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Conserved domains on  [gi|356526023|ref|XP_003531619|]
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DEAD-box ATP-dependent RNA helicase 20 [Glycine max]

Protein Classification

DEAD/DEAH box helicase family protein( domain architecture ID 1000205)

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
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
61-491 0e+00

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.


The actual alignment was detected with superfamily member PTZ00110:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 545  Bit Score: 696.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  61 FEKNFYIESPAVRAMTDAEVNEYRQQREIT-VEGRDIPKPVKTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGR 139
Cdd:PTZ00110  89 FEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGR 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 140 DLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDGPIVLVLAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVR 219
Cdd:PTZ00110 169 DMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIY 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 220 DLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARK 299
Cdd:PTZ00110 249 ALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARD 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 300 FL-YNPYKVIIGSSDLKANHAIRQYVDIVSEKQKYDKLVKLLEDIM-DGSRILIFMDTKKGCDQITRQLRMDGWPALSIH 377
Cdd:PTZ00110 329 LCkEEPVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMrDGDKILIFVETKKGADFLTKELRLDGWPALCIH 408
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 378 GDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAGAKGTAYTYFTAANARF 457
Cdd:PTZ00110 409 GDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRL 488
                        410       420       430
                 ....*....|....*....|....*....|....
gi 356526023 458 AKELIAILEEAGQKVSPELAAMGRGAPPPPSGPR 491
Cdd:PTZ00110 489 ARDLVKVLREAKQPVPPELEKLSNERSNGTERRR 522
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
61-491 0e+00

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 696.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  61 FEKNFYIESPAVRAMTDAEVNEYRQQREIT-VEGRDIPKPVKTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGR 139
Cdd:PTZ00110  89 FEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGR 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 140 DLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDGPIVLVLAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVR 219
Cdd:PTZ00110 169 DMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIY 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 220 DLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARK 299
Cdd:PTZ00110 249 ALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARD 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 300 FL-YNPYKVIIGSSDLKANHAIRQYVDIVSEKQKYDKLVKLLEDIM-DGSRILIFMDTKKGCDQITRQLRMDGWPALSIH 377
Cdd:PTZ00110 329 LCkEEPVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMrDGDKILIFVETKKGADFLTKELRLDGWPALCIH 408
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 378 GDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAGAKGTAYTYFTAANARF 457
Cdd:PTZ00110 409 GDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRL 488
                        410       420       430
                 ....*....|....*....|....*....|....
gi 356526023 458 AKELIAILEEAGQKVSPELAAMGRGAPPPPSGPR 491
Cdd:PTZ00110 489 ARDLVKVLREAKQPVPPELEKLSNERSNGTERRR 522
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
102-475 3.31e-167

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 478.87  E-value: 3.31e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 102 TFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAqpilNPGDGPIVLVLA 181
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDP----SRPRAPQALILA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 182 PTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRML 261
Cdd:COG0513   79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 262 DMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVIIGSSDLKANhAIRQYVDIVSEKQKYDKLVKLLE 341
Cdd:COG0513  159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRYYLVDKRDKLELLRRLLR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 342 DImDGSRILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNY 421
Cdd:COG0513  238 DE-DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 356526023 422 DFPGSLEDYVHRIGRTGRAGAKGTAYTYFTAANARFAKeliAILEEAGQKVSPE 475
Cdd:COG0513  317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLR---AIEKLIGQKIEEE 367
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
112-307 2.35e-142

DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members 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: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 407.14  E-value: 2.35e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDGPIVLVLAPTRELAVQIQ 191
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 192 QETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRK 271
Cdd:cd17966   81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 356526023 272 IVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd17966  161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
125-296 2.95e-65

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: 208.64  E-value: 2.95e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  125 TPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNaqpilNPGDGPIVLVLAPTRELAVQIQQETTKFGASSRIK 204
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD-----KLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  205 STCIYGGVPKGPQVRDLqKGVEIVIATPGRLIDMLESNHTnLQRVTYLVLDEADRMLDMGFDPQLRKIVSQIRPDRQTLY 284
Cdd:pfam00270  76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 356526023  285 WSATWPKEVEQL 296
Cdd:pfam00270 154 LSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
116-323 4.22e-62

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 201.57  E-value: 4.22e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023   116 ITKAGFTEPTPIQSQGWPMALKG-RDLIGIAETGSGKTLAYLLPAIVHvnaqpiLNPGDGPIVLVLAPTRELAVQIQQET 194
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023   195 TKFGASSRIKSTCIYGGVPKGPQVRDLQKGV-EIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRKIV 273
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 356526023   274 SQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVIIGSSdlkANHAIRQY 323
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT---PLEPIEQF 201
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
61-491 0e+00

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 696.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  61 FEKNFYIESPAVRAMTDAEVNEYRQQREIT-VEGRDIPKPVKTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGR 139
Cdd:PTZ00110  89 FEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGR 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 140 DLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDGPIVLVLAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVR 219
Cdd:PTZ00110 169 DMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIY 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 220 DLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARK 299
Cdd:PTZ00110 249 ALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARD 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 300 FL-YNPYKVIIGSSDLKANHAIRQYVDIVSEKQKYDKLVKLLEDIM-DGSRILIFMDTKKGCDQITRQLRMDGWPALSIH 377
Cdd:PTZ00110 329 LCkEEPVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMrDGDKILIFVETKKGADFLTKELRLDGWPALCIH 408
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 378 GDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAGAKGTAYTYFTAANARF 457
Cdd:PTZ00110 409 GDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRL 488
                        410       420       430
                 ....*....|....*....|....*....|....
gi 356526023 458 AKELIAILEEAGQKVSPELAAMGRGAPPPPSGPR 491
Cdd:PTZ00110 489 ARDLVKVLREAKQPVPPELEKLSNERSNGTERRR 522
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
102-475 3.31e-167

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 478.87  E-value: 3.31e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 102 TFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAqpilNPGDGPIVLVLA 181
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDP----SRPRAPQALILA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 182 PTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRML 261
Cdd:COG0513   79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 262 DMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVIIGSSDLKANhAIRQYVDIVSEKQKYDKLVKLLE 341
Cdd:COG0513  159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRYYLVDKRDKLELLRRLLR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 342 DImDGSRILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNY 421
Cdd:COG0513  238 DE-DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 356526023 422 DFPGSLEDYVHRIGRTGRAGAKGTAYTYFTAANARFAKeliAILEEAGQKVSPE 475
Cdd:COG0513  317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLR---AIEKLIGQKIEEE 367
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
112-307 2.35e-142

DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members 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: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 407.14  E-value: 2.35e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDGPIVLVLAPTRELAVQIQ 191
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 192 QETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRK 271
Cdd:cd17966   81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 356526023 272 IVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd17966  161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
50-310 1.82e-137

DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 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: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 397.84  E-value: 1.82e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  50 KRNLSLDGLPHFEKNFYIESPAVRAMTDAEVNEYRQQREITVEGRDIPKPVKTFHDAGFPEYVLQEITKAGFTEPTPIQS 129
Cdd:cd18050   11 KKKWDLSELPKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 130 QGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDGPIVLVLAPTRELAVQIQQETTKFGASSRIKSTCIY 209
Cdd:cd18050   91 QGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIY 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 210 GGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRKIVSQIRPDRQTLYWSATW 289
Cdd:cd18050  171 GGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATW 250
                        250       260
                 ....*....|....*....|.
gi 356526023 290 PKEVEQLARKFLYNPYKVIIG 310
Cdd:cd18050  251 PKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
79-311 2.52e-133

DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 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: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 385.52  E-value: 2.52e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  79 EVNEYRQQREITVEGRDIPKPVKTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLP 158
Cdd:cd18049    2 EVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 159 AIVHVNAQPILNPGDGPIVLVLAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDM 238
Cdd:cd18049   82 AIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356526023 239 LESNHTNLQRVTYLVLDEADRMLDMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVIIGS 311
Cdd:cd18049  162 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
109-487 9.74e-110

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 333.69  E-value: 9.74e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 109 PEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPIlnpgdGPIVLVLAPTRELAV 188
Cdd:PRK11776  12 PPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRF-----RVQALVLCPTRELAD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 189 QIQQETTKFG-ASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDP 267
Cdd:PRK11776  87 QVAKEIRRLArFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 268 QLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVIIGSSDlkANHAIRQYVDIVSEKQKYDKLVKLLEDIMDGS 347
Cdd:PRK11776 167 AIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH--DLPAIEQRFYEVSPDERLPALQRLLLHHQPES 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 348 rILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNYDFPGSL 427
Cdd:PRK11776 245 -CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDP 323
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356526023 428 EDYVHRIGRTGRAGAKGTAYTYFTAANARfakeLIAILEEA-GQKVS----PELAAMGRGAPPPP 487
Cdd:PRK11776 324 EVHVHRIGRTGRAGSKGLALSLVAPEEMQ----RANAIEDYlGRKLNweplPSLSPLSGVPLLPE 384
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
112-307 1.82e-107

