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Conserved domains on  [gi|1782284395|ref|XP_031642960|]
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probable ATP-dependent RNA helicase ddx6 [Oncorhynchus kisutch]

Protein Classification

DDX6/DHH1 family DEAD/DEAH box RNA helicase( domain architecture ID 13028552)

DDX6/DHH1 family DEAD/DEAH box containing ATP-dependent RNA helicase catalyzes the unwinding of RNA; such as ATP-dependent RNA helicase DHH1 that is involved in mRNA turnover, and more specifically in mRNA decapping

CATH:  3.40.50.300
EC:  3.6.4.13
Gene Ontology:  GO:0016887|GO:0003723|GO:0003724|GO:0005524
PubMed:  20206133|21779027|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 90-291 6.18e-135

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: 387.42  E-value: 6.18e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELA 169
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSQISIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFV 249
Cdd:cd17940    81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1782284395 250 VLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEIN 291
Cdd:cd17940   160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 301-430 1.23e-55

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: 181.55  E-value: 1.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 301 ITQYYAYVTERQKVHCLN-TLFSRLQINQSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRN 379
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1782284395 380 LVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGRFGHLGLAINLI 430
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 90-291 6.18e-135

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: 387.42  E-value: 6.18e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELA 169
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSQISIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFV 249
Cdd:cd17940    81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1782284395 250 VLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEIN 291
Cdd:cd17940   160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
90-481 7.91e-133

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 390.66  E-value: 7.91e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDL-KKDHIQAMVMVPTREL 168
Cdd:COG0513     4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPTREL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 169 ALQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDF 248
Cdd:COG0513    84 ALQVAEELRKLAKYLG-LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 249 VVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEINLM-DELTLKGITQYYAYVTERQKVHCLNTLFSRLQIN 327
Cdd:COG0513   163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVApENATAETIEQRYYLVDKRDKLELLRRLLRDEDPE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 328 QSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNA 407
Cdd:COG0513   243 RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDP 322

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1782284395 408 ETYLHRIGRSGRFGHLGLAINLITSEDRFNLKSIEDQLVTDIKPIPGSIDKGLYVAEFHSAEPDTEDEIRGKDG 481
Cdd:COG0513   323 EDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKA 396
PTZ00424 PTZ00424
helicase 45; Provisional
 90-465 4.48e-102

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 311.38  E-value: 4.48e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELA 169
Cdd:PTZ00424   30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFV 249
Cdd:PTZ00424  110 QQIQKVVLALGDYLK-VRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 250 VLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEINL-MDELTLKGITQYYAYV-TERQKVHCLNTLFSRLQIN 327
Cdd:PTZ00424  189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVkKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTIT 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 328 QSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNA 407
Cdd:PTZ00424  269 QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP 348

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1782284395 408 ETYLHRIGRSGRFGHLGLAINLITSEDRFNLKSIEDQLVTDIKPIPgsidkgLYVAEF 465
Cdd:PTZ00424  349 ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMP------MEVADY 400
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 301-430 1.23e-55

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: 181.55  E-value: 1.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 301 ITQYYAYVTERQKVHCLN-TLFSRLQINQSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRN 379
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1782284395 380 LVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGRFGHLGLAINLI 430
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 112-279 1.88e-52

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: 174.74  E-value: 1.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 112 SPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELALQVSQISIQVSKHMgGVKVMAT 191
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 192 TGGTNLRDDIMRLdETVHVVIATPGRILDLIKKGVaKVDKVQMMVMDEADKLLSQDFVVLIEDIISFLAKGRQILLYSAT 271
Cdd:pfam00270  80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157


                  ....*...
gi 1782284395 272 FPISVQKF 279
Cdd:pfam00270 158 LPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
103-304 3.40e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 156.88  E-value: 3.40e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  103 IFEMGWEKPSPVQEESIPIALSG-RDILARAKNGTGKSGAYLIPLLERIdLKKDHIQAMVMVPTRELALQVSQisiQVSK 181
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAE---ELKK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  182 HMG--GVKVMATTGGTNLRDDIMRL-DETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIEDIISF 258
Cdd:smart00487  77 LGPslGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1782284395  259 LAKGRQILLYSATFPISVQKFMAKHLSKPYEINLmDELTLKGITQY 304
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV-GFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 312-421 7.95e-33

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: 120.39  E-value: 7.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 312 QKVHCLNTLFSRLQINQSIIFCNSTQRVEllAKKITQL-GYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGI 390
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1782284395 391 DIQAVNVVINFDFPKNAETYLHRIGRSGRFG 421
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
340-421 3.19e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 104.22  E-value: 3.19e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  340 ELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGR 419
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 1782284395  420 FG 421
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
330-485 7.52e-07

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 51.65  E-value: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 330 IIFCNSTQRVELLAKKITQLGYSC--FYIHAK------MMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINF 401
Cdd:COG1111   357 IVFTQYRDTAEMIVEFLSEPGIKAgrFVGQASkegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFY 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 402 DFPKNAETYLHRIGRSGRFGHlGLAINLITS--------------EDRFNL------KSIEDQLVTDIKP-IPGSIDkgl 460
Cdd:COG1111   437 EPVPSEIRSIQRKGRTGRKRE-GRVVVLIAKgtrdeayywssrrkEKKMKSilkklkKLLDKQEKEKLKEsAQATLD--- 512

                         170       180
                  ....*....|....*....|....*
gi 1782284395 461 yvaEFHSAEPDTEDEIRGKDGELSA 485
Cdd:COG1111   513 ---EFESIKELAEDEINEKDLDEIE 534
mfd TIGR00580
transcription-repair coupling factor (mfd); All proteins in this family for which functions ...
 355-442 1.33e-04

transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273152 [Multi-domain]  Cd Length: 926  Bit Score: 44.66  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 355 YIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFdfpkNAETY----LHRI-GRSGRFGHLGLAINL 429
Cdd:TIGR00580 691 IAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIE----RADKFglaqLYQLrGRVGRSKKKAYAYLL 766

                          90
                  ....*....|...
gi 1782284395 430 ITSEDRFNLKSIE 442
Cdd:TIGR00580 767 YPHQKALTEDAQK 779
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 330-421 1.06e-03

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 41.81  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  330 IIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCrNLVC-TDLFTRGIDIQAVNVVINFDFPKNAE 408
Cdd:PLN03137   684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEI-NIICaTVAFGMGINKPDVRFVIHHSLPKSIE 762

                           90
                   ....*....|...
gi 1782284395  409 TYLHRIGRSGRFG 421
Cdd:PLN03137   763 GYHQECGRAGRDG 775
 
Name Accession Description Interval E-value
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 90-291 6.18e-135

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: 387.42  E-value: 6.18e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELA 169
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSQISIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFV 249
Cdd:cd17940    81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1782284395 250 VLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEIN 291
Cdd:cd17940   160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
90-481 7.91e-133

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 390.66  E-value: 7.91e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDL-KKDHIQAMVMVPTREL 168
Cdd:COG0513     4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPTREL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 169 ALQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDF 248
Cdd:COG0513    84 ALQVAEELRKLAKYLG-LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 249 VVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEINLM-DELTLKGITQYYAYVTERQKVHCLNTLFSRLQIN 327
Cdd:COG0513   163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVApENATAETIEQRYYLVDKRDKLELLRRLLRDEDPE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 328 QSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNA 407
Cdd:COG0513   243 RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDP 322

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1782284395 408 ETYLHRIGRSGRFGHLGLAINLITSEDRFNLKSIEDQLVTDIKPIPGSIDKGLYVAEFHSAEPDTEDEIRGKDG 481
Cdd:COG0513   323 EDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKA 396
PTZ00424 PTZ00424
helicase 45; Provisional
 90-465 4.48e-102

