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Conserved domains on  [gi|26352047|dbj|BAC39660|]
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unnamed protein product [Mus musculus]

Protein Classification

DEAD/DEAH box helicase family protein( domain architecture ID 13029936)

DEAD/DEAH box helicase family protein such as a DEAD/DEAH box-containing ATP-dependent helicase, which catalyzes the unwinding of DNA or RNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
 77-258 4.21e-125

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: 359.71  E-value: 4.21e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  77 CPVRDYQLDISRSALFCNTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEM 156
Cdd:cd18033   1 VPLRDYQFTIVQKALFQNTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACYKITGIPSSQTAEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 157 TGSTQAVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTHFRILALSATP 236
Cdd:cd18033  81 TGSVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHRATGNYAYCQVVRELMRYNSHFRILALTATP 160

                       170       180
                ....*....|....*....|..
gi 26352047 237 GSDIKAVQQVITNLLIGKIELR 258
Cdd:cd18033 161 GSKLEAVQQVIDNLLISHIEIR 182
FANCM_ID cd12091
Insert domain of FANCM and related proteins; FANCM and related proteins, like Mph1 and Fml1, ...
 287-401 1.20e-34

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: 124.71  E-value: 1.20e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 287 AIQKTYIQILETFASSLIHRNVLMKRDIPNLTKYQIILARDQFRKNPSPNIVGiQQGIIEGEFALCISLYHGYELLQQMG 366
Cdd:cd12091   2 EIRDLLAKVLEPFLKRLNQAGILPNRDPAKLSPFRLLQARDKFRANPPGNNEG-QKGSIEGDFALLISLAHAMELLLEHG 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26352047 367 MRSLYFFLSGIMDGTKG-MTRARNELSRNEDFMKLY 401
Cdd:cd12091  81 IRPFYDYLKEIKDETKAkGSKSKKELAKNPNFKALM 116
 
Name Accession Description Interval E-value
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
 77-258 4.21e-125

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: 359.71  E-value: 4.21e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  77 CPVRDYQLDISRSALFCNTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEM 156
Cdd:cd18033   1 VPLRDYQFTIVQKALFQNTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACYKITGIPSSQTAEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 157 TGSTQAVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTHFRILALSATP 236
Cdd:cd18033  81 TGSVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHRATGNYAYCQVVRELMRYNSHFRILALTATP 160

                       170       180
                ....*....|....*....|..
gi 26352047 237 GSDIKAVQQVITNLLIGKIELR 258
Cdd:cd18033 161 GSKLEAVQQVIDNLLISHIEIR 182
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
80-400 6.07e-76

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 250.42  E-value: 6.07e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSALFCNTLVCLPTGLGKTFIAAVVMYNFYRWfPSGKVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEMTGS 159
Cdd:COG1111   5 RLYQLNLAASALRKNTLVVLPTGLGKTAVALLVIAERLHK-KGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 160 TQAVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTHFRILALSATPGSD 239
Cdd:COG1111  84 VSPEKRKELWEKARIIVATPQVIENDLIAGRIDLDDVSLLIFDEAHRAVGNYAYVYIAERYHEDAKDPLILGMTASPGSD 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 240 IKAVQQVITNLLIGKIELRSEESPDILPYSHERRVEKLVVPLGEELGAIQKTYIQILETFASSLIHRNVLMKRDiPNLTK 319
Cdd:COG1111 164 EEKIEEVCENLGIENVEVRTEEDPDVAPYVHDTEVEWIRVELPEELKEIRDLLNEVLDDRLKKLKELGVIVSTS-PDLSK 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 320 YQIILARDQfrknpspnivgIQQGIIEGEFAL---------CISLYHGYELLQQMGMRSLYFFLSGIMDGT--KGMTRAR 388
Cdd:COG1111 243 KDLLALQKK-----------LQRRIREDDSEGyraisilaeALKLRHALELLETQGVEALLRYLERLEEEArsSGGSKAS 311

                       330
                ....*....|..
gi 26352047 389 NELSRNEDFMKL 400
Cdd:COG1111 312 KRLVSDPRFRKA 323
PRK13766 PRK13766
Hef nuclease; Provisional
 80-401 3.11e-58

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 203.57  E-value: 3.11e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047   80 RDYQLDISRSALFCNTLVCLPTGLGKTFIAAVVM-YNFYRwfPSGKVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEMTG 158
Cdd:PRK13766  17 RLYQQLLAATALKKNTLVVLPTGLGKTAIALLVIaERLHK--KGGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  159 STQAVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTHFRILALSATPGS 238
Cdd:PRK13766  95 EVSPEKRAELWEKAKVIVATPQVIENDLIAGRISLEDVSLLIFDEAHRAVGNYAYVYIAERYHEDAKNPLVLGLTASPGS 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  239 DIKAVQQVITNLLIGKIELRSEESPDILPYSHERRVEKLVVPLGEEL----GAIQKTYIQILETFASslihrNVLMKRDI 314
Cdd:PRK13766 175 DEEKIKEVCENLGIEHVEVRTEDDPDVKPYVHKVKIEWVRVELPEELkeirDLLNEALKDRLKKLKE-----LGVIVSIS 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  315 PNLTKYQIILARDQfrknpspnivgIQQGIIEGE---------FALCISLYHGYELLQQMGMRSLYFFLSGIM--DGTKG 383
Cdd:PRK13766 250 PDVSKKELLGLQKK-----------LQQEIANDDsegyeaisiLAEAMKLRHAVELLETQGVEALRRYLERLReeARSSG 318