DEAD-box helicase domain of 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 318.23  E-value: 1.82e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPIlNPGDGPIVLVLAPTRELAVQIQ 191
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-KKGRGPQALVLAPTRELAMQIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 192 QETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRK 271
Cdd:cd00268   80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 356526023 272 IVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd00268  160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
90-308 8.16e-105

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 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: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 312.39  E-value: 8.16e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  90 TVEGRDIPKPVKTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPIL 169
Cdd:cd17953    1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 170 NPGDGPIVLVLAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNH---TNL 246
Cdd:cd17953   81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356526023 247 QRVTYLVLDEADRMLDMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVI 308
Cdd:cd17953  161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
112-307 1.06e-97

DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 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: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 293.17  E-value: 1.06e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDGPIVLVLAPTRELAVQIQ 191
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 192 QETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRK 271
Cdd:cd17952   81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 356526023 272 IVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd17952  161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
102-446 4.40e-96

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 298.65  E-value: 4.40e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 102 TFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDGPI-VLVL 180
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 181 APTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRM 260
Cdd:PRK10590  82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 261 LDMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVIIGSSDlKANHAIRQYVDIVSEKQKYDKLVKLl 340
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN-TASEQVTQHVHFVDKKRKRELLSQM- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 341 edIMDGS--RILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYV 418
Cdd:PRK10590 240 --IGKGNwqQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
                        330       340
                 ....*....|....*....|....*...
gi 356526023 419 VNYDFPGSLEDYVHRIGRTGRAGAKGTA 446
Cdd:PRK10590 318 VNYELPNVPEDYVHRIGRTGRAAATGEA 345
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
58-502 1.46e-95

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 299.01  E-value: 1.46e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  58 LPHFEKNFYIESPAVR-AMTDAEVNEYRQQREITVEGRDIPKPVKTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMAL 136
Cdd:PLN00206  77 LPATDECFYVRDPGSTsGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAAL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 137 KGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGD--GPIVLVLAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPK 214
Cdd:PLN00206 157 SGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEqrNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAM 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 215 GPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRKIVsQIRPDRQTLYWSATWPKEVE 294
Cdd:PLN00206 237 PQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPEVE 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 295 QLARKFLYNPYKVIIGSSDlKANHAIRQYVDIVSEKQKYDKLVklleDIMDGSR-----ILIFMDTKKGCDQITRQLRM- 368
Cdd:PLN00206 316 KFASSLAKDIILISIGNPN-RPNKAVKQLAIWVETKQKKQKLF----DILKSKQhfkppAVVFVSSRLGADLLANAITVv 390
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 369 DGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAGAKGTAYT 448
Cdd:PLN00206 391 TGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIV 470
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 356526023 449 YFTAANARFAKELIAILEEAGQKVSPELAAmgrgapPPPSGPRGFQDRGRGYGS 502
Cdd:PLN00206 471 FVNEEDRNLFPELVALLKSSGAAIPRELAN------SRYLGSGRKRKKKRRYGS 518
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
101-446 4.73e-89

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 279.52  E-value: 4.73e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 101 KTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDgPIVLVL 180
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGP-PRILIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 181 APTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRM 260
Cdd:PRK11192  80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 261 LDMGFDPQLRKIVSQIRPDRQTLYWSATWPKE-VEQLARKFLYNPYKVIIGSSdLKANHAIRQYVDIV-SEKQKYDKLVK 338
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPS-RRERKKIHQWYYRAdDLEHKTALLCH 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 339 LLEDiMDGSRILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYV 418
Cdd:PRK11192 239 LLKQ-PEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHV 317
                        330       340
                 ....*....|....*....|....*...
gi 356526023 419 VNYDFPGSLEDYVHRIGRTGRAGAKGTA 446
Cdd:PRK11192 318 INFDMPRSADTYLHRIGRTGRAGRKGTA 345
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
112-307 3.34e-86

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members 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: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 263.94  E-value: 3.34e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILN-PGDGPIVLVLAPTRELAVQI 190
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPReQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 191 QQETTKFGASSrIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLR 270
Cdd:cd17958   81 EAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 356526023 271 KIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd17958  160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
102-303 4.76e-85

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members 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: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 261.65  E-value: 4.76e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 102 TFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDG-----PI 176
Cdd:cd17967    1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 177 VLVLAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDE 256
Cdd:cd17967   81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 356526023 257 ADRMLDMGFDPQLRKIVSQ----IRPDRQTLYWSATWPKEVEQLARKFLYN 303
Cdd:cd17967  161 ADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKN 211
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
116-489 6.76e-85

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 272.98  E-value: 6.76e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 116 ITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPIL---NPGDgPIVLVLAPTRELAVQIQQ 192
Cdd:PRK04537  24 LESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadrKPED-PRALILAPTRELAIQIHK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 193 ETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHT-NLQRVTYLVLDEADRMLDMGFDPQLRK 271
Cdd:PRK04537 103 DAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEADRMFDLGFIKDIRF 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 272 IVSQI--RPDRQTLYWSATWPKEVEQLARKFLYNPYKVIIGSSDLKANHaIRQYVDIVSEKQKYDKLVKLLEDiMDGSRI 349
Cdd:PRK04537 183 LLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR-VRQRIYFPADEEKQTLLLGLLSR-SEGART 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 350 LIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNYDFPGSLED 429
Cdd:PRK04537 261 MVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAED 340
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356526023 430 YVHRIGRTGRAGAKGTAYTYftaANARFAKELIAILEEAGQKVSPE------LAAMGRGAPPPPSG 489
Cdd:PRK04537 341 YVHRIGRTARLGEEGDAISF---ACERYAMSLPDIEAYIEQKIPVEpvtaelLTPLPRPPRVPVEG 403
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
88-305 6.61e-82

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are 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: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 255.28  E-value: 6.61e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  88 EITVE--GRDIPKPVKTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNA 165
Cdd:cd18052   28 EIPVEvtGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMK 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 166 QPILNPGDG----PIVLVLAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLES 241
Cdd:cd18052  108 EGLTASSFSevqePQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGR 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356526023 242 NHTNLQRVTYLVLDEADRMLDMGFDPQLRKIVSQI----RPDRQTLYWSATWPKEVEQLARKFLYNPY 305
Cdd:cd18052  188 GKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKEDY 255
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
101-466 9.29e-82

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 260.29  E-value: 9.29e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 101 KTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHV--NAQPILNPGDGPIVL 178
Cdd:PRK04837   8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlsHPAPEDRKVNQPRAL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 179 VLAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEAD 258
Cdd:PRK04837  88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 259 RMLDMGFDPQLRKIVSQIRP--DRQTLYWSATWPKEVEQLARKFLYNPYKVIIgSSDLKANHAIRQYVDIVSEKQKYDKL 336
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEV-EPEQKTGHRIKEELFYPSNEEKMRLL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 337 VKLLE-DIMDgsRILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDV 415
Cdd:PRK04837 247 QTLIEeEWPD--RAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAV 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 356526023 416 KYVVNYDFPGSLEDYVHRIGRTGRAGAKGTAYTYftaANARFAKELIAILE 466
Cdd:PRK04837 325 THVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL---ACEEYALNLPAIET 372
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
97-486 1.30e-81

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 261.77  E-value: 1.30e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  97 PKPVKT-FHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNP---G 172
Cdd:PRK01297  82 PQEGKTrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymG 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 173 DgPIVLVLAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQ-KGVEIVIATPGRLIDMLESNHTNLQRVTY 251
Cdd:PRK01297 162 E-PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEV 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 252 LVLDEADRMLDMGFDPQLRKIVSQIRP--DRQTLYWSATWPKEVEQLARKFLYNPYKVIIGSSDlKANHAIRQYVDIVSE 329
Cdd:PRK01297 241 MVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPEN-VASDTVEQHVYAVAG 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 330 KQKYdklvKLLEDIM---DGSRILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVA 406
Cdd:PRK01297 320 SDKY----KLLYNLVtqnPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVA 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 407 ARGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAGAKGTAYTYftaANARFAKELIAILEEAGQKVSPELAAMGRGAPPP 486
Cdd:PRK01297 396 GRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF---AGEDDAFQLPEIEELLGRKISCEMPPAELLKPVP 472
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
102-446 1.06e-80