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 311.38  E-value: 4.48e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELA 169
Cdd:PTZ00424   30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFV 249
Cdd:PTZ00424  110 QQIQKVVLALGDYLK-VRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 250 VLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEINL-MDELTLKGITQYYAYV-TERQKVHCLNTLFSRLQIN 327
Cdd:PTZ00424  189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVkKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTIT 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 328 QSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNA 407
Cdd:PTZ00424  269 QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP 348

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1782284395 408 ETYLHRIGRSGRFGHLGLAINLITSEDRFNLKSIEDQLVTDIKPIPgsidkgLYVAEF 465
Cdd:PTZ00424  349 ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMP------MEVADY 400
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 95-453 4.16e-93

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 290.16  E-value: 4.16e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  95 LKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELALQVSQ 174
Cdd:PRK11776   11 LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 175 ISIQVSKHMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIED 254
Cdd:PRK11776   91 EIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 255 IISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEINLMDELTLKGITQYYAYVTERQKVHCLNTLFSRLQINQSIIFCN 334
Cdd:PRK11776  171 IIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDERLPALQRLLLHHQPESCVVFCN 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 335 STQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRI 414
Cdd:PRK11776  251 TKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRI 330

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1782284395 415 GRSGRFGHLGLAINLITSEDRFNLKSIEDQLVTDIKPIP 453
Cdd:PRK11776  331 GRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEP 369
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 99-290 4.70e-76

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: 236.95  E-value: 4.70e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERID----LKKDHIQAMVMVPTRELALQVSQ 174
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLpepkKKGRGPQALVLAPTRELAMQIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 175 ISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIED 254
Cdd:cd00268    81 VARKLGKGTG-LKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1782284395 255 IISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEI 290
Cdd:cd00268   160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 90-451 1.60e-73

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 238.69  E-value: 1.60e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLER-IDL-KKDHIQAMVMV--PT 165
Cdd:PRK11192    3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHlLDFpRRKSGPPRILIltPT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 166 RELALQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLS 245
Cdd:PRK11192   83 RELAMQVADQARELAKHTH-LDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 246 QDFVVLIEDIiSFLAKGR-QILLYSATFPIS-VQKFMAKHLSKPYEINLMDELTLKG-ITQ-YYAYVTERQKVHCLNTLF 321
Cdd:PRK11192  162 MGFAQDIETI-AAETRWRkQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKkIHQwYYRADDLEHKTALLCHLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 322 SRLQINQSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINF 401
Cdd:PRK11192  241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1782284395 402 DFPKNAETYLHRIGRSGRFGHLGLAINLITSEDRFNLKSIEDQLVTDIKP 451
Cdd:PRK11192  321 DMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKA 370
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 90-442 2.17e-71

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 238.21  E-value: 2.17e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELA 169
Cdd:PRK11634    8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSQISIQVSKHMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFV 249
Cdd:PRK11634   88 VQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 250 VLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEINLMDELTLK-GITQYYAYVTERQKVHCLNTLFSRLQINQ 328
Cdd:PRK11634  168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRpDISQSYWTVWGMRKNEALVRFLEAEDFDA 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 329 SIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNAE 408
Cdd:PRK11634  248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1782284395 409 TYLHRIGRSGRFGHLGLAINLITSEDRFNLKSIE 442
Cdd:PRK11634  328 SYVHRIGRTGRAGRAGRALLFVENRERRLLRNIE 361
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 90-454 1.44e-68

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 226.23  E-value: 1.44e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDH------IQAMVMV 163
Cdd:PRK10590    3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALILT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 164 PTRELALQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKL 243
Cdd:PRK10590   83 PTRELAAQIGENVRDYSKYLN-IRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 244 LSQDFvvlIEDIISFLAK---GRQILLYSATFPISVQKFMAKHLSKPYEINLMDELTL-KGITQYYAYVTERQKVHCLNT 319
Cdd:PRK10590  162 LDMGF---IHDIRRVLAKlpaKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTAsEQVTQHVHFVDKKRKRELLSQ 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 320 LFSRLQINQSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI 399
Cdd:PRK10590  239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1782284395 400 NFDFPKNAETYLHRIGRSGRFGHLGLAINLITSEDRFNLKSIEDQLVTDIK--PIPG 454
Cdd:PRK10590  319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPriAIPG 375
PTZ00110 PTZ00110
helicase; Provisional
 82-438 9.61e-68

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 226.58  E-value: 9.61e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  82 VTSTKGNEFEDYCLKrellmGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERID----LKK-DH 156
Cdd:PTZ00110  129 VVSFEYTSFPDYILK-----SLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINaqplLRYgDG 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 157 IQAMVMVPTRELALQVSQISIQVSKhMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMV 236
Cdd:PTZ00110  204 PIVLVLAPTRELAEQIREQCNKFGA-SSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLV 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 237 MDEADKLLSQDFVVLIEDIISFLAKGRQILLYSATFPISVQKfMAKHLSK--PYEINL--MDELTLKGITQYYAYVTERQ 312
Cdd:PTZ00110  283 LDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQS-LARDLCKeePVHVNVgsLDLTACHNIKQEVFVVEEHE 361

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 313 KVHCLNTLFSRLQINQS--IIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGI 390
Cdd:PTZ00110  362 KRGKLKMLLQRIMRDGDkiLIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGL 441

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1782284395 391 DIQAVNVVINFDFPKNAETYLHRIGRSGRFGHLGLAINLITSeDRFNL 438
Cdd:PTZ00110  442 DVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP-DKYRL 488
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 90-450 3.07e-60

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 204.76  E-value: 3.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLEriDLKKDHIQ---------AM 160
Cdd:PRK01297   89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIIN--QLLQTPPPkerymgeprAL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 161 VMVPTRELALQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDET-VHVVIATPGRILDLIKKGVAKVDKVQMMVMDE 239
Cdd:PRK01297  167 IIAPTRELVVQIAKDAAALTKYTG-LNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 240 ADKLLSQDFVVLIEDIISFLA-KG-RQILLYSATFPISVQKFMAKHLSKPYEINLMDE-LTLKGITQYYAYVTERQKVHC 316
Cdd:PRK01297  246 ADRMLDMGFIPQVRQIIRQTPrKEeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPEnVASDTVEQHVYAVAGSDKYKL 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 317 LNTLFSRLQINQSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVN 396
Cdd:PRK01297  326 LYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGIS 405

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1782284395 397 VVINFDFPKNAETYLHRIGRSGRFGHLGLAINLITSEDRFNLKSIEDQLVTDIK 450
Cdd:PRK01297  406 HVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS 459
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 92-290 8.63e-57

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: 187.15  E-value: 8.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  92 DYCLKRELLMGIFEMGWEKPSPVQEESI-PIaLSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELAL 170
Cdd:cd17939     1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIvPI-IKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 171 QVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVV 250
Cdd:cd17939    80 QIQKVVKALGDYMG-VKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKD 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1782284395 251 LIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEI 290
Cdd:cd17939   159 QIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 90-280 2.02e-56

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: 186.50  E-value: 2.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELA 169
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSQISIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFV 249
Cdd:cd18046    81 QQIQKVVMALGDYM-GIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1782284395 250 VLIEDIISFLAKGRQILLYSATFPISV----QKFM 280
Cdd:cd18046   160 DQIYDIFQKLPPDTQVVLLSATMPNDVlevtTKFM 194
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 99-287 3.70e-56