                        330
                 ....*....|....*...
gi 26352047  384 MTRARNELSRNEDFMKLY 401
Cdd:PRK13766 319 GSKASKRLVEDPRFRKAV 336
FANCM_ID cd12091
Insert domain of FANCM and related proteins; FANCM and related proteins, like Mph1 and Fml1, ...
 287-401 1.20e-34

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: 124.71  E-value: 1.20e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 287 AIQKTYIQILETFASSLIHRNVLMKRDIPNLTKYQIILARDQFRKNPSPNIVGiQQGIIEGEFALCISLYHGYELLQQMG 366
Cdd:cd12091   2 EIRDLLAKVLEPFLKRLNQAGILPNRDPAKLSPFRLLQARDKFRANPPGNNEG-QKGSIEGDFALLISLAHAMELLLEHG 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26352047 367 MRSLYFFLSGIMDGTKG-MTRARNELSRNEDFMKLY 401
Cdd:cd12091  81 IRPFYDYLKEIKDETKAkGSKSKKELAKNPNFKALM 116
DEXDc smart00487
DEAD-like helicases superfamily;
78-252 7.03e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.11  E-value: 7.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047     78 PVRDYQLDISRSALFC--NTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQMEACF-HVMGIPQSHMA 154
Cdd:smart00487   8 PLRPYQKEAIEALLSGlrDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKkLGPSLGLKVVG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047    155 EMTGSTQAVNRKEIWSSR-RVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTHFRILALS 233
Cdd:smart00487  88 LYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLLS 167

                          170
                   ....*....|....*....
gi 26352047    234 ATPGSDIKAVQQVITNLLI 252
Cdd:smart00487 168 ATPPEEIENLLELFLNDPV 186
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 94-243 6.33e-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: 86.14  E-value: 6.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047    94 NTLVCLPTGLGKTFIAAVVMYN-FYRWFPSGKVVFMAPTKPLVTQQMEAC---FHVMGIpqSHMAEMTGSTQAVNRKEIW 169
Cdd:pfam00270  16 DVLVQAPTGSGKTLAFLLPALEaLDKLDNGPQALVLAPTRELAEQIYEELkklGKGLGL--KVASLLGGDSRKEQLEKLK 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352047   170 SSrRVLFLTPQvMVNDLTRGAVPATHVKCLVVDEAHKaLGNYAYCQVVRELVKYT-THFRILALSATPGSDIKAV 243
Cdd:pfam00270  94 GP-DILVGTPG-RLLDLLQERKLLKNLKLLVLDEAHR-LLDMGFGPDLEEILRRLpKKRQILLLSATLPRNLEDL 165
 
Name Accession Description Interval E-value
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
 77-258 4.21e-125

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: 359.71  E-value: 4.21e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  77 CPVRDYQLDISRSALFCNTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEM 156
Cdd:cd18033   1 VPLRDYQFTIVQKALFQNTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACYKITGIPSSQTAEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 157 TGSTQAVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTHFRILALSATP 236
Cdd:cd18033  81 TGSVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHRATGNYAYCQVVRELMRYNSHFRILALTATP 160

                       170       180
                ....*....|....*....|..
gi 26352047 237 GSDIKAVQQVITNLLIGKIELR 258
Cdd:cd18033 161 GSKLEAVQQVIDNLLISHIEIR 182
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
80-400 6.07e-76

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 250.42  E-value: 6.07e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSALFCNTLVCLPTGLGKTFIAAVVMYNFYRWfPSGKVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEMTGS 159
Cdd:COG1111   5 RLYQLNLAASALRKNTLVVLPTGLGKTAVALLVIAERLHK-KGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 160 TQAVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTHFRILALSATPGSD 239
Cdd:COG1111  84 VSPEKRKELWEKARIIVATPQVIENDLIAGRIDLDDVSLLIFDEAHRAVGNYAYVYIAERYHEDAKDPLILGMTASPGSD 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 240 IKAVQQVITNLLIGKIELRSEESPDILPYSHERRVEKLVVPLGEELGAIQKTYIQILETFASSLIHRNVLMKRDiPNLTK 319
Cdd:COG1111 164 EEKIEEVCENLGIENVEVRTEEDPDVAPYVHDTEVEWIRVELPEELKEIRDLLNEVLDDRLKKLKELGVIVSTS-PDLSK 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 320 YQIILARDQfrknpspnivgIQQGIIEGEFAL---------CISLYHGYELLQQMGMRSLYFFLSGIMDGT--KGMTRAR 388
Cdd:COG1111 243 KDLLALQKK-----------LQRRIREDDSEGyraisilaeALKLRHALELLETQGVEALLRYLERLEEEArsSGGSKAS 311