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 263.63  E-value: 1.06e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 102 TFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPaIVHvNAQPILNpgdGPIVLVLA 181
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP-LLH-NLDPELK---APQILVLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 182 PTRELAVQIQQETTKFGASSR-IKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRM 260
Cdd:PRK11634  82 PTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 261 LDMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVIIGSSdLKANHAIRQYVDIVSEKQKYDKLVKLL 340
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSS-VTTRPDISQSYWTVWGMRKNEALVRFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 341 EdIMDGSRILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVN 420
Cdd:PRK11634 241 E-AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVN 319
                        330       340
                 ....*....|....*....|....*.
gi 356526023 421 YDFPGSLEDYVHRIGRTGRAGAKGTA 446
Cdd:PRK11634 320 YDIPMDSESYVHRIGRTGRAGRAGRA 345
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
112-304 2.34e-79

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 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: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 246.85  E-value: 2.34e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPIL---NPGDGPIVLVLAPTRELAV 188
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLdeeTKDDGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 189 QIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQ 268
Cdd:cd17945   81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 356526023 269 LRKI-----VSQIRPD---------------RQTLYWSATWPKEVEQLARKFLYNP 304
Cdd:cd17945  161 VTKIldampVSNKKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRP 216
PTZ00424 PTZ00424
helicase 45; Provisional
100-451 3.83e-77

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 247.82  E-value: 3.83e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 100 VKTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNaqPILNPGDgpiVLV 179
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLID--YDLNACQ---ALI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 180 LAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADR 259
Cdd:PTZ00424 102 LAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 260 MLDMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVIIGSSDLKAnHAIRQ-YVDIVSEKQKYDKLVK 338
Cdd:PTZ00424 182 MLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTL-EGIRQfYVAVEKEEWKFDTLCD 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 339 LLEDIMDGSRIlIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYV 418
Cdd:PTZ00424 261 LYETLTITQAI-IYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLV 339
                        330       340       350
                 ....*....|....*....|....*....|...
gi 356526023 419 VNYDFPGSLEDYVHRIGRTGRAGAKGTAYTYFT 451
Cdd:PTZ00424 340 INYDLPASPENYIHRIGRSGRFGRKGVAINFVT 372
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
88-303 1.69e-75

DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 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: 350809 [Multi-domain]  Cd Length: 249  Bit Score: 238.02  E-value: 1.69e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  88 EITVE--GRDIPKPVKTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIV---- 161
Cdd:cd18051    6 DIPVEatGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSqiye 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 162 --HVNAQPILNPGDG-----PIVLVLAPTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGR 234
Cdd:cd18051   86 qgPGESLPSESGYYGrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGR 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356526023 235 LIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRKIVSQI----RPDRQTLYWSATWPKEVEQLARKFLYN 303
Cdd:cd18051  166 LVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDN 238
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
125-296 2.95e-65

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: 208.64  E-value: 2.95e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  125 TPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNaqpilNPGDGPIVLVLAPTRELAVQIQQETTKFGASSRIK 204
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD-----KLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  205 STCIYGGVPKGPQVRDLqKGVEIVIATPGRLIDMLESNHTnLQRVTYLVLDEADRMLDMGFDPQLRKIVSQIRPDRQTLY 284
Cdd:pfam00270  76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 356526023  285 WSATWPKEVEQL 296
Cdd:pfam00270 154 LSATLPRNLEDL 165
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
102-307 2.17e-64

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 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: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 207.55  E-value: 2.17e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 102 TFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIvhvnaQPILNPGDGPIVLVLA 181
Cdd:cd17954    1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPIL-----QALLENPQRFFALVLA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 182 PTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLE-SNHTNLQRVTYLVLDEADRM 260
Cdd:cd17954   76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEnTKGFSLKSLKFLVMDEADRL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 356526023 261 LDMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd17954  156 LNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEXDc smart00487
DEAD-like helicases superfamily;
116-323 4.22e-62

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 201.57  E-value: 4.22e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023   116 ITKAGFTEPTPIQSQGWPMALKG-RDLIGIAETGSGKTLAYLLPAIVHvnaqpiLNPGDGPIVLVLAPTRELAVQIQQET 194
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023   195 TKFGASSRIKSTCIYGGVPKGPQVRDLQKGV-EIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRKIV 273
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 356526023   274 SQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVIIGSSdlkANHAIRQY 323
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT---PLEPIEQF 201
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
112-307 5.54e-61

DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 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: 350709 [Multi-domain]  Cd Length: 206  Bit Score: 199.10  E-value: 5.54e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQ----PILnPGDGPIVLVLAPTRELA 187
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQekklPFI-KGEGPYGLIVCPSRELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 188 VQ----IQQETTKFGASS--RIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRML 261
Cdd:cd17951   80 RQthevIEYYCKALQEGGypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 356526023 262 DMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd17951  160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
320-450 3.29e-60

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: 194.26  E-value: 3.29e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 320 IRQYVDIVSEKQKYDKLVKLLEDIMDGSRILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPI 399
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 356526023 400 MTATDVAARGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAGAKGTAYTYF 450
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
112-310 7.09e-60

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: 195.89  E-value: 7.09e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQpilNPGDGPIVLVLAPTRELAVQIQ 191
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP---RKKKGLRALILAPTRELASQIY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 192 QETTKFGASSRIKSTCIYGG-VPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLR 270
Cdd:cd17957   78 RELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 356526023 271 KIVSQIR-PDRQTLYWSATWPKEVEQLARKFLYNPYKVIIG 310
Cdd:cd17957  158 EILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
103-305 1.67e-59

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) 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: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 195.14  E-value: 1.67e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 103 FHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPaIVHVNAQpilNPgDGPIVLVLAP 182
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP-ILQRLSE---DP-YGIFALVLTP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 183 TRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHT---NLQRVTYLVLDEADR 259
Cdd:cd17955   76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttkVLSRVKFLVLDEADR 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 356526023 260 MLDMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPY 305
Cdd:cd17955  156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
112-307 3.40e-59

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: 194.01  E-value: 3.40e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVnaqpILNPGDGPI--VLVLAPTRELAVQ 189
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERL----LYRPKKKAAtrVLVLVPTRELAMQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 190 IQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHT-NLQRVTYLVLDEADRMLDMGFDPQ 268
Cdd:cd17947   77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADE 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 356526023 269 LRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd17947  157 LKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
112-308 1.53e-58

DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 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: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 192.80  E-value: 1.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMAL-KGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDGPIVLVLAPTRELAVQI 190
Cdd:cd17964    5 LLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELALQI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 191 QQETTKF-GASSRIKSTCIYGGVPKGPQVRDLQK-GVEIVIATPGRLIDMLESNHT--NLQRVTYLVLDEADRMLDMGFD 266
Cdd:cd17964   85 AAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLDMGFR 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 356526023 267 PQLRKIVSQIRP----DRQTLYWSATWPKEVEQLARKFLYNPYKVI 308
Cdd:cd17964  165 PDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
112-288 2.00e-56

DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 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: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 187.83  E-value: 2.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALK-GRDLIGIAETGSGKTLAYLLPAIVHVNAQ----PILNPGDGPIVLVLAPTREL 186
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQkssnGVGGKQKPLRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 187 AVQIQQETTKFGASSRIKSTCIYGG--VPKgpQVRDLQKGVEIVIATPGRLIDMLESNHT---NLQRVTYLVLDEADRML 261
Cdd:cd17946   81 AVQVKDHLKAIAKYTNIKIASIVGGlaVQK--QERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRML 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 356526023 262 DMGFDPQLRKIVSQI-------RPDRQTLYWSAT 288
Cdd:cd17946  159 EKGHFAELEKILELLnkdragkKRKRQTFVFSAT 192
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
102-304 2.62e-55

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 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: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 184.05  E-value: 2.62e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 102 TFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQpilNPGDGPIVLVLA 181
Cdd:cd17959    2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAH---SPTVGARALILS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 182 PTRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRML 261
Cdd:cd17959   79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 356526023 262 DMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNP 304
Cdd:cd17959  159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEP 201
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
112-304 3.61e-54

DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 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: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 181.24  E-value: 3.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHV-NAQPILNPGDGPIVLVLAPTRELAVQI 190
Cdd:cd17949    2 VSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlSLEPRVDRSDGTLALVLVPTRELALQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 191 QQETTKFGASSR-IKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLEsnHT---NLQRVTYLVLDEADRMLDMGFD 266
Cdd:cd17949   82 YEVLEKLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLK--NTqsfDVSNLRWLVLDEADRLLDMGFE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 356526023 267 PQLRKIVSQIR-------------PDRQTLYWSATWPKEVEQLARKFLYNP 304
Cdd:cd17949  160 KDITKILELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDP 210
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
112-308 8.81e-54

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 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: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 179.67  E-value: 8.81e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVnaqpiLNPGDGPIVLVLAPTRELAVQIQ 191
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRC-----LTEHRNPSALILTPTRELAVQIE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 192 QETTKFGASS-RIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLR 270
Cdd:cd17962   76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 356526023 271 KIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVI 308
Cdd:cd17962  156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
119-304 5.37e-52

DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 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: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 175.17  E-value: 5.37e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 119 AGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPiLNPGDGPIVLVLAPTRELAVQIQQETTKFG 198
Cdd:cd17941    8 AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRER-WTPEDGLGALIISPTRELAMQIFEVLRKVG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 199 ASSRIKSTCIYGGvpkgpqvRDLQK------GVEIVIATPGRLIDMLESNH----TNLQrvtYLVLDEADRMLDMGFDPQ 268
Cdd:cd17941   87 KYHSFSAGLIIGG-------KDVKEekerinRMNILVCTPGRLLQHMDETPgfdtSNLQ---MLVLDEADRILDMGFKET 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 356526023 269 LRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNP 304
Cdd:cd17941  157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNP 192
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
113-304 5.03e-50

DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 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: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 169.85  E-value: 5.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 113 LQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPiLNPGDGPIVLVLAPTRELAVQIQ- 191
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLK-FKPRNGTGVIIISPTRELALQIYg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 192 --QETTKFGASSrikSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESN----HTNLQrvtYLVLDEADRMLDMGF 265
Cdd:cd17942   81 vaKELLKYHSQT---FGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTkgflYKNLQ---CLIIDEADRILEIGF 154
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 356526023 266 DPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNP 304
Cdd:cd17942  155 EEEMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLKKK 193
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
112-307 9.53e-50

DEAD-box helicase domain of DEAD box protein 55; DDX55 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: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 169.29  E-value: 9.53e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDGPIVLVLAPTRELAVQIQ 191
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 192 QETTKF--GASSRIKSTCIYGGVPKGPQVRDL-QKGVEIVIATPGRLIDMLESNHT--NLQRVTYLVLDEADRMLDMGFD 266
Cdd:cd17960   81 EVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKADkvKVKSLEVLVLDEADRLLDLGFE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 356526023 267 PQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd17960  161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
103-307 1.21e-48

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, 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: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 166.32  E-value: 1.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 103 FHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPilnpgDGPIVLVLAP 182
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKK-----DVIQALILVP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 183 TRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLD 262
Cdd:cd17940   76 TRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 356526023 263 MGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd17940  156 QDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
105-308 4.18e-43

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members 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: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 151.71  E-value: 4.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 105 DAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIvhvnaQPILNPGDGPIVLVLAPTR 184
Cdd:cd17939    1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGAL-----QRIDTTVRETQALVLAPTR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 185 ELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMG 264
Cdd:cd17939   76 ELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRG 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 356526023 265 FDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVI 308
Cdd:cd17939  156 FKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
112-304 5.71e-43

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 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: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 151.58  E-value: 5.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIvhvnaQPILN------PGDGPIVLVLAPTRE 185
Cdd:cd17961    5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPII-----QKILKakaesgEEQGTRALILVPTRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 186 LAVQIQQETTKFGA--SSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHT-NLQRVTYLVLDEADRMLD 262
Cdd:cd17961   80 LAQQVSKVLEQLTAycRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 356526023 263 MGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNP 304
Cdd:cd17961  160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
112-307 5.71e-41

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 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: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 145.48  E-value: 5.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQpilnpGDGPIVLVLAPTRELAVQIQ 191
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE-----RRHPQVLILAPTREIAVQIH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 192 QETTKFGASSRIKSTCIY-GGVPKGPQVRDLqKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLR 270
Cdd:cd17943   76 DVFKKIGKKLEGLKCEVFiGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 356526023 271 KIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd17943  155 WIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
120-308 1.17e-39

DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members 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. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 142.68  E-value: 1.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 120 GFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAI--VHVNAQPIlNPGDGPIVLVLAPTRELAVQIQQETTKF 197
Cdd:cd17944    9 GVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIekLQEDQQPR-KRGRAPKVLVLAPTRELANQVTKDFKDI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 198 gaSSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRKIVS-QI 276
Cdd:cd17944   88 --TRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvSY 165
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 356526023 277 RPDR----QTLYWSATWPKEVEQLARKFLYNPYKVI 308
Cdd:cd17944  166 KKDSednpQTLLFSATCPDWVYNVAKKYMKSQYEQV 201
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
112-304 1.25e-38

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 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: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 139.76  E-value: 1.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKA----GFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAqpilnpgdgpivLVLAPTRELA 187
Cdd:cd17938    6 VMPELIKAveelDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVVA------------LILEPSRELA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 188 VQIQQETTKFGA---SSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMG 264
Cdd:cd17938   74 EQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 356526023 265 FDPQLRKIVSQI-----RPDR-QTLYWSATWPK-EVEQLARKFLYNP 304
Cdd:cd17938  154 NLETINRIYNRIpkitsDGKRlQVIVCSATLHSfEVKKLADKIMHFP 200
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
109-307 9.80e-38

DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members 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: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 136.94  E-value: 9.80e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 109 PEYVLQEITKAGFTEPTPIQSQGWPMALKG--RDLIGIAETGSGKTLAYLLPAIVHVNAQPILnpgdgPIVLVLAPTREL 186
Cdd:cd17963    2 KPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKS-----PQALCLAPTREL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 187 AVQIQQETTKFGASSRIKSTCIYggvpKGPQVRDLQKGVE-IVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDM-G 264
Cdd:cd17963   77 ARQIGEVVEKMGKFTGVKVALAV----PGNDVPRGKKITAqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqG 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 356526023 265 FDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKV 307
Cdd:cd17963  153 HGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
103-309 2.36e-37

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 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: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 136.32  E-value: 2.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 103 FHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLpAIVHVnaqpiLNPGDGPI-VLVLA 181
Cdd:cd17950    4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVL-STLQQ-----LEPVDGQVsVLVIC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 182 PTRELAVQIQQETTKFGAS-SRIKSTCIYGGVPKGPQVRDLQKGV-EIVIATPGRLIDMLESNHTNLQRVTYLVLDEADR 259
Cdd:cd17950   78 HTRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDK 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 356526023 260 M---LDMGFDPQlrKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVII 309
Cdd:cd17950  158 MleqLDMRRDVQ--EIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
103-308 4.55e-37

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are 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: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 135.65  E-value: 4.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 103 FHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIvhvnaQPILNPGDGPIVLVLAP 182
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISIL-----QQIDTSLKATQALVLAP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 183 TRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLD 262
Cdd:cd18046   76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 356526023 263 MGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVI 308
Cdd:cd18046  156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
112-296 5.05e-37

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 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: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 136.34  E-value: 5.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPIL--NPGDGPIVLVLAPTRELAVQ 189
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLaeGPFNAPRGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 190 IQQETTKFGASSRIKSTCIYGGVPKGpQVRDLQKG-VEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQ 268
Cdd:cd17948   81 IGSVAQSLTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 356526023 269 LRKIVSQI----RPDRQTLYW---------SATWPKEVEQL 296
Cdd:cd17948  160 LSHFLRRFplasRRSENTDGLdpgtqlvlvSATMPSGVGEV 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
331-441 9.51e-35

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: 126.17  E-value: 9.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  331 QKYDKLVKLLEDiMDGSRILIFMDTKKGCDqiTRQL-RMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARG 409
Cdd:pfam00271   1 EKLEALLELLKK-ERGGKVLIFSQTKKTLE--AELLlEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 356526023  410 LDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAG 441
Cdd:pfam00271  78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
103-308 3.60e-34

DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 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: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 127.58  E-value: 3.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 103 FHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPilnpgDGPIVLVLAP 182
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQV-----RETQALILSP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 183 TRELAVQIQQETTKFGASSRIKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLD 262
Cdd:cd18045   76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 356526023 263 MGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNPYKVI 308
Cdd:cd18045  156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
HELICc smart00490
helicase superfamily c-terminal domain;
360-441 3.21e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 109.99  E-value: 3.21e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023   360 DQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGR 439
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 356526023   440 AG 441
Cdd:smart00490  81 AG 82
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
112-304 1.95e-28

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: 112.73  E-value: 1.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 112 VLQEITKAGFTEPTPIQSQGWPMALKG---------RDLIGIAETGSGKTLAYLLPaIVHvnaqpILNPGDGPIV--LVL 180
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLP-IVQ-----ALSKRVVPRLraLIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 181 APTRELAVQIQQETTKF--GASSRIKSTC----IYG---GVPKGPqVRDLQKGVEIVIATPGRLIDMLESNHT-NLQRVT 250
Cdd:cd17956   75 VPTKELVQQVYKVFESLckGTGLKVVSLSgqksFKKeqkLLLVDT-SGRYLSRVDILVATPGRLVDHLNSTPGfTLKHLR 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356526023 251 YLVLDEADRMLDMGF---------------DPQLRKIVSQIRPDR-----QTLYWSATWPKEVEQLARKFLYNP 304
Cdd:cd17956  154 FLVIDEADRLLNQSFqdwletvmkalgrptAPDLGSFGDANLLERsvrplQKLLFSATLTRDPEKLSSLKLHRP 227
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
123-316 3.85e-27

