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Conserved domains on  [gi|18859541|ref|NP_571132|]
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probable ATP-dependent RNA helicase DDX4 [Danio rerio]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030645)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 245-498 0e+00

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: 543.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 245 SSIFSHYATGINFDKYDDILVDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTG 324
Cdd:cd18052  11 DEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTG 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 325 SGKTAAFLLPILQRFMTDGVAASKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKG 404
Cdd:cd18052  91 SGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKG 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 405 CNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADF 484
Cdd:cd18052 171 CHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEF 250

                       250
                ....*....|....
gi 18859541 485 LKVDYIFLAVGVVG 498
Cdd:cd18052 251 LKEDYLFLTVGRVG 264
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 504-633 1.20e-57

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: 191.57  E-value: 1.20e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 504 VEQTVVQVDQYSKRDQLL-ELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPV 582
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18859541 583 LVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFF 633
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 245-498 0e+00

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: 543.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 245 SSIFSHYATGINFDKYDDILVDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTG 324
Cdd:cd18052  11 DEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTG 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 325 SGKTAAFLLPILQRFMTDGVAASKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKG 404
Cdd:cd18052  91 SGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKG 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 405 CNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADF 484
Cdd:cd18052 171 CHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEF 250

                       250
                ....*....|....
gi 18859541 485 LKVDYIFLAVGVVG 498
Cdd:cd18052 251 LKEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
276-649 1.67e-158

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 464.62  E-value: 1.67e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 276 IMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAAskfseiqeP 355
Cdd:COG0513   1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------P 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 356 EAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLD 435
Cdd:COG0513  73 QALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLD 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 436 EADRMLDMGFEPEMRKLVASpgMPskEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGACSDVEQTVVQVDQYS 515
Cdd:COG0513 153 EADRMLDMGFIEDIERILKL--LP--KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRD 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 516 KRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAARGLDI 595
Cdd:COG0513 228 KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDI 307

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 18859541 596 EQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPEsDTPLARSLVKVL 649
Cdd:COG0513 308 DDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPD-ERRLLRAIEKLI 360
PTZ00110 PTZ00110
helicase; Provisional
 267-677 8.50e-120

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 369.49  E-value: 8.50e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  267 VSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIlqrfMTDGVAA 346
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPA----IVHINAQ 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  347 SKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGL 426
Cdd:PTZ00110 196 PLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNL 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  427 SKVRYLVLDEADRMLDMGFEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKVDYIFLAVGVVG-GACSDVE 505
Cdd:PTZ00110 276 RRVTYLVLDEADRMLDMGFEPQIRKIVSQ----IRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNIK 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  506 QTVVQVDQYSKRDQLLELLRATGNE--RTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVL 583
Cdd:PTZ00110 352 QEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIM 431

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  584 VATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPESDTpLARSLVKVLSGAQQVVPKWLEEV 663
Cdd:PTZ00110 432 IATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYR-LARDLVKVLREAKQPVPPELEKL 510

                        410
                 ....*....|....
gi 18859541  664 AFSAHGTTGFNPRG 677
Cdd:PTZ00110 511 SNERSNGTERRRWG 524
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 504-633 1.20e-57

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: 191.57  E-value: 1.20e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 504 VEQTVVQVDQYSKRDQLL-ELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPV 582
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18859541 583 LVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFF 633
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 301-479 8.53e-57

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: 190.53  E-value: 8.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541   301 TPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAaskfseiqePEAIIVAPTRELINQIYLEARKFAYG 380
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG---------PQALVLAPTRELAEQIYEELKKLGKG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541   381 TCVRPVVVYGGINTGYtIREVLKGCNVLCATPGRLHDLIGRGKiGLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgMPs 460
Cdd:pfam00270  72 LGLKVASLLGGDSRKE-QLEKLKGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146

                         170
                  ....*....|....*....
gi 18859541   461 kEERQTLMFSATYPEDIQR 479
Cdd:pfam00270 147 -KKRQILLLSATLPRNLED 164
DEXDc smart00487
DEAD-like helicases superfamily;
292-506 1.50e-50

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 174.99  E-value: 1.50e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541    292 VSKSGYVKPTPVQKHGIPIISAG-RDLMACAQTGSGKTAAFLLPILQRFMTDGvaaskfseiqEPEAIIVAPTRELINQI 370
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK----------GGRVLVLVPTRELAEQW 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541    371 YLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGC-NVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEM 449
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18859541    450 RKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGvvGGACSDVEQ 506
Cdd:smart00487 151 EKLLKL----LPKNVQLLLLSATPPEEIENLLELFLN-DPVFIDVG--FTPLEPIEQ 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 515-624 2.79e-38

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: 137.73  E-value: 2.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541   515 SKRDQLLELLRATGNERTMVFVETKRSADfIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAARGLD 594
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 18859541   595 IEQVQHVVNFDMPSSIDEYVHRIGRTGRCG 624
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
543-624 3.25e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.07  E-value: 3.25e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541    543 DFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGR 622
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 18859541    623 CG 624
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
512-630 9.80e-18

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 87.48  E-value: 9.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 512 DQYSKRDQLLELLRAT----GNERTMVFVETKRSADFIATFLCQEKISTTSIHG--DRE------QREREKALSDFRLGH 579
Cdd:COG1111 332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18859541 580 CPVLVATSVAARGLDIEQVQHVVNFD-MPSSIdEYVHRIGRTGRcGNTGRAV 630
Cdd:COG1111 412 FNVLVATSVAEEGLDIPEVDLVIFYEpVPSEI-RSIQRKGRTGR-KREGRVV 461
PRK13766 PRK13766
Hef nuclease; Provisional
 516-630 1.78e-14

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 77.22  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  516 KRDQLLELLRAT----GNERTMVFVETKRSADFIATFLCQEKIST------TSIHGDR--EQREREKALSDFRLGHCPVL 583
Cdd:PRK13766 348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVL 427

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18859541  584 VATSVAARGLDIEQVQHVVNFD-MPSSIdEYVHRIGRTGRcGNTGRAV 630
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
 
Name Accession Description Interval E-value
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 245-498 0e+00

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: 543.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 245 SSIFSHYATGINFDKYDDILVDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTG 324
Cdd:cd18052  11 DEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTG 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 325 SGKTAAFLLPILQRFMTDGVAASKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKG 404
Cdd:cd18052  91 SGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKG 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 405 CNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADF 484
Cdd:cd18052 171 CHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEF 250