                       330
                ....*....|..
gi 26352047 389 NELSRNEDFMKL 400
Cdd:COG1111 312 KRLVSDPRFRKA 323
PRK13766 PRK13766
Hef nuclease; Provisional
 80-401 3.11e-58

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 203.57  E-value: 3.11e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047   80 RDYQLDISRSALFCNTLVCLPTGLGKTFIAAVVM-YNFYRwfPSGKVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEMTG 158
Cdd:PRK13766  17 RLYQQLLAATALKKNTLVVLPTGLGKTAIALLVIaERLHK--KGGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  159 STQAVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTHFRILALSATPGS 238
Cdd:PRK13766  95 EVSPEKRAELWEKAKVIVATPQVIENDLIAGRISLEDVSLLIFDEAHRAVGNYAYVYIAERYHEDAKNPLVLGLTASPGS 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  239 DIKAVQQVITNLLIGKIELRSEESPDILPYSHERRVEKLVVPLGEEL----GAIQKTYIQILETFASslihrNVLMKRDI 314
Cdd:PRK13766 175 DEEKIKEVCENLGIEHVEVRTEDDPDVKPYVHKVKIEWVRVELPEELkeirDLLNEALKDRLKKLKE-----LGVIVSIS 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  315 PNLTKYQIILARDQfrknpspnivgIQQGIIEGE---------FALCISLYHGYELLQQMGMRSLYFFLSGIM--DGTKG 383
Cdd:PRK13766 250 PDVSKKELLGLQKK-----------LQQEIANDDsegyeaisiLAEAMKLRHAVELLETQGVEALRRYLERLReeARSSG 318

                        330
                 ....*....|....*...
gi 26352047  384 MTRARNELSRNEDFMKLY 401
Cdd:PRK13766 319 GSKASKRLVEDPRFRKAV 336
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
 80-258 7.20e-51

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: 170.31  E-value: 7.20e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSAL-FCNTLVCLPTGLGKTFIAAVVMYNFYRWFPS---GKVVFMAPTKPLVTQQMEACFHVMGIPQSHMAE 155
Cdd:cd17927   4 RNYQLELAQPALkGKNTIICLPTGSGKTFVAVLICEHHLKKFPAgrkGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 156 MTGSTQ-AVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPA-THVKCLVVDEAHKALGNYAYCQVVRELVKYTTH-----FR 228
Cdd:cd17927  84 LSGDTSeNVSVEQIVESSDVIIVTPQILVNDLKSGTIVSlSDFSLLVFDECHNTTKNHPYNEIMFRYLDQKLGssgplPQ 163

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 26352047 229 ILALSATPGSD--------IKAVQQVITNLLIGKIELR 258
Cdd:cd17927 164 ILGLTASPGVGgaknteeaLEHICKLCANLDISVIATV 201
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 80-259 4.83e-42

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: 146.51  E-value: 4.83e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSALFCNTLVCLPTGLGKTFIAAVVMYNFYRWFpSGKVVFMAPTKPLVTQQMEACFHVMGIPQShMAEMTGS 159
Cdd:cd18035   4 RLYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTKK-GGKVLILAPSRPLVEQHAENLKRVLNIPDK-ITSLTGE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 160 TQAVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTHFRILALSATPGSD 239
Cdd:cd18035  82 VKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHHAVGNYAYVYIAHRYKREANNPLILGLTASPGSD 161

                       170       180
                ....*....|....*....|
gi 26352047 240 IKAVQQVITNLLIGKIELRS 259
Cdd:cd18035 162 KEKIMEICENLGIEHIEIKT 181
FANCM_ID cd12091
Insert domain of FANCM and related proteins; FANCM and related proteins, like Mph1 and Fml1, ...
 287-401 1.20e-34

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: 124.71  E-value: 1.20e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 287 AIQKTYIQILETFASSLIHRNVLMKRDIPNLTKYQIILARDQFRKNPSPNIVGiQQGIIEGEFALCISLYHGYELLQQMG 366
Cdd:cd12091   2 EIRDLLAKVLEPFLKRLNQAGILPNRDPAKLSPFRLLQARDKFRANPPGNNEG-QKGSIEGDFALLISLAHAMELLLEHG 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26352047 367 MRSLYFFLSGIMDGTKG-MTRARNELSRNEDFMKLY 401
Cdd:cd12091  81 IRPFYDYLKEIKDETKAkGSKSKKELAKNPNFKALM 116
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 80-256 2.41e-32