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: 185.16  E-value: 3.70e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELALQVSQISIQ 178
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 179 VSKHMGGVKVMATTGGTNLRDDIMRLDETvHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIEDIISF 258
Cdd:cd17943    81 IGKKLEGLKCEVFIGGTPVKEDKKKLKGC-HIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159

                         170       180
                  ....*....|....*....|....*....
gi 1782284395 259 LAKGRQILLYSATFPISVQKFMAKHLSKP 287
Cdd:cd17943   160 LPKNKQVIAFSATYPKNLDNLLARYMRKP 188
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 301-430 1.23e-55

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: 181.55  E-value: 1.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 301 ITQYYAYVTERQKVHCLN-TLFSRLQINQSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRN 379
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1782284395 380 LVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGRFGHLGLAINLI 430
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 90-443 2.33e-54

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 187.87  E-value: 2.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI-------DLKKDHIQAMVM 162
Cdd:PRK04837   10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpapeDRKVNQPRALIM 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 163 VPTRELALQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADK 242
Cdd:PRK04837   90 APTRELAVQIHADAEPLAQATG-LKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 243 LLSQDFvvlIEDIiSFL------AKGRQILLYSATFPISVQKFMAKHLSKPYEINLM-DELTLKGITQYYAYVTERQKVH 315
Cdd:PRK04837  169 MFDLGF---IKDI-RWLfrrmppANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEpEQKTGHRIKEELFYPSNEEKMR 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 316 CLNTLFSRLQINQSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAV 395
Cdd:PRK04837  245 LLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAV 324

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1782284395 396 NVVINFDFPKNAETYLHRIGRSGRFGHLGLAINLITSEDRFNLKSIED 443
Cdd:PRK04837  325 THVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIET 372
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 90-442 4.53e-54

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 190.55  E-value: 4.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI-------DLKKDHIQAMVM 162
Cdd:PRK04537   11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALIL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 163 VPTRELALQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKK-GVAKVDKVQMMVMDEAD 241
Cdd:PRK04537   91 APTRELAIQIHKDAVKFGADLG-LRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEAD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 242 KLLSQDFvvlIEDIISFLAK-----GRQILLYSATFPISVQKFMAKHLSKPYEINLMDE-LTLKGITQYYAYVTERQKVH 315
Cdd:PRK04537  170 RMFDLGF---IKDIRFLLRRmpergTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETEtITAARVRQRIYFPADEEKQT 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 316 CLNTLFSRLQINQSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAV 395
Cdd:PRK04537  247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1782284395 396 NVVINFDFPKNAETYLHRIGRSGRFGHLGLAINLITSEDRFNLKSIE 442
Cdd:PRK04537  327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIE 373
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 112-279 1.88e-52

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: 174.74  E-value: 1.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 112 SPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELALQVSQISIQVSKHMgGVKVMAT 191
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 192 TGGTNLRDDIMRLdETVHVVIATPGRILDLIKKGVaKVDKVQMMVMDEADKLLSQDFVVLIEDIISFLAKGRQILLYSAT 271
Cdd:pfam00270  80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157


                  ....*...
gi 1782284395 272 FPISVQKF 279
Cdd:pfam00270 158 LPRNLEDL 165
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 90-290 2.39e-51

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: 173.04  E-value: 2.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELA 169
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFV 249
Cdd:cd18045    81 VQIQKVLLALGDYMN-VQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1782284395 250 VLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEI 290
Cdd:cd18045   160 EQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 99-290 2.62e-51

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: 172.82  E-value: 2.62e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI---DLKKDHIQAMVMVPTRELALQVSQI 175
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 176 SIQVSKHmGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVA-KVDKVQMMVMDEADKLLSQDFVVLIED 254
Cdd:cd17947    81 LQQLAQF-TDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADELKE 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1782284395 255 IISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEI 290
Cdd:cd17947   160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 90-453 3.41e-51

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 181.91  E-value: 3.41e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI-DLKKDHIQ------AMVM 162
Cdd:PLN00206  123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCcTIRSGHPSeqrnplAMVL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 163 VPTRELALQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADK 242
Cdd:PLN00206  203 TPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 243 LLSQDFVVLIEDIISFLAKgRQILLYSATFPISVQKF---MAKHL-----SKPYEINlmdeltlKGITQYYAYVTERQKV 314
Cdd:PLN00206  282 MLERGFRDQVMQIFQALSQ-PQVLLFSATVSPEVEKFassLAKDIilisiGNPNRPN-------KAVKQLAIWVETKQKK 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 315 HclnTLFSRLQINQ-----SIIFCNSTQRVELLAKKITQL-GYSCFYIHA-KMMQEyRNRVFHDFRNGLCRNLVCTDLFT 387
Cdd:PLN00206  354 Q---KLFDILKSKQhfkppAVVFVSSRLGADLLANAITVVtGLKALSIHGeKSMKE-RREVMKSFLVGEVPVIVATGVLG 429

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1782284395 388 RGIDIQAVNVVINFDFPKNAETYLHRIGRSGRFGHLGLAINLITSEDRFNLKSIEDQLVTDIKPIP 453
Cdd:PLN00206  430 RGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIP 495
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 90-290 1.26e-50

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: 171.35  E-value: 1.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELA 169
Cdd:cd17954     2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSqisiQVSKHMG---GVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIK--KGVaKVDKVQMMVMDEADKLL 244
Cdd:cd17954    82 QQIS----EQFEALGssiGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEntKGF-SLKSLKFLVMDEADRLL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1782284395 245 SQDFVVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEI 290
Cdd:cd17954   157 NMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 90-290 3.51e-49

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: 167.52  E-value: 3.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELA 169
Cdd:cd17950     4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSQISIQVSKHMGGVKVMATTGGTNLRDDIMRL-DETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQ-D 247
Cdd:cd17950    84 FQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQlD 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1782284395 248 FVVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEI 290
Cdd:cd17950   164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 95-278 3.03e-47

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: 162.37  E-value: 3.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  95 LKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI------DLKKDHIQAMVMVPTREL 168
Cdd:cd17961     1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 169 ALQVSQISIQVSKHMGG-VKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKV-DKVQMMVMDEADKLLSQ 246
Cdd:cd17961    81 AQQVSKVLEQLTAYCRKdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1782284395 247 DFVVLIEDIISFLAKGRQILLYSATFPISVQK 278
Cdd:cd17961   161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEA 192
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 98-289 5.72e-46

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: 159.29  E-value: 5.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  98 ELLMGIFEMGWEKPSPVQEESIPIALS-GRDILARAKNGTGKSGAYLIPLLERI-----DLKKDHIQAMVMVPTRELALQ 171
Cdd:cd17964     4 SLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTRELALQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 172 VSQISIQVSKHMGGVKVMATTGGTNLRDDIMRL-DETVHVVIATPGRILDLIKK-GVAKV-DKVQMMVMDEADKLLSQDF 248
Cdd:cd17964    84 IAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENpGVAKAfTDLDYLVLDEADRLLDMGF 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1782284395 249 VVLIEDIISFL----AKGRQILLYSATFPISVQKFMAKHLSKPYE 289
Cdd:cd17964   164 RPDLEQILRHLpeknADPRQTLLFSATVPDEVQQIARLTLKKDYK 208
DEXDc smart00487
DEAD-like helicases superfamily;
103-304 3.40e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 156.88  E-value: 3.40e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  103 IFEMGWEKPSPVQEESIPIALSG-RDILARAKNGTGKSGAYLIPLLERIdLKKDHIQAMVMVPTRELALQVSQisiQVSK 181
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAE---ELKK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  182 HMG--GVKVMATTGGTNLRDDIMRL-DETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIEDIISF 258
Cdd:smart00487  77 LGPslGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1782284395  259 LAKGRQILLYSATFPISVQKFMAKHLSKPYEINLmDELTLKGITQY 304
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV-GFTPLEPIEQF 201
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 95-290 3.42e-45

