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Conserved domains on  [gi|2124614986|ref|XP_044686440|]
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3'-5' DNA helicase [Fusarium musae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MPH1 super family cl34113
ERCC4-related helicase [Replication, recombination and repair];
156-634 1.42e-130

ERCC4-related helicase [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG1111:

Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 414.13  E-value: 1.42e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLFNNTLVALPTGLGKTFIAATVMLNFYRwTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTGD 235
Cdd:COG1111      5 RLYQLNLAASALRKNTLVVLPTGLGKTAVALLVIAERLH-KKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  236 IPPALRVDEWESRRVFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTATPGSK 315
Cdd:COG1111     84 VSPEKRKELWEKARIIVATPQVIENDLIAGRIDLDDVSLLIFDEAHRAVGNYAYVYIAERYHEDAKDPLILGMTASPGSD 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  316 IETVQEVIDNLGISHCEIRTEDSIDIRQYVHQRNIEQVVLDPSDEMVLVSELFTKALKPMTDKLSSQNIWFGRSPmAITA 395
Cdd:COG1111    164 EEKIEEVCENLGIENVEVRTEEDPDVAPYVHDTEVEWIRVELPEELKEIRDLLNEVLDDRLKKLKELGVIVSTSP-DLSK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  396 YGLMQSQREWFaSRGRHANQGVQHMMRAVFSVLtSIAHSIKLLNFHGIKPFYDNLvdLRSEQEGKGEKGSKYKRQLIQDS 475
Cdd:COG1111    243 KDLLALQKKLQ-RRIREDDSEGYRAISILAEAL-KLRHALELLETQGVEALLRYL--ERLEEEARSSGGSKASKRLVSDP 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  476 NFQEMMDRISKWlRTEgfvgHPKLTALADTVLNHFMDQSDNsatRVIVFSEYRDSAEDIVRMLNKhqPLIKASVFVGQAD 555
Cdd:COG1111    319 RFRKAMRLAEEA-DIE----HPKLSKLREILKEQLGTNPDS---RIIVFTQYRDTAEMIVEFLSE--PGIKAGRFVGQAS 388
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124614986  556 GKRGEGMKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGRKRAGNIVLLLMRG 634
Cdd:COG1111    389 KEGDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGRVVVLIAKG 467
 
Name Accession Description Interval E-value
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
156-634 1.42e-130

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 414.13  E-value: 1.42e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLFNNTLVALPTGLGKTFIAATVMLNFYRwTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTGD 235
Cdd:COG1111      5 RLYQLNLAASALRKNTLVVLPTGLGKTAVALLVIAERLH-KKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  236 IPPALRVDEWESRRVFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTATPGSK 315
Cdd:COG1111     84 VSPEKRKELWEKARIIVATPQVIENDLIAGRIDLDDVSLLIFDEAHRAVGNYAYVYIAERYHEDAKDPLILGMTASPGSD 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  316 IETVQEVIDNLGISHCEIRTEDSIDIRQYVHQRNIEQVVLDPSDEMVLVSELFTKALKPMTDKLSSQNIWFGRSPmAITA 395
Cdd:COG1111    164 EEKIEEVCENLGIENVEVRTEEDPDVAPYVHDTEVEWIRVELPEELKEIRDLLNEVLDDRLKKLKELGVIVSTSP-DLSK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  396 YGLMQSQREWFaSRGRHANQGVQHMMRAVFSVLtSIAHSIKLLNFHGIKPFYDNLvdLRSEQEGKGEKGSKYKRQLIQDS 475
Cdd:COG1111    243 KDLLALQKKLQ-RRIREDDSEGYRAISILAEAL-KLRHALELLETQGVEALLRYL--ERLEEEARSSGGSKASKRLVSDP 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  476 NFQEMMDRISKWlRTEgfvgHPKLTALADTVLNHFMDQSDNsatRVIVFSEYRDSAEDIVRMLNKhqPLIKASVFVGQAD 555
Cdd:COG1111    319 RFRKAMRLAEEA-DIE----HPKLSKLREILKEQLGTNPDS---RIIVFTQYRDTAEMIVEFLSE--PGIKAGRFVGQAS 388
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124614986  556 GKRGEGMKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGRKRAGNIVLLLMRG 634
Cdd:COG1111    389 KEGDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGRVVVLIAKG 467
PRK13766 PRK13766
Hef nuclease; Provisional
156-654 2.12e-124

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 399.25  E-value: 2.12e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLFNNTLVALPTGLGKTFIAATVMLnfYRWTKK-AKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTG 234
Cdd:PRK13766    17 RLYQQLLAATALKKNTLVVLPTGLGKTAIALLVIA--ERLHKKgGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  235 DIPPALRVDEWESRRVFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTATPGS 314
Cdd:PRK13766    95 EVSPEKRAELWEKAKVIVATPQVIENDLIAGRISLEDVSLLIFDEAHRAVGNYAYVYIAERYHEDAKNPLVLGLTASPGS 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  315 KIETVQEVIDNLGISHCEIRTEDSIDIRQYVHQRNIEQVVLDPSDEMVLVSELFTKALKPMTDKLSSQNIwfgrspmaIT 394
Cdd:PRK13766   175 DEEKIKEVCENLGIEHVEVRTEDDPDVKPYVHKVKIEWVRVELPEELKEIRDLLNEALKDRLKKLKELGV--------IV 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  395 AYGLMQSQREWFASRGRhanqgVQHMMR----AVF---SVLTSI---AHSIKLLNFHGIKPFYDNLVDLRSEQEGKGekG 464
Cdd:PRK13766   247 SISPDVSKKELLGLQKK-----LQQEIAnddsEGYeaiSILAEAmklRHAVELLETQGVEALRRYLERLREEARSSG--G 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  465 SKYKRQLIQDSNFQEMMdriSKWLRTEgfVGHPKLTALADtVLNHFMDQSDNSatRVIVFSEYRDSAEDIVRMLNKHQpl 544
Cdd:PRK13766   320 SKASKRLVEDPRFRKAV---RKAKELD--IEHPKLEKLRE-IVKEQLGKNPDS--RIIVFTQYRDTAEKIVDLLEKEG-- 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  545 IKASVFVGQADGKRGEGMKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGRKRA 624
Cdd:PRK13766   390 IKAVRFVGQASKDGDKGMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGRQEE 469
                          490       500       510
                   ....*....|....*....|....*....|.
gi 2124614986  625 GNIVLLLMRGKEEDQFAKSKDNYEK-MQTLI 654
Cdd:PRK13766   470 GRVVVLIAKGTRDEAYYWSSRRKEKkMKEEL 500
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
155-334 7.93e-111

DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 342.00  E-value: 7.93e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  155 IRNYQFSIVKNSLFNNTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTG 234
Cdd:cd18033      3 LRDYQFTIVQKALFQNTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACYKITGIPSSQTAELTG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  235 DIPPALRVDEWESRRVFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTATPGS 314
Cdd:cd18033     83 SVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHRATGNYAYCQVVRELMRYNSHFRILALTATPGS 162
                          170       180
                   ....*....|....*....|
gi 2124614986  315 KIETVQEVIDNLGISHCEIR 334
Cdd:cd18033    163 KLEAVQQVIDNLLISHIEIR 182
DEXDc smart00487
DEAD-like helicases superfamily;
156-344 2.73e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 116.05  E-value: 2.73e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986   156 RNYQFSIVK--NSLFNNTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLT 233
Cdd:smart00487   10 RPYQKEAIEalLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLY 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986   234 GDIPPALRVDEWESRR--VFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTAT 311
Cdd:smart00487   90 GGDSKREQLRKLESGKtdILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLLSAT 169
                           170       180       190
                    ....*....|....*....|....*....|...
gi 2124614986   312 PGSKIETVQEVIDNlGISHCEIRTEDSIDIRQY 344
Cdd:smart00487  170 PPEEIENLLELFLN-DPVFIDVGFTPLEPIEQF 201
ResIII pfam04851
Type III restriction enzyme, res subunit;
154-312 7.32e-25

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 101.98  E-value: 7.32e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  154 AIRNYQFSIVKNslFNNTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLT 233
Cdd:pfam04851   11 AIENLLESIKNG--QKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIIS 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  234 GDippaLRVDEWESRRVFFMTPQTLLNDISHGY--ADPKSIALLVIDEAHRAVGEyAYAKVTKlirrFSKSFRVLALTAT 311
Cdd:pfam04851   89 GD----KKDESVDDNKIVVTTIQSLYKALELASleLLPDFFDVIIIDEAHRSGAS-SYRNILE----YFKPAFLLGLTAT 159

                   .
gi 2124614986  312 P 312
Cdd:pfam04851  160 P 160
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
560-626 5.58e-04