                       250
                ....*....|....
gi 18859541 485 LKVDYIFLAVGVVG 498
Cdd:cd18052 251 LKEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
276-649 1.67e-158

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 464.62  E-value: 1.67e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 276 IMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAAskfseiqeP 355
Cdd:COG0513   1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------P 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 356 EAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLD 435
Cdd:COG0513  73 QALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLD 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 436 EADRMLDMGFEPEMRKLVASpgMPskEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGACSDVEQTVVQVDQYS 515
Cdd:COG0513 153 EADRMLDMGFIEDIERILKL--LP--KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRD 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 516 KRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAARGLDI 595
Cdd:COG0513 228 KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDI 307

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 18859541 596 EQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPEsDTPLARSLVKVL 649
Cdd:COG0513 308 DDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPD-ERRLLRAIEKLI 360
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 278-498 1.69e-144

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: 420.74  E-value: 1.69e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 278 TFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASK-FSEIQEPE 356
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGrGRRKAYPS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 357 AIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDE 436
Cdd:cd17967  81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18859541 437 ADRMLDMGFEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVG 498
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 257-498 7.01e-123

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: 366.67  E-value: 7.01e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 257 FDKYDDILVDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIL 336
Cdd:cd18051   1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 337 QRFMTDGVAASKFSEI-------QEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLC 409
Cdd:cd18051  81 SQIYEQGPGESLPSESgyygrrkQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 410 ATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADFLKvDY 489
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLD-NY 239


                ....*....
gi 18859541 490 IFLAVGVVG 498
Cdd:cd18051 240 IFLAVGRVG 248
PTZ00110 PTZ00110
helicase; Provisional
 267-677 8.50e-120

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 369.49  E-value: 8.50e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  267 VSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIlqrfMTDGVAA 346
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPA----IVHINAQ 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  347 SKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGL 426
Cdd:PTZ00110 196 PLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNL 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  427 SKVRYLVLDEADRMLDMGFEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKVDYIFLAVGVVG-GACSDVE 505
Cdd:PTZ00110 276 RRVTYLVLDEADRMLDMGFEPQIRKIVSQ----IRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNIK 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  506 QTVVQVDQYSKRDQLLELLRATGNE--RTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVL 583
Cdd:PTZ00110 352 QEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIM 431

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  584 VATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPESDTpLARSLVKVLSGAQQVVPKWLEEV 663
Cdd:PTZ00110 432 IATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYR-LARDLVKVLREAKQPVPPELEKL 510

                        410
                 ....*....|....
gi 18859541  664 AFSAHGTTGFNPRG 677
Cdd:PTZ00110 511 SNERSNGTERRRWG 524
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 277-636 1.71e-95

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 303.26  E-value: 1.71e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  277 MTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRfmtdgVAASKFSeIQepe 356
Cdd:PRK11776   4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK-----LDVKRFR-VQ--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  357 AIIVAPTRELINQIYLEARKFAYGT-CVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLD 435
Cdd:PRK11776  75 ALVLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  436 EADRMLDMGFEPEMRKLVASpgMPskEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGAcSDVEQTVVQVDQyS 515
Cdd:PRK11776 155 EADRMLDMGFQDAIDAIIRQ--AP--ARRQTLLFSATYPEGIAAISQRFQR-DPVEVKVESTHDL-PAIEQRFYEVSP-D 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  516 KRDQLLELLRATGN-ERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAARGLD 594
Cdd:PRK11776 228 ERLPALQRLLLHHQpESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLD 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 18859541  595 IEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPE 636
Cdd:PRK11776 308 IKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 277-631 8.84e-94

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 299.03  E-value: 8.84e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  277 MTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKFSEIQepe 356
Cdd:PRK10590   1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVR--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  357 AIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDE 436
Cdd:PRK10590  78 ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  437 ADRMLDMGFEPEMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGACSDVEQTVVQVDQYSK 516
Cdd:PRK10590 158 ADRMLDMGFIHDIRRVLAK--LPAK--RQNLLFSATFSDDIKALAEKLLH-NPLEIEVARRNTASEQVTQHVHFVDKKRK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  517 RdQLLELLRATGN-ERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAARGLDI 595
Cdd:PRK10590 233 R-ELLSQMIGKGNwQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDI 311

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 18859541  596 EQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVS 631
Cdd:PRK10590 312 EELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALS 347
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 265-660 6.46e-86

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 280.14  E-value: 6.46e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  265 VDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgV 344
Cdd:PLN00206 109 IHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCT--I 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  345 AASKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKI 424
Cdd:PLN00206 187 RSGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDI 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  425 GLSKVRYLVLDEADRMLDMGFEPEMRKLVASPGMPskeerQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGACSDV 504
Cdd:PLN00206 267 ELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAK-DIILISIGNPNRPNKAV 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  505 EQTVVQVDQYSKRDQLLELLRATGNER--TMVFVETKRSADFIAtflcqEKISTT------SIHGDREQREREKALSDFR 576
Cdd:PLN00206 341 KQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLA-----NAITVVtglkalSIHGEKSMKERREVMKSFL 415

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  577 LGHCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNpESDTPLARSLVKVLSGAQQVV 656
Cdd:PLN00206 416 VGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVN-EEDRNLFPELVALLKSSGAAI 494


                 ....
gi 18859541  657 PKWL 660
Cdd:PLN00206 495 PREL 498
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 277-632 8.03e-84

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 271.82  E-value: 8.03e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  277 MTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQrFMTDgvAASKFSeiQEPE 356
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQ-HLLD--FPRRKS--GPPR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  357 AIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGyTIREVLKGC-NVLCATPGRLHDLIGRGKIGLSKVRYLVLD 435
Cdd:PRK11192  76 ILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYM-NHAEVFSENqDIVVATPGRLLQYIKEENFDCRAVETLILD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  436 EADRMLDMGFEPEMRKLVASpgmpSKEERQTLMFSATYP-EDIQRMAADFLKvDYIFLAVgvvggACSDVEQTVVQV--- 511
Cdd:PRK11192 155 EADRMLDMGFAQDIETIAAE----TRWRKQTLLFSATLEgDAVQDFAERLLN-DPVEVEA-----EPSRRERKKIHQwyy 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  512 ---DQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSV 588
Cdd:PRK11192 225 radDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDV 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 18859541  589 AARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSF 632
Cdd:PRK11192 305 AARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 288-492 3.80e-83