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: 121.60  E-value: 2.41e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSALFCNTLVCLPTGLGKTFIAAVVMYNFYRWF----PSGK-VVFMAPTKPLVTQQMEACfhvmgipQSH-- 152
Cdd:cd18034   4 RSYQLELFEAALKRNTIVVLPTGSGKTLIAVMLIKEMGELNrkekNPKKrAVFLVPTVPLVAQQAEAI-------RSHtd 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 153 --MAEMTGSTQ-AVNRKEIW----SSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTT 225
Cdd:cd18034  77 lkVGEYSGEMGvDKWTKERWkeelEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDECHHATGDHPYARIMKEFYHLEG 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 26352047 226 HF---RILALSATP---GSDIKAVQ---QVITNLLIGKIE 256
Cdd:cd18034 157 RTsrpRILGLTASPvngKGDPKSVEkkiQQLEELLNSTIK 196
DEXDc smart00487
DEAD-like helicases superfamily;
78-252 7.03e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.11  E-value: 7.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047     78 PVRDYQLDISRSALFC--NTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQMEACF-HVMGIPQSHMA 154
Cdd:smart00487   8 PLRPYQKEAIEALLSGlrDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKkLGPSLGLKVVG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047    155 EMTGSTQAVNRKEIWSSR-RVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTHFRILALS 233
Cdd:smart00487  88 LYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLLS 167

                          170
                   ....*....|....*....
gi 26352047    234 ATPGSDIKAVQQVITNLLI 252
Cdd:smart00487 168 ATPPEEIENLLELFLNDPV 186
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 94-243 6.33e-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: 86.14  E-value: 6.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047    94 NTLVCLPTGLGKTFIAAVVMYN-FYRWFPSGKVVFMAPTKPLVTQQMEAC---FHVMGIpqSHMAEMTGSTQAVNRKEIW 169
Cdd:pfam00270  16 DVLVQAPTGSGKTLAFLLPALEaLDKLDNGPQALVLAPTRELAEQIYEELkklGKGLGL--KVASLLGGDSRKEQLEKLK 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352047   170 SSrRVLFLTPQvMVNDLTRGAVPATHVKCLVVDEAHKaLGNYAYCQVVRELVKYT-THFRILALSATPGSDIKAV 243
Cdd:pfam00270  94 GP-DILVGTPG-RLLDLLQERKLLKNLKLLVLDEAHR-LLDMGFGPDLEEILRRLpKKRQILLLSATLPRNLEDL 165
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
 80-237 9.17e-20

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: 87.15  E-value: 9.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSALFC-NTLVCLPTGLGKTFIAAVVMYNFYRWFPS----GKVVFMAPTKPLVTQQMEACFHVMgipqSHMA 154
Cdd:cd18036   4 RNYQLELVLPALRGkNTIICAPTGSGKTRVAVYICRHHLEKRRSagekGRVVVLVNKVPLVEQQLEKFFKYF----RKGY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 155 EMTG----STQAVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPA----THVKCLVVDEAHKALGNYAYCQVVRELVKYTTH 226
Cdd:cd18036  80 KVTGlsgdSSHKVSFGQIVKASDVIICTPQILINNLLSGREEErvylSDFSLLIFDECHHTQKEHPYNKIMRMYLDKKLS 159

                       170
                ....*....|....*.
gi 26352047 227 FR-----ILALSATPG 237
Cdd:cd18036 160 SQgplpqILGLTASPG 175
ResIII pfam04851
Type III restriction enzyme, res subunit;
76-236 1.19e-19

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 85.42  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047    76 NCPVRDYQLDISRSALFC------NTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQMEACFHVMGIP 149
Cdd:pfam04851   1 KLELRPYQIEAIENLLESikngqkRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047   150 QSHMAEMTGStqavNRKEIWSSRRVLFLTPQVMVNDLTRGAVPA--THVKCLVVDEAHKALGNyAYcqvvRELVKYTTHF 227
Cdd:pfam04851  81 VEIGEIISGD----KKDESVDDNKIVVTTIQSLYKALELASLELlpDFFDVIIIDEAHRSGAS-SY----RNILEYFKPA 151


                  ....*....
gi 26352047   228 RILALSATP 236
Cdd:pfam04851 152 FLLGLTATP 160
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
 80-216 1.45e-18

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: 83.72  E-value: 1.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSALFC-NTLVCLPTGLGKTFIAAVVMYNFYRWFPSG---KVVFMAPTKPLVTQQMEACFHVMGIPQSHMAE 155
Cdd:cd18073   4 RNYQLELALPAMKGkNTIICAPTGCGKTFVSLLICEHHLKKFPQGqkgKVVFFATKVPVYEQQKSVFSKYFERHGYRVTG 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26352047 156 MTGST-QAVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVV-DEAHKALGNYAYCQV 216
Cdd:cd18073  84 ISGATaENVPVEQIIENNDIIILTPQILVNNLKKGTIPSLSIFTLMIfDECHNTSGNHPYNMI 146
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 81-235 1.67e-18

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: 82.69  E-value: 1.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  81 DYQLDISRSALF--CNTLVCLPTGLGKTFIAAVVMYNfyRWFPSG-KVVFMAPTKPLVtQQMEACF-HVMGIPQSHMAEM 156
Cdd:cd17921   4 PIQREALRALYLsgDSVLVSAPTSSGKTLIAELAILR--ALATSGgKAVYIAPTRALV-NQKEADLrERFGPLGKNVGLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 157 TGSTQaVNRKEIwSSRRVLFLTPQVMVNDLTRGAVPAT-HVKCLVVDEAHKaLGNYAYCQVVRELVKYTT----HFRILA 231
Cdd:cd17921  81 TGDPS-VNKLLL-AEADILVATPEKLDLLLRNGGERLIqDVRLVVVDEAHL-IGDGERGVVLELLLSRLLrinkNARFVG 157


