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Conserved domains on  [gi|18407327|ref|NP_566099|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423521)

DEAD/DEAH box-containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0005524
PubMed:  20206133
SCOP:  4000282|3002019

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
229-584 9.27e-157

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 461.54  E-value: 9.27e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 229 TFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQpelqRDEGPIGVICA 308
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS----RPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 309 PTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMF 388
Cdd:COG0513  79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 389 DLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVGMANEDITQVVnVIPSDAEKLPwLLEKLP 468
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRY-YLVDKRDKLE-LLRRLL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 469 GMIDEGDVLVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNY 548
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 18407327 549 DIAKDMDMHVHRIGRTGRAGdRDGVAYTLVTQREAR 584
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAG-AEGTAISLVTPDERR 351
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
229-584 9.27e-157

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 461.54  E-value: 9.27e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 229 TFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQpelqRDEGPIGVICA 308
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS----RPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 309 PTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMF 388
Cdd:COG0513  79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 389 DLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVGMANEDITQVVnVIPSDAEKLPwLLEKLP 468
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRY-YLVDKRDKLE-LLRRLL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 469 GMIDEGDVLVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNY 548
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 18407327 549 DIAKDMDMHVHRIGRTGRAGdRDGVAYTLVTQREAR 584
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAG-AEGTAISLVTPDERR 351
PTZ00110 PTZ00110
helicase; Provisional
178-609 4.50e-149

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 446.53  E-value: 4.50e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  178 LDHSSIDYEPINKDFYEELESISGMTEQETTDYRQRLGIR-VSGFDVHRPVKTFEDCGFSSQIMSAIKKQAYEKPTAIQC 256
Cdd:PTZ00110  79 IDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQV 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  257 QALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDEGPIGVICAPTRELAHQIFLEAKKFSKAYGLRVSAVY 336
Cdd:PTZ00110 159 QGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAY 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  337 GGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQIRPDRQTLLFSATM 416
Cdd:PTZ00110 239 GGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATW 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  417 PWKVEKLAREILSD-PIRVTVGEVGM-ANEDITQVVNVIpSDAEK---LPWLLEKLpgMIDEGDVLVFASKKATVDEIEA 491
Cdd:PTZ00110 319 PKEVQSLARDLCKEePVHVNVGSLDLtACHNIKQEVFVV-EEHEKrgkLKMLLQRI--MRDGDKILIFVETKKGADFLTK 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  492 QLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNYDIAKDMDMHVHRIGRTGRAGDRd 571
Cdd:PTZ00110 396 ELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAK- 474
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 18407327  572 GVAYTLVTQREARFAGELVNSLVAAGQNVPPELTDLAM 609
Cdd:PTZ00110 475 GASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSN 512
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
239-435 2.44e-135

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: 397.94  E-value: 2.44e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDEGPIGVICAPTRELAHQIF 318
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 319 LEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRS 398
Cdd:cd17952  81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18407327 399 IVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVT 435
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
252-423 7.82e-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: 212.87  E-value: 7.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327   252 TAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDqpelqRDEGPIGVICAPTRELAHQIFLEAKKFSKAYGLR 331
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK-----LDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327   332 VSAVYGGMSKHEQFKELKaGCEIVVATPGRLIDMLKmKALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQIRPDRQTLL 411
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 18407327   412 FSATMPWKVEKL 423
Cdd:pfam00270 154 LSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
243-449 4.62e-58

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 196.17  E-value: 4.62e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327    243 IKKQAYEKPTAIQCQALPIVLSG-RDVIGIAKTGSGKTAAFVLPMIVHimdqpeLQRDEGPIGVICAPTRELAHQIFLEA 321
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327    322 KKFSKAYGLRVSAVYGGMSKHEQFKELKAGC-EIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIV 400
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 18407327    401 GQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTVGEvgMANEDITQV 449
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
229-584 9.27e-157

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 461.54  E-value: 9.27e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 229 TFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQpelqRDEGPIGVICA 308
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS----RPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 309 PTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMF 388
Cdd:COG0513  79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 389 DLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVGMANEDITQVVnVIPSDAEKLPwLLEKLP 468
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRY-YLVDKRDKLE-LLRRLL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 469 GMIDEGDVLVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNY 548
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 18407327 549 DIAKDMDMHVHRIGRTGRAGdRDGVAYTLVTQREAR 584
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAG-AEGTAISLVTPDERR 351
PTZ00110 PTZ00110
helicase; Provisional
178-609 4.50e-149

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 446.53  E-value: 4.50e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  178 LDHSSIDYEPINKDFYEELESISGMTEQETTDYRQRLGIR-VSGFDVHRPVKTFEDCGFSSQIMSAIKKQAYEKPTAIQC 256
Cdd:PTZ00110  79 IDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQV 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  257 QALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDEGPIGVICAPTRELAHQIFLEAKKFSKAYGLRVSAVY 336
Cdd:PTZ00110 159 QGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAY 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  337 GGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQIRPDRQTLLFSATM 416
Cdd:PTZ00110 239 GGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATW 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  417 PWKVEKLAREILSD-PIRVTVGEVGM-ANEDITQVVNVIpSDAEK---LPWLLEKLpgMIDEGDVLVFASKKATVDEIEA 491
Cdd:PTZ00110 319 PKEVQSLARDLCKEePVHVNVGSLDLtACHNIKQEVFVV-EEHEKrgkLKMLLQRI--MRDGDKILIFVETKKGADFLTK 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  492 QLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNYDIAKDMDMHVHRIGRTGRAGDRd 571
Cdd:PTZ00110 396 ELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAK- 474
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 18407327  572 GVAYTLVTQREARFAGELVNSLVAAGQNVPPELTDLAM 609
Cdd:PTZ00110 475 GASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSN 512
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
239-435 2.44e-135

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: 397.94  E-value: 2.44e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDEGPIGVICAPTRELAHQIF 318
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 319 LEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRS 398
Cdd:cd17952  81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18407327 399 IVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVT 435
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
217-435 2.74e-113

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: 342.05  E-value: 2.74e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 217 RVSGFDVHRPVKTFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPEL 296
Cdd:cd17953   1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 297 QRDEGPIGVICAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKM---KALTM 373
Cdd:cd17953  81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTAnngRVTNL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18407327 374 MRASYLVLDEADRMFDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVT 435
Cdd:cd17953 161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
239-435 1.99e-99

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: 305.06  E-value: 1.99e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDEGPIGVICAPTRELAHQIF 318
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 319 LEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRS 398
Cdd:cd17966  81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18407327 399 IVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVT 435
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
239-435 1.14e-96

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: 297.82  E-value: 1.14e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDeGPIGVICAPTRELAHQIF 318
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGR-GPQALVLAPTRELAMQIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 319 LEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRS 398
Cdd:cd00268  80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18407327 399 IVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVT 435
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
248-589 3.69e-95