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: 156.58  E-value: 3.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  95 LKRELLMGIFEMGWEKPSPVQEESIPIALSG--RDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELALQV 172
Cdd:cd17963     1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 173 SqisiQVSKHMG---GVKVMATtggtnLRDDIMRLDETV--HVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQD 247
Cdd:cd17963    81 G----EVVEKMGkftGVKVALA-----VPGNDVPRGKKItaQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTQ 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1782284395 248 -FVVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEI 290
Cdd:cd17963   152 gHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 90-287 7.83e-45

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: 155.93  E-value: 7.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIdlkKDH-----IQAMVMVP 164
Cdd:cd17959     3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL---KAHsptvgARALILSP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 165 TRELALQVSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLL 244
Cdd:cd17959    80 TRELALQTLKVTKELGKFTD-LRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1782284395 245 SQDFVVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKP 287
Cdd:cd17959   159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEP 201
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 90-271 3.08e-44

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: 154.40  E-value: 3.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIdlkkdhiQAMVMVPTRELA 169
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSQISIQVSKHMGGVKV--MATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQD 247
Cdd:cd17938    74 EQTYNCIENFKKYLDNPKLrvALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 1782284395 248 FVVLIEDIISFLAKGR------QILLYSAT 271
Cdd:cd17938   154 NLETINRIYNRIPKITsdgkrlQVIVCSAT 183
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 90-288 9.62e-43

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: 151.10  E-value: 9.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIdLKKDHI-----------Q 158
Cdd:cd17967     2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKL-LEDGPPsvgrgrrkaypS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 159 AMVMVPTRELALQVSQISIQVSKHmGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMD 238
Cdd:cd17967    81 ALILAPTRELAIQIYEEARKFSYR-SGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1782284395 239 EADKLLSQDFVVLIEDII---SFLAKG-RQILLYSATFPISVQKfMAKHLSKPY 288
Cdd:cd17967   160 EADRMLDMGFEPQIRKIVehpDMPPKGeRQTLMFSATFPREIQR-LAADFLKNY 212
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 99-287 6.05e-42

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: 148.62  E-value: 6.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERID--------LKKDHIQAMVMVPTRELAL 170
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlppldeeTKDDGPYALILAPTRELAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 171 QVSQISIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVV 250
Cdd:cd17945    81 QIEEETQKFAKPL-GIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1782284395 251 LIEDIISFL--------------------AKGRQILLYSATFPISVQKFMAKHLSKP 287
Cdd:cd17945   160 QVTKILDAMpvsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRRP 216
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 99-290 8.69e-42

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: 147.56  E-value: 8.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI----DLKK-DHIQAMVMVPTRELALQVS 173
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdqrELEKgEGPIAVIVAPTRELAQQIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 174 QISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIE 253
Cdd:cd17952    81 LEAKKFGKAYN-LRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1782284395 254 DIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEI 290
Cdd:cd17952   160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 90-290 1.12e-41

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: 147.37  E-value: 1.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERidLKKD--HIQAMVMVPTRE 167
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQR--LSEDpyGIFALVLTPTRE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 168 LALQVS-QISIqVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIK---KGVAKVDKVQMMVMDEADKL 243
Cdd:cd17955    79 LAYQIAeQFRA-LGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1782284395 244 LSQDFVVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEI 290
Cdd:cd17955   157 LTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFW 203
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 99-280 6.87e-41

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: 145.41  E-value: 6.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI-----DLKKDHIQAMVMVPTRELALQVS 173
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 174 QISIQVSKHMGG-VKVMATTGGTN-LRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDK--VQMMVMDEADKLLSQDFV 249
Cdd:cd17960    81 EVLQSFLEHHLPkLKCQLLIGGTNvEEDVKKFKRNGPNILVGTPGRLEELLSRKADKVKVksLEVLVLDEADRLLDLGFE 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1782284395 250 VLIEDIISFLAKGRQILLYSATFPISVQKFM 280
Cdd:cd17960   161 ADLNRILSKLPKQRRTGLFSATQTDAVEELI 191
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 99-290 1.82e-40

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: 143.84  E-value: 1.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRELALQVSQisiQ 178
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIED---Q 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 179 VSKHMGGVKVMATT---GGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIEDI 255
Cdd:cd17962    78 AKELMKGLPPMKTAllvGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDI 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1782284395 256 ISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEI 290
Cdd:cd17962   158 LENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 103-291 2.07e-40

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: 144.05  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 103 IFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIdLKKDHIQ------AMVMVPTRELALQVSQIS 176
Cdd:cd17966     5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI-NAQPPLErgdgpiVLVLAPTRELAQQIQQEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 177 IQVSkHMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIEDII 256
Cdd:cd17966    84 NKFG-GSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIV 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1782284395 257 SFLAKGRQILLYSATFPISVQKFMAKHLSKPYEIN 291
Cdd:cd17966   163 DQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 88-288 2.50e-40

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: 145.88  E-value: 2.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  88 NEFEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERidLKKDHI---------- 157
Cdd:cd18052    43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTG--MMKEGLtassfsevqe 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 158 -QAMVMVPTRELALqvsQISIQVSK--HMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQM 234
Cdd:cd18052   121 pQALIVAPTRELAN---QIFLEARKfsYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKY 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1782284395 235 MVMDEADKLLSQDFVVLIEDIISFL---AKG-RQILLYSATFPISVQKFMAKHLSKPY 288
Cdd:cd18052   198 LILDEADRMLDMGFGPEIRKLVSEPgmpSKEdRQTLMFSATFPEEIQRLAAEFLKEDY 255
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 95-290 8.57e-40

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: 143.29  E-value: 8.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  95 LKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIdlkKDHIQ--------AMVMVPTR 166
Cdd:cd17953    19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI---KDQRPvkpgegpiGLIMAPTR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 167 ELALQVSQISIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKV---DKVQMMVMDEADKL 243
Cdd:cd17953    96 ELALQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVtnlRRVTYVVLDEADRM 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1782284395 244 LSQDFVVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEI 290
Cdd:cd17953   175 FDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 100-292 1.52e-39

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: 141.66  E-value: 1.52e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 100 LMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKK----DHIQAMVMVPTRELALQVSQI 175
Cdd:cd17941     2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwtpeDGLGALIISPTRELAMQIFEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 176 SIQVSKHmggvKVMAT---TGGTNLRDDIMRLDeTVHVVIATPGRILDLIKKGVA-KVDKVQMMVMDEADKLLSQDFVVL 251
Cdd:cd17941    82 LRKVGKY----HSFSAgliIGGKDVKEEKERIN-RMNILVCTPGRLLQHMDETPGfDTSNLQMLVLDEADRILDMGFKET 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1782284395 252 IEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEINL 292
Cdd:cd17941   157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 99-287 1.55e-37

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: 136.18  E-value: 1.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI--DLKKDHIQAMVMVPTRELAlqvSQIS 176
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELA---SQIY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 177 IQVSKHMGG----VKVMATTGGTNLRDDImRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLI 252
Cdd:cd17957    78 RELLKLSKGtglrIVLLSKSLEAKAKDGP-KSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1782284395 253 EDIISFL-AKGRQILLYSATFPISVQKFMAKHLSKP 287
Cdd:cd17957   157 DEILAACtNPNLQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 99-287 6.28e-37

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: 134.51  E-value: 6.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDL------KKDHIQAMVMVPTRELALQv 172
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLqpipreQRNGPGVLVLTPTRELALQ- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 173 sqISIQVSKHM-GGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVL 251
Cdd:cd17958    80 --IEAECSKYSyKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1782284395 252 IEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKP 287
Cdd:cd17958   158 IRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 88-277 1.55e-35