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 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: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 109.77  E-value: 3.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 123 EPTPIQS------QGWPMALKGRDLIGI----------AETGSGKTLAYLLPAI-------------VHVNAQPILNPGD 173
Cdd:cd17965   30 KPSPIQTlaikklLKTLMRKVTKQTSNEepklevfllaAETGSGKTLAYLAPLLdylkrqeqepfeeAEEEYESAKDTGR 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 174 gPIVLVLAPTRELAVQIQQ------ETTKFGASSrIKSTciyggvpKGPQVRDLQ----KGVEIVIATPGRLIDMLESNH 243
Cdd:cd17965  110 -PRSVILVPTHELVEQVYSvlkklsHTVKLGIKT-FSSG-------FGPSYQRLQlafkGRIDILVTTPGKLASLAKSRP 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356526023 244 TNLQRVTYLVLDEADRMLDMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLynPYKVIIGSSDLKA 316
Cdd:cd17965  181 KILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLF--PDVVRIATPRLHA 251
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
89-304 3.36e-22

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) 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: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 95.09  E-value: 3.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  89 ITVEGRDIPKP---VKTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKG--RDLIGIAETGSGKTLAYLLPAIVHV 163
Cdd:cd18048    3 VEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 164 NAQPILnpgdgPIVLVLAPTRELAVQ---IQQETTKFGASSRIKSTCIYGGVPKGPQVRdlqkgVEIVIATPGRLID-ML 239
Cdd:cd18048   83 DALKLY-----PQCLCLSPTFELALQtgkVVEEMGKFCVGIQVIYAIRGNRPGKGTDIE-----AQIVIGTPGTVLDwCF 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356526023 240 ESNHTNLQRVTYLVLDEADRMLDM-GFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNP 304
Cdd:cd18048  153 KLRLIDVTNISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
135-463 2.14e-20

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 94.05  E-value: 2.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 135 ALKGRDLIGIAETGSGKTLAYLLPAIvhvnaqpiLNPGdgpIVLVLAPTreLAV---QIQQettkfgASSR-IKSTCIYG 210
Cdd:COG0514   29 VLAGRDALVVMPTGGGKSLCYQLPAL--------LLPG---LTLVVSPL--IALmkdQVDA------LRAAgIRAAFLNS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 211 GVPKGPQ---VRDLQKG-VEIVIATPGRL-----IDMLESNHTNLqrvtyLVLDEA--------DrmldmgFDP---QLR 270
Cdd:COG0514   90 SLSAEERrevLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 271 KIVSQIrPDRQTLYWSATWPKEV-----EQLArkfLYNPyKVIIGSSDlKANhaIRQYVDIVSEKQKYDKLVKLLEDIMD 345
Cdd:COG0514  159 ELRERL-PNVPVLALTATATPRVradiaEQLG---LEDP-RVFVGSFD-RPN--LRLEVVPKPPDDKLAQLLDFLKEHPG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 346 GSRIlIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATdVA-ARGLDVKDVKYVVNYDFP 424
Cdd:COG0514  231 GSGI-VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLP 308
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 356526023 425 GSLEDYVHRIGRTGRAGAKGTAYTYFTAANARFAKELIA 463
Cdd:COG0514  309 KSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
137-463 4.99e-20

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 93.17  E-value: 4.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 137 KGRDLIGIAETGSGKTLAYLLpAIVHVnaqpilnpGDGPIVLVLAPTRELAVQIQQETTKFgassrikstciYGGVPKGP 216
Cdd:COG1061   99 GGGRGLVVAPTGTGKTVLALA-LAAEL--------LRGKRVLVLVPRRELLEQWAEELRRF-----------LGDPLAGG 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 217 QVRDLQKgvEIVIATPGRLIDMLESNHTNlQRVTYLVLDEADRmldmGFDPQLRKIVSQI-------------RPDRQTL 283
Cdd:COG1061  159 GKKDSDA--PITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFpaayrlgltatpfRSDGREI 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 284 YW--------SATWPkevEQLARKFLyNPYKVIIGSSDL----KANHAIRQYVD---IVSEKQKYDKLVKLLEDIMDGSR 348
Cdd:COG1061  232 LLflfdgivyEYSLK---EAIEDGYL-APPEYYGIRVDLtderAEYDALSERLRealAADAERKDKILRELLREHPDDRK 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 349 ILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNYDFPGSLE 428
Cdd:COG1061  308 TLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPR 387
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 356526023 429 DYVHRIGRTGR-AGAKGTAYTYFTAANARFAKELIA 463
Cdd:COG1061  388 EFIQRLGRGLRpAPGKEDALVYDFVGNDVPVLEELA 423
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
138-288 2.53e-16

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: 75.90  E-value: 2.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 138 GRDLIGIAETGSGKTLAYLLPAIVHVNAQpilnpgdGPIVLVLAPTRELAVQIQQEttkFGASSRIKSTC--IYGGVPKG 215
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLKK-------GKKVLVLVPTKALALQTAER---LRELFGPGIRVavLVGGSSAE 70
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356526023 216 PQ-VRDLQKGVeIVIATPGRLIDMLESNHTNLQR-VTYLVLDEADRMLDMGFDPQLRK--IVSQIRPDRQTLYWSAT 288
Cdd:cd00046   71 EReKNKLGDAD-IIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
101-304 9.03e-15

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 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: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 73.22  E-value: 9.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 101 KTFHDAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKG--RDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPgdgpiVL 178
Cdd:cd18047    1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ-----CL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 179 VLAPTRELAVQ---IQQETTKFGASSRIKSTCIYGGVPKGPQVRDlqkgvEIVIATPGRLID-MLESNHTNLQRVTYLVL 254
Cdd:cd18047   76 CLSPTYELALQtgkVIEQMGKFYPELKLAYAVRGNKLERGQKISE-----QIVIGTPGTVLDwCSKLKFIDPKKIKVFVL 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 356526023 255 DEADRML-DMGFDPQLRKIVSQIRPDRQTLYWSATWPKEVEQLARKFLYNP 304
Cdd:cd18047  151 DEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
105-448 6.08e-14

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: 74.49  E-value: 6.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 105 DAGFPEYVLQEITKAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIvhvnaQPILNpGDGPIVLVLAPTR 184
Cdd:COG1205   38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVL-----EALLE-DPGATALYLYPTK 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 185 ELAV-Q---IQQETTKFGAssRIKSTCIYGGVPkgPQVRD-LQKGVEIVIATPgrliDMLES----NHTN----LQRVTY 251
Cdd:COG1205  112 ALARdQlrrLRELAEALGL--GVRVATYDGDTP--PEERRwIREHPDIVLTNP----DMLHYgllpHHTRwarfFRNLRY 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 252 LVLDEA---------------DRML----DMGFDPQLrkIVSqirpdrqtlywSATW--PKEveqLARKFLYNPYKVIIG 310
Cdd:COG1205  184 VVIDEAhtyrgvfgshvanvlRRLRricrHYGSDPQF--ILA-----------SATIgnPAE---HAERLTGRPVTVVDE 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 311 SSdlkANHAIRQYV-------DIVSEKQKYDKLVKLLEDIM-DGSRILIFMDTKKGCDQITRQLR---MDGWPALSIHG- 378
Cdd:COG1205  248 DG---SPRGERTFVlwnpplvDDGIRRSALAEAARLLADLVrEGLRTLVFTRSRRGAELLARYARralREPDLADRVAAy 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 379 -------DKSQAERDwvlseFKSGKSPIMTAT-------DVAarGLDVkdvkyVVNYDFPGSLEDYVHRIGRTGRAGAKG 444
Cdd:COG1205  325 ragylpeERREIERG-----LRSGELLGVVSTnalelgiDIG--GLDA-----VVLAGYPGTRASFWQQAGRAGRRGQDS 392

                 ....
gi 356526023 445 TAYT 448
Cdd:COG1205  393 LVVL 396
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
310-445 8.11e-14

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 74.00  E-value: 8.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 310 GSSDLKANHAIRQYVDIVSEKQ----KYDKLVKLLEDIMD---GSRILIFMDTKKGCDQITRQLRMDGWPAL------SI 376
Cdd:COG1111  310 ASKRLVSDPRFRKAMRLAEEADiehpKLSKLREILKEQLGtnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSK 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 377 HGDK--SQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNYDfPGSLE-DYVHRIGRTGRAG--------AKGT 445
Cdd:COG1111  390 EGDKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGRKRegrvvvliAKGT 468
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
328-450 1.15e-13

