDTAIQHKVVILTGGPGTGKTTITRAIIELAEELGGLLP 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  388 LAIVTPTGRATININNIQEKTnAVTIHSFLEWDVDNDKFMINEKnakPIEC--LIIDEFSMVSVDLFYSLLKGIKKNSlk 465
Cdd:TIGR01448 371 VGLAAPTGRAAKRLGEVTGLT-ASTIHRLLGYGPDTFRHNHLED---PIDCdlLIVDESSMMDTWLALSLLAALPDHA-- 444

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  466 RIILVGDKDQLPAIGAGYLIRDFIESNIFQTIVLSKIFRQAENFDIIQDALDINKGKLPE-----FKGNNSQFIETKQSD 540
Cdd:TIGR01448 445 RLLLVGDTDQLPSVGPGQVLKDLILSQAIPVTRLTKVYRQAAGSPIITLAHGILHGEAPAwgdfkFLNLTRSEPEGAARH 524

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  541 LKSMLLFKLNDLLQQGYSKRDIAILSPIYNYETGIDQINETLNNFFR-KLDGNEQIKYRDHVLAIDDKVINLVNDPKTKV 619
Cdd:TIGR01448 525 IPLMVEKIVGMARVGGIPGADIQVLAPMYKGPLGIDALNQHLQALLNpYQKGQGGIEIAEGEYRKGDRVMQTKNDYNNEI 604

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  620 FNGEIGYISH--FGFENKKNSfekvlasISVDFenDSKTVSYSRKDFFaNTYPAYCTSVHKYQGSECKCVIVVLFSEAKK 697
Cdd:TIGR01448 605 FNGDLGMIVKieGAKQGKKDQ-------VVVDF--DGNEVELTRAELF-NLTLAYATSIHKSQGSEFPTVILPIHTAHMR 674

                         650       660       670
                  ....*....|....*....|....*....|....
gi 738493081  698 LLSKKLIYTAITRAKKYCVVIGEKEALITGINND 731
Cdd:TIGR01448 675 MLYRNLLYTALTRAKKRVILVGSAEAFDIAAARQ 708
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
 278-730 1.02e-51

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: 189.59  E-value: 1.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  278 VETFNNSVELLVQNKYLIeieYEDGTYLSAKDVFdmeKYIVKRL-KHIESSSNPKFINFMPSEMFHPLQLQAIETALTSK 356
Cdd:TIGR01447  87 VGLPGETAPPLVLCDGRL---YLRRYWREEEKLA---AKLRTLLeARKRTAPSAILENLFPLLNEQNWRKTAVALALKSN 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  357 LTLITGNPGTGKTLITNEIIKQLLS---VYDEDDLAIVTPTGRATININNIQEK----------------TNAVTIHSFL 417
Cdd:TIGR01447 161 FSLITGGPGTGKTTTVARLLLALVKqspKQGKLRIALAAPTGKAAARLAESLRKavknlaaaealiaalpSEAVTIHRLL 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  418 EWDVDNDKFMINEKNAKPIECLIIDEFSMVSVDLFYSLLKGIKKNSlkRIILVGDKDQLPAIGAGYLIRDFIE------- 490
Cdd:TIGR01447 241 GIKPDTKRFRHHERNPLPLDVLVVDEASMVDLPLMAKLLKALPPNT--KLILLGDKNQLPSVEAGAVLGDLCElasigks 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  491 -------------SNIF--QTIVLSKIFRQAENFDIIQDALDINKGKLPEFKGNNS-------QFIETKqSDLKSML--- 545
Cdd:TIGR01447 319 ilyalckkinsktRNPLsdNVCFLKTSHRFGKDSGIGQLAKAINSGDIEAVLNNLRsgqliefEFLNSK-EDAIERLknl 397

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  546 ----------LFKLNDLLQQGYSKRDIAILSPIYNYETGIDQINETLNNFFRKLDGNEQikyrDHVLAIDDKVINLVNDP 615
Cdd:TIGR01447 398 yvkyrtflqkLAALSDAKEILETFDRLRLLTALRDGPFGVLGLNRRIEQELQEKYFDPD----EEGWYIGRPIMVTENDY 473

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  616 KTKVFNGEIGYISHFGFENKKNSFEkvlasisvdFENDSKTVSYSRkdfFANTYPAYCTSVHKYQGSECKCVIVVLFSEA 695
Cdd:TIGR01447 474 TLGLFNGDIGVLLRDPDGILTVWFH---------FADGSKAVLPSR---LPNYETAFAMTVHKSQGSEFDHVILILPNGN 541