                ....
gi 26352047 232 LSAT 235
Cdd:cd17921 158 LSAT 161
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
 80-236 2.17e-18

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: 81.84  E-value: 2.17e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDI------SRSALFCNTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQMEACFHVMGIpqshm 153
Cdd:cd18032   2 RYYQQEAiealeeAREKGQRRALLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQAERSFKEVLPD----- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 154 AEMTGStqaVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKAL-GNYaycqvvRELVKYTTHFRILAL 232
Cdd:cd18032  77 GSFGNL---KGGKKKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHHAIaSSY------RKILEYFEPAFLLGL 147


                ....
gi 26352047 233 SATP 236
Cdd:cd18032 148 TATP 151
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
80-236 8.14e-15

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 76.22  E-value: 8.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSALFCNT------LVCLPTGLGKTFIAAVVMYNFYRwfpSGKVVFMAPTKPLVTQQMEACFHVMGIPQSHm 153
Cdd:COG1061  82 RPYQQEALEALLAALErgggrgLVVAPTGTGKTVLALALAAELLR---GKRVLVLVPRRELLEQWAEELRRFLGDPLAG- 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 154 aemtgstqaVNRKEIwsSRRVLFLTPQVMVNDLTRGAVPAtHVKCLVVDEAHKALGNyaycqVVRELVKYTTHFRILALS 233
Cdd:COG1061 158 ---------GGKKDS--DAPITVATYQSLARRAHLDELGD-RFGLVIIDEAHHAGAP-----SYRRILEAFPAAYRLGLT 220


                ...
gi 26352047 234 ATP 236
Cdd:COG1061 221 ATP 223
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 94-235 2.42e-14

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: 70.12  E-value: 2.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  94 NTLVCLPTGLGKTFIAAVVMYNFYRWFPsGKVVFMAPTKPLVTQQMEAcFHVMGIPQSHMAEMTGSTQAV-NRKEIWSSR 172
Cdd:cd00046   3 NVLITAPTGSGKTLAALLAALLLLLKKG-KKVLVLVPTKALALQTAER-LRELFGPGIRVAVLVGGSSAEeREKNKLGDA 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26352047 173 RVLFLTPQVMVNDLTR-GAVPATHVKCLVVDEAHKALGNYAY----CQVVRELVKYTThfRILALSAT 235
Cdd:cd00046  81 DIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGalilDLAVRKAGLKNA--QVILLSAT 146
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
94-235 8.98e-10

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 60.68  E-value: 8.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  94 NTLVCLPTGLGKTFIAAVVMYNfyRWFPSGKVVFMAPTKPLVTQ---QMEACFHVMGIpqshmaEMTGSTQAVNRKEIWS 170
Cdd:COG1204  40 NLVVSAPTASGKTLIAELAILK--ALLNGGKALYIVPLRALASEkyrEFKRDFEELGI------KVGVSTGDYDSDDEWL 111

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 171 SRR-VLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKaLGNYA----YCQVVRELVKYTTHFRILALSAT 235
Cdd:COG1204 112 GRYdILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHL-IDDESrgptLEVLLARLRRLNPEAQIVALSAT 180
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 80-236 1.36e-09

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: 56.16  E-value: 1.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSALFCNT----LVCLPTGLGKTFIAAVVMynFYRWfpSGKVVFMAPTKPLVTQQMEACfhvmgipqshmaE 155
Cdd:cd17926   2 RPYQEEALEAWLAHKNnrrgILVLPTGSGKTLTALALI--AYLK--ELRTLIVVPTDALLDQWKERF------------E 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 156 MTGSTQAVNR-----KEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHK--ALGNyaycqvvRELVKYTTHFR 228
Cdd:cd17926  66 DFLGDSSIGLigggkKKDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHlpAKTF-------SEILKELNAKY 138


                ....*...
gi 26352047 229 ILALSATP 236
Cdd:cd17926 139 RLGLTATP 146
DEXHc_RLR-2 cd18074
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma ...
 79-237 1.61e-08

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: 54.87  E-value: 1.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  79 VRDYQLDISRSALFC-NTLVCLPTGLGKTFIAAVVMYNFY----RWFPSGKVVFMAPTKPLVTQQMEACFHVMGIPQSHM 153
Cdd:cd18074   3 LRDYQMEVAKPALEGkNIIICLPTGSGKTRVAVYITKDHLdkkrKASEPGKVIVLVNKVPLVEQHYRKEFNPFLKHWYQV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 154 AEMTGSTQ-AVNRKEIWSSRRVLFLTPQVMVNDLTRGA------VPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTH 226
Cdd:cd18074  83 IGLSGDSQlKISFPEVVKRYDVIICTAQILENSLLNATeeedegVQLSDFSLIIIDECHHTQKEAVYNNIMRRYLKQKIK 162

                       170       180
                ....*....|....*....|....*
gi 26352047 227 FR--------------ILALSATPG 237
Cdd:cd18074 163 NRkqkkenkpliplpqILGLTASPG 187
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
 93-205 6.06e-08