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 43.60  E-value: 5.58e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124614986  560 EGMKQAQQIEAINRFKR-GDFNVLVATSIGEEGLDIgQVDLIVcydSSASPI-RMLQRMGRTGRKRAGN 626
Cdd:TIGR01587  260 EKDRAKKEAELLREMKKsNEKFVIVATQVIEASLDI-SADVMI---TELAPIdSLIQRLGRLHRYGRKI 324
 
Name Accession Description Interval E-value
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
156-634 1.42e-130

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 414.13  E-value: 1.42e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLFNNTLVALPTGLGKTFIAATVMLNFYRwTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTGD 235
Cdd:COG1111      5 RLYQLNLAASALRKNTLVVLPTGLGKTAVALLVIAERLH-KKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  236 IPPALRVDEWESRRVFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTATPGSK 315
Cdd:COG1111     84 VSPEKRKELWEKARIIVATPQVIENDLIAGRIDLDDVSLLIFDEAHRAVGNYAYVYIAERYHEDAKDPLILGMTASPGSD 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  316 IETVQEVIDNLGISHCEIRTEDSIDIRQYVHQRNIEQVVLDPSDEMVLVSELFTKALKPMTDKLSSQNIWFGRSPmAITA 395
Cdd:COG1111    164 EEKIEEVCENLGIENVEVRTEEDPDVAPYVHDTEVEWIRVELPEELKEIRDLLNEVLDDRLKKLKELGVIVSTSP-DLSK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  396 YGLMQSQREWFaSRGRHANQGVQHMMRAVFSVLtSIAHSIKLLNFHGIKPFYDNLvdLRSEQEGKGEKGSKYKRQLIQDS 475
Cdd:COG1111    243 KDLLALQKKLQ-RRIREDDSEGYRAISILAEAL-KLRHALELLETQGVEALLRYL--ERLEEEARSSGGSKASKRLVSDP 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  476 NFQEMMDRISKWlRTEgfvgHPKLTALADTVLNHFMDQSDNsatRVIVFSEYRDSAEDIVRMLNKhqPLIKASVFVGQAD 555
Cdd:COG1111    319 RFRKAMRLAEEA-DIE----HPKLSKLREILKEQLGTNPDS---RIIVFTQYRDTAEMIVEFLSE--PGIKAGRFVGQAS 388
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124614986  556 GKRGEGMKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGRKRAGNIVLLLMRG 634
Cdd:COG1111    389 KEGDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGRVVVLIAKG 467
PRK13766 PRK13766
Hef nuclease; Provisional
156-654 2.12e-124

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 399.25  E-value: 2.12e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLFNNTLVALPTGLGKTFIAATVMLnfYRWTKK-AKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTG 234
Cdd:PRK13766    17 RLYQQLLAATALKKNTLVVLPTGLGKTAIALLVIA--ERLHKKgGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  235 DIPPALRVDEWESRRVFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTATPGS 314
Cdd:PRK13766    95 EVSPEKRAELWEKAKVIVATPQVIENDLIAGRISLEDVSLLIFDEAHRAVGNYAYVYIAERYHEDAKNPLVLGLTASPGS 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  315 KIETVQEVIDNLGISHCEIRTEDSIDIRQYVHQRNIEQVVLDPSDEMVLVSELFTKALKPMTDKLSSQNIwfgrspmaIT 394
Cdd:PRK13766   175 DEEKIKEVCENLGIEHVEVRTEDDPDVKPYVHKVKIEWVRVELPEELKEIRDLLNEALKDRLKKLKELGV--------IV 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  395 AYGLMQSQREWFASRGRhanqgVQHMMR----AVF---SVLTSI---AHSIKLLNFHGIKPFYDNLVDLRSEQEGKGekG 464
Cdd:PRK13766   247 SISPDVSKKELLGLQKK-----LQQEIAnddsEGYeaiSILAEAmklRHAVELLETQGVEALRRYLERLREEARSSG--G 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  465 SKYKRQLIQDSNFQEMMdriSKWLRTEgfVGHPKLTALADtVLNHFMDQSDNSatRVIVFSEYRDSAEDIVRMLNKHQpl 544
Cdd:PRK13766   320 SKASKRLVEDPRFRKAV---RKAKELD--IEHPKLEKLRE-IVKEQLGKNPDS--RIIVFTQYRDTAEKIVDLLEKEG-- 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  545 IKASVFVGQADGKRGEGMKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGRKRA 624
Cdd:PRK13766   390 IKAVRFVGQASKDGDKGMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGRQEE 469
                          490       500       510
                   ....*....|....*....|....*....|.
gi 2124614986  625 GNIVLLLMRGKEEDQFAKSKDNYEK-MQTLI 654
Cdd:PRK13766   470 GRVVVLIAKGTRDEAYYWSSRRKEKkMKEEL 500
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
155-334 7.93e-111

DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 342.00  E-value: 7.93e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  155 IRNYQFSIVKNSLFNNTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTG 234
Cdd:cd18033      3 LRDYQFTIVQKALFQNTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACYKITGIPSSQTAELTG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  235 DIPPALRVDEWESRRVFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTATPGS 314
Cdd:cd18033     83 SVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHRATGNYAYCQVVRELMRYNSHFRILALTATPGS 162
                          170       180
                   ....*....|....*....|
gi 2124614986  315 KIETVQEVIDNLGISHCEIR 334
Cdd:cd18033    163 KLEAVQQVIDNLLISHIEIR 182
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
496-631 8.93e-73

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 237.64  E-value: 8.93e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  496 HPKLTALADTVLNHFMDQSDNSATRVIVFSEYRDSAEDIVRMLNKHQPLIKASVFVGQADGKRGEGMKQAQQIEAINRFK 575
Cdd:cd18801      8 HPKLEKLEEIVKEHFKKKQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATRFIGQASGKSSKGMSQKEQKEVIEQFR 87
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2124614986  576 RGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGRKRAGNIVLLL 631
Cdd:cd18801     88 KGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQGRVVVLL 143
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
156-334 4.66e-49

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part 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: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 173.00  E-value: 4.66e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIV-KNSLFNNTLVALPTGLGKTFIAATVMLNFYRWTK---KAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTL 231
Cdd:cd17927      4 RNYQLELAqPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPagrKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  232 LTGDIPPALRVDE-WESRRVFFMTPQTLLNDISHG-YADPKSIALLVIDEAHRAVGEYAYAKVTKL-----IRRFSKSFR 304
Cdd:cd17927     84 LSGDTSENVSVEQiVESSDVIIVTPQILVNDLKSGtIVSLSDFSLLVFDECHNTTKNHPYNEIMFRyldqkLGSSGPLPQ 163
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2124614986  305 VLALTATPGS--------KIETVQEVIDNLGISHCEIR 334
Cdd:cd17927    164 ILGLTASPGVggaknteeALEHICKLCANLDISVIATV 201
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
156-335 7.86e-44

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 157.29  E-value: 7.86e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLFNNTLVALPTGLGKTFIAATVMLnfYRWTKK-AKLVFVAPTKPLVAQQVDACYNIAGIPrSETTLLTG 234
Cdd:cd18035      4 RLYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAA--DRLTKKgGKVLILAPSRPLVEQHAENLKRVLNIP-DKITSLTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  235 DIPPALRVDEWESRRVFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTATPGS 314
Cdd:cd18035     81 EVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHHAVGNYAYVYIAHRYKREANNPLILGLTASPGS 160
                          170       180
                   ....*....|....*....|.
gi 2124614986  315 KIETVQEVIDNLGISHCEIRT 335
Cdd:cd18035    161 DKEKIMEICENLGIEHIEIKT 181
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
156-326 4.26e-35

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 132.78  E-value: 4.26e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLFNNTLVALPTGLGKTFIAATVMLNFYRWTKKAKL-----VFVAPTKPLVAQQVDACyniagipRSETT 230
Cdd:cd18034      4 RSYQLELFEAALKRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNpkkraVFLVPTVPLVAQQAEAI-------RSHTD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  231 LLTGDIPPALRVDEWESRR---------VFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSK 301
Cdd:cd18034     77 LKVGEYSGEMGVDKWTKERwkeelekydVLVMTAQILLDALRHGFLSLSDINLLIFDECHHATGDHPYARIMKEFYHLEG 156
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2124614986  302 SF---RVLALTATP---GSKIETVQEVIDNL 326
Cdd:cd18034    157 RTsrpRILGLTASPvngKGDPKSVEKKIQQL 187
FANCM_ID cd12091
Insert domain of FANCM and related proteins; FANCM and related proteins, like Mph1 and Fml1, ...
364-481 3.48e-33

Insert domain of FANCM and related proteins; FANCM and related proteins, like Mph1 and Fml1, are DNA junction-specific helicases/translocases that bind to and process perturbed replication forks and intermediates of homologous recombination. FANCM contains an N-terminal superfamily 2 helicase (SF2) domain, although FANCM, in contrast to other members of this family, does not exhibit DNA helicase activity. The SF2 helicase domain is comprised of 3 structural domains, the 2 generally conserved helicase domains and a helical domain inserted between the two domains. FANCM is a component of the Fanconi anaemia (FA) core complex. FA is a rare genetic disease in humans that is associated with progressive bone marrow failure, a variety of developmental abnormalities, and a high incidence of cancer. A key role of this complex is to monoubiquitination of FANCD2 and FANCI during S-phase and in response to DNA damage. The role of FANCM during this process seems to be the recruitment of the complex to chromatin.