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. 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: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 68.00  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 328 SEKQKYDKLVKLLEDIMDGSRIlIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAA 407
Cdd:cd18794   13 KKDEKLDLLKRIKVEHLGGSGI-IYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFG 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 356526023 408 RGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAGAKGTAYTYF 450
Cdd:cd18794   92 MGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
109-462 7.97e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 70.69  E-value: 7.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 109 PEYVLQEITKAGFTEPTPIQSQGWPMAL-KGRDLIGIAETGSGKTL-AYLlpAIVHVnaqpILNpgdGPIVLVLAPTREL 186
Cdd:COG1204    8 LEKVIEFLKERGIEELYPPQAEALEAGLlEGKNLVVSAPTASGKTLiAEL--AILKA----LLN---GGKALYIVPLRAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 187 AVQIQQETTKFGASSRIKSTCIYGGVPKGPqvRDLQKgVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEAdRMLDmgfD 266
Cdd:COG1204   79 ASEKYREFKRDFEELGIKVGVSTGDYDSDD--EWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLID---D 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 267 PQ----LRKIVSQIR---PDRQTLYWSATWPkEVEQLARKFLYNPYKVIIGSSDLKAN---HAIRQYVDivSEKQKYDKL 336
Cdd:COG1204  152 ESrgptLEVLLARLRrlnPEAQIVALSATIG-NAEEIAEWLDAELVKSDWRPVPLNEGvlyDGVLRFDD--GSRRSKDPT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 337 VKLLED-IMDGSRILIFMDTKKGC----------------DQITRQLRMDGWPALSI---------------------HG 378
Cdd:COG1204  229 LALALDlLEEGGQVLVFVSSRRDAeslakkladelkrrltPEEREELEELAEELLEVseethtnekladclekgvafhHA 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 379 DKSQAERDWVLSEFKSGKSPIMTATD-------VAARGLDVKDVKYVVNYDFPGSleDYVHRIGRTGRAGA--KGTAYTY 449
Cdd:COG1204  309 GLPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIPVL--EFKQMAGRAGRPGYdpYGEAILV 386
                        410
                 ....*....|...
gi 356526023 450 ftAANARFAKELI 462
Cdd:COG1204  387 --AKSSDEADELF 397
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
109-480 1.97e-12

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 69.36  E-value: 1.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 109 PEYVLQEITkaGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHvnaqpilnpgDGpIVLVLAPTRELAV 188
Cdd:PRK11057  13 AKQVLQETF--GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL----------DG-LTLVVSPLISLMK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 189 -QIQQETTKFGASSRIKSTciyggvpkgpQVRDLQKGV---------EIVIATPGRLI--DMLES-NHTNLqrvTYLVLD 255
Cdd:PRK11057  80 dQVDQLLANGVAAACLNST----------QTREQQLEVmagcrtgqiKLLYIAPERLMmdNFLEHlAHWNP---ALLAVD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 256 EADRMLDMG--FDPQLRKIvSQIR---PDRQTLYWSATWPKEVEQ--LARKFLYNPYkVIIGSSDlKANhaIRqYVdiVS 328
Cdd:PRK11057 147 EAHCISQWGhdFRPEYAAL-GQLRqrfPTLPFMALTATADDTTRQdiVRLLGLNDPL-IQISSFD-RPN--IR-YT--LV 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 329 EKQK-YDKLVKLLEDIMDGSRIlIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAA 407
Cdd:PRK11057 219 EKFKpLDQLMRYVQEQRGKSGI-IYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFG 297
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356526023 408 RGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAGAKGTAYTYFTAANARFAKELiaiLEE--AGQKVSPE---LAAMG 480
Cdd:PRK11057 298 MGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRC---LEEkpAGQQQDIErhkLNAMG 372
PRK13766 PRK13766
Hef nuclease; Provisional
312-456 8.74e-11

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 64.51  E-value: 8.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 312 SDLKANHAIRQYVDIVSEKQKYDKLVKLLEDIM---DGSRILIFM---DTKKgcdQITRQLRMDGWPAL------SIHGD 379
Cdd:PRK13766 328 EDPRFRKAVRKAKELDIEHPKLEKLREIVKEQLgknPDSRIIVFTqyrDTAE---KIVDLLEKEGIKAVrfvgqaSKDGD 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 380 K--SQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAG--------AKGTA-YT 448
Cdd:PRK13766 405 KgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGRQEegrvvvliAKGTRdEA 484

                 ....*...
gi 356526023 449 YFTAANAR 456
Cdd:PRK13766 485 YYWSSRRK 492
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
136-462 1.51e-10

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 63.76  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  136 LKGRDLIGIAETGSGKTLAYLLPAIVhvnaqpilNPGdgpIVLVLAPTRELavqIQQETTKFgASSRIKSTCIYGGVPKG 215
Cdd:PLN03137  473 MSGYDVFVLMPTGGGKSLTYQLPALI--------CPG---ITLVISPLVSL---IQDQIMNL-LQANIPAASLSAGMEWA 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  216 PQVRDLQK------GVEIVIATPGR------LIDMLESNHTN--LQRVtylVLDEADRMLDMGFDpqlrkivsqIRPDRQ 281
Cdd:PLN03137  538 EQLEILQElsseysKYKLLYVTPEKvaksdsLLRHLENLNSRglLARF---VIDEAHCVSQWGHD---------FRPDYQ 605
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  282 TLywsatwpkevEQLARKFLYNPYKVIIGSSDLKANHAIRQ---YVDIVSEKQKYD----------KLVKLLEDI----- 343
Cdd:PLN03137  606 GL----------GILKQKFPNIPVLALTATATASVKEDVVQalgLVNCVVFRQSFNrpnlwysvvpKTKKCLEDIdkfik 675
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  344 ---MDGSRIlIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDVKDVKYVVN 420
Cdd:PLN03137  676 enhFDECGI-IYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIH 754
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 356526023  421 YDFPGSLEDYVHRIGRTGRAGAKGTAYTYFTAANARFAKELI 462
Cdd:PLN03137  755 HSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMI 796
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
332-437 4.31e-10

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 62.16  E-value: 4.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 332 KYDKLVKLLEDIMD-GSRILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSP--IMTATDVAAR 408
Cdd:COG0553  534 KLEALLELLEELLAeGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGE 613
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 356526023 409 GLDVKDVKYVVNYDF---PGSLE---DYVHRIGRT 437
Cdd:COG0553  614 GLNLTAADHVIHYDLwwnPAVEEqaiDRAHRIGQT 648
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
348-451 1.77e-09

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: 54.25  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 348 RILIFMDTKKGCDQITRQLRmdgwpalsihgdksqaerdwvlsefksgkspIMTATDVAARGLDVKDVKYVVNYDFPGSL 427
Cdd:cd18785    5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
                         90       100
                 ....*....|....*....|....
gi 356526023 428 EDYVHRIGRTGRAGAKGTAYTYFT 451
Cdd:cd18785   54 ASYIQRVGRAGRGGKDEGEVILFV 77
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
332-435 3.33e-09

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: 55.18  E-value: 3.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 332 KYDKLVKLLEDI-MDGSRILIFMDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFKSGKSP--IMTATDVAAR 408
Cdd:cd18793   12 KLEALLELLEELrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGV 91
                         90       100       110
                 ....*....|....*....|....*....|...
gi 356526023 409 GLDVKDVKYVVNYDF---PGSLE---DYVHRIG 435
Cdd:cd18793   92 GLNLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
125-257 5.54e-09

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: 55.73  E-value: 5.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 125 TPIQSQGWPMALKGRD--LIGiAETGSGKTLAYLLpAIVHVNAQpilnpgDGPIVLVLAPTRELAVQIQQETTKFGASSR 202
Cdd:cd17921    3 NPIQREALRALYLSGDsvLVS-APTSSGKTLIAEL-AILRALAT------SGGKAVYIAPTRALVNQKEADLRERFGPLG 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 356526023 203 IKSTCIYG-GVPKGPQVRDLQkgveIVIATPGRLIDMLESNHT-NLQRVTYLVLDEA 257
Cdd:cd17921   75 KNVGLLTGdPSVNKLLLAEAD----ILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
121-192 1.39e-08

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 57.42  E-value: 1.39e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356526023 121 FTEPTPIQSQGWPMALKGRD-LIgIAETGSGKTLAYLLPAIVH-VNAQPILNPGDGPIVLVLAPTRELAVQIQQ 192
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGEStLL-IAPTGSGKTLAAFLPALDElARRPRPGELPDGLRVLYISPLKALANDIER 94
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
135-257 5.63e-08

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: 52.59  E-value: 5.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 135 ALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPilnpgdGPIVLVLAPTRELAvQIQQET-TKFGAS--SRIKSTCIYGG 211
Cdd:cd17923   12 ARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALA-QDQLRSlRELLEQlgLGIRVATYDGD 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 356526023 212 VPKGPQVRDLQKGVEIVIATPgrliDMLES----NHTN----LQRVTYLVLDEA 257
Cdd:cd17923   85 TPREERRAIIRNPPRILLTNP----DMLHYallpHHDRwarfLRNLRYVVLDEA 134
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
332-439 5.91e-08