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 738493081  696 KKLLSKKLIYTAITRAKKYCVVIGEKEALITGINN 730
Cdd:TIGR01447 542 SPVLTRELLYTGITRAKDQLSVWSDKETLNAAIKR 576
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 345-503 3.73e-44

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: 155.79  E-value: 3.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 345 QLQAIETALTSKLTLITGNPGTGKTLITNEIIKQLLSVydEDDLAIVTPTGRATINInniQEKTN--AVTIHSFLEWDVD 422
Cdd:cd17933    2 QKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALEAE--GKRVVLAAPTGKAAKRL---SESTGieASTIHRLLGINPG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 423 NDKFMINEKNAKPIECLIIDEFSMVSVDLFYSLLKGIKKNSlkRIILVGDKDQLPAIGAGYLIRDFIESNIFQTIVLSKI 502
Cdd:cd17933   77 GGGFYYNEENPLDADLLIVDEASMVDTRLMAALLSAIPAGA--RLILVGDPDQLPSVGAGNVLRDLIASKGVPTVELTEV 154


                 .
gi 738493081 503 F 503
Cdd:cd17933  155 F 155
AAA_19 pfam13245
AAA domain;
345-481 5.03e-41

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 146.59  E-value: 5.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  345 QLQAIETALTSKLTLITGNPGTGKTLITNEIIKQLLSVYDEDD-LAIVTPTGRATININniqEKTN--AVTIHSFLEWD- 420
Cdd:pfam13245   1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGVSFpILLAAPTGRAAKRLS---ERTGlpASTIHRLLGFDd 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738493081  421 VDNDKFMINEKNAKPIECLIIDEFSMVSVDLFYSLLKGIKKNslKRIILVGDKDQLPAIGA 481
Cdd:pfam13245  78 LEAGGFLRDEEEPLDGDLLIVDEFSMVDLPLAYRLLKALPDG--AQLLLVGDPDQLPSVGP 136
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 345-525 1.84e-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: 98.41  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  345 QLQAIETALTS--KLTLITGNPGTGKTlitnEIIKQLLSVYDEDDLAIV--TPTGRATiniNNIQEKT--NAVTIHSFLE 418
Cdd:pfam13604   6 QAAAVRALLTSgdRVAVLVGPAGTGKT----TALKALREAWEAAGYRVIglAPTGRAA---KVLGEELgiPADTIAKLLH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  419 WDVDNDKFmineknaKPIECLIIDEFSMVSVDLFYSLLKGIKKNSLkRIILVGDKDQLPAIGAGYLIRDFIESNIfQTIV 498
Cdd:pfam13604  79 RLGGRAGL-------DPGTLLIVDEAGMVGTRQMARLLKLAEDAGA-RVILVGDPRQLPSVEAGGAFRDLLAAGI-GTAE 149

                         170       180
                  ....*....|....*....|....*..
gi 738493081  499 LSKIFRQAENfDIIQDALDINKGKLPE 525
Cdd:pfam13604 150 LTEIVRQRDP-WQRAASLALRDGDPAE 175
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
 345-504 1.63e-18

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: 83.84  E-value: 1.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 345 QLQAIETALTSKLTLITGNPGTGKTLITNEIIKQLLSvyDEDDLAIVTPTGRATINInniqektNAVTIHSF-------- 416
Cdd:cd18037    2 QRRVLDLVLDGKNVFFTGSAGTGKSYLLRRIIRALPS--RPKRVAVTASTGIAACNI-------GGTTLHSFagiglgse 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 417 -LEWDVDNDKFMINEKNA-KPIECLIIDEFSMVSVDLFYSL---LKGIKKNSLK----RIILVGDKDQLPAI-------- 479
Cdd:cd18037   73 pAEDLLERVKRSPYLVQRwRKCDVLIIDEISMLDADLFDKLdrvAREVRGSDKPfggiQLILCGDFLQLPPVtknserqa 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 738493081 480 -GAGYLIRDFIESN-----IFQTIVLSKIFR 504
Cdd:cd18037  153 fFFRGDQQFCFEAKswercIFLTVELTKVFR 183
SF1_C_RecD cd18809
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ...
 671-719 6.58e-16