Pssm-ID: 277190 [Multi-domain]  Cd Length: 116  Bit Score: 123.94  E-value: 3.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  364 VSELFTKALKPMTDKLSSQNIWFGRSPMAITAYGLMQSQREWFASRGRHaNQGVQHMMRAVFSVLTSIAHSIKLLNFHGI 443
Cdd:cd12091      3 IRDLLAKVLEPFLKRLNQAGILPNRDPAKLSPFRLLQARDKFRANPPGN-NEGQKGSIEGDFALLISLAHAMELLLEHGI 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2124614986  444 KPFYDNLVDLRSEQEGkgeKGSKYKRQLIQDSNFQEMM 481
Cdd:cd12091     82 RPFYDYLKEIKDETKA---KGSKSKKELAKNPNFKALM 116
DEXDc smart00487
DEAD-like helicases superfamily;
156-344 2.73e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 116.05  E-value: 2.73e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986   156 RNYQFSIVK--NSLFNNTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLT 233
Cdd:smart00487   10 RPYQKEAIEalLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLY 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986   234 GDIPPALRVDEWESRR--VFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTAT 311
Cdd:smart00487   90 GGDSKREQLRKLESGKtdILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLLSAT 169
                           170       180       190
                    ....*....|....*....|....*....|...
gi 2124614986   312 PGSKIETVQEVIDNlGISHCEIRTEDSIDIRQY 344
Cdd:smart00487  170 PPEEIENLLELFLN-DPVFIDVGFTPLEPIEQF 201
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
156-625 1.72e-25

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 112.43  E-value: 1.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSL------FNNTLVALPTGLGKTFIAATVMLNFYRwtkKAKLVFVAPTKPLVAQQVDACYNIAGIPRSET 229
Cdd:COG1061     82 RPYQQEALEALLaalergGGRGLVVAPTGTGKTVLALALAAELLR---GKRVLVLVPRRELLEQWAEELRRFLGDPLAGG 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  230 TlltgdippalrvDEWESRRVFFMTPQTLLNDISHGYADPKsIALLVIDEAHRAVGEyayaKVTKLIRRFSKSFRvLALT 309
Cdd:COG1061    159 G------------KKDSDAPITVATYQSLARRAHLDELGDR-FGLVIIDEAHHAGAP----SYRRILEAFPAAYR-LGLT 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  310 ATPgskietvqevidnlgishceIRTEDS-IDIRQYVHqrnieqvvldpsdemvLVSELftkalkpmtdklssqniwfgR 388
Cdd:COG1061    221 ATP--------------------FRSDGReILLFLFDG----------------IVYEY--------------------S 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  389 SPMAItayglmqsqrewfasrgrhaNQGVqhmmravfsvltsiahsIKLLNFHGIKpfydnlVDLRSEQEGKGEKGSKYK 468
Cdd:COG1061    245 LKEAI--------------------EDGY-----------------LAPPEYYGIR------VDLTDERAEYDALSERLR 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  469 RQLIQDSnfQEMMDRISKWLRTEGfvghpkltaladtvlnhfmdqsdnSATRVIVFSEYRDSAEDIVRMLNKHQplIKAS 548
Cdd:COG1061    282 EALAADA--ERKDKILRELLREHP------------------------DDRKTLVFCSSVDHAEALAELLNEAG--IRAA 333
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124614986  549 VFVGQadgkrgegMKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGRKRAG 625
Cdd:COG1061    334 VVTGD--------TPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPG 402
ResIII pfam04851
Type III restriction enzyme, res subunit;
154-312 7.32e-25

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 101.98  E-value: 7.32e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  154 AIRNYQFSIVKNslFNNTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLT 233
Cdd:pfam04851   11 AIENLLESIKNG--QKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIIS 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  234 GDippaLRVDEWESRRVFFMTPQTLLNDISHGY--ADPKSIALLVIDEAHRAVGEyAYAKVTKlirrFSKSFRVLALTAT 311
Cdd:pfam04851   89 GD----KKDESVDDNKIVVTTIQSLYKALELASleLLPDFFDVIIIDEAHRSGAS-SYRNILE----YFKPAFLLGLTAT 159

                   .
gi 2124614986  312 P 312
Cdd:pfam04851  160 P 160
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
520-621 2.19e-23

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 95.74  E-value: 2.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  520 RVIVFSEYRDSAEdiVRMLNKHQPlIKASVFVGQadgkrgegMKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDL 599
Cdd:pfam00271   17 KVLIFSQTKKTLE--AELLLEKEG-IKVARLHGD--------LSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDL 85
                           90       100
                   ....*....|....*....|..
gi 2124614986  600 IVCYDSSASPIRMLQRMGRTGR 621
Cdd:pfam00271   86 VINYDLPWNPASYIQRIGRAGR 107
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
491-631 2.88e-23

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 96.89  E-value: 2.88e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  491 EGFVGHPKLTALADTVLNHFmdqSDNSATRVIVFSEYRDSAEDIVRMLNKHQ---PLIKASVFVGQA--DGKRGEGMKQA 565
Cdd:cd18802      1 EEIVVIPKLQKLIEILREYF---PKTPDFRGIIFVERRATAVVLSRLLKEHPstlAFIRCGFLIGRGnsSQRKRSLMTQR 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124614986  566 QQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRtGRKRAGNIVLLL 631
Cdd:cd18802     78 KQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNSKYILMV 142
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
170-319 1.60e-20

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 89.61  E-value: 1.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  170 NTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFV-APTKPLVAQQVDACYNIAGIPRSETTLLTGDIPPALRVDEWESR 248
Cdd:pfam00270   16 DVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVlAPTRELAEQIYEELKKLGKGLGLKVASLLGGDSRKEQLEKLKGP 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124614986  249 RVFFMTPQTLLnDISHGYADPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTATPGSKIETV 319
Cdd:pfam00270   96 DILVGTPGRLL-DLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATLPRNLEDL 165
HELICc smart00490
helicase superfamily c-terminal domain;
561-622 3.23e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 83.03  E-value: 3.23e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124614986   561 GMKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGRK 622
Cdd:smart00490   20 GLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
156-312 3.27e-19

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 85.69  E-value: 3.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSL------FNNTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFVAPTKPLVAQQVDACYNIagIPRSET 229
Cdd:cd18032      2 RYYQQEAIEALEearekgQRRALLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQAERSFKEV--LPDGSF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  230 TLLTGDIppalrvDEWESRRVFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVgeyaYAKVTKLIRRFSKSFrVLALT 309
Cdd:cd18032     80 GNLKGGK------KKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHHAI----ASSYRKILEYFEPAF-LLGLT 148

                   ...
gi 2124614986  310 ATP 312
Cdd:cd18032    149 ATP 151
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
169-331 3.83e-17

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 80.38  E-value: 3.83e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  169 NNTLVALPTGLGKTFIAATVMLNFYRwTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTGDIPPALRVDewESR 248
Cdd:cd17921     18 DSVLVSAPTSSGKTLIAELAILRALA-TSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVNKLLL--AEA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  249 RVFFMTP---QTLLNDISHGYADPksIALLVIDEAHrAVGEYAYAKV----TKLIRRFSKSFRVLALTATpgskIETVQE 321
Cdd:cd17921     95 DILVATPeklDLLLRNGGERLIQD--VRLVVVDEAH-LIGDGERGVVlellLSRLLRINKNARFVGLSAT----LPNAED 167
                          170
                   ....*....|
gi 2124614986  322 VIDNLGISHC 331
Cdd:cd17921    168 LAEWLGVEDL 177
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
514-626 1.77e-16

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 76.78  E-value: 1.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  514 SDNSATRVIVFSEYRDSAEDIVRMLNKHQplIKASVFVGqadgkrgeGMKQAQQIEAINRFKRGDFNVLVATSIGEEGLD 593
Cdd:cd18787     23 EKLKPGKAIIFVNTKKRVDRLAELLEELG--IKVAALHG--------DLSQEERERALKKFRSGKVRVLVATDVAARGLD 92
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2124614986  594 IGQVDLIVCYDSSASPIRMLQRMGRTGrkRAGN 626
Cdd:cd18787     93 IPGVDHVINYDLPRDAEDYVHRIGRTG--RAGR 123
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
156-321 2.33e-15