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: 52.38  E-value: 6.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  93 CNTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQMEACFH----VMGIpqsHMAEMTGST----QAVN 164
Cdd:cd18022  18 NNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKrfeeKLGK---KVVELTGDVtpdmKALA 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 26352047 165 RKEIwssrrvLFLTPQ----VMVNDLTRGAVpaTHVKCLVVDEAH 205
Cdd:cd18022  95 DADI------IITTPEkwdgISRSWQTREYV--QQVSLIIIDEIH 131
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
 94-235 9.57e-07

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: 49.35  E-value: 9.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  94 NTLVCLPTGLGKTFIAAVVMYNFYRWF--PSG-------KVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEMTGSTQaVN 164
Cdd:cd18020  19 NMLICAPTGAGKTNIAMLTILHEIRQHvnQGGvikkddfKIVYIAPMKALAAEMVEKFSKRLAPLGIKVKELTGDMQ-LT 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 165 RKEIWSSrRVLFLTPQ---VMVNDLTRGAVPATHVKCLVVDEAH---KALGNYAYCQVVREL--VKYT-THFRILALSAT 235
Cdd:cd18020  98 KKEIAET-QIIVTTPEkwdVVTRKSSGDVALSQLVRLLIIDEVHllhDDRGPVIESLVARTLrqVESTqSMIRIVGLSAT 176
DEXHc_RLR-3 cd18075
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ...
 79-250 1.40e-06

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: 48.70  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  79 VRDYQLDISRSALFC-NTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEMT 157
Cdd:cd18075   3 LHGYQWEVVAPALRGkNSIIWLPTGAGKTRAAVYVARRHLETKRGAKVAVLVNKVHLVDQHLEKEFHVLLDKYTVTAISG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 158 GSTQAVNRKEIWSSRRVLFLTPQVMVNDLTRGA----VPATHVKCLVVDEAHKALGNYAYCQVV-----RELVKYTTHFR 228
Cdd:cd18075  83 DSSHKCFFGQLARGSDVVICTAQILQNALLSGEeeahVELTDFSLLVIDECHHTHKEAVYNKIMlsyleKKLSRQGDLPQ 162

                       170       180       190
                ....*....|....*....|....*....|
gi 26352047 229 ILALSATPGSD--------IKAVQQVITNL 250
Cdd:cd18075 163 ILGLTASPGTGgatsfdgaVEHILQICANL 192
DEXHc_DDX60 cd18025
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ...
 83-137 3.53e-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: 47.36  E-value: 3.53e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26352047  83 QLDISRSALfcntlVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQ 137
Cdd:cd18025  12 IVDRRESAL-----IVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQ 61
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 94-205 9.25e-06

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: 46.20  E-value: 9.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  94 NTLVCLPTGLGKTFIAAVVMYNFYRWFPSG-----KVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEMTGSTQAVNRKEI 168
Cdd:cd18023  19 NFVVSAPTGSGKTVLFELAILRLLKERNPLpwgnrKVVYIAPIKALCSEKYDDWKEKFGPLGLSCAELTGDTEMDDTFEI 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 26352047 169 wSSRRVLFLTPQVMvNDLTR----GAVPATHVKCLVVDEAH 205
Cdd:cd18023  99 -QDADIILTTPEKW-DSMTRrwrdNGNLVQLVALVLIDEVH 137
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 94-237 1.10e-05

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: 45.79  E-value: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  94 NTLVCLPTGLGKTFIAAVVMYNFyrWFPSGKVVFMAPTKPLVTQQME--ACFHVMGIpqshmaEMTGSTQAVNRKEIWSS 171
Cdd:cd18028  19 NLLISIPTASGKTLIAEMAMVNT--LLEGGKALYLVPLRALASEKYEefKKLEEIGL------KVGISTGDYDEDDEWLG 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26352047 172 RRVLFLTPQVMVNDLTR-GAVPATHVKCLVVDEAHkALGNYAYCQVVRELVKYTTHF----RILALSATPG 237
Cdd:cd18028  91 DYDIIVATYEKFDSLLRhSPSWLRDVGVVVVDEIH-LISDEERGPTLESIVARLRRLnpntQIIGLSATIG 160
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
 80-235 1.49e-05

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: 45.60  E-value: 1.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSAL-FCNTLVCLPTGLGKTfiaavVMYNFYRWFPSGKVVFMAPTKPLVTQQMEACfHVMGIPqshMAEMTG 158
Cdd:cd17920  14 RPGQLEAINAVLaGRDVLVVMPTGGGKS-----LCYQLPALLLDGVTLVVSPLISLMQDQVDRL-QQLGIR---AAALNS 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 159 STQAVNRKEIWSSR-----RVLFLTP----QVMVNDLTRGAVPATHVKCLVVDEAH-------------KALGnyaycqv 216
Cdd:cd17920  85 TLSPEEKREVLLRIkngqyKLLYVTPerllSPDFLELLQRLPERKRLALIVVDEAHcvsqwghdfrpdyLRLG------- 157