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: 72.98  E-value: 6.58e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 738493081 671 AYCTSVHKYQGSECKCVIVVLfSEAKKLLSKKLIYTAITRAKKYCVVIG 719
Cdd:cd18809   33 AYAMTIHKSQGSEFDRVIVVL-PTSHPMLSRGLLYTALTRARKLLTLVG 80
UvrD_C_2 pfam13538
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ...
 670-718 5.85e-12

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: 61.05  E-value: 5.85e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 738493081  670 PAYCTSVHKYQGSECKCVIVV---LFSEAKKLLSKKLIYTAITRAKKYCVVI 718
Cdd:pfam13538   1 LAYALTVHKAQGSEFPAVFLVdpdLTAHYHSMLRRRLLYTAVTRARKKLVLV 52
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
 357-479 3.35e-09

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: 55.32  E-value: 3.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 357 LTLITGNPGTGKTLITNEIIKQLLSVYDEDDLAIVTPTGRAtininniqektnavtihsflewdVDNdkfmineknakpI 436
Cdd:cd17934    1 ISLIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVA-----------------------VDN------------V 45

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 738493081 437 ECLIIDEFSMVSVdlfYSLLKGIKKnsLKRIILVGDKDQLPAI 479
Cdd:cd17934   46 DVVIIDEASQITE---PELLIALIR--AKKVVLVGDPKQLPPV 83
TraI_TIGR TIGR02760
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome ...
 291-508 1.61e-07

conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome complex. In the process of conjugative plasmid transfer the realaxosome binds to the plasmid at the oriT (origin of transfer) site. The relaxase protein TraI mediates the single-strand nicking and ATP-dependent unwinding (relaxation, helicase activity) of the plasmid molecule. These two activities reside in separate domains of the protein.


Pssm-ID: 274285 [Multi-domain]  Cd Length: 1960  Bit Score: 55.29  E-value: 1.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081   291 NKYLIEIEYEDGTYLSAKDVFDMEKYIvkrLKHIESSSN---------PKFINFMPSEMFHPLQLQAIETALTSK--LTL 359
Cdd:TIGR02760  964 LYRLLSAEYGDGTRWTTRAALRTETSI---LLHILPGKEtvtplatraQVFLNLELLERLTHGQKQAIHLIISTKdrFVA 1040

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081   360 ITGNPGTGKTLITNEIIKQLLSVYDEDDLAIV--TPTGRAT--ININNIQEKTNAVTIHSFLEWDVDNDKFmineKNAkp 435
Cdd:TIGR02760 1041 VQGLAGVGKTTMLESRYKPVLQAFESEQLQVIglAPTHEAVgeLKSAGVQAQTLDSFLTDISLYRNSGGDF----RNT-- 1114

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738493081   436 ieCLIIDEFSMVSvDLFYSLLKGIKKNSLKRIILVGDKDQLPAIGAGYLIRDFIESNIFQTIVLSKIFRQAEN 508
Cdd:TIGR02760 1115 --LFILDESSMVS-NFQLTHATELVQKSGSRAVSLGDIAQLQSLAAGKPFELAITFDIIDTAIMKEIVRQNNS 1184
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 345-477 2.72e-07

DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases 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: 350801 [Multi-domain]  Cd Length: 127  Bit Score: 49.89  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 345 QLQAIETALTSKLTLITGNPGTGKT-LITNeIIKQLL----SVydeddlaIVTPTGRATINInnIQEKTNAVTIHSFLE- 418
Cdd:cd18043    4 QEAAIISARNGKNVVIQGPPGTGKSqTIAN-IIANALargkRV-------LFVSEKKAALDV--VRFPCWIMSPLSVSQy 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 419 WDVDNDKFMIneknakpiecLIIDEFSMVSV-DLFYSLLKGikknslKRIILVGDKDQLP 477
Cdd:cd18043   74 LPLNRNLFDL----------VIFDEASQIPIeEALPALFRG------KQVVVVGDDKQLP 117
recD PRK10875
exodeoxyribonuclease V subunit alpha;
352-482 4.56e-07