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) 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: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 75.98  E-value: 2.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLFN-NTLVALPTGLGKTFIAATVMLN----FYRWTKKAKLVFVAPTKPLVAQQVDA-------CYNIAG 223
Cdd:cd18036      4 RNYQLELVLPALRGkNTIICAPTGSGKTRVAVYICRHhlekRRSAGEKGRVVVLVNKVPLVEQQLEKffkyfrkGYKVTG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  224 IPRSETTLLTGDippalrvDEWESRRVFFMTPQTLLNDISHGYADPK----SIALLVIDEAHRAVGEYAYAKVTKLIRRF 299
Cdd:cd18036     84 LSGDSSHKVSFG-------QIVKASDVIICTPQILINNLLSGREEERvylsDFSLLIFDECHHTQKEHPYNKIMRMYLDK 156
                          170       180
                   ....*....|....*....|....*..
gi 2124614986  300 SKSFR-----VLALTATPGSKIETVQE 321
Cdd:cd18036    157 KLSSQgplpqILGLTASPGVGGARSFE 183
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
159-327 1.44e-14

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 78.01  E-value: 1.44e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  159 QFSIVKNSLFN--NTLVALPTGLGKTFIAATVMLNfyRWTKKAKLVFVAPTKPLVAQ---QVDACYNIAGIprsETTLLT 233
Cdd:COG1204     27 QAEALEAGLLEgkNLVVSAPTASGKTLIAELAILK--ALLNGGKALYIVPLRALASEkyrEFKRDFEELGI---KVGVST 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  234 GDIPPAlrvDEW-ESRRVFFMTPQTLLNDISHGYADPKSIALLVIDEAHrAVGEYA-----YAKVTKLiRRFSKSFRVLA 307
Cdd:COG1204    102 GDYDSD---DEWlGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAH-LIDDESrgptlEVLLARL-RRLNPEAQIVA 176
                          170       180
                   ....*....|....*....|
gi 2124614986  308 LTATpgskIETVQEVIDNLG 327
Cdd:COG1204    177 LSAT----IGNAEEIAEWLD 192
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
156-312 2.80e-14

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part 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: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 71.18  E-value: 2.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLFNNT----LVALPTGLGKTFIAATVMLNFYrwtkKAKLVFVAPTKPLVAQQVDAC--YNiagiPRSET 229
Cdd:cd17926      2 RPYQEEALEAWLAHKNnrrgILVLPTGSGKTLTALALIAYLK----ELRTLIVVPTDALLDQWKERFedFL----GDSSI 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  230 TLLTGDippalRVDEWESRRVFFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVGEyayaKVTKLIRRFSKSFRvLALT 309
Cdd:cd17926     74 GLIGGG-----KKKDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAK----TFSEILKELNAKYR-LGLT 143

                   ...
gi 2124614986  310 ATP 312
Cdd:cd17926    144 ATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
169-311 4.10e-13

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 67.81  E-value: 4.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  169 NNTLVALPTGLGKTFIAATVMLNFYRwTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSeTTLLTGDIPPALRVDEWESR 248
Cdd:cd00046      2 ENVLITAPTGSGKTLAALLAALLLLL-KKGKKVLVLVPTKALALQTAERLRELFGPGIR-VAVLVGGSSAEEREKNKLGD 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124614986  249 -RVFFMTPQTLLNDI-SHGYADPKSIALLVIDEAHRAVGEYAYAKVTKL--IRRFSKSFRVLALTAT 311
Cdd:cd00046     80 aDIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALILDLavRKAGLKNAQVILLSAT 146
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
502-626 8.37e-13

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 71.90  E-value: 8.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  502 LADTV------LNHFMDQSDnsATRVIVFSEYRDSAEDIVRMLNKHQplIKASVFvgqadgkRGEgMKQAQQIEAINRFK 575
Cdd:PRK11192   225 RADDLehktalLCHLLKQPE--VTRSIVFVRTRERVHELAGWLRKAG--INCCYL-------EGE-MVQAKRNEAIKRLT 292
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2124614986  576 RGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGrkRAGN 626
Cdd:PRK11192   293 DGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTG--RAGR 341
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
506-642 1.52e-12

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 70.95  E-value: 1.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  506 VLNHFMDQSDNSatRVIVFSEYRDSAEDIVRMLNKHQplIKASVFVGqadgkrgeGMKQAQQIEAINRFKRGDFNVLVAT 585
Cdd:COG0513    231 LLRRLLRDEDPE--RAIVFCNTKRGADRLAEKLQKRG--ISAAALHG--------DLSQGQRERALDAFRNGKIRVLVAT 298
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2124614986  586 SIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGrkRAGN--IVLLLMRGKEEDQFAK 642
Cdd:COG0513    299 DVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTG--RAGAegTAISLVTPDERRLLRA 355
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
170-336 8.14e-12

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 65.63  E-value: 8.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  170 NTLVALPTGLGKT--FIAATVMLnfyrwtKKAKLVfVAPTKPLVAQQVDACyNIAGIPrseTTLLTGDIPPALRVDEWES 247
Cdd:cd17920     29 DVLVVMPTGGGKSlcYQLPALLL------DGVTLV-VSPLISLMQDQVDRL-QQLGIR---AAALNSTLSPEEKREVLLR 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  248 R-----RVFFMTPQTLLND-----ISHGYADpKSIALLVIDEAH---------RAvgeyAYAKVTKLIRRFSKsFRVLAL 308
Cdd:cd17920     98 IkngqyKLLYVTPERLLSPdflelLQRLPER-KRLALIVVDEAHcvsqwghdfRP----DYLRLGRLRRALPG-VPILAL 171
                          170       180       190
                   ....*....|....*....|....*....|
gi 2124614986  309 TAT--PgskiETVQEVIDNLGISHCEIRTE 336
Cdd:cd17920    172 TATatP----EVREDILKRLGLRNPVIFRA 197
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
502-622 1.48e-11

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 63.44  E-value: 1.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  502 LADTVLNHFMDQSDNSATrVIVFSEYRDSAEDIVRMLNKHQPLIKASVFVGQADGKrgegMKQAQQIEAINRFKRGDFNV 581
Cdd:cd18796     23 SGADAYAEVIFLLERHKS-TLVFTNTRSQAERLAQRLRELCPDRVPPDFIALHHGS----LSRELREEVEAALKRGDLKV 97
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2124614986  582 LVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGRK 622
Cdd:cd18796     98 VVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHR 138
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
159-335 2.25e-11

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 64.20  E-value: 2.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  159 QFSIVKnSLFN--NTLVALPTGLGKT---FIAATvmlnFYRWTKKAKLVFVAPTKPLVAQQVDACyniagIPRSETTLLT 233
Cdd:cd18018     17 QEEAIA-RLLSgrSTLVVLPTGAGKSlcyQLPAL----LLRRRGPGLTLVVSPLIALMKDQVDAL-----PRAIKAAALN 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  234 GDIPPALRVDEWESRR-----VFFMTPQTLLN-DISHGYADPKSIALLVIDEAHrAVGEY------AYAKVTKLIRRFSK 301
Cdd:cd18018     87 SSLTREERRRILEKLRagevkILYVSPERLVNeSFRELLRQTPPISLLVVDEAH-CISEWshnfrpDYLRLCRVLRELLG 165
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2124614986  302 SFRVLALTATpgSKIETVQEVIDNLGI-SHCEIRT 335
Cdd:cd18018    166 APPVLALTAT--ATKRVVEDIASHLGIpESGVVRG 198
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
156-326 1.81e-10

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 61.76  E-value: 1.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLF-NNTLVALPTGLGKTFIAATVM---LNFYRWTKKAKLVFVAPTKPLVAQQVDAC--------YNIAG 223
Cdd:cd18073      4 RNYQLELALPAMKgKNTIICAPTGCGKTFVSLLICehhLKKFPQGQKGKVVFFATKVPVYEQQKSVFskyferhgYRVTG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  224 IprsettllTGDIPPALRVdEW--ESRRVFFMTPQTLLNDISHGYADPKSI-ALLVIDEAHRAVGEYAYAKV------TK 294
Cdd:cd18073     84 I--------SGATAENVPV-EQiiENNDIIILTPQILVNNLKKGTIPSLSIfTLMIFDECHNTSGNHPYNMImfryldQK 154
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2124614986  295 LIRRFSKSFRVLALTATPG-SKIETVQEVIDNL 326
Cdd:cd18073    155 LGGSSGPLPQIIGLTASVGvGDAKNTDEALDYI 187
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
497-618 8.19e-10