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 303.65  E-value: 3.69e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  248 YEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHI-MDQPELQRdegpiGVICaPTRELAHQIFLEAKKFSK 326
Cdd:PRK11776  24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLdVKRFRVQA-----LVLC-PTRELADQVAKEIRRLAR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  327 A-YGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQIRP 405
Cdd:PRK11776  98 FiPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  406 DRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVGmANEDITQVVNVIpSDAEKLPwLLEKLPGMIDEGDVLVFASKKAT 485
Cdd:PRK11776 178 RRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH-DLPAIEQRFYEV-SPDERLP-ALQRLLLHHQPESCVVFCNTKKE 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  486 VDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNYDIAKDMDMHVHRIGRTG 565
Cdd:PRK11776 255 CQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTG 334
                        330       340
                 ....*....|....*....|....
gi 18407327  566 RAGDRdGVAYTLVTQREARFAGEL 589
Cdd:PRK11776 335 RAGSK-GLALSLVAPEEMQRANAI 357
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
229-578 1.53e-86

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 280.93  E-value: 1.53e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  229 TFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDEGPI-GVIC 307
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  308 APTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRM 387
Cdd:PRK10590  82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  388 FDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVGMANEDITQVVNVIPSDAEKlpwllEKL 467
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKR-----ELL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  468 PGMIDEGD---VLVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKT 544
Cdd:PRK10590 237 SQMIGKGNwqqVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPH 316
                        330       340       350
                 ....*....|....*....|....*....|....
gi 18407327  545 VVNYDIAKDMDMHVHRIGRTGRAgDRDGVAYTLV 578
Cdd:PRK10590 317 VVNYELPNVPEDYVHRIGRTGRA-AATGEALSLV 349
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
229-440 2.87e-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: 268.97  E-value: 2.87e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 229 TFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDEG-----PI 303
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 304 GVICAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDE 383
Cdd:cd17967  81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18407327 384 ADRMFDLGFEPQVRSIVGQ----IRPDRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVG 440
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
228-578 1.16e-84

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 275.28  E-value: 1.16e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  228 KTFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPelQRDEGPIGV-I 306
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP--RRKSGPPRIlI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  307 CAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADR 386
Cdd:PRK11192  79 LTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  387 MFDLGFEPQVRSIVGQIRPDRQTLLFSATMPWK-VEKLAREILSDPIRVTVGEVGMANEDITQVVNVIPSDAEKLPwLLE 465
Cdd:PRK11192 159 MLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTA-LLC 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  466 KLpgmIDEGDV---LVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSL 542
Cdd:PRK11192 238 HL---LKQPEVtrsIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 18407327  543 KTVVNYDIAKDMDMHVHRIGRTGRAGdRDGVAYTLV 578
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAG-RKGTAISLV 349
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
229-584 2.17e-84

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 280.58  E-value: 2.17e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  229 TFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHImdQPELQrdeGPIGVICA 308
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPELK---APQILVLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  309 PTRELAHQIFLEAKKFSK-AYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRM 387
Cdd:PRK11634  82 PTRELAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  388 FDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVGMANEDITQ----VVNVIPSDAeklpwL 463
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQsywtVWGMRKNEA-----L 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  464 LEKLPGMIDEGDVLVFASKKATVDEIEAqLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLK 543
Cdd:PRK11634 237 VRFLEAEDFDAAIIFVRTKNATLEVAEA-LERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERIS 315
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 18407327  544 TVVNYDIAKDMDMHVHRIGRTGRAGdRDGVAYTLVTQREAR 584
Cdd:PRK11634 316 LVVNYDIPMDSESYVHRIGRTGRAG-RAGRALLFVENRERR 355
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
205-437 2.68e-83

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: 264.56  E-value: 2.68e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 205 QETTDYRQRLGIRVSGFDVHRPVKTFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVL 284
Cdd:cd18049   1 QEVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 285 PMIVHIMDQPELQRDEGPIGVICAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLID 364
Cdd:cd18049  81 PAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18407327 365 MLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTVG 437
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
190-437 3.24e-83

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: 265.72  E-value: 3.24e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 190 KDFYEELESISGMTEQETTDYRQRLGIRVSGFDVHRPVKTFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVI 269
Cdd:cd18050  24 KNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 270 GIAKTGSGKTAAFVLPMIVHIMDQPELQRDEGPIGVICAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELK 349
Cdd:cd18050 104 GIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLE 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 350 AGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILS 429
Cdd:cd18050 184 RGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLR 263

                ....*...
gi 18407327 430 DPIRVTVG 437
Cdd:cd18050 264 DYVQINIG 271
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
230-588 1.67e-81

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 268.32  E-value: 1.67e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  230 FEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQP-ELQRDEG-PIGVIC 307
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPpPKERYMGePRALII 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  308 APTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAG-CEIVVATPGRLIDMLKMKALTMMRASYLVLDEADR 386
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  387 MFDLGFEPQVRSIVGQIRP--DRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVGMANEDITQ-VVNVIPSDAEKLpwl 463
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQhVYAVAGSDKYKL--- 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  464 LEKLPGMIDEGDVLVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLK 543
Cdd:PRK01297 326 LYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGIS 405
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 18407327  544 TVVNYDIAKDMDMHVHRIGRTGRAGDrDGVAYTlvtqrearFAGE 588
Cdd:PRK01297 406 HVINFTLPEDPDDYVHRIGRTGRAGA-SGVSIS--------FAGE 441
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
239-435 1.44e-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: 254.17  E-value: 1.44e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQP---ELQRDEGPIGVICAPTRELAH 315
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPpldEETKDDGPYALILAPTRELAQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 316 QIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQ 395
Cdd:cd17945  81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 396 VRSIVGQI-----RPD---------------RQTLLFSATMPWKVEKLAREILSDPIRVT 435
Cdd:cd17945 161 VTKILDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
228-568 2.36e-78

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 257.98  E-value: 2.36e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  228 KTFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQP--ELQRDEGPIGV 305
Cdd:PRK04837   8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPapEDRKVNQPRAL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  306 ICAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEAD 385
Cdd:PRK04837  88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  386 RMFDLGFEPQVRSIVGQIRP--DRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVGMANEDITQVVnVIPSDAEKLPWL 463
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEEL-FYPSNEEKMRLL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  464 LEklpgMIDE---GDVLVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIK 540
Cdd:PRK04837 247 QT----LIEEewpDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIP 322
                        330       340
                 ....*....|....*....|....*...
gi 18407327  541 SLKTVVNYDIAKDMDMHVHRIGRTGRAG 568
Cdd:PRK04837 323 AVTHVFNYDLPDDCEDYVHRIGRTGRAG 350
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
216-440 2.67e-78

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: 252.58  E-value: 2.67e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 216 IRVSGFDVHRPVKTFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQ-- 293
Cdd:cd18052  31 VEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgl 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 294 --PELQRDEGPIGVICAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKAL 371
Cdd:cd18052 111 taSSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKI 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18407327 372 TMMRASYLVLDEADRMFDLGFEPQVRSIVGQI----RPDRQTLLFSATMPWKVEKLAREIL-SDPIRVTVGEVG 440
Cdd:cd18052 191 SLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVGRVG 264
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
228-583 4.64e-76