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: 132.47  E-value: 1.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  88 NEFEDYCLKrELLMGIFEMG-WEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI---------------- 150
Cdd:cd18051    21 ETFSDLDLG-EIIRNNIELArYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgeslpsesgyy 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 151 DLKKDHIQAMVMVPTRELALQVSQISIQVSkHMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVD 230
Cdd:cd18051   100 GRRKQYPLALVLAPTRELASQIYDEARKFA-YRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLD 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1782284395 231 KVQMMVMDEADKLLSQDFVVLIEDII---SFLAKG-RQILLYSATFPISVQ 277
Cdd:cd18051   179 YCKYLVLDEADRMLDMGFEPQIRRIVeqdTMPPTGeRQTLMFSATFPKEIQ 229
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 106-287 2.48e-35

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: 130.78  E-value: 2.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 106 MGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQ------AMVMVPTRELALQVSQISIQV 179
Cdd:cd17949     9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 180 SKHMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVA-KVDKVQMMVMDEADKLLSQDFVVLIEDIISF 258
Cdd:cd17949    89 LKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMGFEKDITKILEL 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1782284395 259 LAKG-------------RQILLYSATFPISVQKFMAKHLSKP 287
Cdd:cd17949   169 LDDKrskaggekskpsrRQTVLVSATLTDGVKRLAGLSLKDP 210
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 68-297 3.37e-34

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: 128.22  E-value: 3.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  68 LQLPQKDcrfRTSDVTSTKgnEFEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSG--RDILARAKNGTGKSGAYLIP 145
Cdd:cd18048     3 VEVLQRD---PTSPLFSVK--SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 146 LLERIDLKKDHIQAMVMVPTRELALQVSQISIQVSKHMGGVKVMATTGGTNLRDDImrlDETVHVVIATPGRILD-LIKK 224
Cdd:cd18048    78 MLSRVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGT---DIEAQIVIGTPGTVLDwCFKL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1782284395 225 GVAKVDKVQMMVMDEADKLLS-QDFVVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEINL-MDELT 297
Cdd:cd18048   155 RLIDVTNISVFVLDEADVMINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLkKEELT 229
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 100-271 4.10e-34

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: 127.09  E-value: 4.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 100 LMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERID----LKKDHIQAMVMVPTRELALQVSQI 175
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYklkfKPRNGTGVIIISPTRELALQIYGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 176 SIQVSKHmGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDK-VQMMVMDEADKLLSQDFVVLIED 254
Cdd:cd17942    82 AKELLKY-HSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFEEEMRQ 160

                         170
                  ....*....|....*..
gi 1782284395 255 IISFLAKGRQILLYSAT 271
Cdd:cd17942   161 IIKLLPKRRQTMLFSAT 177
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 99-291 2.88e-33

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: 125.14  E-value: 2.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPL----LERiDLKKDHIQ-----AMVMVPTRELA 169
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLimfaLEQ-EKKLPFIKgegpyGLIVCPSRELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 170 LQVSQISIQVSKH-----MGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLL 244
Cdd:cd17951    80 RQTHEVIEYYCKAlqeggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1782284395 245 SQDFVVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEIN 291
Cdd:cd17951   160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 312-421 7.95e-33

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: 120.39  E-value: 7.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 312 QKVHCLNTLFSRLQINQSIIFCNSTQRVEllAKKITQL-GYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGI 390
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1782284395 391 DIQAVNVVINFDFPKNAETYLHRIGRSGRFG 421
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 77-292 1.62e-31

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: 121.27  E-value: 1.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  77 FRTSDVTSTKGN-------EFEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLER 149
Cdd:cd18049     6 YRRSKEITVRGHncpkpvlNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 150 IDLKK-----DHIQAMVMVPTRELALQVSQISIQVSKhMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKK 224
Cdd:cd18049    86 INHQPflergDGPICLVLAPTRELAQQVQQVAAEYGR-ACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1782284395 225 GVAKVDKVQMMVMDEADKLLSQDFVVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLSKPYEINL 292
Cdd:cd18049   165 GKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 99-272 2.33e-31

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: 120.81  E-value: 2.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALS-GRDILARAKNGTGKSGAYLIPLLERI-DLKKDHI--------QAMVMVPTREL 168
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlSQKSSNGvggkqkplRALILTPTREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 169 ALQVSQISIQVSKHmGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKG---VAKVDKVQMMVMDEADKLLS 245
Cdd:cd17946    81 AVQVKDHLKAIAKY-TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLE 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1782284395 246 QDFVVLIEDIISFL-------AKGRQILLYSATF 272
Cdd:cd17946   160 KGHFAELEKILELLnkdragkKRKRQTFVFSATL 193
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 103-292 5.80e-31

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: 120.50  E-value: 5.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 103 IFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDL-----KKDHIQAMVMVPTRELALQVSQISI 177
Cdd:cd18050    77 LLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHqpyleRGDGPICLVLAPTRELAQQVQQVAD 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 178 QVSKHmGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIEDIIS 257
Cdd:cd18050   157 DYGKS-SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD 235

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1782284395 258 FLAKGRQILLYSATFPISVQKFMAKHLSKPYEINL 292
Cdd:cd18050   236 QIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 99-282 1.09e-30

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: 118.62  E-value: 1.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  99 LLMGIFEMGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKK-------DHIQAMVMVPTRELALQ 171
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKllaegpfNAPRGLVITPSRELAEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 172 VSQISIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVL 251
Cdd:cd17948    81 IGSVAQSLTEGLG-LKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1782284395 252 IEDIISF-------------LAKGRQILLYSATFPISVQKFMAK 282
Cdd:cd17948   160 LSHFLRRfplasrrsentdgLDPGTQLVLVSATMPSGVGEVLSK 203
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 90-287 1.66e-29

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: 114.82  E-value: 1.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  90 FEDYCLKRELLMGIFEMGWEKPSPVQEESIPIALSG--RDILARAKNGTGKSGAYLIPLLERIDLKKDHIQAMVMVPTRE 167
Cdd:cd18047     3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 168 LALQVSQISIQVSKHMGGVKVMATTGGTNLRDDIMRLDEtvhVVIATPGRILD-LIKKGVAKVDKVQMMVMDEADKLLS- 245
Cdd:cd18047    83 LALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIAt 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1782284395 246 ---QDFVVLIEDIisfLAKGRQILLYSATFPISVQKFMAKHLSKP 287
Cdd:cd18047   160 qghQDQSIRIQRM---LPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
HELICc smart00490
helicase superfamily c-terminal domain;
340-421 3.19e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 104.22  E-value: 3.19e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  340 ELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGR 419
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 1782284395  420 FG 421
Cdd:smart00490  81 AG 82
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 113-289 1.68e-26

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: 106.47  E-value: 1.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 113 PVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHI------QAMVMVPTRELALQVSQISIQVSKHMggv 186
Cdd:cd17944    15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVTKDFKDITRKL--- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 187 KVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIEDIISFLAKGR--- 263
Cdd:cd17944    92 SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYKKDsed 171

                         170       180
                  ....*....|....*....|....*...
gi 1782284395 264 --QILLYSATFPISVQKFMAKHLSKPYE 289
Cdd:cd17944   172 npQTLLFSATCPDWVYNVAKKYMKSQYE 199
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 105-248 2.84e-25