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 57.87  E-value: 8.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  497 PKLTALADTVLNHFMDQsdnsaTRVIVFSEYRDSAEDIVRMLNKHqpLIKASVFvgqaDGKrgegMKQAQQIEAINRFKR 576
Cdd:cd18793     11 GKLEALLELLEELREPG-----EKVLIFSQFTDTLDILEEALRER--GIKYLRL----DGS----TSSKERQKLVDRFNE 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2124614986  577 --GDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGR 618
Cdd:cd18793     76 dpDIRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDR 119
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
122-623 1.10e-09

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 62.55  E-value: 1.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  122 RVFRVDLPREEPTHHEVDTEAMQTWVYPTNLGA-IRNYQFSIVK--NSLFNNTLVAL----PtGLGKTFIAATVMLNFYR 194
Cdd:COG0553    208 LLELELLAEAAVDAFRLRRLREALESLPAGLKAtLRPYQLEGAAwlLFLRRLGLGGLladdM-GLGKTIQALALLLELKE 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  195 WTKKAKLVFVAPTkPLVAQQVDACYNIAGIPRseTTLLTGDIPPALRVDEWESRRVFFMTPQTLLNDISHgYADPKsIAL 274
Cdd:COG0553    287 RGLARPVLIVAPT-SLVGNWQRELAKFAPGLR--VLVLDGTRERAKGANPFEDADLVITSYGLLRRDIEL-LAAVD-WDL 361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  275 LVIDEAHRAVGeyAYAKVTKLIRRFSKSFRvLALTATP--------------------GSKIETVQEVIDNLgishcEIR 334
Cdd:COG0553    362 VILDEAQHIKN--PATKRAKAVRALKARHR-LALTGTPvenrleelwslldflnpgllGSLKAFRERFARPI-----EKG 433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  335 TEDSID-----IRQYVHQRNIEQVVLD--PSDEMVLVSELftkalkpmtdklssqniwfgrSPMAITAY-GLMQSQREWF 406
Cdd:COG0553    434 DEEALErlrrlLRPFLLRRTKEDVLKDlpEKTEETLYVEL---------------------TPEQRALYeAVLEYLRREL 492
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  407 ASRGRHANQGVqhmmraVFSVLTsiahsiKLlnfhgikpfydnlvdlrseqegkgekgskykRQL-----IQDSNFQEMM 481
Cdd:COG0553    493 EGAEGIRRRGL------ILAALT------RL-------------------------------RQIcshpaLLLEEGAELS 529
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  482 DRiskwlrtegfvgHPKLTALADTVLNHFMDQSdnsatRVIVFSEYRDSAEDIVRMLNKHQplIKASVFvgqaDGkrgeG 561
Cdd:COG0553    530 GR------------SAKLEALLELLEELLAEGE-----KVLVFSQFTDTLDLLEERLEERG--IEYAYL----HG----G 582
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124614986  562 MKQAQQIEAINRFKRG-DFNV-LVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRT---GRKR 623
Cdd:COG0553    583 TSAEERDELVDRFQEGpEAPVfLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAhriGQTR 649
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
520-631 2.95e-08

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 53.80  E-value: 2.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  520 RVIVFSEYRDSAEDIVRMLNkhQPLIKASVFVGQADGKRGeGMKQA--QQIEAinRFKRGDFNVLVATSIGEEGLDIGQV 597
Cdd:cd18797     37 KTIVFCRSRKLAELLLRYLK--ARLVEEGPLASKVASYRA-GYLAEdrREIEA--ELFNGELLGVVATNALELGIDIGGL 111
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2124614986  598 DLIVCYDSSASPIRMLQRMGRTGRKRAGNIVLLL 631
Cdd:cd18797    112 DAVVLAGYPGSLASLWQQAGRAGRRGKDSLVILV 145
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
519-626 8.79e-08

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 52.64  E-value: 8.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  519 TRVIVFSEYRDSAEDIVRMLNKhqPLIKASVfvgqadgkrgegmKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVD 598
Cdd:cd18789     50 DKIIVFTDNVEALYRYAKRLLK--PFITGET-------------PQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEAN 114
                           90       100
                   ....*....|....*....|....*....
gi 2124614986  599 LIVCYDSSASPIR-MLQRMGRTGRKRAGN 626
Cdd:cd18789    115 VAIQISGHGGSRRqEAQRLGRILRPKKGG 143
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
520-630 1.78e-07

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 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: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 49.62  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  520 RVIVFSEYRDSAEDIVRMLNkhqplikasvfvgqadgkrgegmkqaqqieainrfkrgdfnVLVATSIGEEGLDIGQVDL 599
Cdd:cd18785      5 KIIVFTNSIEHAEEIASSLE-----------------------------------------ILVATNVLGEGIDVPSLDT 43
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2124614986  600 IVCYDSSASPIRMLQRMGRTGR--KRAGNIVLL 630
Cdd:cd18785     44 VIFFDPPSSAASYIQRVGRAGRggKDEGEVILF 76
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
169-333 6.30e-07

Superfamily II DNA helicase RecQ [Replication, recombination and repair];


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 53.22  E-value: 6.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  169 NNTLVALPTGLGKT---FIAAtvmlnfyrwtkkakLVFVAPT---KPLVA---QQVDACyNIAGIPrseTTLLTGdippA 239
Cdd:COG0514     33 RDALVVMPTGGGKSlcyQLPA--------------LLLPGLTlvvSPLIAlmkDQVDAL-RAAGIR---AAFLNS----S 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  240 LRVDEWESR---------RVFFMTPQTLLND-----ISHGyadpkSIALLVIDEAH---------RAvgeyAYAKVTKLI 296
Cdd:COG0514     91 LSAEERREVlralragelKLLYVAPERLLNPrflelLRRL-----KISLFAIDEAHcisqwghdfRP----DYRRLGELR 161
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2124614986  297 RRFSKsFRVLALTAT--PgskiETVQEVIDNLGISHCEI 333
Cdd:COG0514    162 ERLPN-VPVLALTATatP----RVRADIAEQLGLEDPRV 195
DEXHc_RLR-3 cd18075
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ...
155-318 9.14e-07

DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 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: 350833 [Multi-domain]  Cd Length: 200  Bit Score: 50.63  E-value: 9.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  155 IRNYQFSIVKNSLF-NNTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFVAPTKPLVAQQVDACYNIAgIPRSETTLLT 233
Cdd:cd18075      3 LHGYQWEVVAPALRgKNSIIWLPTGAGKTRAAVYVARRHLETKRGAKVAVLVNKVHLVDQHLEKEFHVL-LDKYTVTAIS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  234 GDIPPA------LRVDEwesrrVFFMTPQTLLNDISHGYADPK----SIALLVIDEAHRAVGEYAYAK-----VTKLIRR 298
Cdd:cd18075     82 GDSSHKcffgqlARGSD-----VVICTAQILQNALLSGEEEAHveltDFSLLVIDECHHTHKEAVYNKimlsyLEKKLSR 156
                          170       180
                   ....*....|....*....|
gi 2124614986  299 FSKSFRVLALTATPGSKIET 318
Cdd:cd18075    157 QGDLPQILGLTASPGTGGAT 176
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
178-312 1.62e-06

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part 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: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 49.98  E-value: 1.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  178 GLGKTFIAATVMLNFYRWTKKAKLVFVAPtKPLVAQQVDACYNIAGIPRsetTLLTGDIPPALRvdeWESRRVFFMTPQT 257
Cdd:cd18011     27 GLGKTIEAGLIIKELLLRGDAKRVLILCP-ASLVEQWQDELQDKFGLPF---LILDRETAAQLR---RLIGNPFEEFPIV 99
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124614986  258 LlndISHGYADPKSI----------ALLVIDEAHRAVGEY--AYAKVTKLIRRFSKSFR-VLALTATP 312
Cdd:cd18011    100 I---VSLDLLKRSEErrglllseewDLVVVDEAHKLRNSGggKETKRYKLGRLLAKRARhVLLLTATP 164
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
514-641 1.79e-06

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 51.84  E-value: 1.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  514 SDNSATRVIVFSEYRDSaediVRMLNKHqpLIKASVFVGQADGKrgegMKQAQQIEAINRFKRGDFNVLVATSIGEEGLD 593
Cdd:PRK01297   331 TQNPWERVMVFANRKDE----VRRIEER--LVKDGINAAQLSGD----VPQHKRIKTLEGFREGKIRVLVATDVAGRGIH 400
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2124614986  594 IGQVDLIVCYDSSASPIRMLQRMGRTGrkRAGNIVLLLMRGKEEDQFA 641
Cdd:PRK01297   401 IDGISHVINFTLPEDPDDYVHRIGRTG--RAGASGVSISFAGEDDAFQ 446
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
163-310 2.35e-06