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: 261.61  E-value: 3.80e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 288 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKfseiqEPEAIIVAPTRELI 367
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGR-----GPQALVLAPTRELA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 368 NQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEP 447
Cdd:cd00268  76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEE 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 18859541 448 EMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADFLKvDYIFL 492
Cdd:cd00268 156 DVEKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLK-NPVRI 195
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 259-632 1.34e-80

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 264.85  E-value: 1.34e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  259 KYDDILVDvsgsnPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQR 338
Cdd:PRK01297  74 KLEDFVVE-----PQEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQ 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  339 FMTDGVAASKFseIQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREV-LKGCNVLCATPGRLHD 417
Cdd:PRK01297 149 LLQTPPPKERY--MGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLD 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  418 LIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgMPSKEERQTLMFSATYPEDIQRMAADFLkVDYIFLAVGVV 497
Cdd:PRK01297 227 FNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQ--TPRKEERQTLLFSATFTDDVMNLAKQWT-TDPAIVEIEPE 303

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  498 GGACSDVEQTVVQVDQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRL 577
Cdd:PRK01297 304 NVASDTVEQHVYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFRE 383

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18859541  578 GHCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSF 632
Cdd:PRK01297 384 GKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 270-632 3.26e-71

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 242.55  E-value: 3.26e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  270 SNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKF 349
Cdd:PRK04537   2 SDKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  350 SEiqEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTiREVL-KGCNVLCATPGRLHDLIGRGKI-GLS 427
Cdd:PRK04537  82 PE--DPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQ-RELLqQGVDVIIATPGRLIDYVKQHKVvSLH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  428 KVRYLVLDEADRMLDMGFEPEMRKLVASpgMPSKEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGACSDVEQT 507
Cdd:PRK04537 159 ACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMN-EPEKLVVETETITAARVRQR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  508 VVQVDQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATS 587
Cdd:PRK04537 236 IYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATD 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 18859541  588 VAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSF 632
Cdd:PRK04537 316 VAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 279-632 1.02e-70

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 236.79  E-value: 1.02e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  279 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvAASKFSEIQEPEAI 358
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSH--PAPEDRKVNQPRAL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  359 IVAPTRELINQIYLEARKFAYGTCVRPVVVYGGinTGYTI-REVL-KGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDE 436
Cdd:PRK04837  88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGG--DGYDKqLKVLeSGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  437 ADRMLDMGFEPEMRKLVASpgMPSKEERQTLMFSATYPEDIQRMAADFLkvdyiflavgvvggacSDVEQTVVQVDQ--- 513
Cdd:PRK04837 166 ADRMFDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHM----------------NNPEYVEVEPEQktg 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  514 --------Y-SKRDQ---LLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCP 581
Cdd:PRK04837 228 hrikeelfYpSNEEKmrlLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLD 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18859541  582 VLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSF 632
Cdd:PRK04837 308 ILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 277-632 2.35e-70

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 241.68  E-value: 2.35e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  277 MTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMtdgvaaskfSEIQEPE 356
Cdd:PRK11634   6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD---------PELKAPQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  357 AIIVAPTRELINQIYLEARKFA-YGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLD 435
Cdd:PRK11634  77 ILVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  436 EADRMLDMGFEPEMRKLVASpgMPskEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGACSDVEQTVVQVDQYS 515
Cdd:PRK11634 157 EADEMLRMGFIEDVETIMAQ--IP--EGHQTALFSATMPEAIRRITRRFMK-EPQEVRIQSSVTTRPDISQSYWTVWGMR 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  516 KRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAARGLDI 595
Cdd:PRK11634 232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 18859541  596 EQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSF 632
Cdd:PRK11634 312 ERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 290-492 6.21e-66

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: 216.08  E-value: 6.21e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 290 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIL-----QRFMTDGvaaskfseiQEPEAIIVAPTR 364
Cdd:cd17966   3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaQPPLERG---------DGPIVLVLAPTR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 365 ELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMG 444
Cdd:cd17966  74 ELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18859541 445 FEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKvDYIFL 492
Cdd:cd17966 154 FEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRRLAEDFLK-DYIQV 196
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 267-486 5.88e-61

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: 203.76  E-value: 5.88e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 267 VSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIL-----QRFMT 341
Cdd:cd17953   2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikdQRPVK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 342 DGvaaskfseiQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIG- 420
Cdd:cd17953  82 PG---------EGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTa 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859541 421 -RGKI-GLSKVRYLVLDEADRMLDMGFEPEMRKLVaspgMPSKEERQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd17953 153 nNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIV----NNIRPDRQTVLFSATFPRKVEALARKVLH 216
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 288-485 1.69e-60

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: 201.87  E-value: 1.69e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 288 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMtdgvaASKFSEIQE-PEAIIVAPTREL 366
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-----DQRELEKGEgPIAVIVAPTREL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 367 INQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFE 446
Cdd:cd17952  76 AQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFE 155

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 18859541 447 PEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFL 485
Cdd:cd17952 156 YQVRSIVGH----VRPDRQTLLFSATFKKKIEQLARDIL 190
PTZ00424 PTZ00424
helicase 45; Provisional
 270-636 1.24e-58

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 203.52  E-value: 1.24e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  270 SNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAAskf 349
Cdd:PTZ00424  21 SNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNAC--- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  350 seiqepEAIIVAPTRELINQI---------YLEARKFAygtCVrpvvvyGGINTGYTIREVLKGCNVLCATPGRLHDLIG 420
Cdd:PTZ00424  98 ------QALILAPTRELAQQIqkvvlalgdYLKVRCHA---CV------GGTVVRDDINKLKAGVHMVVGTPGRVYDMID 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  421 RGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgMPSkeERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGA 500
Cdd:PTZ00424 163 KRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKK--LPP--DVQVALFSATMPNEILELTTKFMR-DPKRILVKKDELT 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  501 CSDVEQTVVQVDQYS-KRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGH 579
Cdd:PTZ00424 238 LEGIRQFYVAVEKEEwKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGS 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18859541  580 CPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPE 636
Cdd:PTZ00424 318 TRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPD 374
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 504-633 1.20e-57

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: 191.57  E-value: 1.20e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 504 VEQTVVQVDQYSKRDQLL-ELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPV 582
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18859541 583 LVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFF 633
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 265-495 1.71e-57