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 53.41  E-value: 4.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 352 ALTSKLTLITGNPGTGKTLITNEIIKQLLSVYDEDDLAI--VTPTGRAT-------------ININNIQEK---TNAVTI 413
Cdd:PRK10875 164 ALTRRISVISGGPGTGKTTTVAKLLAALIQLADGERCRIrlAAPTGKAAarlteslgkalrqLPLTDEQKKripEEASTL 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738493081 414 HSFLEWDVDNDKFMINEKNAKPIECLIIDEFSMVSVDLFYSLLKGIKKNSlkRIILVGDKDQLPAIGAG 482
Cdd:PRK10875 244 HRLLGAQPGSQRLRYHAGNPLHLDVLVVDEASMVDLPMMARLIDALPPHA--RVIFLGDRDQLASVEAG 310
SH3_13 pfam18335
ATP-dependent RecD-like DNA helicase SH3 domain; This is an SH3 (SRC homology domain 3) domain ...
 590-650 4.61e-07

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: 47.47  E-value: 4.61e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738493081  590 DGNEQIKYRDHVLAIDDKVINLVNDPKTKVFNGEIGYISHFGFENKKnsfekvlasISVDF 650
Cdd:pfam18335  14 PGKKEIKFGGRIFRVGDKVMQTKNNYDLGVFNGDIGIIVAIDKEEKT---------LTVDF 65
COG3972 COG3972
Superfamily I DNA and RNA helicases [Replication, recombination and repair];
344-726 4.99e-07

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


Pssm-ID: 443172 [Multi-domain]  Cd Length: 565  Bit Score: 52.91  E-value: 4.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 344 LQLQAIETALTSKLTLITGNPGTGKTLITNEIIKQLLSVYDEDDLAIVT------PTGRATIN-------INNIQEKTNA 410
Cdd:COG3972  162 LQQERIARSIPDGPQRIRGVAGSGKTVLLAAKAAYLALKHPGWRILVTCfnrslaDHLRDLIPrflrrfsNGEPEDNVKL 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 411 VTIHS------------FLEWDVDNDKFM---------INEKNAKPI-ECLIIDE---FSmvsvDLFYSLLKGIKKNSLK 465
Cdd:COG3972  242 IVFHAwggkllkqygipPLTFSQPNEAFDeackalleaIQGEIIPPIyDAILIDEaqdFE----PEFLRLLYQLLKPPKK 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 466 RIILVGDK----DQLPAIGAGYlirdfIESNIFQTIVLSKIFRQAENfdIIQDALDINKGkLPEFKGnnsqfietkqsdl 541
Cdd:COG3972  318 RLIWAYDEaqniYGRKIPSAGG-----IPAGIGRDTILKKNYRNTRP--ILTFAHAFGMG-LLRPPG------------- 376

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 542 ksmLLFKLNDLLQQGYSKRDIAILSPIYNyetgiDQINETLNNFFRKLDGNEQIKyrdhvlAIDDKVINLVNDPKTKVfn 621
Cdd:COG3972  377 ---LLQGDAEDYEVERPGDKVTLIRPPEP-----AGRKGPLPEFKKYDDRAEELE------AIAEEIKKNLRDEGLRP-- 440

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 622 GEIGYISHFGFENKK--NSFEKVLASISVDFENDSKTvsYSRKDFFAN---TYpaycTSVHKYQGSECKCVIVVLFSEAK 696
Cdd:COG3972  441 SDIAVIYLGNNEAKElgDRLAAALERQGIDSYIAGAR--SDPNFFWKDggvTI----STIHRAKGLEAPVVIIVGLDQLA 514

                        410       420       430
                 ....*....|....*....|....*....|....
gi 738493081 697 KLLS----KKLIYTAITRAKKYCVVIGEKEALIT 726
Cdd:COG3972  515 KGESlerlRNLLYVAMTRARGWLVVSGSGESMAE 548
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
 345-379 5.23e-07

DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain]  Cd Length: 234  Bit Score: 51.48  E-value: 5.23e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 738493081 345 QLQAIETALTSKLTLITGNPGTGKTLITNEIIKQL 379
Cdd:cd18039    6 QVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHL 40
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 345-478 7.22e-07

DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain]  Cd Length: 218  Bit Score: 50.67  E-value: 7.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 345 QLQAIETAL--TSKLTLITGNPGTGKTLITNEIIKQLLSVYDEDDLAIVTPTGRA-TININNIQEK--------TNAVT- 412
Cdd:cd18042    5 QLEAIASALqnSPGITLIQGPPGTGKTKTIVGILSVLLAGKYRKYYEKVKKKLRKlQRNLNNKKKKnrilvcapSNAAVd 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 413 -----IHSFLEWDVDNDKFMIN--------------------------------EKNAKPIECLIIDEFSMvSVDLfySL 455
Cdd:cd18042   85 eivlrLLSEGFLDGDGRSYKPNvvrvgrqelrasilneadivcttlsssgsdllESLPRGFDTVIIDEAAQ-AVEL--ST 161