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 49.18  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  163 VKNSLFN---NTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFVAPTKPLVAQQVDACYN-IAGIPRSETTLLTGDIPP 238
Cdd:cd18021     11 VFNSLYNtddNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAkFGPLLGKKVVKLTGETST 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  239 ALRVdeWESRRVFFMTPQTLlnDI-SHGYADPK---SIALLVIDEAHRAVGEYAYAKVTKLIR-RF-----SKSFRVLAL 308
Cdd:cd18021     91 DLKL--LAKSDVILATPEQW--DVlSRRWKQRKnvqSVELFIADELHLIGGENGPVYEVVVSRmRYissqlEKPIRIVGL 166

                   ..
gi 2124614986  309 TA 310
Cdd:cd18021    167 SS 168
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
520-624 2.47e-06

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 51.35  E-value: 2.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  520 RVIVFSEYRDSAEDIVRMLNKHQplIKASVFVGQAdgkrgegmKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDL 599
Cdd:PRK10590   247 QVLVFTRTKHGANHLAEQLNKDG--IRSAAIHGNK--------SQGARTRALADFKSGDIRVLVATDIAARGLDIEELPH 316
                           90       100
                   ....*....|....*....|....*
gi 2124614986  600 IVCYDSSASPIRMLQRMGRTGRKRA 624
Cdd:PRK10590   317 VVNYELPNVPEDYVHRIGRTGRAAA 341
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
562-631 2.96e-06

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 51.39  E-value: 2.96e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124614986  562 MKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGRK-RAGNIVLLL 631
Cdd:PRK11634   279 MNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAgRAGRALLFV 349
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
159-313 4.84e-06

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 48.10  E-value: 4.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  159 QFSIVKNSLF--NNTLVALPTGLGKTFIAATVMLNFyrWTKKAKLVFVAPTKPLVAQQVD--ACYNIAGIprsETTLLTG 234
Cdd:cd18028      6 QAEAVRAGLLkgENLLISIPTASGKTLIAEMAMVNT--LLEGGKALYLVPLRALASEKYEefKKLEEIGL---KVGISTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  235 DIPpalRVDEWESRR-VFFMTPQTLLNDISHGYADPKSIALLVIDEAHrAVGEYAYAKV----TKLIRRFSKSFRVLALT 309
Cdd:cd18028     81 DYD---EDDEWLGDYdIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIH-LISDEERGPTlesiVARLRRLNPNTQIIGLS 156

                   ....
gi 2124614986  310 ATPG 313
Cdd:cd18028    157 ATIG 160
DEXHc_DDX60 cd18025
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ...
169-258 5.09e-06

DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350783 [Multi-domain]  Cd Length: 192  Bit Score: 48.52  E-value: 5.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  169 NNTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFVAPTKPLVAQ---QVDACYNIAGIPRSET--TLLTGDippaLRVD 243
Cdd:cd18025     17 ESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQvvaEVYARFSKKYPPSGKSlwGVFTRD----YRHN 92
                           90
                   ....*....|....*
gi 2124614986  244 EWESRRVFFMTPQTL 258
Cdd:cd18025     93 NPMNCQVLITVPECL 107
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
172-312 6.95e-06

Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 50.23  E-value: 6.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  172 LVALPTGLGKTFIAATVMlnfYR-W-TKKAKLV-FVAPTKPLVAQQVDA--CYNIAGIPRSETTLLTGDIPPalrvdewe 246
Cdd:COG4096    182 LLVMATGTGKTRTAIALI---YRlLkAGRAKRIlFLADRNALVDQAKNAfkPFLPDLDAFTKLYNKSKDIDK-------- 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  247 SRRVFFMTPQTLLNDISHGYADPK----SIA---LLVIDEAHR-------AVGEYayakvtklirrFSkSFRVlALTATP 312
Cdd:COG4096    251 SARVYFSTYQTMMNRIDGEEEEPGyrqfPPDffdLIIIDECHRgiyskwrAILDY-----------FD-ALQI-GLTATP 317
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
169-281 1.01e-05

C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350780 [Multi-domain]  Cd Length: 189  Bit Score: 47.37  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  169 NNTLVALPTGLGKTFIAATVMLNFYRWTKKAKLVFVAPTKPLVAQQVD----ACYNIAGIPRSEttlLTGDIPPALRvdE 244
Cdd:cd18022     18 NNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDdwkkRFEEKLGKKVVE---LTGDVTPDMK--A 92
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2124614986  245 WESRRVFFMTPQTlLNDISHGYADP---KSIALLVIDEAH 281
Cdd:cd18022     93 LADADIIITTPEK-WDGISRSWQTReyvQQVSLIIIDEIH 131
PTZ00110 PTZ00110
helicase; Provisional
507-626 2.11e-05

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 48.62  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  507 LNHFMDQSDNSATRVIVFSEYRDSAEDIVRMLnkhqplikasvfvgqadgkRGEGM---------KQAQQIEAINRFKRG 577
Cdd:PTZ00110   366 LKMLLQRIMRDGDKILIFVETKKGADFLTKEL-------------------RLDGWpalcihgdkKQEERTWVLNEFKTG 426
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2124614986  578 DFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGrkRAGN 626
Cdd:PTZ00110   427 KSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTG--RAGA 473
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
520-633 3.36e-05

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 47.91  E-value: 3.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  520 RVIVFSEYRDSAEDIVRMLNKHqplIKASVFVGQADGKRGeGMKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDL 599
Cdd:COG1205    290 RTLVFTRSRRGAELLARYARRA---LREPDLADRVAAYRA-GYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDA 365
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2124614986  600 IVCYD---SSASpirMLQRMGRTGRKRAGNIVLLLMR 633
Cdd:COG1205    366 VVLAGypgTRAS---FWQQAGRAGRRGQDSLVVLVAG 399
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
140-335 3.51e-05

DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.


Pssm-ID: 350774 [Multi-domain]  Cd Length: 208  Bit Score: 45.97  E-value: 3.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  140 TEAMQTWVYPTNLGAIRNYQFSIVKNSLF-NNTLVALPTGLGKTF---IAATVMlnfyrwtkKAKLVFVAPTKPLVAQQV 215
Cdd:cd18016      3 KEMMKIFHKKFGLHQFRTNQLEAINAALLgEDCFVLMPTGGGKSLcyqLPACVS--------PGVTVVISPLRSLIVDQV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  216 DACYNIaGIPrseTTLLTGDI--PPALRVDEWESR-----RVFFMTPQTL-----LNDISHGYADPKSIALLVIDEAHrA 283
Cdd:cd18016     75 QKLTSL-DIP---ATYLTGDKtdAEATKIYLQLSKkdpiiKLLYVTPEKIsasnrLISTLENLYERKLLARFVIDEAH-C 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2124614986  284 VGEYA------YAKVTKLIRRFsKSFRVLALTATPGSKIETvqEVIDNLGISHCEIRT 335
Cdd:cd18016    150 VSQWGhdfrpdYKRLNMLRQKF-PSVPMMALTATATPRVQK--DILNQLKMLRPQVFT 204
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
560-657 5.44e-05

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 46.65  E-value: 5.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  560 EGMKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIgQVDLIVcydSSASPI-RMLQRMGRT---GRKRAGNIVLLLMRGK 635
Cdd:cd09639    256 EKDRAKKEAELLLEFKKSEKFVIVATQVIEASLDI-SVDVMI---TELAPIdSLIQRLGRLhryGEKNGEEVYIITDAPD 331
                           90       100
                   ....*....|....*....|..
gi 2124614986  636 EEDQFAKSKDNYEKMQTLICEG 657
Cdd:cd09639    332 GKGQKPYPYDLVERTIELLEEG 353
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
520-625 7.30e-05

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 43.32  E-value: 7.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  520 RVIVFSEYRDSAEDIVRMLNKHQPlikasvfvgQADGKRGEGMKQAQQIEAINRFKRGD--FNVLVATSIGEEGLDIGQV 597
Cdd:cd18799      8 KTLIFCVSIEHAEFMAEAFNEAGI---------DAVALNSDYSDRERGDEALILLFFGElkPPILVTVDLLTTGVDIPEV 78
                           90       100
                   ....*....|....*....|....*...
gi 2124614986  598 DLIVCYDSSASPIRMLQRMGRTGRKRAG 625
Cdd:cd18799     79 DNVVFLRPTESRTLFLQMLGRGLRLHEG 106
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
514-621 7.92e-05

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 46.48  E-value: 7.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  514 SDNSATRVIVFSEYRDSAEDIVRMLNKHQplIKASVFVGQADGKRGEGMkqaqqieaINRFKRGDFNVLVATSIGEEGLD 593
Cdd:PRK04537   253 SRSEGARTMVFVNTKAFVERVARTLERHG--YRVGVLSGDVPQKKRESL--------LNRFQKGQLEILVATDVAARGLH 322
                           90       100
                   ....*....|....*....|....*...
gi 2124614986  594 IGQVDLIVCYDSSASPIRMLQRMGRTGR 621
Cdd:PRK04537   323 IDGVKYVYNYDLPFDAEDYVHRIGRTAR 350
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
169-326 8.35e-05

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 44.50  E-value: 8.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  169 NNTLVALPTGLGKT---FIAAtvmlnFYR--WTKKAKLVFVAPTKPLVAQQVDACYNIA--GIPRSETTLLTGDIPPALR 241
Cdd:cd17923     16 RSVVVTTGTASGKSlcyQLPI-----LEAllRDPGSRALYLYPTKALAQDQLRSLRELLeqLGLGIRVATYDGDTPREER 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  242 VDEWESR-RVFFMTP----QTLLNdiSHGYADP--KSIALLVIDEAHRAVGEYAyAKVTKLIRRFS-------KSFRVLA 307
Cdd:cd17923     91 RAIIRNPpRILLTNPdmlhYALLP--HHDRWARflRNLRYVVLDEAHTYRGVFG-SHVALLLRRLRrlcrrygADPQFIL 167
                          170
                   ....*....|....*....
gi 2124614986  308 LTATpgskIETVQEVIDNL 326
Cdd:cd17923    168 TSAT----IGNPAEHARTL 182
DEAD-like_helicase_N cd17912
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
170-215 9.49e-05

N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.