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 256.42  E-value: 4.64e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  228 KTFEDCGFSS-----QIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPEL--QRDE 300
Cdd:PRK04537   4 KPLTDLTFSSfdlhpALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadRKPE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  301 GPIGVICAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYL- 379
Cdd:PRK04537  84 DPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEIc 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  380 VLDEADRMFDLGFEPQVRSIVGQI--RPDRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVGMANEDITQVVnVIPSDA 457
Cdd:PRK04537 164 VLDEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRI-YFPADE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  458 EKLPWLLeklpGMIDEGD---VLVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAA 534
Cdd:PRK04537 243 EKQTLLL----GLLSRSEgarTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAA 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 18407327  535 RGLDIKSLKTVVNYDIAKDMDMHVHRIGRTGRAGDrDGVAYTLVTQREA 583
Cdd:PRK04537 319 RGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGE-EGDAISFACERYA 366
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
189-604 6.61e-72

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 243.93  E-value: 6.61e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  189 NKDFY-EELESISGMTEQETTDYRQRLGIRVSGFDVHRPVKTFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRD 267
Cdd:PLN00206  81 DECFYvRDPGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRS 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  268 VIGIAKTGSGKTAAFVLPMIVH--IMDQPELQRDEGPIGVICAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQF 345
Cdd:PLN00206 161 LLVSADTGSGKTASFLVPIISRccTIRSGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQL 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  346 KELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIVgQIRPDRQTLLFSATMPWKVEKLAR 425
Cdd:PLN00206 241 YRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPEVEKFAS 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  426 EILSDPIRVTVGEVGMANEDITQVVNVIPSDAEKlpwllEKLPGMIDEGD-----VLVFASKKATVDEI-EAQLTLNSFK 499
Cdd:PLN00206 320 SLAKDIILISIGNPNRPNKAVKQLAIWVETKQKK-----QKLFDILKSKQhfkppAVVFVSSRLGADLLaNAITVVTGLK 394
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  500 VAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNYDIAKDMDMHVHRIGRTGRAGDrDGVAYTLVT 579
Cdd:PLN00206 395 ALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGE-KGTAIVFVN 473
                        410       420
                 ....*....|....*....|....*
gi 18407327  580 QREARFAGELVNSLVAAGQNVPPEL 604
Cdd:PLN00206 474 EEDRNLFPELVALLKSSGAAIPREL 498
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
216-440 8.58e-72

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: 234.55  E-value: 8.58e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 216 IRVSGFDVHRPVKTFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQ-- 293
Cdd:cd18051   9 VEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgp 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 294 -PELQRDEG--------PIGVICAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLID 364
Cdd:cd18051  89 gESLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 365 MLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQI----RPDRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVG 440
Cdd:cd18051 169 MLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVGRVG 248
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
239-437 1.15e-70

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: 229.78  E-value: 1.15e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHImdqPELQRDEGPIGVICAPTRELAHQIF 318
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKL---GKPRKKKGLRALILAPTRELASQIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 319 LEAKKFSKAYGLRVSAVYGGMS-KHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVR 397
Cdd:cd17957  78 RELLKLSKGTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18407327 398 SIVGQIR-PDRQTLLFSATMPWKVEKLAREILSDPIRVTVG 437
Cdd:cd17957 158 EILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
239-435 1.59e-67

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: 221.18  E-value: 1.59e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPEL--QRDeGPIGVICAPTRELAHQ 316
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPreQRN-GPGVLVLTPTRELALQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 317 IFLEAKKFSKAyGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQV 396
Cdd:cd17958  80 IEAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 18407327 397 RSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVT 435
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
239-434 1.68e-66

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: 218.75  E-value: 1.68e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQ----PELQRdEGPIGVICAPTRELA 314
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQekklPFIKG-EGPYGLIVCPSRELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 315 HQIFLEAKKFSKAY------GLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMF 388
Cdd:cd17951  80 RQTHEVIEYYCKALqeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 18407327 389 DLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRV 434
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
PTZ00424 PTZ00424
helicase 45; Provisional
227-579 4.35e-65

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 222.01  E-value: 4.35e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  227 VKTFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHImdQPELQRDEGpigVI 306
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI--DYDLNACQA---LI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  307 CAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADR 386
Cdd:PTZ00424 102 LAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  387 MFDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTVGEVGMANEDITQVVNVIPSDAEKLPWLLEk 466
Cdd:PTZ00424 182 MLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCD- 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  467 LPGMIDEGDVLVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVV 546
Cdd:PTZ00424 261 LYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVI 340
                        330       340       350
                 ....*....|....*....|....*....|...
gi 18407327  547 NYDIAKDMDMHVHRIGRTGRAGdRDGVAYTLVT 579
Cdd:PTZ00424 341 NYDLPASPENYIHRIGRSGRFG-RKGVAINFVT 372
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
252-423 7.82e-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: 212.87  E-value: 7.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327   252 TAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDqpelqRDEGPIGVICAPTRELAHQIFLEAKKFSKAYGLR 331
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK-----LDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327   332 VSAVYGGMSKHEQFKELKaGCEIVVATPGRLIDMLKmKALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQIRPDRQTLL 411
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 18407327   412 FSATMPWKVEKL 423
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 ...
229-434 1.58e-63

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: 210.64  E-value: 1.58e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 229 TFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPelqrdEGPIGVICA 308
Cdd:cd17954   1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENP-----QRFFALVLA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 309 PTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLK-MKALTMMRASYLVLDEADRM 387
Cdd:cd17954  76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEnTKGFSLKSLKFLVMDEADRL 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 18407327 388 FDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRV 434
Cdd:cd17954 156 LNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
229-434 4.27e-63

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: 209.85  E-value: 4.27e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 229 TFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHimdqpeLQRDEGPIGV--- 305
Cdd:cd17959   2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEK------LKAHSPTVGAral 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 306 ICAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEAD 385
Cdd:cd17959  76 ILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEAD 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18407327 386 RMFDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRV 434
Cdd:cd17959 156 RLFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
235-428 1.01e-59

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: 200.89  E-value: 1.01e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 235 FSSQIMSAIKKQAYEKPTAIQCQALPIVLS-GRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDEGPIGVICAPTREL 313
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 314 AHQIFLEAKKF-SKAYGLRVSAVYGGMSKHEQFKEL-KAGCEIVVATPGRLIDMLK--MKALTMMRASYLVLDEADRMFD 389
Cdd:cd17964  81 ALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 18407327 390 LGFEPQVRSIVGQIRP----DRQTLLFSATMPWKVEKLAREIL 428
Cdd:cd17964 161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTL 203
DEXDc smart00487
DEAD-like helicases superfamily;
243-449 4.62e-58

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 196.17  E-value: 4.62e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327    243 IKKQAYEKPTAIQCQALPIVLSG-RDVIGIAKTGSGKTAAFVLPMIVHimdqpeLQRDEGPIGVICAPTRELAHQIFLEA 321
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327    322 KKFSKAYGLRVSAVYGGMSKHEQFKELKAGC-EIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIV 400
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 18407327    401 GQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTVGEvgMANEDITQV 449
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
230-431 1.96e-57