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: 195.23  E-value: 1.71e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 265 VDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIL-----QRF 339
Cdd:cd18049  12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIvhinhQPF 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 340 MTDGvaaskfseiQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLI 419
Cdd:cd18049  92 LERG---------DGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18859541 420 GRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVG 495
Cdd:cd18049 163 EAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRQLAEDFLK-DYIHINIG 233
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 292-486 4.28e-57

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: 193.31  E-value: 4.28e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 292 VSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRfMTDGVAASKFSEIQEPEAIIVAPTRELINQIY 371
Cdd:cd17945   5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVY-ISRLPPLDEETKDDGPYALILAPTRELAQQIE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 372 LEARKFAYGTCVRPVVVYGGIN---TGYTIRevlKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPE 448
Cdd:cd17945  84 EETQKFAKPLGIRVVSIVGGHSieeQAFSLR---NGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18859541 449 MRKLVASpgMPS------------------KEERQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd17945 161 VTKILDA--MPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLR 214
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 288-495 7.41e-57

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: 192.03  E-value: 7.41e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 288 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAAskfseiqEPEAIIVAPTRELI 367
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-------GLRALILAPTRELA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 368 NQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVL-KGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFE 446
Cdd:cd17957  74 SQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSiTKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFR 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18859541 447 PEMRKLVASPGMPSKeerQTLMFSATYPEDIQRMAADFLKvDYIFLAVG 495
Cdd:cd17957 154 EQTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMK-DPIRIIVG 198
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 301-479 8.53e-57

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: 190.53  E-value: 8.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541   301 TPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAaskfseiqePEAIIVAPTRELINQIYLEARKFAYG 380
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG---------PQALVLAPTRELAEQIYEELKKLGKG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541   381 TCVRPVVVYGGINTGYtIREVLKGCNVLCATPGRLHDLIGRGKiGLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgMPs 460
Cdd:pfam00270  72 LGLKVASLLGGDSRKE-QLEKLKGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146

                         170
                  ....*....|....*....
gi 18859541   461 kEERQTLMFSATYPEDIQR 479
Cdd:pfam00270 147 -KKRQILLLSATLPRNLED 164
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 286-492 4.11e-55

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: 187.79  E-value: 4.11e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 286 DSLSKNVSKSGYVKPTPVQKHGI-PIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKfSEIQepeAIIVAPTR 364
Cdd:cd17964   3 PSLLKALTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRR-SGVS---ALIISPTR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 365 ELINQIYLEARKFAYG-TCVRPVVVYGGINTGYTIREVLK-GCNVLCATPGRLHDLIG--RGKIGLSKVRYLVLDEADRM 440
Cdd:cd17964  79 ELALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 18859541 441 LDMGFEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADFLKVDYIFL 492
Cdd:cd17964 159 LDMGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 290-486 1.49e-53

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: 183.05  E-value: 1.49e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 290 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILqrFMTDGVAASKFSEIQePEAIIVAPTRELINQ 369
Cdd:cd17958   3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF--IHLDLQPIPREQRNG-PGVLVLTPTRELALQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 370 IYLEARKFAYGTcVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEM 449
Cdd:cd17958  80 IEAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18859541 450 RKLVaspgMPSKEERQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd17958 159 RKIL----LDIRPDRQTIMTSATWPDGVRRLAQSYLK 191
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 265-495 1.12e-52

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: 183.29  E-value: 1.12e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 265 VDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIL-----QRF 339
Cdd:cd18050  50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIvhinhQPY 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 340 MTDGvaaskfseiQEPEAIIVAPTRELINQIYLEArkFAYGTCVR--PVVVYGGINTGYTIREVLKGCNVLCATPGRLHD 417
Cdd:cd18050 130 LERG---------DGPICLVLAPTRELAQQVQQVA--DDYGKSSRlkSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 198

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859541 418 LIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVG 495
Cdd:cd18050 199 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRQLAEDFLR-DYVQINIG 271
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 279-486 1.33e-52

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: 180.50  E-value: 1.33e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 279 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAaskfseiqePEAI 358
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYG---------IFAL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 359 IVAPTRELINQIyleARKF-AYGTC--VRPVVVYGGINtgyTIREVL---KGCNVLCATPGRLHDLI---GRGKIGLSKV 429
Cdd:cd17955  72 VLTPTRELAYQI---AEQFrALGAPlgLRCCVIVGGMD---MVKQALelsKRPHIVVATPGRLADHLrssDDTTKVLSRV 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18859541 430 RYLVLDEADRMLDMGFEPEMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd17955 146 KFLVLDEADRLLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGN 198
DEXDc smart00487
DEAD-like helicases superfamily;
292-506 1.50e-50

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 174.99  E-value: 1.50e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541    292 VSKSGYVKPTPVQKHGIPIISAG-RDLMACAQTGSGKTAAFLLPILQRFMTDGvaaskfseiqEPEAIIVAPTRELINQI 370
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK----------GGRVLVLVPTRELAEQW 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541    371 YLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGC-NVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEM 449
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18859541    450 RKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGvvGGACSDVEQ 506
Cdd:smart00487 151 EKLLKL----LPKNVQLLLLSATPPEEIENLLELFLN-DPVFIDVG--FTPLEPIEQ 200
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 288-486 3.06e-50

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: 173.98  E-value: 3.06e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 288 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvaasKFSEIQEPEAIIVAPTRELI 367
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY------RPKKKAATRVLVLVPTRELA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 368 NQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGK-IGLSKVRYLVLDEADRMLDMGFE 446
Cdd:cd17947  75 MQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFA 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 18859541 447 PEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd17947 155 DELKEILRL----CPRTRQTMLFSATMTDEVKDLAKLSLN 190
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 278-472 4.18e-49

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: 170.96  E-value: 4.18e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 278 TFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvaASKFSeiqepeA 357
Cdd:cd17954   1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---PQRFF------A 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 358 IIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGK-IGLSKVRYLVLDE 436
Cdd:cd17954  72 LVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDE 151

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 18859541 437 ADRMLDMGFEPEMRKLVASpgMPSkeERQTLMFSAT 472
Cdd:cd17954 152 ADRLLNMDFEPEIDKILKV--IPR--ERTTYLFSAT 183
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 288-492 3.60e-48