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: 103.87  E-value: 2.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 105 EMGWEKPSPVQEESIPIALSG---------RDILARAKNGTGKSGAYLIPLLERI-DLKKDHIQAMVMVPTRELALQVSQ 174
Cdd:cd17956     7 NNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKELVQQVYK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 175 ISIQVSKHMgGVKVMATTGGTNLRDDIM--------RLDETVHVVIATPGRILDLIKKGVA-KVDKVQMMVMDEADKLLS 245
Cdd:cd17956    87 VFESLCKGT-GLKVVSLSGQKSFKKEQKlllvdtsgRYLSRVDILVATPGRLVDHLNSTPGfTLKHLRFLVIDEADRLLN 165


                  ...
gi 1782284395 246 QDF 248
Cdd:cd17956   166 QSF 168
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 110-293 1.51e-20

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: 90.90  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 110 KPSPVQEESIPIALSGRDILAR----------------AKNGTGKSGAYLIPLL---------------ERIDLKKDH-- 156
Cdd:cd17965    30 KPSPIQTLAIKKLLKTLMRKVTkqtsneepklevfllaAETGSGKTLAYLAPLLdylkrqeqepfeeaeEEYESAKDTgr 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 157 IQAMVMVPTRELALQVSQISIQVSKHMG-GVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVDKVQMM 235
Cdd:cd17965   110 PRSVILVPTHELVEQVYSVLKKLSHTVKlGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHL 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1782284395 236 VMDEADKLLSQDFVVLIEDIISFLAKGRQILLYSATFPISVQKFMAKHLskPYEINLM 293
Cdd:cd17965   190 VVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLF--PDVVRIA 245
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 125-271 1.51e-14

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 70.90  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 125 GRDILARAKNGTGKSGAYLIPLLERIDLKKDhiQAMVMVPTRELALQVSQISIQVSKHmgGVKVMATTGGTNLRDDIMRL 204
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLLKKGK--KVLVLVPTKALALQTAERLRELFGP--GIRVAVLVGGSSAEEREKNK 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 205 DETVHVVIATPGRILDLIKKGVAKVDK-VQMMVMDEADKLLSQDFVVLIED--IISFLAKGRQILLYSAT 271
Cdd:cd00046    77 LGDADIIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 330-421 8.78e-14

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 68.00  E-value: 8.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 330 IIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNAET 409
Cdd:cd18794    34 IIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMES 113

                          90
                  ....*....|..
gi 1782284395 410 YLHRIGRSGRFG 421
Cdd:cd18794   114 YYQESGRAGRDG 125
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
135-416 1.18e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 73.14  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 135 GTGKS--GAYLIpllERIDLKKdhiQAMVMVPTRELalqVSQISIQVSKHMGGVKVmatTGGtnlrddimRLDETVHVVI 212
Cdd:COG1061   110 GTGKTvlALALA---AELLRGK---RVLVLVPRREL---LEQWAEELRRFLGDPLA---GGG--------KKDSDAPITV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 213 ATpgrildlikkgvakvdkVQMMVMDEADKLLSQDFVVLI------------EDIISFLAKGRQILLySAT--------- 271
Cdd:COG1061   170 AT-----------------YQSLARRAHLDELGDRFGLVIideahhagapsyRRILEAFPAAYRLGL-TATpfrsdgrei 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 272 ---------FPISVQKFMAKHLSKPYEI-----------NLMDELTlKGITQYYAYVTERqKVHCLNTLFSRL-QINQSI 330
Cdd:COG1061   232 llflfdgivYEYSLKEAIEDGYLAPPEYygirvdltderAEYDALS-ERLREALAADAER-KDKILRELLREHpDDRKTL 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 331 IFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETY 410
Cdd:COG1061   310 VFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREF 389


                  ....*.
gi 1782284395 411 LHRIGR 416
Cdd:COG1061   390 IQRLGR 395
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
81-452 2.13e-12

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 69.15  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  81 DVTSTKGNEFEDYCLKRellmGIFEMgwekpSPVQEESIP-IALSGRDILARAKNGTGKSgayLI---PLLERIDLKKDh 156
Cdd:COG1204     2 KVAELPLEKVIEFLKER----GIEEL-----YPPQAEALEaGLLEGKNLVVSAPTASGKT---LIaelAILKALLNGGK- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 157 iqAMVMVPTRELAlqvSQISIQVSKHMG--GVKVMATTGGTNLRDdimRLDETVHVVIATPGRILDLIKKGVAKVDKVQM 234
Cdd:COG1204    69 --ALYIVPLRALA---SEKYREFKRDFEelGIKVGVSTGDYDSDD---EWLGRYDILVATPEKLDSLLRNGPSWLRDVDL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 235 MVMDEADKLLSQDFVVLIEDIISFL---AKGRQILLYSATFPiSVQKFmAKHL-SKPYE-----INLMdELTLKGITQYY 305
Cdd:COG1204   141 VVVDEAHLIDDESRGPTLEVLLARLrrlNPEAQIVALSATIG-NAEEI-AEWLdAELVKsdwrpVPLN-EGVLYDGVLRF 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 306 AYVTERQKVHCLNTLFSRLQIN-QSIIFCNSTQRVELLAKKITQ-LGYSCFYI--------------------------- 356
Cdd:COG1204   218 DDGSRRSKDPTLALALDLLEEGgQVLVFVSSRRDAESLAKKLADeLKRRLTPEereeleelaeellevseethtneklad 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 357 ---------HAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI------------NFDFpKNAetylhrIG 415
Cdd:COG1204   298 clekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIrdtkrggmvpipVLEF-KQM------AG 370

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1782284395 416 RSGRFGH--LGLAInLITSEDRFNLKSIEDQLVTDIKPI 452
Cdd:COG1204   371 RAGRPGYdpYGEAI-LVAKSSDEADELFERYILGEPEPI 408
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
113-419 6.17e-12

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 67.47  E-value: 6.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 113 PVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLER----------IDLKKDHIQAMvmvptRELalqvsqisiqvskh 182
Cdd:COG0514    20 PGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLpgltlvvsplIALMKDQVDAL-----RAA-------------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 183 mgGVKVMATTGGTNL--RDDIMR--LDETVHVVIATP-----GRILDLIKKGvakvdKVQMMVMDEAdKLLSQ---DF-- 248
Cdd:COG0514    81 --GIRAAFLNSSLSAeeRREVLRalRAGELKLLYVAPerllnPRFLELLRRL-----KISLFAIDEA-HCISQwghDFrp 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 249 -----VVLIEDIisflaKGRQILLYSATFPISVQKFMAKHLskpyeiNLMDELTLKG------ItqYYAyVTERQKVHCL 317
Cdd:COG0514   153 dyrrlGELRERL-----PNVPVLALTATATPRVRADIAEQL------GLEDPRVFVGsfdrpnL--RLE-VVPKPPDDKL 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 318 NTLFSRL--QINQS-IIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQA 394
Cdd:COG0514   219 AQLLDFLkeHPGGSgIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPD 298

                         330       340
                  ....*....|....*....|....*
gi 1782284395 395 VNVVINFDFPKNAETYLHRIGRSGR 419
Cdd:COG0514   299 VRFVIHYDLPKSIEAYYQEIGRAGR 323
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 107-421 2.00e-11

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 66.28  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 107 GWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLER----------IDLKKDHIQAMVM----------VPTR 166
Cdd:PRK11057   22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLdgltlvvsplISLMKDQVDQLLAngvaaaclnsTQTR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 167 ElalqvSQISIQVSKHMGGVKVMATTGGTNLRDDIM-RLDETVHVVIATPG---------------RILDLIKKGVAKVD 230
Cdd:PRK11057  102 E-----QQLEVMAGCRTGQIKLLYIAPERLMMDNFLeHLAHWNPALLAVDEahcisqwghdfrpeyAALGQLRQRFPTLP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 231 KvqMMVMDEADKLLSQDfvvliedIISFLAKgRQILLYSATF--PISVQKFMAKHlsKPyeinlmdeltlkgITQYYAYV 308
Cdd:PRK11057  177 F--MALTATADDTTRQD-------IVRLLGL-NDPLIQISSFdrPNIRYTLVEKF--KP-------------LDQLMRYV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 309 TErQKVHClntlfsrlqinqSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTR 388
Cdd:PRK11057  232 QE-QRGKS------------GIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGM 298