                        170       180
                 ....*....|....*....|...
gi 738493081 456 LKGIKKNSlKRIILVGDKDQLPA 478
Cdd:cd18042  162 LIPLRLGC-KRLILVGDPKQLPA 183
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 345-387 8.34e-07

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: 49.85  E-value: 8.34e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 738493081 345 QLQAIETALTSKLTLITGNPGTGKTLITNEIIKQLLSVYDEDD 387
Cdd:cd17936    6 QLEALKHALTSELALIQGPPGTGKTFLGVKLVRALLQNQDLSI 48
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 341-479 1.43e-06

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: 49.73  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 341 FHPLQLQAIETALTSKLTLITGNPGTGKTLITNEIIKQLLSVYDEDDLAIVTPTGRAtinINNIQEKTNAVtihsflewD 420
Cdd:cd17935    6 FTPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQA---LNQLFEKIMAL--------D 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 421 VDNDKFMINEKNAKPIEC---------------------LIIDEFSMVS-VDLFYSLLKGIK---KNSLKRIILVGDKDQ 475
Cdd:cd17935   75 IDERHLLRLGHGAKIIAMtcthaalkrgelvelgfkydnILMEEAAQILeIETFIPLLLQNPedgPNRLKRLIMIGDHHQ 154


                 ....
gi 738493081 476 LPAI 479
Cdd:cd17935  155 LPPV 158
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 345-380 1.16e-04

DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain]  Cd Length: 191  Bit Score: 43.75  E-value: 1.16e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 738493081 345 QLQAIETALTSK-LTLITGNPGTGKTLITNEIIKQLL 380
Cdd:cd18044    6 QKEAVKFALSQKdVALIHGPPGTGKTTTVVEIILQAV 42
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 673-724 1.98e-04

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They 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: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 42.99  E-value: 1.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 738493081 673 CTSVHKYQGSECKCVIVVL-FSEAKK-----LLSKKLIYTAITRAKKYCVVIGEKEAL 724
Cdd:cd18808  113 VGTVDNFQGREKDVIILSLvRSNESGgsigfLSDPRRLNVALTRAKRGLIIVGNPDTL 170
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 675-719 2.79e-04

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: 40.50  E-value: 2.79e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 738493081 675 SVHKYQGSECKCVIVVLFSEakKLLSKKLIYTAITRAKKYCVVIG 719
Cdd:cd18786   47 TIDSSQGLTFDVVTLYLPTA--NSLTPRRLYVALTRARKRLVIYD 89
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
 345-479 4.55e-04

DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain]  Cd Length: 203  Bit Score: 42.22  E-value: 4.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 345 QLQAIETALTSK-LTLITGNPGTGKTLITNEIIKQLL----SVYdeddlaIVTPTGRATINI-----------------N 402
Cdd:cd18041    6 QRQAIKKVLNAKdYALILGMPGTGKTTTIAALVRILValgkSVL------LTSYTHSAVDNIllklkkfgvnflrlgrlK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 403 NIQEKTNAVTIHSFLEW--DVDNDKFMINEKNAKPIECL---------------IIDEFSMVSVD-----LFYSllkgik 460
Cdd:cd18041   80 KIHPDVQEFTLEAILKSckSVEELESKYESVSVVATTCLginhpifrrrtfdycIVDEASQITLPiclgpLRLA------ 153

                        170
                 ....*....|....*....
gi 738493081 461 knslKRIILVGDKDQLPAI 479
Cdd:cd18041  154 ----KKFVLVGDHYQLPPL 168
PIF1 pfam05970
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ...
 347-580 5.81e-04

PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits telomerase activity and is cell cycle regulated. This family includes a large number of largely uncharacterized plant proteins. This family includes a P-loop motif that is involved in nucleotide binding.