Pssm-ID: 350670 [Multi-domain]  Cd Length: 81  Bit Score: 42.12  E-value: 9.49e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2124614986  170 NTLVALPTGLGKTFIAatVMLNFYRWTKKAKLVFVAPTKPLVAQQV 215
Cdd:cd17912      1 NILHLGPTGSGKTLVA--IQKIASAMSSGKSVLVVTPTKLLAHEIL 44
PTZ00424 PTZ00424
helicase 45; Provisional
562-621 1.18e-04

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 45.97  E-value: 1.18e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  562 MKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGR 621
Cdd:PTZ00424   301 MDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGR 360
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
170-312 2.02e-04

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins 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: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 43.32  E-value: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  170 NTLVALPTGLGKTFIAATVMLnfYRWTKKAK----LVfVAPtKPLVAQQVDACYNIAgiPRSETTLLTGDIPPALRVDEW 245
Cdd:cd17919     21 GGILADEMGLGKTLQAIAFLA--YLLKEGKErgpvLV-VCP-LSVLENWEREFEKWT--PDLRVVVYHGSQRERAQIRAK 94
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  246 ESRR---VFFMTPQTLLNDISHGYADPKSiaLLVIDEAHRAVGEyaYAKVTKLIRRFSKSFRVLaLTATP 312
Cdd:cd17919     95 EKLDkfdVVLTTYETLRRDKASLRKFRWD--LVVVDEAHRLKNP--KSQLSKALKALRAKRRLL-LTGTP 159
PRK13767 PRK13767
ATP-dependent helicase; Provisional
572-620 2.16e-04

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 45.26  E-value: 2.16e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2124614986  572 NRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTG 620
Cdd:PRK13767   334 EKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
DEXHc_RecQ3 cd18017
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ...
156-328 2.35e-04

DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome.


Pssm-ID: 350775 [Multi-domain]  Cd Length: 193  Bit Score: 43.22  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLFN--NTLVALPTGLGK--TFIAATVMLNfyrwtkKAKLVfVAPTKPLVAQQVDACyNIAGIPRSettL 231
Cdd:cd18017     14 RPVQWKVIRSVLEErrDNLVVMATGYGKslCYQYPSVLLN------SLTLV-ISPLISLMEDQVLQL-VMSNIPAC---F 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  232 LTGDIPPALRVDEWESR-RVFFMTPQTLLNDISHGYADPKSIALLVIDEAHrAVGEY------AYAKVTKlIRRFSKSFR 304
Cdd:cd18017     83 LGSAQSQNVLDDIKMGKiRVIYVTPEFVSKGLELLQQLRNGITLIAIDEAH-CVSQWghdfrsSYRHLGS-IRNRLPNVP 160
                          170       180
                   ....*....|....*....|....
gi 2124614986  305 VLALTATPGSKIEtvQEVIDNLGI 328
Cdd:cd18017    161 IVALTATATPSVR--DDIIKNLNL 182
uvsW PHA02558
UvsW helicase; Provisional
156-286 3.37e-04

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 44.62  E-value: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  156 RNYQFSIVKNSLFNN-TLVALPTGLGKTFIAAtVMLNFYRWTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTG 234
Cdd:PHA02558   116 HWYQYDAVYEGLKNNrRLLNLPTSAGKSLIQY-LLSRYYLENYEGKVLIIVPTTSLVTQMIDDFVDYRLFPREAMHKIYS 194
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2124614986  235 DippalrVDEWESRRVFFMTPQTLlndishgYADPKS----IALLVIDEAHRAVGE 286
Cdd:PHA02558   195 G------TAKDTDAPIVVSTWQSA-------VKQPKEwfdqFGMVIVDECHLFTGK 237
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
169-311 3.92e-04

N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 43.13  E-value: 3.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  169 NNTLVALPTGLGKTFIAATVMLN---FYRWTKKA------KLVFVAPTKPLVAQQVD------ACYniaGIPRSEttlLT 233
Cdd:cd18019     34 ENLLLCAPTGAGKTNVALLTILReigKHRNPDGTinldafKIVYIAPMKALVQEMVGnfskrlAPY---GITVAE---LT 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  234 GDipPALRVDEWESRRVFFMTPQTLlnDI----SHGYADPKSIALLVIDEAH-----RA-VGEYAYAKVTKLIRRFSKSF 303
Cdd:cd18019    108 GD--QQLTKEQISETQIIVTTPEKW--DIitrkSGDRTYTQLVRLIIIDEIHllhddRGpVLESIVARTIRQIEQTQEYV 183

                   ....*...
gi 2124614986  304 RVLALTAT 311
Cdd:cd18019    184 RLVGLSAT 191
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
170-311 4.99e-04

N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 42.42  E-value: 4.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  170 NTLVALPTGLGKTFIAATVMLN---------FYRWTKKAKLVFVAPTKPLVAQQVDACYN---IAGIPRSEttlLTGDIp 237
Cdd:cd18020     19 NMLICAPTGAGKTNIAMLTILHeirqhvnqgGVIKKDDFKIVYIAPMKALAAEMVEKFSKrlaPLGIKVKE---LTGDM- 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  238 pALRVDEWESRRVFFMTPQ---TLLNDISHGYADPKSIALLVIDEAHR------AVGEYAYAKVTKLIRRFSKSFRVLAL 308
Cdd:cd18020     95 -QLTKKEIAETQIIVTTPEkwdVVTRKSSGDVALSQLVRLLIIDEVHLlhddrgPVIESLVARTLRQVESTQSMIRIVGL 173

                   ...
gi 2124614986  309 TAT 311
Cdd:cd18020    174 SAT 176
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
560-626 5.58e-04

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 43.60  E-value: 5.58e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124614986  560 EGMKQAQQIEAINRFKR-GDFNVLVATSIGEEGLDIgQVDLIVcydSSASPI-RMLQRMGRTGRKRAGN 626
Cdd:TIGR01587  260 EKDRAKKEAELLREMKKsNEKFVIVATQVIEASLDI-SADVMI---TELAPIdSLIQRLGRLHRYGRKI 324
PRK00254 PRK00254
ski2-like helicase; Provisional
170-317 6.08e-04

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 44.04  E-value: 6.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  170 NTLVALPTGLGKTFIAATVMLNFYrWTKKAKLVFVAPTKPLVAQQVDAC--YNIAGIprsETTLLTGDIPPAlrvDEWES 247
Cdd:PRK00254    41 NLVLAIPTASGKTLVAEIVMVNKL-LREGGKAVYLVPLKALAEEKYREFkdWEKLGL---RVAMTTGDYDST---DEWLG 113
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124614986  248 R-RVFFMTPQTLLNDISHGYADPKSIALLVIDEAHrAVGEYAY-AKVTKLIRRFSKSFRVLALTATPGSKIE 317
Cdd:PRK00254   114 KyDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIH-LIGSYDRgATLEMILTHMLGRAQILGLSATVGNAEE 184
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
566-620 6.78e-04

Lhr-like helicase [Replication, recombination and repair];


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 43.94  E-value: 6.78e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2124614986  566 QQIEAinRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTG 620
Cdd:COG1201    316 LEVEE--ALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
157-311 9.11e-04