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: 51.97  E-value: 5.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 332 KYDKLVKLL------EDIMDGSRILIFMDTKKGCDQITRQLRMDGW---PALSI-HGDK------SQAERDWVLSEFKSG 395
Cdd:cd18801   10 KLEKLEEIVkehfkkKQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPgirATRFIgQASGksskgmSQKEQKEVIEQFRKG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 356526023 396 KSPIMTATDVAARGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGR 439
Cdd:cd18801   90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
332-443 6.55e-08

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: 51.44  E-value: 6.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 332 KYDKLVKLLEDIM------DGSRILIFMDTKKGCDQITRQLR-----MDGWPALSI--HGDKSQAERDW--------VLS 390
Cdd:cd18802    5 VIPKLQKLIEILReyfpktPDFRGIIFVERRATAVVLSRLLKehpstLAFIRCGFLigRGNSSQRKRSLmtqrkqkeTLD 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 356526023 391 EFKSGKSPIMTATDVAARGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAGAK 443
Cdd:cd18802   85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSK 137
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
339-439 4.64e-07

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: 49.18  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 339 LLEDIMDGSRILIFMDTKKGCDQITRQLRM---DGWPALSI---HGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLDV 412
Cdd:cd18796   31 VIFLLERHKSTLVFTNTRSQAERLAQRLRElcpDRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDI 110
                         90       100
                 ....*....|....*....|....*..
gi 356526023 413 KDVKYVVNYDFPGSLEDYVHRIGRTGR 439
Cdd:cd18796  111 GDVDLVIQIGSPKSVARLLQRLGRSGH 137
PRK01172 PRK01172
ATP-dependent DNA helicase;
105-455 1.22e-06

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 51.04  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 105 DAGFPEYVLQEITKAGFtEPTPIQSQGWPMALKGRDLIGIAETGSGKTLayllpaIVHVNAQPILNPGDGPIVLVlaPTR 184
Cdd:PRK01172   5 DLGYDDEFLNLFTGNDF-ELYDHQRMAIEQLRKGENVIVSVPTAAGKTL------IAYSAIYETFLAGLKSIYIV--PLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 185 ELAVQIQQETTKFGA-SSRIK-STCIYGGVPkgpqvrDLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLD 262
Cdd:PRK01172  76 SLAMEKYEELSRLRSlGMRVKiSIGDYDDPP------DFIKRYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 263 MGFDPQLRKIVSQIR---PDRQTLYWSATwPKEVEQLAR---------KFLYNPYKV-IIGSSDLKANHAIRQYVDIVSe 329
Cdd:PRK01172 150 EDRGPTLETVLSSARyvnPDARILALSAT-VSNANELAQwlnasliksNFRPVPLKLgILYRKRLILDGYERSQVDINS- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 330 kqkydkLVKllEDIMDGSRILIFMDTKKGCDQITRQL---------------RMDGWPALSI----------HGDKSQAE 384
Cdd:PRK01172 228 ------LIK--ETVNDGGQVLVFVSSRKNAEDYAEMLiqhfpefndfkvsseNNNVYDDSLNemlphgvafhHAGLSNEQ 299
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356526023 385 RDWVLSEFKSGKSPIMTATDVAARGLD-------VKDV-KYVVNYDFPGSLEDYVHRIGRTGRAGAKGTAYTYFTAANA 455
Cdd:PRK01172 300 RRFIEEMFRNRYIKVIVATPTLAAGVNlparlviVRDItRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIYAASP 378
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
332-450 1.27e-06

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: 48.01  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 332 KYDKLVKLLEDIMDGSRILIFMDTKkgcDQITRQLRMDGWPAlsIHGDKSQAERDWVLSEFKSGKSPIMTATDVAARGLD 411
Cdd:cd18789   35 KLRALEELLKRHEQGDKIIVFTDNV---EALYRYAKRLLKPF--ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGID 109
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 356526023 412 VKD--VKYVVNYDFpGSLEDYVHRIGRTGRAGaKGTAYTYF 450
Cdd:cd18789  110 LPEanVAIQISGHG-GSRRQEAQRLGRILRPK-KGGGKNAF 148
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
135-295 2.23e-06

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: 48.30  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 135 ALKGRDLIGIAETGSGKTLAYLLPAIVhvnaqpilnpgDGPIVLVLAPTRELAV-QIQQETTKfgassRIKSTCIYGGVP 213
Cdd:cd17920   24 VLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVDRLQQL-----GIRAAALNSTLS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 214 KGPQVRDLQK----GVEIVIATPGRL-----IDMLESNHtNLQRVTYLVLDEADRMLDMGFD--PQLRKIvSQIR---PD 279
Cdd:cd17920   88 PEEKREVLLRikngQYKLLYVTPERLlspdfLELLQRLP-ERKRLALIVVDEAHCVSQWGHDfrPDYLRL-GRLRralPG 165
                        170
                 ....*....|....*.
gi 356526023 280 RQTLYWSATWPKEVEQ 295
Cdd:cd17920  166 VPILALTATATPEVRE 181
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
135-259 4.07e-06

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: 47.43  E-value: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 135 ALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDgpiVLVLAPTRELavqIQQETTKFGASSRI---KSTCIYGG 211
Cdd:cd17927   14 ALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGK---VVFLANKVPL---VEQQKEVFRKHFERpgyKVTGLSGD 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 356526023 212 VPKGPQVRDLQKGVEIVIATPGRLIDMLES-NHTNLQRVTYLVLDEADR 259
Cdd:cd17927   88 TSENVSVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHN 136
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
120-295 4.39e-06

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: 47.64  E-value: 4.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 120 GFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIvhvnaqpILNPGDGPIVLVLAPTreLAVQIQQETtkfGA 199
Cdd:cd18018    9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL-------LLRRRGPGLTLVVSPL--IALMKDQVD---AL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 200 SSRIKSTCIYGGVPKGPQVRDLQK----GVEIVIATPGRLID-MLESNHTNLQRVTYLVLDEADRMLDMGFD--P---QL 269
Cdd:cd18018   77 PRAIKAAALNSSLTREERRRILEKlragEVKILYVSPERLVNeSFRELLRQTPPISLLVVDEAHCISEWSHNfrPdylRL 156
                        170       180
                 ....*....|....*....|....*.
gi 356526023 270 RKIVSQIRPDRQTLYWSATWPKEVEQ 295
Cdd:cd18018  157 CRVLRELLGAPPVLALTATATKRVVE 182
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
123-256 5.21e-06

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: 47.47  E-value: 5.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 123 EPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPilNPGDGPIVLVLAPTRELavqIQQETTKFGASSR 202
Cdd:cd18036    2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRR--SAGEKGRVVVLVNKVPL---VEQQLEKFFKYFR 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 203 --IKSTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMLESNHTN----LQRVTYLVLDE 256
Cdd:cd18036   77 kgYKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDE 136
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
147-288 1.77e-05

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: 44.60  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 147 TGSGKTLAYLLpAIVHVNAQPilnpgdgpiVLVLAPTRELAVQIQQETTKFGASSRIkstCIYGGVPKgpqvrDLQKGVE 226
Cdd:cd17926   27 TGSGKTLTALA-LIAYLKELR---------TLIVVPTDALLDQWKERFEDFLGDSSI---GLIGGGKK-----KDFDDAN 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356526023 227 IVIATPGRLIDMLESNHTNLQRVTYLVLDEADRmldmGFDPQLRKIVSQIRPDRQtLYWSAT 288
Cdd:cd17926   89 VVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEILKELNAKYR-LGLTAT 145
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
138-256 1.86e-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: 44.88  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 138 GRDLIGIAETGSGKTLAYLLPAIVHVNAqpilNPGDGPIVLVLAPTRELAVQIQQettkfgassRIK--STCIYGGVPKG 215
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLAD----EPEKGVQVLYISPLKALINDQER---------RLEepLDEIDLEIPVA 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 356526023 216 PQVRD---------LQKGVEIVIATPGRLIDMLESNHTN--LQRVTYLVLDE 256
Cdd:cd17922   68 VRHGDtsqsekakqLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
135-259 4.29e-05