Pssm-ID: 428699 [Multi-domain]  Cd Length: 361  Bit Score: 42.75  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  347 QAIETALTSK--LTLITGNPGTGKTLITNEIIKQLLSvydEDDLAIVTP-TGRATININNiqektnAVTIHSFLEWDVDN 423
Cdd:pfam05970  11 AIIESVINNKggVFFVYGYGGTGKTFLWKAIITSLRS---EGKIVLAVAsSGVAALLLPG------GRTAHSRFGIPLDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  424 DKF---------MINE--KNAKPIeclIIDEFSMVSVDLFYSL---LKGIKKNSL------KRIILVGDKDQLP------ 477
Cdd:pfam05970  82 DELstckikrgsKLAEllEKTSLI---VWDEAPMTHRHCFEALdrtLRDILSETDdkpfggKTVVLGGDFRQILpvipkg 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081  478 --------AIGAGYLIRDFIesnifqTIVLSKIFRQAENFDIIQDA----------LDINKGKLPEfkGNNSQFIETKQS 539
Cdd:pfam05970 159 srpeivnaSITNSYLWKHVK------VLELTKNMRLLADSLDQTEAkelqdfsdwlLAIGDGKIND--ENEREQLIDIPI 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 738493081  540 DL---------KSMLLFKLNDLLQQGYSK---RDIAILSPiyNYETgIDQINE 580
Cdd:pfam05970 231 DIllntggdpiEAIVSEVYPDILQNSTDPnylEERAILCP--TNED-VDEINN 280
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
439-724 7.26e-04

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 43.19  E-value: 7.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 439 LIIDEFSMVSV-DLFYSLLKGikknslKRIILVGDKDQLPAIGAGYLIRDFIESNIFQTIvLSKIFRQAENF-------- 509
Cdd:COG1112  559 VIIDEASQATLaEALGALARA------KRVVLVGDPKQLPPVVFGEEAEEVAEEGLDESL-LDRLLARLPERgvmlrehy 631

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 510 ----DIIQ-----------DALDINKGKLPEFKGNNSQFIETKQSDLKS-----------MLLFKLNDLLQQGYSKRDIA 563
Cdd:COG1112  632 rmhpEIIAfsnrlfydgklVPLPSPKARRLADPDSPLVFIDVDGVYERRggsrtnpeeaeAVVELVRELLEDGPDGESIG 711

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 564 ILSPiynyetgidqinetlnnffrkldgneqikYRDHVLAIDDKVINLVNDPktkvfngeigyishfgfenkknsfekvl 643
Cdd:COG1112  712 VITP-----------------------------YRAQVALIRELLREALGDG---------------------------- 734

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 644 asisvdfendsktvsysRKDFFANTypayctsVHKYQGSECKCVIVVL-FSEAKKLL--------SKKLIYTAITRAKKY 714
Cdd:COG1112  735 -----------------LEPVFVGT-------VDRFQGDERDVIIFSLvYSNDEDVPrnfgflngGPRRLNVAVSRARRK 790

                        330
                 ....*....|
gi 738493081 715 CVVIGEKEAL 724
Cdd:COG1112  791 LIVVGSRELL 800
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 345-381 1.25e-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: 41.18  E-value: 1.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 738493081  345 QLQAIETALTSK-LTLITGNPGTGKTLITNEIIKQLLS 381
Cdd:pfam13086   2 QREAIRSALSSShFTLIQGPPGTGKTTTIVELIRQLLS 39
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 354-494 4.28e-03

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: 38.51  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081   354 TSKLTLITGNPGTGKTLITNEIIKQLLsvYDEDDLAIVTPTGRATININNIQEKTNAVTIHSFLewDVDNDKFMINEKNA 433
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELG--PPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS--GELRLRLALALARK 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738493081   434 KPIECLIIDE-FSMVSVDLFYSLLKGIKKNSLKRIILvgdKDQLPAIGAGYLIRDFIESNIF 494
Cdd:smart00382  77 LKPDVLILDEiTSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGPALLR 135
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 254-392 4.44e-03

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.14  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738493081 254 RILKDYLYDQLINFASQDTEWPRDVETFNNSVELLVQNKYLIEIEYEDGTYLSAKDVFDMEKYIVKRLKHIESSSNPKFI 333
Cdd:COG1401  115 AVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLES 194

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738493081 334 NFMPSEMF----HPLQLQAIETAL-TSKLTLITGNPGTGKTLITNEIIKQLLSvYDEDDLAIVT 392
Cdd:COG1401  195 EDDYLKDLlrekFEETLEAFLAALkTKKNVILAGPPGTGKTYLARRLAEALGG-EDNGRIEFVQ 257
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 345-380 5.77e-03

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: 39.14  E-value: 5.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 738493081 345 QLQAIETALTSKLT----LITGNPGTGKTLITNEIIKQLL 380
Cdd:cd18038    6 QKLAVRNIVTGTSRpppyIIFGPPGTGKTVTLVEAILQVL 45
 
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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