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: 194.37  E-value: 1.96e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 230 FEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPelqrdEGPIGVICAP 309
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDP-----YGIFALVLTP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 310 TRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALT---MMRASYLVLDEADR 386
Cdd:cd17955  76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTtkvLSRVKFLVLDEADR 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 18407327 387 MFDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDP 431
Cdd:cd17955 156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
239-434 2.29e-57

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: 2.29e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRdeGPIGVICAPTRELAHQIF 318
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKA--ATRVLVLVPTRELAMQCF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 319 LEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLK-MKALTMMRASYLVLDEADRMFDLGFEPQVR 397
Cdd:cd17947  79 SVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRnSPSFDLDSIEILVLDEADRMLEEGFADELK 158
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18407327 398 SIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRV 434
Cdd:cd17947 159 EILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
248-435 1.29e-55

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: 189.72  E-value: 1.29e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 248 YEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIM-DQPELQRDEGPIGVICAPTRELAHQIFLEAKKF-S 325
Cdd:cd17949  11 IEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPRVDRSDGTLALVLVPTRELALQIYEVLEKLlK 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 326 KAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKM-KALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQIR 404
Cdd:cd17949  91 PFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKILELLD 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 18407327 405 -------------PDRQTLLFSATMPWKVEKLAREILSDPIRVT 435
Cdd:cd17949 171 dkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
239-435 6.30e-51

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: 176.61  E-value: 6.30e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPmIVHIMDQPELQRDEGPIG-VICAPTRELAHQI 317
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIP-VLEILLKRKANLKKGQVGaLIISPTRELATQI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 318 FLEAKKFSKAYGLRVSA--VYGGMSKHEQFKELKA-GCEIVVATPGRLIDMLKMKALTM-MRA-SYLVLDEADRMFDLGF 392
Cdd:cd17960  80 YEVLQSFLEHHLPKLKCqlLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVkVKSlEVLVLDEADRLLDLGF 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 18407327 393 EPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVT 435
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
239-416 1.18e-50

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: 177.05  E-value: 1.18e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALP-IVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQ----PELQRDEGPIGVICAPTREL 313
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQkssnGVGGKQKPLRALILTPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 314 AHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKM--KALTMMRA-SYLVLDEADRMFDL 390
Cdd:cd17946  81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEgnEHLANLKSlRFLVLDEADRMLEK 160
                       170       180       190
                ....*....|....*....|....*....|....
gi 18407327 391 G-FEpQVRSIVGQI-------RPDRQTLLFSATM 416
Cdd:cd17946 161 GhFA-ELEKILELLnkdragkKRKRQTFVFSATL 193
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
446-578 1.17e-49

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: 170.38  E-value: 1.17e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 446 ITQVVNVIPSDaEKLPWLLEKLPGMIDEGDVLVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHH 525
Cdd:cd18787   1 IKQLYVVVEEE-EKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18407327 526 VLIATDVAARGLDIKSLKTVVNYDIAKDMDMHVHRIGRTGRAGdRDGVAYTLV 578
Cdd:cd18787  80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAG-RKGTAITFV 131
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
239-435 5.01e-48

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: 168.11  E-value: 5.01e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQpelqrDEGPIGVICAPTRELAHQIF 318
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTE-----HRNPSALILTPTRELAVQIE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 319 LEAKKFSKAY-GLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVR 397
Cdd:cd17962  76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 18407327 398 SIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVT 435
Cdd:cd17962 156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
230-434 2.03e-47

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: 166.70  E-value: 2.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 230 FEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHI-MDQPELQrdegpiGVICA 308
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdPKKDVIQ------ALILV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 309 PTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMF 388
Cdd:cd17940  75 PTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 18407327 389 DLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRV 434
Cdd:cd17940 155 SQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
239-425 1.86e-46

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: 164.07  E-value: 1.86e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDeGPIGVICAPTRELAHQIF 318
Cdd:cd17942   1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRN-GTGVIIISPTRELALQIY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 319 LEAKKF----SKAYGLrvsaVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMR-ASYLVLDEADRMFDLGFE 393
Cdd:cd17942  80 GVAKELlkyhSQTFGI----VIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFE 155
                       170       180       190
                ....*....|....*....|....*....|..
gi 18407327 394 PQVRSIVGQIRPDRQTLLFSATMPWKVEKLAR 425
Cdd:cd17942 156 EEMRQIIKLLPKRRQTMLFSATQTRKVEDLAR 187
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
239-436 3.31e-46

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: 163.23  E-value: 3.31e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQpELQRDEGPIGVICAPTRELAHQIF 318
Cdd:cd17941   1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE-RWTPEDGLGALIISPTRELAMQIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 319 LEAKKFSKAYGLRVSAVYGGMS-KHEqfKELKAGCEIVVATPGRLI-----------DMLKMkaltmmrasyLVLDEADR 386
Cdd:cd17941  80 EVLRKVGKYHSFSAGLIIGGKDvKEE--KERINRMNILVCTPGRLLqhmdetpgfdtSNLQM----------LVLDEADR 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18407327 387 MFDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTV 436
Cdd:cd17941 148 ILDMGFKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
232-434 2.23e-45

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: 160.95  E-value: 2.23e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 232 DCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHI-MDQPELQrdegpiGVICAPT 310
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQ------ALVLAPT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 311 RELAHQI---FLEAKKFSKAyglRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRM 387
Cdd:cd17939  75 RELAQQIqkvVKALGDYMGV---KVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEM 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 18407327 388 FDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRV 434
Cdd:cd17939 152 LSRGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
237-436 1.59e-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: 156.20  E-value: 1.59e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 237 SQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDE-GPIGVICAPTRELAH 315
Cdd:cd17961   3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqGTRALILVPTRELAQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 316 QIFLEAKKFSKAYG--LRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRA-SYLVLDEADRMFDLGF 392
Cdd:cd17961  83 QVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTlKYLVIDEADLVLSYGY 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 18407327 393 EPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTV 436
Cdd:cd17961 163 EEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
230-434 1.75e-40

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: 147.59  E-value: 1.75e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 230 FEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHI-MDQPELQrdegpiGVICA 308
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIdTSLKATQ------ALVLA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 309 PTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMF 388
Cdd:cd18046  75 PTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEML 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 18407327 389 DLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRV 434
Cdd:cd18046 155 SRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
230-434 1.18e-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: 142.46  E-value: 1.18e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 230 FEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMdqpelqrdegpiGVICAP 309
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------ALILEP 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 310 TRELAHQI---FLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADR 386
Cdd:cd17938  69 SRELAEQTyncIENFKKYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADR 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18407327 387 MFDLGFEPQVRSIVGQI-----RPDR-QTLLFSATM-PWKVEKLAREILSDPIRV 434
Cdd:cd17938 149 LLSQGNLETINRIYNRIpkitsDGKRlQVIVCSATLhSFEVKKLADKIMHFPTWV 203
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
238-435 4.02e-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: 140.40  E-value: 4.02e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 238 QIMSAIKKQAYEKPTAIQCQALPIVLSG--RDVIGIAKTGSGKTAAFVLPMIVHImdQPELQRdegPIGVICAPTRELAH 315
Cdd:cd17963   4 ELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV--DPTLKS---PQALCLAPTRELAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 316 QIFLEAKKFSKAYGLRV-SAVYGGMSKHEqfKELKAgcEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDL-GFE 393
Cdd:cd17963  79 QIGEVVEKMGKFTGVKVaLAVPGNDVPRG--KKITA--QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHG 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 18407327 394 PQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVT 435
Cdd:cd17963 155 DQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
230-436 7.77e-38