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: 168.92  E-value: 3.60e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 288 LSKN-VSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvaASKFSEIQEPEAIIVAPTREL 366
Cdd:cd17949   1 LVSHlKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSL---EPRVDRSDGTLALVLVPTREL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 367 INQIYLEARKFaygtcVRPV--VVYGGINTGYT-------IRevlKGCNVLCATPGRLHDLIGRGK-IGLSKVRYLVLDE 436
Cdd:cd17949  78 ALQIYEVLEKL-----LKPFhwIVPGYLIGGEKrksekarLR---KGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDE 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18859541 437 ADRMLDMGFEPEMRKLV-----------ASPGMPSKeeRQTLMFSATYPEDIQRMaADFLKVDYIFL 492
Cdd:cd17949 150 ADRLLDMGFEKDITKILellddkrskagGEKSKPSR--RQTVLVSATLTDGVKRL-AGLSLKDPVYI 213
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 290-481 4.24e-47

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: 165.59  E-value: 4.24e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 290 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQrFMTDGVAASKFSEIQEPEAIIVAPTRELINQ 369
Cdd:cd17951   3 KGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIM-FALEQEKKLPFIKGEGPYGLIVCPSRELARQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 370 IY---------LEARKFAYgtcVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRM 440
Cdd:cd17951  82 THevieyyckaLQEGGYPQ---LRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18859541 441 LDMGFEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMA 481
Cdd:cd17951 159 IDMGFEEDIRTIFSY----FKGQRQTLLFSATMPKKIQNFA 195
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 278-487 5.48e-46

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: 162.47  E-value: 5.48e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 278 TFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvaaskfSEIQEPEA 357
Cdd:cd17959   2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAH-------SPTVGARA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 358 IIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEA 437
Cdd:cd17959  75 LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEA 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18859541 438 DRMLDMGFEPEMRKLVASpgMPskEERQTLMFSATYPEdiqrMAADFLKV 487
Cdd:cd17959 155 DRLFEMGFAEQLHEILSR--LP--ENRQTLLFSATLPK----LLVEFAKA 196
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 279-486 5.61e-46

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: 162.47  E-value: 5.61e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 279 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQrfMTDgvaaSKFSEIQepeAI 358
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILE--KID----PKKDVIQ---AL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 359 IVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEAD 438
Cdd:cd17940  72 ILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEAD 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18859541 439 RMLDMGFEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd17940 152 KLLSQDFQPIIEKILNF----LPKERQILLFSATFPLTVKNFMDRHMH 195
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 279-482 2.28e-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: 158.25  E-value: 2.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 279 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMtdgvaaskfseiqepeAI 358
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV----------------AL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 359 IVAPTRELINQIYLEARKFAY---GTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLD 435
Cdd:cd17938  65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18859541 436 EADRMLDMGFEPEMRKLVAS-PGMPSKEER-QTLMFSAT-YPEDIQRMAA 482
Cdd:cd17938 145 EADRLLSQGNLETINRIYNRiPKITSDGKRlQVIVCSATlHSFEVKKLAD 194
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 292-481 4.80e-43

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: 154.27  E-value: 4.80e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 292 VSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRfMTDGVAASKFSEIQepeAIIVAPTRELINQIY 371
Cdd:cd17960   5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEI-LLKRKANLKKGQVG---ALIISPTRELATQIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 372 LEARKFA--YGTCVRPVVVYGGINTGYTIREVL-KGCNVLCATPGRLHDLIGR--GKIGLSKVRYLVLDEADRMLDMGFE 446
Cdd:cd17960  81 EVLQSFLehHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDEADRLLDLGFE 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 18859541 447 PEMRKLVASpgMPskEERQTLMFSATYPEDIQRMA 481
Cdd:cd17960 161 ADLNRILSK--LP--KQRRTGLFSATQTDAVEELI 191
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 290-494 4.30e-42

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: 151.67  E-value: 4.30e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 290 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFM------TDGVAaskfseiqepeAIIVAPT 363
Cdd:cd17941   3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwtpEDGLG-----------ALIISPT 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 364 RELINQIYLEARKFAYGTCVRPVVVYGGINTGYTiREVLKGCNVLCATPGR-LHDLIGRGKIGLSKVRYLVLDEADRMLD 442
Cdd:cd17941  72 RELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE-KERINRMNILVCTPGRlLQHMDETPGFDTSNLQMLVLDEADRILD 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 18859541 443 MGFEPEMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADFLKvDYIFLAV 494
Cdd:cd17941 151 MGFKETLDAIVEN--LPKS--RQTLLFSATQTKSVKDLARLSLK-NPEYISV 197
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 288-486 2.96e-41

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: 149.24  E-value: 2.96e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 288 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvaaskfsEIQEPEAIIVAPTRELI 367
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT---------EHRNPSALILTPTRELA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 368 NQIYLEARKFAYGTC-VRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFE 446
Cdd:cd17962  72 VQIEDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQ 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18859541 447 PE-MRKLVASPGMPskeerQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd17962 152 QQvLDILENISHDH-----QTILVSATIPRGIEQLAGQLLQ 187
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 288-478 1.31e-39

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: 145.84  E-value: 1.31e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 288 LSKNVSKSGYVKPTPVQKHGIP-IISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKFSEIQEPEAIIVAPTREL 366
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTREL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 367 INQI--YLEArkFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLS---KVRYLVLDEADRML 441
Cdd:cd17946  81 AVQVkdHLKA--IAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLAnlkSLRFLVLDEADRML 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18859541 442 DMG-FEpEMRKL---VASPGMPSKEERQTLMFSATYPEDIQ 478
Cdd:cd17946 159 EKGhFA-ELEKIlelLNKDRAGKKRKRQTFVFSATLTLDHQ 198
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 288-486 1.24e-38

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: 141.95  E-value: 1.24e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 288 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvAASKFSEIQEPEAIIVAPTRELI 367
Cdd:cd17961   5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILK---AKAESGEEQGTRALILVPTRELA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 368 NQIYLEARKFAYGTC--VRPVVVYGGINTGyTIREVLKGC-NVLCATPGRLHDLIGRGKIGL-SKVRYLVLDEADRMLDM 443
Cdd:cd17961  82 QQVSKVLEQLTAYCRkdVRVVNLSASSSDS-VQRALLAEKpDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 18859541 444 GFEPEMRKLVAS-PGMPskeerQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd17961 161 GYEEDLKSLLSYlPKNY-----QTFLMSATLSEDVEALKKLVLH 199
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 515-624 2.79e-38

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: 137.73  E-value: 2.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541   515 SKRDQLLELLRATGNERTMVFVETKRSADfIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAARGLD 594
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 18859541   595 IEQVQHVVNFDMPSSIDEYVHRIGRTGRCG 624
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 290-492 2.83e-38