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: 44.43  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 135 ALKGRDLIgIAETGSGKTLAYLLPAivhvnaQPILNPGDGPiVLVLAPTRELAVQiQQETTKFGASSRIKSTCIYGGVPk 214
Cdd:cd18035   14 ALNGNTLI-VLPTGLGKTIIAILVA------ADRLTKKGGK-VLILAPSRPLVEQ-HAENLKRVLNIPDKITSLTGEVK- 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 356526023 215 gPQVR-DLQKGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEADR 259
Cdd:cd18035   84 -PEERaERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
118-283 4.34e-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: 44.82  E-value: 4.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 118 KAGFTEPTPIQSQGWPMALKGRDLIGIAETGSGKTLAYLLPAIVhvnaqpilNPGdgpIVLVLAPTRELAV-QIQQETT- 195
Cdd:cd18016   12 KFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACV--------SPG---VTVVISPLRSLIVdQVQKLTSl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 196 ------KFGASSRIKSTCIYGGVPKG-PQVRDLQKGVEIVIATpGRLIDMLESNHTNlQRVTYLVLDEADRMLDMGFDpq 268
Cdd:cd18016   81 dipatyLTGDKTDAEATKIYLQLSKKdPIIKLLYVTPEKISAS-NRLISTLENLYER-KLLARFVIDEAHCVSQWGHD-- 156
                        170
                 ....*....|....*
gi 356526023 269 lrkivsqIRPDRQTL 283
Cdd:cd18016  157 -------FRPDYKRL 164
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
135-257 4.51e-05

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: 44.56  E-value: 4.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 135 ALKgRDLIGIAETGSGKTL-AYLLpaIVHVNAQPILNPGDGPIVLVLAPTRELAVQ----IQQETTKfgassriKSTCIY 209
Cdd:cd18034   14 ALK-RNTIVVLPTGSGKTLiAVML--IKEMGELNRKEKNPKKRAVFLVPTVPLVAQqaeaIRSHTDL-------KVGEYS 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 356526023 210 G--GVPKGPQVRDLQ--KGVEIVIATPGRLIDMLESNHTNLQRVTYLVLDEA 257
Cdd:cd18034   84 GemGVDKWTKERWKEelEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
335-441 2.35e-04

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: 41.47  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 335 KLVKLLedIMDGSRILIFMDTKKGCDQITRQL--RMDGWPAL-----SIHGDKSQAERDWVLSEFKSGKSPIMTATDVAA 407
Cdd:cd18797   26 RLFADL--VRAGVKTIVFCRSRKLAELLLRYLkaRLVEEGPLaskvaSYRAGYLAEDRREIEAELFNGELLGVVATNALE 103
                         90       100       110
                 ....*....|....*....|....*....|....
gi 356526023 408 RGLDVKDVKYVVNYDFPGSLEDYVHRIGRTGRAG 441
Cdd:cd18797  104 LGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRG 137
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
58-162 3.15e-04

bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 43.40  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  58 LPHFEKNFYIESPAVRAMTDAEVNEYRQqreITVEGRDIPKPVKTFHDAGFPEYvLQEITKAgFTEPTPI----QSQgWP 133
Cdd:PRK08074 191 IAELLDENILKKMMHGKPLDEEFDEYRG---IALRKREVEKNLEETCRSDFDAF-LEKTEEK-LSLAMPKyekrEGQ-QE 264
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 356526023 134 M------ALKGRD--LIGiAETGSGKTLAYLLPAIVH 162
Cdd:PRK08074 265 MmkevytALRDSEhaLIE-AGTGTGKSLAYLLPAAYF 300
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
127-256 7.53e-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: 40.80  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 127 IQSQGWPMALKG-RDLIGIAETGSGKTLAYLLpAIVHVNAQPILNPGDGPIVLVLAPTRELAVQIQQE-TTKFGaSSRIK 204
Cdd:cd18023    5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFEL-AILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDwKEKFG-PLGLS 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 356526023 205 STCIYGGVPKGPqVRDLQKgVEIVIATPGR--LIDMLESNHTNL-QRVTYLVLDE 256
Cdd:cd18023   83 CAELTGDTEMDD-TFEIQD-ADIILTTPEKwdSMTRRWRDNGNLvQLVALVLIDE 135
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
137-166 8.14e-04

Rad3-related DNA helicase DinG [Replication, recombination and repair];


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 42.22  E-value: 8.14e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 356526023 137 KGRDLIGIAETGSGKTLAYLLPAIVHVNAQ 166
Cdd:COG1199   32 EGRHLLIEAGTGTGKTLAYLVPALLAARET 61
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
139-260 8.57e-04

DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part 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: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 40.48  E-value: 8.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 139 RDLIGIAETGSGKTLAYLLPAIVHVNAqpilnpgdGPIVLVLAPTRELAVQIQQETTKFGASSRIKStciyggVPKGPQV 218
Cdd:cd17918   37 MDRLLSGDVGSGKTLVALGAALLAYKN--------GKQVAILVPTEILAHQHYEEARKFLPFINVEL------VTGGTKA 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 356526023 219 RDLQkGVEIVIATPGrLIDMLESNHtnlqRVTYLVLDEADRM 260
Cdd:cd17918  103 QILS-GISLLVGTHA-LLHLDVKFK----NLDLVIVDEQHRF 138
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
136-297 9.18e-04

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: 40.40  E-value: 9.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 136 LKGRDLIGIAETGSGKTLAYLLpAIVHVnaqpILNPGDGpivLVLAPTRELAVQIQQEttkFGASSRIkstciygGVPKG 215
Cdd:cd18028   15 LKGENLLISIPTASGKTLIAEM-AMVNT----LLEGGKA---LYLVPLRALASEKYEE---FKKLEEI-------GLKVG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 216 PQVRDLQKGVE------IVIATPGRLIDMLESNHTNLQRVTYLVLDEADRMLDMGFDPQLRKIVSQIR---PDRQTLYWS 286
Cdd:cd18028   77 ISTGDYDEDDEwlgdydIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnPNTQIIGLS 156
                        170
                 ....*....|.
gi 356526023 287 ATWPKeVEQLA 297
Cdd:cd18028  157 ATIGN-PDELA 166
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
286-443 2.61e-03

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: 40.11  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 286 SATWPKEVEQLARKFLYNPYKViigSSDLKANHA----IRQYVDIVSEKQKYDklvkLLEDIMDGSRILIFMDTKKGCDQ 361
Cdd:cd09639  161 SATLPKFLKEYAEKIGYVEENE---PLDLKPNERapfiKIESDKVGEISSLER----LLEFIKKGGSVAIIVNTVDRAQE 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 362 ITRQLRMDG--WPALSIHG-----DKSQAERDwVLSEFKSGKSPIMTATDVAARGLDVkDVKYVVNYDFPGSLedYVHRI 434
Cdd:cd09639  234 FYQQLKEKGpeEEIMLIHSrftekDRAKKEAE-LLLEFKKSEKFVIVATQVIEASLDI-SVDVMITELAPIDS--LIQRL 309

                 ....*....
gi 356526023 435 GRTGRAGAK 443
Cdd:cd09639  310 GRLHRYGEK 318
DEXHc_RecQ5 cd18014
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ...
125-283 3.35e-03

DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) 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.


Pssm-ID: 350772 [Multi-domain]  Cd Length: 205  Bit Score: 38.99  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 125 TPIQSQGWPMALKGR-DLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDGPIVLVLAPTRELAVQIQQETTKFGASSRI 203
Cdd:cd18014   15 SPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRVDSLNSKLSAQERK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 204 KstcIYGGV-PKGPQVRDLQKGVEIViATPG--RLIDMLESNHtnlqRVTYLVLDEADRMLDMGFDpqlrkivsqIRPDR 280
Cdd:cd18014   95 R---IIADLeSEKPQTKFLYITPEMA-ATSSfqPLLSSLVSRN----LLSYLVVDEAHCVSQWGHD---------FRPDY 157

                 ...
gi 356526023 281 QTL 283
Cdd:cd18014  158 LRL 160
ResIII pfam04851
Type III restriction enzyme, res subunit;
147-288 4.90e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.04  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023  147 TGSGKTL-AYLLPAIVHvNAQPILNpgdgpiVLVLAPTRELAVQIQQETTKFGASSRIKSTCIYGgvPKGPQVRDlqkGV 225
Cdd:pfam04851  32 TGSGKTLtAAKLIARLF-KKGPIKK------VLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISG--DKKDESVD---DN 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356526023  226 EIVIATPGRL--IDMLESNHTNLQRVTYLVLDEADRmldmGFDPQLRKIVSQIRPDRQtLYWSAT 288
Cdd:pfam04851 100 KIVVTTIQSLykALELASLELLPDFFDVIIIDEAHR----SGASSYRNILEYFKPAFL-LGLTAT 159
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
135-256 8.10e-03

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: 37.88  E-value: 8.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356526023 135 ALKGRDLIGIAETGSGKTLAYLLPAIVHVNAQPILNPGDgpiVLVLAptRELAVQIQQET--TKFGASSRIKSTCIYGGV 212
Cdd:cd18073   14 AMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGK---VVFFA--TKVPVYEQQKSvfSKYFERHGYRVTGISGAT 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 356526023 213 PKGPQVRDLQKGVEIVIATPGRLIDMLESNH-TNLQRVTYLVLDE 256
Cdd:cd18073   89 AENVPVEQIIENNDIIILTPQILVNNLKKGTiPSLSIFTLMIFDE 133
 
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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