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: 140.17  E-value: 7.77e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 230 FEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIvhimdqPELQRDEGPIGVIC-A 308
Cdd:cd17950   4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL------QQLEPVDGQVSVLViC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 309 PTRELAHQIFLEAKKFSKaY--GLRVSAVYGGMSKHEQFKELKAGC-EIVVATPGRLIDMLKMKALTMMRASYLVLDEAD 385
Cdd:cd17950  78 HTRELAFQISNEYERFSK-YmpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECD 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 18407327 386 RMF-DLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRVTV 436
Cdd:cd17950 157 KMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
239-434 3.25e-36

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: 135.08  E-value: 3.25e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMiVHIMDqPELQRdegPIGVICAPTRELAHQIF 318
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIA-LESLD-LERRH---PQVLILAPTREIAVQIH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 319 LEAKKFSKAY-GLRVSAVYGGMSKHEQFKELKaGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVR 397
Cdd:cd17943  76 DVFKKIGKKLeGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18407327 398 SIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRV 434
Cdd:cd17943 155 WIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
230-434 5.97e-35

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: 131.82  E-value: 5.97e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 230 FEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHImdqpELQRDEgPIGVICAP 309
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL----DIQVRE-TQALILSP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 310 TRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFD 389
Cdd:cd18045  76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 18407327 390 LGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDPIRV 434
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
254-426 2.48e-34

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: 129.97  E-value: 2.48e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 254 IQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIM-DQPELQRDEGPIGVICAPTRELAHQIFLEAKKFSKAygLRV 332
Cdd:cd17944  16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITRK--LSV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 333 SAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIVG-QIRPDR---- 407
Cdd:cd17944  94 ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvSYKKDSednp 173
                       170
                ....*....|....*....
gi 18407327 408 QTLLFSATMPWKVEKLARE 426
Cdd:cd17944 174 QTLLFSATCPDWVYNVAKK 192
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
239-434 5.71e-33

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: 127.10  E-value: 5.71e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQ--RDEGPIGVICAPTRELAHQ 316
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAegPFNAPRGLVITPSRELAEQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 317 IFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQV 396
Cdd:cd17948  81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 18407327 397 RSI-----VGQIRPDR--------QTLLFSATMPwkveKLAREILSDPIRV 434
Cdd:cd17948 161 SHFlrrfpLASRRSENtdgldpgtQLVLVSATMP----SGVGEVLSKVIDV 207
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
458-568 1.92e-29

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: 112.69  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327   458 EKLPWLLEKLPGmideGDVLVFASKKATVDEiEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGL 537
Cdd:pfam00271   4 EALLELLKKERG----GKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 18407327   538 DIKSLKTVVNYDIAKDMDMHVHRIGRTGRAG 568
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
239-425 3.25e-29

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: 116.19  E-value: 3.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALPIVLSG---------RDVIGIAKTGSGKTAAFVLPmIVHIMDQ---PELQrdegpiGVI 306
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLP-IVQALSKrvvPRLR------ALI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 307 CAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQFKELKAGCE--------IVVATPGRLIDMLKMK---ALTMMR 375
Cdd:cd17956  74 VVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTpgfTLKHLR 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 376 asYLVLDEADRMFDLGFE---PQV-RSIVGQIRPDR----------------QTLLFSATMPWKVEKLAR 425
Cdd:cd17956 154 --FLVIDEADRLLNQSFQdwlETVmKALGRPTAPDLgsfgdanllersvrplQKLLFSATLTRDPEKLSS 221
HELICc smart00490
helicase superfamily c-terminal domain;
487-568 9.78e-26

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 101.13  E-value: 9.78e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327    487 DEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNYDIAKDMDMHVHRIGRTGR 566
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 18407327    567 AG 568
Cdd:smart00490  81 AG 82
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
221-435 5.42e-24

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: 101.68  E-value: 5.42e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 221 FDVHRPVKtfedcgfsSQIMSAIKKQAYE-----KPTAIQCQALPIVL---------------SGRDVIGIA-KTGSGKT 279
Cdd:cd17965   4 LKLLPSVR--------EAIIKEILKGSNKtdeeiKPSPIQTLAIKKLLktlmrkvtkqtsneePKLEVFLLAaETGSGKT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 280 AAFVLPMIVHIMDQ-----------PELQRDEG-PIGVICAPTRELAHQIFLEAKKFSKAYGLRVSAVYGGMSKHEQ--F 345
Cdd:cd17965  76 LAYLAPLLDYLKRQeqepfeeaeeeYESAKDTGrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQrlQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 346 KELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAR 425
Cdd:cd17965 156 LAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLR 235
                       250
                ....*....|
gi 18407327 426 EILSDPIRVT 435
Cdd:cd17965 236 KLFPDVVRIA 245
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
227-431 2.76e-21

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: 93.16  E-value: 2.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 227 VKTFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSG--RDVIGIAKTGSGKTAAFVLPMIVHImDQPELQrdegPIG 304
Cdd:cd18048  17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV-DALKLY----PQC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 305 VICAPTRELAHQ---IFLEAKKFSKA----YGLRVSAVYGGMSKHEQfkelkagceIVVATPGRLID-MLKMKALTMMRA 376
Cdd:cd18048  92 LCLSPTFELALQtgkVVEEMGKFCVGiqviYAIRGNRPGKGTDIEAQ---------IVIGTPGTVLDwCFKLRLIDVTNI 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18407327 377 SYLVLDEADRMFDL-GFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDP 431
Cdd:cd18048 163 SVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
228-431 1.85e-20

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: 90.16  E-value: 1.85e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 228 KTFEDCGFSSQIMSAIKKQAYEKPTAIQCQALPIVLSG--RDVIGIAKTGSGKTAAFVLPMIVHImdQPELQRDEgpigV 305
Cdd:cd18047   1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYPQ----C 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 306 IC-APTRELAHQIFLEAKKFSKAYGlRVSAVYgGMSKHEQFKELKAGCEIVVATPGRLID-MLKMKALTMMRASYLVLDE 383
Cdd:cd18047  75 LClSPTYELALQTGKVIEQMGKFYP-ELKLAY-AVRGNKLERGQKISEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDE 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18407327 384 ADRMFDL-GFEPQVRSIVGQIRPDRQTLLFSATMPWKVEKLAREILSDP 431
Cdd:cd18047 153 ADVMIATqGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
265-587 1.68e-18