                       170
                ....*....|....*....
gi 26352047 217 vrELVKYTTHFRILALSAT 235
Cdd:cd17920 158 --RLRRALPGVPILALTAT 174
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
 94-235 1.87e-05

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: 45.44  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  94 NTLVCLPTGLGKTFIAAVVM-------YNfyrwfPSG-------KVVFMAPTKPLVtQQMEACFH----VMGIpqsHMAE 155
Cdd:cd18019  35 NLLLCAPTGAGKTNVALLTIlreigkhRN-----PDGtinldafKIVYIAPMKALV-QEMVGNFSkrlaPYGI---TVAE 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 156 MTGSTQaVNRKEIwSSRRVLFLTPQVMvNDLTRGAVPATH---VKCLVVDEA---HKALGNYAYCQVVREL--VKYTTHF 227
Cdd:cd18019 106 LTGDQQ-LTKEQI-SETQIIVTTPEKW-DIITRKSGDRTYtqlVRLIIIDEIhllHDDRGPVLESIVARTIrqIEQTQEY 182


                ....*....
gi 26352047 228 -RILALSAT 235
Cdd:cd18019 183 vRLVGLSAT 191
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 96-206 7.59e-05

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: 43.35  E-value: 7.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  96 LVCLPTGLGKT--FIAAVVMYNFYRWFPSG-KVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEMTGSTQAVNRKEIWSSR 172
Cdd:cd17957  31 LACAPTGSGKTlaFLIPILQKLGKPRKKKGlRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSIT 110

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26352047 173 R--VLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHK 206
Cdd:cd17957 111 KydILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADK 146
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 94-238 8.22e-05

DEXH-box helicase domain of LHR; 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 from 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: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 42.96  E-value: 8.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  94 NTLVCLPTGLGKTFiaAVVMYNFYRWF----PSGKVVFMAPTKPLVTQQM----EACFHV-MGIPQSHmaeMTGST-QAV 163
Cdd:cd17922   3 NVLIAAPTGSGKTE--AAFLPALSSLAdepeKGVQVLYISPLKALINDQErrleEPLDEIdLEIPVAV---RHGDTsQSE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 164 NRKEIWSSRRVLFLTPQ----VMVNdlTRGAVPATHVKCLVVDEAHKALGN----YAYCQVVReLVKYT-THFRILALSA 234
Cdd:cd17922  78 KAKQLKNPPGILITTPEslelLLVN--KKLRELFAGLRYVVVDEIHALLGSkrgvQLELLLER-LRKLTgRPLRRIGLSA 154


                ....
gi 26352047 235 TPGS 238
Cdd:cd17922 155 TLGN 158
DEAD-like_helicase_N cd17912
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 94-137 2.86e-04

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: 39.42  E-value: 2.86e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 26352047  94 NTLVCLPTGLGKTFIAavVMYNFYRWFPSGKVVFMAPTKPLVTQ 137
Cdd:cd17912   1 NILHLGPTGSGKTLVA--IQKIASAMSSGKSVLVVTPTKLLAHE 42
PRK00254 PRK00254
ski2-like helicase; Provisional
 94-238 4.80e-04

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 42.50  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047   94 NTLVCLPTGLGKTFIAAVVMYN-FYRwfPSGKVVFMAPTKPLVTQQMEAC--FHVMGIpqsHMAEMTGStqaVNRKEIWS 170
Cdd:PRK00254  41 NLVLAIPTASGKTLVAEIVMVNkLLR--EGGKAVYLVPLKALAEEKYREFkdWEKLGL---RVAMTTGD---YDSTDEWL 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26352047  171 SR-RVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHkALGNY---AYCQVVreLVKYTTHFRILALSATPGS 238
Cdd:PRK00254 113 GKyDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIH-LIGSYdrgATLEMI--LTHMLGRAQILGLSATVGN 181
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
 94-234 6.22e-04

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: 40.70  E-value: 6.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  94 NTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQME---ACF-HVMGIpqsHMAEMTGSTQAVNRkeIW 169
Cdd:cd18021  21 NVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKdwrAKFgPLLGK---KVVKLTGETSTDLK--LL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 170 SSRRVLFLTPQVMvnDL------TRGAVPAthVKCLVVDEAHKALGNYAYcqvVRELVKYTTHF---------RILALSA 234
Cdd:cd18021  96 AKSDVILATPEQW--DVlsrrwkQRKNVQS--VELFIADELHLIGGENGP---VYEVVVSRMRYissqlekpiRIVGLSS 168
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 94-250 8.34e-04

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: 40.26  E-value: 8.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  94 NTLVCLPTGLGKTFIAAV-VMYNFYRwFPSGKVVFMAPTKPLVTQQMEAC--FHVMGIPQSHMAEMTGSTQAVNRKEIWS 170
Cdd:cd17923  17 SVVVTTGTASGKSLCYQLpILEALLR-DPGSRALYLYPTKALAQDQLRSLreLLEQLGLGIRVATYDGDTPREERRAIIR 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 171 SR-RVLFLTPQVMVNDLTRGAVP----ATHVKCLVVDEAHK---ALGNYAYCqVVREL----VKYTTHFRILALSATpgs 238
Cdd:cd17923  96 NPpRILLTNPDMLHYALLPHHDRwarfLRNLRYVVLDEAHTyrgVFGSHVAL-LLRRLrrlcRRYGADPQFILTSAT--- 171