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: 140.96  E-value: 2.83e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 290 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRfmtdgVAASKFSEIQEPEAIIVAPTRELINQ 369
Cdd:cd17942   3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEL-----LYKLKFKPRNGTGVIIISPTRELALQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 370 IYLEARKF-AYGTCVRPVVVyGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSK-VRYLVLDEADRMLDMGFEP 447
Cdd:cd17942  78 IYGVAKELlKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFEE 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 18859541 448 EMRKLVASpgMPSkeERQTLMFSATYPEDIQRMAADFLKVDYIFL 492
Cdd:cd17942 157 EMRQIIKL--LPK--RRQTMLFSATQTRKVEDLARISLKKKPLYV 197
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 290-486 1.54e-36

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 135.85  E-value: 1.54e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 290 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMtdgvaaskfSEIQEPEAIIVAPTRELINQ 369
Cdd:cd17943   3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD---------LERRHPQVLILAPTREIAVQ 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 370 IYlearkfaygTCVRPVVVY-GGINTGYTI--------REVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRM 440
Cdd:cd17943  74 IH---------DVFKKIGKKlEGLKCEVFIggtpvkedKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKL 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 18859541 441 LDMGFEPEMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd17943 145 MEGSFQKDVNWIFSS--LPKN--KQVIAFSATYPKNLDNLLARYMR 186
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 279-486 6.25e-35

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: 131.70  E-value: 6.25e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 279 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGvaaskfseiQEPEAI 358
Cdd:cd17950   4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD---------GQVSVL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 359 IVAPTRELINQIYLEARKFA-YGTCVRPVVVYGGINTGYTIrEVLK--GCNVLCATPGRLHDLIGRGKIGLSKVRYLVLD 435
Cdd:cd17950  75 VICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDI-EVLKnkCPHIVVGTPGRILALVREKKLKLSHVKHFVLD 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 18859541 436 EADRMLDmgfEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd17950 154 ECDKMLE---QLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQ 201
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 281-485 1.14e-33

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: 127.83  E-value: 1.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 281 EAGLCDSLSKNVSKSGYVKPTPVQKHGI-PIISaGRDLMACAQTGSGKTAAFLLPILQRFmtdgvaASKFSEIQepeAII 359
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIvPIIK-GRDVIAQAQSGTGKTATFSIGALQRI------DTTVRETQ---ALV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 360 VAPTRELINQI---------YLEARKFAygtCVrpvvvyGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVR 430
Cdd:cd17939  71 LAPTRELAQQIqkvvkalgdYMGVKVHA---CI------GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIK 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18859541 431 YLVLDEADRMLDMGFEPEMRKLVASpgMPSkeERQTLMFSATYPEDIQRMAADFL 485
Cdd:cd17939 142 MFVLDEADEMLSRGFKDQIYDIFQF--LPP--ETQVVLFSATMPHEVLEVTKKFM 192
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 288-490 6.84e-33

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 126.71  E-value: 6.84e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 288 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKfsEIQEPEAIIVAPTRELI 367
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEG--PFNAPRGLVITPSRELA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 368 NQIYLEARKFAYGTCVRPVVVYGGiNTGYTIRE-VLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFE 446
Cdd:cd17948  79 EQIGSVAQSLTEGLGLKVKVITGG-RTKRQIRNpHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18859541 447 PEMRKL-----VASPGMPSKEER----QTLMFSATYPEDIQRMAADFLKVDYI 490
Cdd:cd17948 158 EKLSHFlrrfpLASRRSENTDGLdpgtQLVLVSATMPSGVGEVLSKVIDVDSI 210
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 279-486 1.76e-32

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: 124.48  E-value: 1.76e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 279 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvaaskfsEIQEPEAI 358
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDT---------SLKATQAL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 359 IVAPTRELINQI---------YLEARKFAygtCVrpvvvyGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKV 429
Cdd:cd18046  72 VLAPTRELAQQIqkvvmalgdYMGIKCHA---CI------GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYI 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18859541 430 RYLVLDEADRMLDMGFEPEMRKLVASpgMPskEERQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd18046 143 KMFVLDEADEMLSRGFKDQIYDIFQK--LP--PDTQVVLLSATMPNDVLEVTTKFMR 195
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 287-486 3.15e-32

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: 123.45  E-value: 3.15e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 287 SLSKNVSKSGYVKPTPVQKHGIPIISAG--RDLMACAQTGSGKTAAFLLPILQRFMTDgvaaskfseIQEPEAIIVAPTR 364
Cdd:cd17963   4 ELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPT---------LKSPQALCLAPTR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 365 ELINQIYLEARKFAYgtcvrpvvvYGGINTGYTIREVLKGCN------VLCATPGRLHDLIGRGKIGLSKVRYLVLDEAD 438
Cdd:cd17963  75 ELARQIGEVVEKMGK---------FTGVKVALAVPGNDVPRGkkitaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEAD 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18859541 439 RMLDM-GFEPEMRKLVASPGMPSkeerQTLMFSATYPEDIQRMAADFLK 486
Cdd:cd17963 146 VMLDTqGHGDQSIRIKRMLPRNC----QILLFSATFPDSVRKFAEKIAP 190
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 302-490 6.47e-32

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: 123.03  E-value: 6.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 302 PVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvaASKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGT 381
Cdd:cd17944  15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQED---QQPRKRGRAPKVLVLAPTRELANQVTKDFKDITRKL 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 382 CVrpVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLV-ASPGMPS 460
Cdd:cd17944  92 SV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsVSYKKDS 169

                       170       180       190
                ....*....|....*....|....*....|
gi 18859541 461 KEERQTLMFSATYPEDIQRMAADFLKVDYI 490
Cdd:cd17944 170 EDNPQTLLFSATCPDWVYNVAKKYMKSQYE 199
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 279-485 3.52e-30

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: 117.95  E-value: 3.52e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 279 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvaaskfsEIQEPEAI 358
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDI---------QVRETQAL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 359 IVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEAD 438
Cdd:cd18045  72 ILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEAD 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 18859541 439 RMLDMGFEPEM----RKLVASPgmpskeerQTLMFSATYPEDIQRMAADFL 485
Cdd:cd18045 152 EMLNKGFKEQIydvyRYLPPAT--------QVVLVSATLPQDILEMTNKFM 194
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 288-492 1.41e-28