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 89.70  E-value: 1.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 265 GRDVIGIAKTGSGKT--AAFVlpmIVHIMDQPELqrdegpigVICAPTRELAHQIFLEAKKFskaygLRVSAVYGGmskh 342
Cdd:COG1061 100 GGRGLVVAPTGTGKTvlALAL---AAELLRGKRV--------LVLVPRRELLEQWAEELRRF-----LGDPLAGGG---- 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 343 eqfkELKAGCEIVVATPGRLIDMLKMKALTMmRASYLVLDEADRMFDLGFepqvRSIVGQIRPDRqTLLFSAT------- 415
Cdd:COG1061 160 ----KKDSDAPITVATYQSLARRAHLDELGD-RFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTATpfrsdgr 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 416 -------------MPWKvEKLAREILSDP----IRVTVGEVGMANEDITQVVN--VIPSDAEKLPWLLEKLPGMIDEGDV 476
Cdd:COG1061 230 eillflfdgivyeYSLK-EAIEDGYLAPPeyygIRVDLTDERAEYDALSERLReaLAADAERKDKILRELLREHPDDRKT 308
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 477 LVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNYDIAKDMDM 556
Cdd:COG1061 309 LVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPRE 388
                       330       340       350
                ....*....|....*....|....*....|...
gi 18407327 557 HVHRIGRT--GRAGDRDGVAYTLVTQREARFAG 587
Cdd:COG1061 389 FIQRLGRGlrPAPGKEDALVYDFVGNDVPVLEE 421
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
239-575 1.87e-15

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 79.94  E-value: 1.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 239 IMSAIKKQAYEKPTAIQCQALP-IVLSGRDVIGIAKTGSGKTAAFVLPMIVHImdqpelqrDEGPIGVICAPTRELAHQI 317
Cdd:COG1204  11 VIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKAL--------LNGGKALYIVPLRALASEK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 318 FLEAKKFSKAYGLRVSAVYGGMSKHEqfkELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEA------DRmfdlG 391
Cdd:COG1204  83 YREFKRDFEELGIKVGVSTGDYDSDD---EWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR----G 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 392 fePQVRSIVGQIR---PDRQTLLFSATMPwKVEKLAR----EILSDPIRVTVGEVGMANEDITQVVNVIPSDAEKLPWLL 464
Cdd:COG1204 156 --PTLEVLLARLRrlnPEAQIVALSATIG-NAEEIAEwldaELVKSDWRPVPLNEGVLYDGVLRFDDGSRRSKDPTLALA 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 465 EKLpgMIDEGDVLVFASKK-----------------------ATVDEIEAQL------TLNSFKVAAL--------HGD- 506
Cdd:COG1204 233 LDL--LEEGGQVLVFVSSRrdaeslakkladelkrrltpeerEELEELAEELlevseeTHTNEKLADClekgvafhHAGl 310
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18407327 507 -KDQASRMETLqkFKSGVHHVLIATDVAARGLDIKSlKTVVNYDI----AKDMD-MHVHR-IGRTGRAG-DRDGVAY 575
Cdd:COG1204 311 pSELRRLVEDA--FREGLIKVLVATPTLAAGVNLPA-RRVIIRDTkrggMVPIPvLEFKQmAGRAGRPGyDPYGEAI 384
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
458-579 7.14e-14

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 75.54  E-value: 7.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 458 EKLPWLLEKLPGMIDEGDVLVFASKKATVDEIEAQLTLNSFKV------AALHGDK--DQASRMETLQKFKSGVHHVLIA 529
Cdd:COG1111 338 SKLREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDKglTQKEQIEILERFRAGEFNVLVA 417
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18407327 530 TDVAARGLDIKSLKTVVNYD-IAKDMDMhVHRIGRTGRAgdRDGVAYTLVT 579
Cdd:COG1111 418 TSVAEEGLDIPEVDLVIFYEpVPSEIRS-IQRKGRTGRK--REGRVVVLIA 465
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
265-415 1.78e-13

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 68.20  E-value: 1.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 265 GRDVIGIAKTGSGKTAAfVLPMIVHIMDQPELQRdegpigVICAPTRELAHQIFLEAKKFSKaYGLRVSAVYGGMSKHEQ 344
Cdd:cd00046   1 GENVLITAPTGSGKTLA-ALLAALLLLLKKGKKV------LVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEER 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18407327 345 FKELKAGCEIVVATPGRLIDMLK-MKALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQ--IRPDRQTLLFSAT 415
Cdd:cd00046  73 EKNKLGDADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
459-562 9.14e-13

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: 65.96  E-value: 9.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 459 KLPWLLEKLPGMIDEGD-VLVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFK--SGVHHVLIATDVAAR 535
Cdd:cd18793  12 KLEALLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGV 91
                        90       100       110
                ....*....|....*....|....*....|....
gi 18407327 536 GLDIKSLKTVVNYDI----AKD---MDmHVHRIG 562
Cdd:cd18793  92 GLNLTAANRVILYDPwwnpAVEeqaID-RAHRIG 124
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
477-567 1.74e-12

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: 65.31  E-value: 1.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 477 LVFASKKATVDEI-----EAQLTLNSFKVAAL----HGDKDQASRM------ETLQKFKSGVHHVLIATDVAARGLDIKS 541
Cdd:cd18802  29 IIFVERRATAVVLsrllkEHPSTLAFIRCGFLigrgNSSQRKRSLMtqrkqkETLDKFRDGELNLLIATSVLEEGIDVPA 108
                        90       100
                ....*....|....*....|....*.
gi 18407327 542 LKTVVNYDIAKDMDMHVHRIGRtGRA 567
Cdd:cd18802 109 CNLVIRFDLPKTLRSYIQSRGR-ARA 133
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
397-580 1.62e-10

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 64.48  E-value: 1.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 397 RSIVGQIRPDRQTLLFSATMpwkvekLAREILSDPirvtvgevGMANEDITQvvnvIPSDAEKLPWLLEKLPGMIDEGD- 475
Cdd:COG0553 490 RELEGAEGIRRRGLILAALT------RLRQICSHP--------ALLLEEGAE----LSGRSAKLEALLELLEELLAEGEk 551
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 476 VLVFASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSG--VHHVLIATDVAARGLDIKSLKTVVNYDI--- 550
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGEGLNLTAADHVIHYDLwwn 631
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 18407327 551 ------AKDmdmHVHRIGRTgragdRDGVAYTLVTQ 580
Cdd:COG0553 632 paveeqAID---RAHRIGQT-----RDVQVYKLVAE 659
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
459-577 4.90e-10

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: 58.52  E-value: 4.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 459 KLPWLLE------KLPGMIDEGDVLVFASKKATVDEIEAQLTLNSFKVAAL----HGDKDQASRM------ETLQKFKSG 522
Cdd:cd18801  10 KLEKLEEivkehfKKKQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGKSSKGMsqkeqkEVIEQFRKG 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18407327 523 VHHVLIATDVAARGLDIKSLKTVVNYDIAKDMDMHVHRIGRTGRAgdRDGVAYTL 577
Cdd:cd18801  90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRK--RQGRVVVL 142
PRK13766 PRK13766
Hef nuclease; Provisional
422-580 1.89e-09