                       170
                ....*....|..
gi 26352047 239 dIKAVQQVITNL 250
Cdd:cd17923 172 -IGNPAEHARTL 182
uvsW PHA02558
UvsW helicase; Provisional
 62-209 1.07e-03

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 41.15  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047   62 GFCAAAGALWIYPTNCPV--RDYQLDISRSALFCNTLVC-LPTGLGKTFIAAVvMYNFYRWFPSGKVVFMAPTKPLVTqQ 138
Cdd:PHA02558  96 DFDEWVSSLEIYSGNKKIepHWYQYDAVYEGLKNNRRLLnLPTSAGKSLIQYL-LSRYYLENYEGKVLIIVPTTSLVT-Q 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352047  139 MEACFHVMG-IPQSHMAEMTGSTqavnrkEIWSSRRVLFLTPQVMVNdltrgaVPATHVK---CLVVDEAHKALG 209
Cdd:PHA02558 174 MIDDFVDYRlFPREAMHKIYSGT------AKDTDAPIVVSTWQSAVK------QPKEWFDqfgMVIVDECHLFTG 236
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
 80-236 1.09e-03

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


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 41.37  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSAL--FCN----TLVCLPTGLGKTFIAAVVMYNF--YRWFPsgKVVFMAPTKPLVTQQMEAcFHVMGIPQS 151
Cdd:COG4096 160 RYYQIEAIRRVEeaIAKgqrrALLVMATGTGKTRTAIALIYRLlkAGRAK--RILFLADRNALVDQAKNA-FKPFLPDLD 236

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 152 HMAEMTGSTqavnrKEIWSSRRVLFLTPQVMVNDLTRG-------AVPATHVKCLVVDEAHKalgnyAYCQVVRELVKYt 224
Cdd:COG4096 237 AFTKLYNKS-----KDIDKSARVYFSTYQTMMNRIDGEeeepgyrQFPPDFFDLIIIDECHR-----GIYSKWRAILDY- 305

                       170
                ....*....|....
gi 26352047 225 thF--RILALSATP 236
Cdd:COG4096 306 --FdaLQIGLTATP 317
DEXHc_RecG cd17992
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ...
 102-168 1.32e-03

DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350750 [Multi-domain]  Cd Length: 225  Bit Score: 40.21  E-value: 1.32e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26352047 102 GLGKTFIAAVVMYNFYRwfpSG-KVVFMAPTKPLVTQQMEAC---FHVMGIpqsHMAEMTGSTQAVNRKEI 168
Cdd:cd17992  76 GSGKTVVAALAMLAAVE---NGyQVALMAPTEILAEQHYDSLkklLEPLGI---RVALLTGSTKAKEKREI 140
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 80-236 3.35e-03

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: 38.32  E-value: 3.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  80 RDYQLDISRSALFC-----NTLVCLPTGLGKT-----FIA-----------------AVVMYN----FYRWFPSGKVVfm 128
Cdd:cd17919   2 RPYQLEGLNFLLELyengpGGILADEMGLGKTlqaiaFLAyllkegkergpvlvvcpLSVLENwereFEKWTPDLRVV-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 129 aptkplvtqqmeaCFHvmgipqshmaEMTGSTQAVNRKEIWSSRRVLFLTPQVMVNDltRGAVPATHVKCLVVDEAHKaL 208
Cdd:cd17919  80 -------------VYH----------GSQRERAQIRAKEKLDKFDVVLTTYETLRRD--KASLRKFRWDLVVVDEAHR-L 133

                       170       180
                ....*....|....*....|....*...
gi 26352047 209 GNYAyCQVVRELVKYTTHFRILaLSATP 236
Cdd:cd17919 134 KNPK-SQLSKALKALRAKRRLL-LTGTP 159
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
 94-252 4.65e-03

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: 38.01  E-value: 4.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047  94 NTLVCLPTGLGKT---FIAAVvmynFYRWFPSGKVVFMAPTKPLVTQQME--------ACFHVMgipqSHMAEMTGSTQA 162
Cdd:cd18018  29 STLVVLPTGAGKSlcyQLPAL----LLRRRGPGLTLVVSPLIALMKDQVDalpraikaAALNSS----LTREERRRILEK 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352047 163 VNRKEIwssrRVLFLTPQVMVNDLTRGAV-PATHVKCLVVDEAH--KALGNY---AY---CQVVRELVKYTThfrILALS 233
Cdd:cd18018 101 LRAGEV----KILYVSPERLVNESFRELLrQTPPISLLVVDEAHciSEWSHNfrpDYlrlCRVLRELLGAPP---VLALT 173

                       170
                ....*....|....*....
gi 26352047 234 ATPGSdiKAVQQVITNLLI 252
Cdd:cd18018 174 ATATK--RVVEDIASHLGI 190
 
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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