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1782284395 389 GIDIQAVNVVINFDFPKNAETYLHRIGRSGRFG 421
Cdd:PRK11057  299 GINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 313-416 3.12e-09

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: 55.29  E-value: 3.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 313 KVHCL-NTL---FSRLQINQSIIFCNSTQRVELLAKKITQLGYSCFYIHA-------------------KMMQEyrnrVF 369
Cdd:cd18802     8 KLQKLiEILreyFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCgfligrgnssqrkrslmtqRKQKE----TL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1782284395 370 HDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRIGR 416
Cdd:cd18802    84 DKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 380-421 7.83e-09

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 52.32  E-value: 7.83e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1782284395 380 LVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGRFG 421
Cdd:cd18785    26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 115-434 3.38e-08

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: 56.00  E-value: 3.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 115 QEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIdLKKDHIQAMVMVPTRELAL-QVSQISiQVSKHMG-GVKVMATT 192
Cdd:COG1205    61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALARdQLRRLR-ELAEALGlGVRVATYD 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 193 GGT--NLRDDIMrldETVHVVIATPgrildlikkgvakvDKVQMMVMDEADK---LLSQ-DFVVLIE------------- 253
Cdd:COG1205   139 GDTppEERRWIR---EHPDIVLTNP--------------DMLHYGLLPHHTRwarFFRNlRYVVIDEahtyrgvfgshva 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 254 -------DIISFLAKGRQILLYSATF--PisvQKFMAKHLSKPYEinLMDE----------------LTLKGITQYYAYV 308
Cdd:COG1205   202 nvlrrlrRICRHYGSDPQFILASATIgnP---AEHAERLTGRPVT--VVDEdgsprgertfvlwnppLVDDGIRRSALAE 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 309 TERqkvhclntLFSRLQIN--QSIIFCNSTQRVELLAKKITQL-----------GYscfyiHAKMMQEYRNRVFHDFRNG 375
Cdd:COG1205   277 AAR--------LLADLVREglRTLVFTRSRRGAELLARYARRAlrepdladrvaAY-----RAGYLPEERREIERGLRSG 343

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1782284395 376 LCRNLVCT---DLftrGIDIQAVNVVINFDFPKNAETYLHRIGRSGRFGHLGLAInLITSED 434
Cdd:COG1205   344 ELLGVVSTnalEL---GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGDD 401
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
 328-427 5.58e-08

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 51.87  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 328 QSIIFCNSTQRVELLAKKITQLGYSCFYIHAKMM-------QEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVIN 400
Cdd:cd18797    37 KTIVFCRSRKLAELLLRYLKARLVEEGPLASKVAsyragylAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116

                          90       100
                  ....*....|....*....|....*..
gi 1782284395 401 FDFPKNAETYLHRIGRSGRFGHLGLAI 427
Cdd:cd18797   117 AGYPGSLASLWQQAGRAGRRGKDSLVI 143
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 329-421 7.88e-08

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: 50.94  E-value: 7.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 329 SIIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGL--CRNLVCTDLFTRGIDIQAVNVVINFDFPKN 406
Cdd:cd18793    30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPWWN 109

                          90
                  ....*....|....*
gi 1782284395 407 AETYLHRIGRSGRFG 421
Cdd:cd18793   110 PAVEEQAIDRAHRIG 124
PRK00254 PRK00254
ski2-like helicase; Provisional
 105-434 1.34e-07

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 54.05  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 105 EMGWEKPSPVQEESIPI-ALSGRDILARAKNGTGKSGAYLIPLLERidLKKDHIQAMVMVPTRELALQVSQISIQVSKHm 183
Cdd:PRK00254   18 ERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNK--LLREGGKAVYLVPLKALAEEKYREFKDWEKL- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 184 gGVKVMATTGGTNLRDDIM-RLDetvhVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIEDIISFLAKG 262
Cdd:PRK00254   95 -GLRVAMTTGDYDSTDEWLgKYD----IIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 263 RQILLYSATfpISVQKFMAKHLSKPYEINLMDELTLKGITQYYAYVT-ERQKVHCLNTLFSRLQIN------QSIIFCNS 335
Cdd:PRK00254  170 AQILGLSAT--VGNAEELAEWLNAELVVSDWRPVKLRKGVFYQGFLFwEDGKIERFPNSWESLVYDavkkgkGALVFVNT 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 336 TQRVE----LLAKKITQL------------------------------GYSCFYiHAKMMQEYRNRVFHDFRNGLCRNLV 381
Cdd:PRK00254  248 RRSAEkealELAKKIKRFltkpelralkeladsleenptneklkkalrGGVAFH-HAGLGRTERVLIEDAFREGLIKVIT 326

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1782284395 382 CTDLFTRGIDIQAVNVVINfDFPKNAETYLHRI---------GRSGR--FGHLGLAINLITSED 434
Cdd:PRK00254  327 ATPTLSAGINLPAFRVIIR-DTKRYSNFGWEDIpvleiqqmmGRAGRpkYDEVGEAIIVATTEE 389
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 320-419 4.29e-07

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 49.57  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 320 LFSRLQINQSIIFCNSTQRVELLAKKITQLGYSC-----FYIHAKMM-QEYRNRVFHDFRNGLCRNLVCT---DLftrGI 390
Cdd:cd18796    32 IFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRvppdfIALHHGSLsRELREEVEAALKRGDLKVVVATsslEL---GI 108

                          90       100
                  ....*....|....*....|....*....
gi 1782284395 391 DIQAVNVVINFDFPKNAETYLHRIGRSGR 419
Cdd:cd18796   109 DIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 115-215 4.53e-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: 49.89  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 115 QEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIdLKKDHIQAMVMVPTRELAL-QVSQISIQVSKHMGGVKVMATTG 193
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDG 83

                          90       100
                  ....*....|....*....|..
gi 1782284395 194 GTNLRDDIMRLDETVHVVIATP 215
Cdd:cd17923    84 DTPREERRAIIRNPPRILLTNP 105
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
330-485 7.52e-07

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 51.65  E-value: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 330 IIFCNSTQRVELLAKKITQLGYSC--FYIHAK------MMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINF 401
Cdd:COG1111   357 IVFTQYRDTAEMIVEFLSEPGIKAgrFVGQASkegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFY 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 402 DFPKNAETYLHRIGRSGRFGHlGLAINLITS--------------EDRFNL------KSIEDQLVTDIKP-IPGSIDkgl 460
Cdd:COG1111   437 EPVPSEIRSIQRKGRTGRKRE-GRVVVLIAKgtrdeayywssrrkEKKMKSilkklkKLLDKQEKEKLKEsAQATLD--- 512

                         170       180
                  ....*....|....*....|....*
gi 1782284395 461 yvaEFHSAEPDTEDEIRGKDGELSA 485
Cdd:COG1111   513 ---EFESIKELAEDEINEKDLDEIE 534
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 330-416 9.94e-07

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: 47.55  E-value: 9.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 330 IIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNR-VFHDFRNG--LCRNLVCTDLFTRGIDIQAVNVVInFDFPKN 406
Cdd:cd18799    10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV-FLRPTE 88