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 61.04  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  422 KLAREILSDPirvtvgevgmaneDITQVVNVIPS-DAE--KLPWLLEKLPGMIDEGD---VLVFASKKATVDEIEAQLTL 495
Cdd:PRK13766 321 KASKRLVEDP-------------RFRKAVRKAKElDIEhpKLEKLREIVKEQLGKNPdsrIIVFTQYRDTAEKIVDLLEK 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  496 NSFKVAALHGdkdQASR-----------METLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNYD-IAKDMDMhVHRIGR 563
Cdd:PRK13766 388 EGIKAVRFVG---QASKdgdkgmsqkeqIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGR 463
                        170
                 ....*....|....*..
gi 18407327  564 TGRagDRDGVAYTLVTQ 580
Cdd:PRK13766 464 TGR--QEEGRVVVLIAK 478
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
254-384 6.63e-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: 56.12  E-value: 6.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 254 IQCQAL-PIVLSGRDVIGIAKTGSGKTAAFVLPMIVHImdqpelqRDEGPIGVICAPTRELAHQIFLEAKKFSKAYGLRV 332
Cdd:cd17921   5 IQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRAL-------ATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNV 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18407327 333 SAVYGGMSKheqFKELKAGCEIVVATPGRLIDML-KMKALTMMRASYLVLDEA 384
Cdd:cd17921  78 GLLTGDPSV---NKLLLAEADILVATPEKLDLLLrNGGERLIQDVRLVVVDEA 127
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
234-384 9.37e-09

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: 59.08  E-value: 9.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 234 GFSSQIMSAIKKQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMdqpelqRDEGPIGVICAPTREL 313
Cdd:COG1205  40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL------EDPGATALYLYPTKAL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 314 AH-QifLEA-KKFSKAYGLRVS-AVY-GGMSKHEQfKELKAGCEIVVATPgrliDMLKMkalTMM-----------RASY 378
Cdd:COG1205 114 ARdQ--LRRlRELAEALGLGVRvATYdGDTPPEER-RWIREHPDIVLTNP----DMLHY---GLLphhtrwarffrNLRY 183

                ....*.
gi 18407327 379 LVLDEA 384
Cdd:COG1205 184 VVIDEA 189
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
526-578 1.06e-08

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: 52.71  E-value: 1.06e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 18407327 526 VLIATDVAARGLDIKSLKTVVNYDIAKDMDMHVHRIGRTGRAGDRDGVAYTLV 578
Cdd:cd18785  25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
255-384 1.84e-07

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: 51.82  E-value: 1.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 255 QCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMdqpelqRDEGPIGVICAPTRELAHQIFLEAKKFSKAYGLRVS- 333
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL------RDPGSRALYLYPTKALAQDQLRSLRELLEQLGLGIRv 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18407327 334 AVYGGMSKHEQ-FKELKAGCEIVVATPgrliDMLKmkaLTMMRAS-----------YLVLDEA 384
Cdd:cd17923  79 ATYDGDTPREErRAIIRNPPRILLTNP----DMLH---YALLPHHdrwarflrnlrYVVLDEA 134
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
262-417 3.58e-07

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: 50.80  E-value: 3.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 262 VLSGRDVIGIAKTGSGKTAAFVLPMIVHIMdqpelqrdEGPIGVICAPTRELAHQIFLEAKKFSKaYGLRVSAVYGgmsK 341
Cdd:cd18028  14 LLKGENLLISIPTASGKTLIAEMAMVNTLL--------EGGKALYLVPLRALASEKYEEFKKLEE-IGLKVGISTG---D 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18407327 342 HEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLGFEPQVRSIVGQIR---PDRQTLLFSATMP 417
Cdd:cd18028  82 YDEDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnPNTQIIGLSATIG 160
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
265-383 7.38e-07

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: 49.89  E-value: 7.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 265 GRDVIGIAKTGSGKTAAFVLPMIVHIMDQPelqrdEGPIGVI-CAPTRELAHQIF--LEAKKFSKAYGLRVSAVYGGMSK 341
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADEP-----EKGVQVLyISPLKALINDQErrLEEPLDEIDLEIPVAVRHGDTSQ 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18407327 342 HEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRAS--YLVLDE 383
Cdd:cd17922  76 SEKAKQLKNPPGILITTPESLELLLVNKKLRELFAGlrYVVVDE 119
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
266-384 1.75e-06

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: 49.19  E-value: 1.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 266 RDVIGIAKTGSGKTaaFVLPMIvhIMDQPELQRDEGPIGVIC---APTRELAHQiflEAKKFSKAYGLRVSAVYGGMSK- 341
Cdd:cd18034  17 RNTIVVLPTGSGKT--LIAVML--IKEMGELNRKEKNPKKRAvflVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEMGVd 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 18407327 342 ---HEQFKELKAGCEIVVATPGRLIDMLKMKALTMMRASYLVLDEA 384
Cdd:cd18034  90 kwtKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
255-568 4.05e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 50.10  E-value: 4.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  255 QCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHimdqpelqrdEGpIGVICAPTREL----AHQIfleakkfsKAYGL 330
Cdd:PRK11057  30 QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL----------DG-LTLVVSPLISLmkdqVDQL--------LANGV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  331 RVSAVYGGMSKHEQFkELKAGC-----EIVVATPGRLIDMLKMKALTMMRASYLVLDEADRMFDLG--FEPQVRSIvGQI 403
Cdd:PRK11057  91 AAACLNSTQTREQQL-EVMAGCrtgqiKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGhdFRPEYAAL-GQL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  404 RPDRQTLLFSATMPWKVEKLAREI-----LSDPIrVTVGEVGMANEDITQVVNVIPSDaeKLPWLLEKLPGMIDegdvLV 478
Cdd:PRK11057 169 RQRFPTLPFMALTATADDTTRQDIvrllgLNDPL-IQISSFDRPNIRYTLVEKFKPLD--QLMRYVQEQRGKSG----II 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327  479 FASKKATVDEIEAQLTLNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNYDIAKDMDMHV 558
Cdd:PRK11057 242 YCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYY 321
                        330
                 ....*....|
gi 18407327  559 HRIGRTGRAG 568
Cdd:PRK11057 322 QETGRAGRDG 331
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
252-359 4.94e-06

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 48.12  E-value: 4.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 252 TAIQCQALPIVL-SGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPELQRDEgPIGVICAPTRELAHQIFLEAK-KFSKaYG 329
Cdd:cd18023   3 NRIQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDWKeKFGP-LG 80
                        90       100       110
                ....*....|....*....|....*....|
gi 18407327 330 LRVSAVYGGmSKHEQFKELKaGCEIVVATP 359
Cdd:cd18023  81 LSCAELTGD-TEMDDTFEIQ-DADIILTTP 108
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
245-306 2.60e-05