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


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 114.27  E-value: 1.41e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 288 LSKNVSKSGYVKPTPVQKHGIPIISAG---------RDLMACAQTGSGKTAAFLLPILQRFMTDGVAaskfsEIQepeAI 358
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVP-----RLR---AL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 359 IVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGC--------NVLCATPGRLHDLIgRGKIG--LSK 428
Cdd:cd17956  73 IVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDHL-NSTPGftLKH 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 429 VRYLVLDEADRMLDMGFEPEMRKLVASPGMPSKEER----------------QTLMFSATYPEDIQRMAAdfLKVDYIFL 492
Cdd:cd17956 152 LRFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLgsfgdanllersvrplQKLLFSATLTRDPEKLSS--LKLHRPRL 229
HELICc smart00490
helicase superfamily c-terminal domain;
543-624 3.25e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.07  E-value: 3.25e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541    543 DFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGR 622
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 18859541    623 CG 624
Cdd:smart00490  81 AG 82
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 288-484 2.81e-21

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: 93.60  E-value: 2.81e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 288 LSKNVSKSGYVKPTPVQKHGIPIISAGR----------------DLMACAQTGSGKTAAFLLPILQRFMTDGVAASKFSE 351
Cdd:cd17965  19 LKGSNKTDEEIKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPFEEAE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 352 IQE--------PEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYtIREVL---KGCNVLCATPGRLHDLIG 420
Cdd:cd17965  99 EEYesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSY-QRLQLafkGRIDILVTTPGKLASLAK 177

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18859541 421 -RGKIgLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADF 484
Cdd:cd17965 178 sRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APKL--KHLILCSATIPKEFDKTLRKL 237
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
312-634 2.40e-20

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 95.48  E-value: 2.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 312 SAGRDLMACAQTGSGKTAAFLLpILQRFMTDGVAaskfseiqepeaIIVAPTRELINQIYLEARKFaygtcvrpvvvYGG 391
Cdd:COG1061  98 RGGGRGLVVAPTGTGKTVLALA-LAAELLRGKRV------------LVLVPRRELLEQWAEELRRF-----------LGD 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 392 INTGYTIREVlkGCNVLCATPGRLHDLIGRGKIGlSKVRYLVLDEA--------DRMLDMgFEPemRKLV---ASPG-MP 459
Cdd:COG1061 154 PLAGGGKKDS--DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAhhagapsyRRILEA-FPA--AYRLgltATPFrSD 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 460 SKEERQTLMFSATYPEDIQRMAADFLKVDYIFLAVGV-------VGGACSDVEQTVVQVDQYSKRDQLLELLRATGN-ER 531
Cdd:COG1061 228 GREILLFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRVdltderaEYDALSERLREALAADAERKDKILRELLREHPDdRK 307

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 532 TMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAARGLDIEQVQHVVNFDMPSSID 611
Cdd:COG1061 308 TLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPR 387

                       330       340
                ....*....|....*....|...
gi 18859541 612 EYVHRIGRTGRCGNTGRAVSFFN 634
Cdd:COG1061 388 EFIQRLGRGLRPAPGKEDALVYD 410
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 270-481 3.61e-19

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: 87.00  E-value: 3.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 270 SNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAG--RDLMACAQTGSGKTAAFLLPILQRfmtdgVAAS 347
Cdd:cd18048  11 TSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR-----VDAL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 348 KfseiQEPEAIIVAPTRELINQ---IYLEARKFaygtCVrpvvvygGINTGYTIR--EVLKGCN----VLCATPGRLHDL 418
Cdd:cd18048  86 K----LYPQCLCLSPTFELALQtgkVVEEMGKF----CV-------GIQVIYAIRgnRPGKGTDieaqIVIGTPGTVLDW 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18859541 419 IGRGK-IGLSKVRYLVLDEADRMLDM-GFEPEMRKLVASpgMPSkeERQTLMFSATYPEDIQRMA 481
Cdd:cd18048 151 CFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKRS--MPK--ECQMLLFSATFEDSVWAFA 211
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
512-630 9.80e-18

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 87.48  E-value: 9.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 512 DQYSKRDQLLELLRAT----GNERTMVFVETKRSADFIATFLCQEKISTTSIHG--DRE------QREREKALSDFRLGH 579
Cdd:COG1111 332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18859541 580 CPVLVATSVAARGLDIEQVQHVVNFD-MPSSIdEYVHRIGRTGRcGNTGRAV 630
Cdd:COG1111 412 FNVLVATSVAEEGLDIPEVDLVIFYEpVPSEI-RSIQRKGRTGR-KREGRVV 461
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
311-636 1.56e-17

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 85.96  E-value: 1.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 311 ISAGRDLMACAQTGSGKTAAFLLPILqrfMTDGVAaskfseiqepeaIIVAPtreLI----NQI-YLEARKFAygtcvrp 385
Cdd:COG0514  29 VLAGRDALVVMPTGGGKSLCYQLPAL---LLPGLT------------LVVSP---LIalmkDQVdALRAAGIR------- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 386 vVVYggIN---TGYTIREVLKGCN-----VLCATPGRL-----HDLIGRGKIGLskvryLVLDEA--------Drmldmg 444
Cdd:COG0514  84 -AAF--LNsslSAEERREVLRALRagelkLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------ 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 445 FEPEMRKLV----ASPGMPskeerqTLMFSATYP----EDIQRM--AADFLKVDY------IFLAVgvvggacsdveqtv 508
Cdd:COG0514 150 FRPDYRRLGelreRLPNVP------VLALTATATprvrADIAEQlgLEDPRVFVGsfdrpnLRLEV-------------- 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 509 VQVDQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSv 588
Cdd:COG0514 210 VPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI- 288

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 18859541 589 aARGL--DIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPE 636
Cdd:COG0514 289 -AFGMgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
PRK13766 PRK13766
Hef nuclease; Provisional
 516-630 1.78e-14

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 77.22  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  516 KRDQLLELLRAT----GNERTMVFVETKRSADFIATFLCQEKIST------TSIHGDR--EQREREKALSDFRLGHCPVL 583
Cdd:PRK13766 348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVL 427

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18859541  584 VATSVAARGLDIEQVQHVVNFD-MPSSIdEYVHRIGRTGRcGNTGRAV 630
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 516-630 5.68e-14