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 41.96  E-value: 9.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  157 NYQFSIVKNSLFN---NTLVALPTGLGKTFIAATVMLNFYR------WTkKAKLVFVAPTKPLVAQQVD---ACYNIAGI 224
Cdd:cd18023      3 NRIQSEVFPDLLYsdkNFVVSAPTGSGKTVLFELAILRLLKernplpWG-NRKVVYIAPIKALCSEKYDdwkEKFGPLGL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  225 prsETTLLTGDiPPALRVDEWESRRVFFMTPQTlLNDISHGYADP----KSIALLVIDEAHrAVGEY------AYAKVTK 294
Cdd:cd18023     82 ---SCAELTGD-TEMDDTFEIQDADIILTTPEK-WDSMTRRWRDNgnlvQLVALVLIDEVH-IIKENrgatleVVVSRMK 155
                          170       180
                   ....*....|....*....|....
gi 2124614986  295 LIRRFSK-------SFRVLALTAT 311
Cdd:cd18023    156 TLSSSSElrgstvrPMRFVAVSAT 179
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
573-626 1.03e-03

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 42.87  E-value: 1.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2124614986  573 RFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGrkRAGN 626
Cdd:PRK11776   287 RFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTG--RAGS 338
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
559-653 1.15e-03

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 40.79  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  559 GEGMKQAQQIEAI-NRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRML-QRMGRTGR-KRAGNIVLLLmrgk 635
Cdd:cd18810     57 AHGQMTENELEEVmLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLyQLRGRVGRsKERAYAYFLY---- 132
                           90
                   ....*....|....*...
gi 2124614986  636 eEDQFAKSKDNYEKMQTL 653
Cdd:cd18810    133 -PDQKKLTEDALKRLEAI 149
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
566-654 1.21e-03

CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 42.76  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  566 QQIEA--INRFKRGDFNVLVATSIGEEGLDIgqvDLIVCYdSSASPIRML-QRMGRT---GRKRAGNIVLLLMRGKEEDQ 639
Cdd:COG1203    408 SEIEKeiKERLERGKPCILVSTQVVEAGVDI---DFDVVI-RDLAPLDSLiQRAGRCnrhGRKEEEGNVYVFDPEDEGGG 483
                           90
                   ....*....|....*
gi 2124614986  640 FAKSKDNYEKMQTLI 654
Cdd:COG1203    484 YVYDKPLLERTRELL 498
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
172-282 1.24e-03

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 41.85  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  172 LVALPTGLGKT--FIAATVMLNFYRWTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTGDI--------PPALR 241
Cdd:cd17956     40 CVSAPTGSGKTlaYVLPIVQALSKRVVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKsfkkeqklLLVDT 119
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2124614986  242 VDEWESR-RVFFMTPQTLLNdisHGYADP----KSIALLVIDEAHR 282
Cdd:cd17956    120 SGRYLSRvDILVATPGRLVD---HLNSTPgftlKHLRFLVIDEADR 162
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
522-653 1.57e-03

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 40.33  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  522 IVFSEYRD--SAEDIVRMLNKHQPLIKasvfVGQADGKrgegMKQAQQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDL 599
Cdd:cd18792     36 IEESEKLDlkSIEALAEELKELVPEAR----VALLHGK----MTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANT 107
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2124614986  600 IVCYDSSASPIRML-QRMGRTGR-KRAGNIVLLLmrgkeEDQFAKSKDNYEKMQTL 653
Cdd:cd18792    108 MIIEDADRFGLSQLhQLRGRVGRgKHQSYCYLLY-----PDPKKLTETAKKRLRAI 158
Hef_ID cd12089
insert domain of Archaeal Hef helicase/nuclease; Archaeal Hef helicase/nuclease, originally ...
431-487 1.84e-03

insert domain of Archaeal Hef helicase/nuclease; Archaeal Hef helicase/nuclease, originally identified in the hyperthermophilic archaeon Pyrococcus furiosus, contains an N-terminal SF2 helicase domain and a C-terminal XPF/Mus81-type nuclease domain. Hef has been shown to process flap- or fork-DNA structures, and that both helicase and nuclease domain independently recognize branched DNA, with a strong preference for the forked DNA. The SF2 helicase domain is comprised of 3 structural domains, the 2 generally conserved helicase domains and a helical domain inserted between the two domains. This domain which is not present in all SF2 helicases, has been shown to play an important role in branched structure processing.


Pssm-ID: 277188 [Multi-domain]  Cd Length: 119  Bit Score: 39.12  E-value: 1.84e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2124614986  431 IAHSIKLLNFHGIKPFYDNLVDLRSEqegkGEKGSKYKRQLIQDSNFQEMMDRISKW 487
Cdd:cd12089     67 LDHAIELLETQGVEALLKYLERLEEE----AGSGSKAAKRLLEDPRFRKAVELLKEA 119
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
176-326 2.26e-03

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 40.65  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  176 PTGLGKT--FIAATVM-LNFYRWTKKAKLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTGDIPPALRVDEWESRR--V 250
Cdd:cd17957     35 PTGSGKTlaFLIPILQkLGKPRKKKGLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKydI 114
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124614986  251 FFMTPQTLLNDISHGYADPKSIALLVIDEAHRAVgEYAYAKVTKLIRRF--SKSFRVLALTATPGSKIET-VQEVIDNL 326
Cdd:cd17957    115 LVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLF-EPGFREQTDEILAActNPNLQRSLFSATIPSEVEElARSVMKDP 192
DEXHc_RLR-2 cd18074
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma ...
155-313 2.36e-03

DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma differentiation-associated protein 5 or Mda5 and IFIH1) is a viral double-stranded RNA (dsRNA) receptor that shares sequence similarity and signaling pathways with RIG-I, yet plays essential functions in antiviral immunity through distinct specificity for viral RNA. RLR-2 recognizes the internal duplex structure, whereas RIG-I recognizes the terminus of dsRNA. RLR-2 uses direct protein-protein contacts to stack along dsRNA in a head-to-tail arrangement. The signaling domain (tandem CARD), which decorates the outside of the core RLR-2 filament, also has an intrinsic propensity to oligomerize into an elongated structure that activates the signaling adaptor, MAVS. RLR-2 uses long dsRNA as a signaling platform to cooperatively assemble the core filament, which in turn promotes stochastic assembly of the tandem CARD oligomers for signaling. LGP2 appears to positively and negatively regulate RLR-2 and RIG-I signaling, respectively. RLR-2 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: 350832 [Multi-domain]  Cd Length: 216  Bit Score: 40.61  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  155 IRNYQFSIVKNSL-FNNTLVALPTGLGKTFIAATVMLNFYRWTKKA----KLVFVAPTKPLVAQQVDACYNIAGIPRSET 229
Cdd:cd18074      3 LRDYQMEVAKPALeGKNIIICLPTGSGKTRVAVYITKDHLDKKRKAsepgKVIVLVNKVPLVEQHYRKEFNPFLKHWYQV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  230 TLLTGDIPPALRVDE-WESRRVFFMTPQTLLNDISHGYADPKS------IALLVIDEAHRAVGEYAYAKVTKLI------ 296
Cdd:cd18074     83 IGLSGDSQLKISFPEvVKRYDVIICTAQILENSLLNATEEEDEgvqlsdFSLIIIDECHHTQKEAVYNNIMRRYlkqkik 162
                          170       180
                   ....*....|....*....|....*
gi 2124614986  297 -RRFSKSFR-------VLALTATPG 313
Cdd:cd18074    163 nRKQKKENKpliplpqILGLTASPG 187
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
568-634 4.13e-03

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 38.15  E-value: 4.13e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124614986  568 IEAINR-FKRGDFNVLVATSiGEEGLDI---GQVDLIVCyDssaspirmlQRM-GRTG-------RKRAGNIVLLLMRG 634
Cdd:cd17569     13 LKALKRlLRREGYEVLTATS-GEEALEIlkqEPVDVVIS-D---------QRMpGMDGaellkrvRERYPDTVRILLTG 80
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
566-625 4.40e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.45  E-value: 4.40e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  566 QQIEAINRFKRGDFNVLVATSIGEEGLDIGQVDLIVCYDSSASPIRMLQRMGRTGRKRAG 625
Cdd:PRK09751   315 QRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGG 374
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
177-317 9.78e-03

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 38.39  E-value: 9.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  177 TGLGKT--FIAATVMLNFYRWTKKA--KLVFVAPTKPLVAQQVDACYNIAGIPRSETTLLTGDIPpaLRVDEWESRR--- 249
Cdd:cd17947     36 TGSGKTaaFLLPILERLLYRPKKKAatRVLVLVPTRELAMQCFSVLQQLAQFTDITFALAVGGLS--LKAQEAALRArpd 113
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124614986  250 VFFMTPQTLLNDI--SHGYaDPKSIALLVIDEAHRAVGEYAYAKVTKLIRRFSKSFRVLALTATPGSKIE 317
Cdd:cd17947    114 IVIATPGRLIDHLrnSPSF-DLDSIEILVLDEADRMLEEGFADELKEILRLCPRTRQTMLFSATMTDEVK 182
 
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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