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 47.79  E-value: 2.60e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18407327 245 KQAYEKPTAIQCQALPIVLSGRDVIGIAKTGSGKT-AAFvLPMIVHIMDQPELQRDEGPIGVI 306
Cdd:COG1201  19 AARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGLRVL 80
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
244-539 1.16e-04

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 45.46  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 244 KKQAYEKPTAIQCQALPIVLSGRDVIG-----IAKTGSGKT-AAFVLpmIVHIMDQPELQRdegpiGVICAPTRELAHQI 317
Cdd:COG1203 121 KSKPRTPINPLQNEALELALEAAEEEPglfilTAPTGGGKTeAALLF--ALRLAAKHGGRR-----IIYALPFTSIINQT 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 318 FLEAKKF---------SKAYGLRVSAVYGGMSKHEQFKELKAG--CEIVVATPGRLIDML-------KMKALTMMRaSYL 379
Cdd:COG1203 194 YDRLRDLfgedvllhhSLADLDLLEEEEEYESEARWLKLLKELwdAPVVVTTIDQLFESLfsnrkgqERRLHNLAN-SVI 272
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 380 VLDEADrMFDLGFEPQVRSIVGQIR-PDRQTLLFSATMP-WKVEKL--AREILSDPIRVTVGEVGMANEDITQVVNVIPS 455
Cdd:COG1203 273 ILDEVQ-AYPPYMLALLLRLLEWLKnLGGSVILMTATLPpLLREELleAYELIPDEPEELPEYFRAFVRKRVELKEGPLS 351
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 456 DAEKLPWLLEKLPgmiDEGDVLV-FASKK---ATVDEIEAQltLNSFKVAALHGDKDQASRMETLQK----FKSGVHHVL 527
Cdd:COG1203 352 DEELAELILEALH---KGKSVLViVNTVKdaqELYEALKEK--LPDEEVYLLHSRFCPADRSEIEKEikerLERGKPCIL 426
                       330
                ....*....|..
gi 18407327 528 IATDVAARGLDI 539
Cdd:COG1203 427 VSTQVVEAGVDI 438
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
452-566 1.67e-04

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: 42.64  E-value: 1.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 452 VIPSDAEKLPWLLEKLPGMIDE--------GDVLVFASKKATVDEIEAQL------TLNSFKVAALHGDKDQASRMETLQ 517
Cdd:cd18796   9 ILPVAPEIFPWAGESGADAYAEvifllerhKSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEA 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 18407327 518 KFKSGVHHVLIATDVAARGLDIKSLKTVVNYDIAKDMDMHVHRIGRTGR 566
Cdd:cd18796  89 ALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
454-578 5.33e-04

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: 41.08  E-value: 5.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 454 PSDAEKLPWLLEKLpgmiDEGD-VLVFASKKATVDEIeAQLtlnsFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDV 532
Cdd:cd18789  33 PNKLRALEELLKRH----EQGDkIIVFTDNVEALYRY-AKR----LLKPFITGETPQSEREEILQNFREGEYNTLVVSKV 103
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18407327 533 AARGLDIKSLktvvnyDIAKDMDMH-------VHRIGRTGRAGDRDG---VAYTLV 578
Cdd:cd18789 104 GDEGIDLPEA------NVAIQISGHggsrrqeAQRLGRILRPKKGGGknaFFYSLV 153
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
258-367 5.38e-04

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: 42.08  E-value: 5.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 258 ALPiVLSGRDVIGIAKTGSGKTAAFVLPMIVHImdqpELQRDEGPIG--VICAPTRELAHQiflEAKKFSKAY--GLRVS 333
Cdd:cd18036  11 VLP-ALRGKNTIICAPTGSGKTRVAVYICRHHL----EKRRSAGEKGrvVVLVNKVPLVEQ---QLEKFFKYFrkGYKVT 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 18407327 334 AVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLK 367
Cdd:cd18036  83 GLSGDSSHKVSFGQIVKASDVIICTPQILINNLL 116
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
250-386 5.96e-04

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: 41.65  E-value: 5.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 250 KPTAIQCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIVHIMDQPelQRDEGPIgVICAPTRELAHQIFLEAKKFSKAYG 329
Cdd:cd17927   2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFP--AGRKGKV-VFLANKVPLVEQQKEVFRKHFERPG 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18407327 330 LRVSAVYGGMSKHEQFKELKAGCEIVVATPGRLIDMLKMKALT-MMRASYLVLDEADR 386
Cdd:cd17927  79 YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVsLSDFSLLVFDECHN 136
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
471-578 7.76e-04

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 40.71  E-value: 7.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 471 IDEGDVLVFASkkatVDEIEAQLT--LNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVVNY 548
Cdd:cd18792  36 IEESEKLDLKS----IEALAEELKelVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIE 111
                        90       100       110
                ....*....|....*....|....*....|...
gi 18407327 549 DiAKDM---DMHVHRiGRTGRaGDRDGVAYTLV 578
Cdd:cd18792 112 D-ADRFglsQLHQLR-GRVGR-GKHQSYCYLLY 141
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
477-546 1.81e-03

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 38.69  E-value: 1.81e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18407327 477 LVFASKKATVDEIEAQLTLNSFKVAALHGD-KDQASRMETLQKFKSG--VHHVLIATDVAARGLDIKSLKTVV 546
Cdd:cd18799  10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDySDRERGDEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
484-583 6.55e-03

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 38.09  E-value: 6.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 484 ATVDEIEAQLT--LNSFKVAALHGDKDQASRMETLQKFKSGVHHVLIATDVAARGLDIKSLKTVV--NYDIAKDMDMHVH 559
Cdd:cd18810  36 ESIEKLATQLRqlVPEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQL 115
                        90       100
                ....*....|....*....|....
gi 18407327 560 RiGRTGRAGDRdGVAYTLVTQREA 583
Cdd:cd18810 116 R-GRVGRSKER-AYAYFLYPDQKK 137
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
255-431 6.71e-03

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


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 38.78  E-value: 6.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 255 QCQALPIVLSGRDVIGIAKTGSGKTAAFVLPMIvhimdqpeLQRDEGP-IGVICAPTRELAHQIFLEAKKFSKAYglrvs 333
Cdd:cd18018  17 QEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL--------LLRRRGPgLTLVVSPLIALMKDQVDALPRAIKAA----- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407327 334 AVYGGMSKHEQFKE---LKAG-CEIVVATPGRLID-MLKMKALTMMRASYLVLDEADRMFDLG--FEP---QVRSIVGQI 403
Cdd:cd18018  84 ALNSSLTREERRRIlekLRAGeVKILYVSPERLVNeSFRELLRQTPPISLLVVDEAHCISEWShnFRPdylRLCRVLREL 163
                       170       180
                ....*....|....*....|....*...
gi 18407327 404 RPDRQTLLFSATMPWKVEKLAREILSDP 431
Cdd:cd18018 164 LGAPPVLALTATATKRVVEDIASHLGIP 191
 
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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