                          90
                  ....*....|.
gi 1782284395 407 AET-YLHRIGR 416
Cdd:cd18799    89 SRTlFLQMLGR 99
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 330-421 4.96e-06

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 49.07  E-value: 4.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 330 IIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCRN--LVCTDLFTRGIDIQAVNVVINFDFPKNA 407
Cdd:COG0553   553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPvfLISLKAGGEGLNLTAADHVIHYDLWWNP 632

                          90
                  ....*....|....
gi 1782284395 408 ETYLHRIGRSGRFG 421
Cdd:COG0553   633 AVEEQAIDRAHRIG 646
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
 338-442 1.43e-05

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: 45.03  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 338 RVELLAKKITQLG-----YSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLH 412
Cdd:cd18810    34 RIESIEKLATQLRqlvpeARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLY 113

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1782284395 413 RI-GRSGRFGHLGLAINLITSEDRFNLKSIE 442
Cdd:cd18810   114 QLrGRVGRSKERAYAYFLYPDQKKLTEDALK 144
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 327-419 1.91e-05

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA 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: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 44.85  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 327 NQSIIFCNSTQRVELLAKKITQLGyscfYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKN 406
Cdd:cd18795    44 KPVLVFCSSRKECEKTAKDLAGIA----FHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119

                          90       100
                  ....*....|....*....|.
gi 1782284395 407 AET--------YLHRIGRSGR 419
Cdd:cd18795   120 GKGyrelspleYLQMIGRAGR 140
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 360-419 2.57e-05

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: 44.27  E-value: 2.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 360 MMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGR 419
Cdd:cd18801    74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 110-240 2.97e-05

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 44.95  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 110 KPSPVQEESIPIALSgRDILARAKNGTGKSgayLIPLL------ERID-LKKDHIQAMVMVPTRELALQ-VSQISI---- 177
Cdd:cd18034     2 TPRSYQLELFEAALK-RNTIVVLPTGSGKT---LIAVMlikemgELNRkEKNPKKRAVFLVPTVPLVAQqAEAIRShtdl 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1782284395 178 QVSKHMGGVKVMATTGGTNLRDDimrldETVHVVIATPGRILDLIKKGVAKVDKVQMMVMDEA 240
Cdd:cd18034    78 KVGEYSGEMGVDKWTKERWKEEL-----EKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
 112-287 6.53e-05

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: 43.78  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 112 SPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDlKKDHIqAMVMVPTreLALQVSQISiQVSKHMGGVKVMAT 191
Cdd:cd18018    14 RPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRR-RGPGL-TLVVSPL--IALMKDQVD-ALPRAIKAAALNSS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 192 TGGTNLRDDIMRLDE-TVHVVIATPGRILDL-IKKGVAKVDKVQMMVMDEADKL--LSQDF---VVLIEDIISFLAKGRQ 264
Cdd:cd18018    89 LTREERRRILEKLRAgEVKILYVSPERLVNEsFRELLRQTPPISLLVVDEAHCIseWSHNFrpdYLRLCRVLRELLGAPP 168

                         170       180
                  ....*....|....*....|...
gi 1782284395 265 ILLYSATFPISVQKFMAKHLSKP 287
Cdd:cd18018   169 VLALTATATKRVVEDIASHLGIP 191
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 337-443 7.34e-05

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: 43.02  E-value: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 337 QRVELLAKKITQL--GYSCFYIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFdfpkNAETY---- 410
Cdd:cd18792    45 KSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIE----DADRFglsq 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1782284395 411 LH----RIGRSGRFGHLGLAIN---LITSEDRFNLKSIED 443
Cdd:cd18792   121 LHqlrgRVGRGKHQSYCYLLYPdpkKLTETAKKRLRAIAE 160
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
329-418 1.30e-04

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 44.71  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 329 SIIFCNSTQRVELLAKKITQLGYSCFYI----HAKMMQEYRNRVFHDFRNGLCRNLVCT---DLftrGIDIQAVNVVINF 401
Cdd:COG1201   275 TLVFTNTRSQAERLFQRLNELNPEDALPiaahHGSLSREQRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQV 351

                          90
                  ....*....|....*..
gi 1782284395 402 DFPKNAETYLHRIGRSG 418
Cdd:COG1201   352 GSPKSVARLLQRIGRAG 368
mfd TIGR00580
transcription-repair coupling factor (mfd); All proteins in this family for which functions ...
 355-442 1.33e-04

transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273152 [Multi-domain]  Cd Length: 926  Bit Score: 44.66  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 355 YIHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFdfpkNAETY----LHRI-GRSGRFGHLGLAINL 429
Cdd:TIGR00580 691 IAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIE----RADKFglaqLYQLrGRVGRSKKKAYAYLL 766

                          90
                  ....*....|...
gi 1782284395 430 ITSEDRFNLKSIE 442
Cdd:TIGR00580 767 YPHQKALTEDAQK 779
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 330-421 1.06e-03

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 41.81  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395  330 IIFCNSTQRVELLAKKITQLGYSCFYIHAKMMQEYRNRVFHDFRNGLCrNLVC-TDLFTRGIDIQAVNVVINFDFPKNAE 408
Cdd:PLN03137   684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEI-NIICaTVAFGMGINKPDVRFVIHHSLPKSIE 762

                           90
                   ....*....|...
gi 1782284395  409 TYLHRIGRSGRFG 421
Cdd:PLN03137   763 GYHQECGRAGRDG 775
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
 110-239 1.06e-03

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: 40.54  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 110 KPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDHIQ---AMVMVPTRELalqVSQISIQVSKHM-GG 185
Cdd:cd18036     2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEkgrVVVLVNKVPL---VEQQLEKFFKYFrKG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1782284395 186 VKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGvAKVDKVQ-----MMVMDE 239
Cdd:cd18036    79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSG-REEERVYlsdfsLLIFDE 136
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 113-273 1.88e-03

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: 39.24  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 113 PVQEESIPIAL-SGRDILARAKNGTGKSgayLIPLLERIDLKKDHIQAMVMVPTRELAlqvSQISIQVSKHMG-GVKVMA 190
Cdd:cd18028     4 PPQAEAVRAGLlKGENLLISIPTASGKT---LIAEMAMVNTLLEGGKALYLVPLRALA---SEKYEEFKKLEEiGLKVGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 191 TTGGTNLRDDimRLDETvHVVIATPGRILDLIKKGVAKVDKVQMMVMDEADKLLSQDFVVLIEDIIS---FLAKGRQILL 267
Cdd:cd18028    78 STGDYDEDDE--WLGDY-DIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVArlrRLNPNTQIIG 154


                  ....*.
gi 1782284395 268 YSATFP 273
Cdd:cd18028   155 LSATIG 160
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 356-422 3.47e-03

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It 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: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 38.09  E-value: 3.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1782284395 356 IHAKMMQEYRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVInfdfPKNAETY----LHRI-GRSGRFGH 422
Cdd:cd18811    67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMV----IEDAERFglsqLHQLrGRVGRGDH 134
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
 106-240 6.62e-03

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 37.90  E-value: 6.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782284395 106 MGWEKPSPVQEESIPIALSGRDILARAKNGTGKSGAYLIP--LLERIdlkkdhiqAMVMVPTreLALQVSQISiqvSKHM 183
Cdd:cd17920     8 FGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV--------TLVVSPL--ISLMQDQVD---RLQQ 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1782284395 184 GGVKVMATTGGT----NLRDDIMRLDETVHVVIATP-----GRILDLIKKgVAKVDKVQMMVMDEA 240
Cdd:cd17920    75 LGIRAAALNSTLspeeKREVLLRIKNGQYKLLYVTPerllsPDFLELLQR-LPERKRLALIVVDEA 139
 
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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