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: 69.69  E-value: 5.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 516 KRDQLLELLR-------ATGNERTMVFVETKRSADFIATFLCQEK--------ISTTSIHGDR--EQREREKALSDFRLG 578
Cdd:cd18801  10 KLEKLEEIVKehfkkkqEGSDTRVIIFSEFRDSAEEIVNFLSKIRpgiratrfIGQASGKSSKgmSQKEQKEVIEQFRKG 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18859541 579 HCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRcGNTGRAV 630
Cdd:cd18801  90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 514-619 1.61e-13

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: 68.39  E-value: 1.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 514 YSKRDQLLELLRA----TGNERTMVFVETKRSADFIATFLCQEKISTTSIHGD---------------REQREREKALSD 574
Cdd:cd18802   6 IPKLQKLIEILREyfpkTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDK 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18859541 575 FRLGHCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGR 619
Cdd:cd18802  86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 281-630 2.90e-12

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: 70.25  E-value: 2.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 281 EAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAAskfseiqepeAIIV 360
Cdd:COG1205  38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGAT----------ALYL 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 361 APTRELINQIYLEARKFA--YGTCVRPVVVYGGinTGYTIR-EVLKGCNVLCATPGRLHDLI--GRGKIG--LSKVRYLV 433
Cdd:COG1205 108 YPTKALARDQLRRLRELAeaLGLGVRVATYDGD--TPPEERrWIREHPDIVLTNPDMLHYGLlpHHTRWArfFRNLRYVV 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 434 LDEA---------------DRMLDMgfepeMRKLVASPgmpskeerQTLMFSATY--PEDiqrMAADFLKVDyiFLAVGV 496
Cdd:COG1205 186 IDEAhtyrgvfgshvanvlRRLRRI-----CRHYGSDP--------QFILASATIgnPAE---HAERLTGRP--VTVVDE 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 497 VGGACSdvEQTVV-----QVDQYSKRDQLLE----LLRATGNE-RTMVFVETKRSADFIATFL---CQEKISTTSIHGDR 563
Cdd:COG1205 248 DGSPRG--ERTFVlwnppLVDDGIRRSALAEaarlLADLVREGlRTLVFTRSRRGAELLARYArraLREPDLADRVAAYR 325

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18859541 564 ------EQREREKALSDFRLGhcpVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAV 630
Cdd:COG1205 326 agylpeERREIERGLRSGELL---GVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
292-622 4.15e-12

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 69.15  E-value: 4.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 292 VSKSGYVKPTPVQKHGIP-IISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGvaaskfseiqepEAIIVAPTRELINQI 370
Cdd:COG1204  15 LKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------KALYIVPLRALASEK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 371 YLEARKF--AYGtcVRPVVVYGGINTGytiREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEA----------- 437
Cdd:COG1204  83 YREFKRDfeELG--IKVGVSTGDYDSD---DEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddesrgpt 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 438 -----DRMLDMGfePEMRKLVASPGMPSkeerqtlmfsatyPEDIQR-MAADFLKVDY--IFLAVGVvggacsdVEQTVV 509
Cdd:COG1204 158 levllARLRRLN--PEAQIVALSATIGN-------------AEEIAEwLDAELVKSDWrpVPLNEGV-------LYDGVL 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 510 QVDQYSKR--DQLLELLRAT--GNERTMVFVETKRSA-----------------------DFIATFL--CQEKISTTSI- 559
Cdd:COG1204 216 RFDDGSRRskDPTLALALDLleEGGQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELleVSEETHTNEKl 295

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 560 -----------HGD--REQRER-EKAlsdFRLGHCPVLVATSVAARGL----------DIEQvqhvvNFDMPSSIDEYVH 615
Cdd:COG1204 296 adclekgvafhHAGlpSELRRLvEDA---FREGLIKVLVATPTLAAGVnlparrviirDTKR-----GGMVPIPVLEFKQ 367


                ....*..
gi 18859541 616 RIGRTGR 622
Cdd:COG1204 368 MAGRAGR 374
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 515-618 7.25e-12

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: 63.26  E-value: 7.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 515 SKRDQLLELLRA--TGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFR--LGHCPVLVATSVAA 590
Cdd:cd18793  11 GKLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGG 90

                        90       100       110
                ....*....|....*....|....*....|....
gi 18859541 591 RGLDIEQVQHVVNFDMP--SSIDEY----VHRIG 618
Cdd:cd18793  91 VGLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 278-481 8.61e-12

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: 65.13  E-value: 8.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 278 TFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAG--RDLMACAQTGSGKTAAFLLPILQRFMtdgvAASKFSeiqep 355
Cdd:cd18047   2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE----PANKYP----- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 356 EAIIVAPTRELINQ---IYLEARKFAYGTCVRPVVVYGGINTGYTIREvlkgcNVLCATPGRLHDLIGRGK-IGLSKVRY 431
Cdd:cd18047  73 QCLCLSPTYELALQtgkVIEQMGKFYPELKLAYAVRGNKLERGQKISE-----QIVIGTPGTVLDWCSKLKfIDPKKIKV 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18859541 432 LVLDEADRMldmgfepemrklVASPGMPSKEER---------QTLMFSATYPEDIQRMA 481
Cdd:cd18047 148 FVLDEADVM------------IATQGHQDQSIRiqrmlprncQMLLFSATFEDSVWKFA 194
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 310-437 2.12e-11

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 63.05  E-value: 2.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 310 IISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvaaskfseiQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVY 389
Cdd:cd17921  13 LYLSGDSVLVSAPTSSGKTLIAELAILRALAT-----------SGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 18859541 390 GGINTGytiREVLKGCNVLCATPGRLHDLIGRGKI-GLSKVRYLVLDEA 437
Cdd:cd17921  82 GDPSVN---KLLLAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 512-633 1.02e-10

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: 59.91  E-value: 1.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 512 DQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAAR 591
Cdd:cd18794  13 KKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGM 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18859541 592 GLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFF 633
Cdd:cd18794  93 GIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 314-452 2.77e-10

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: 58.95  E-value: 2.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 314 GRDLMACAQTGSGKTAAFLLPILQRFmtdgvaaskfsEIQEPEAIIVAPTRELINQIYLEARKFAygtcvRPVVVYGGIN 393
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLL-----------LKKGKKVLVLVPTKALALQTAERLRELF-----GPGIRVAVLV 64

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859541 394 TGYTIREVLKGCN----VLCATPGRLHDLIGR-GKIGLSKVRYLVLDEADRMLDMGFEPEMRKL 452
Cdd:cd00046  65 GGSSAEEREKNKLgdadIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDL 128
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 515-620 1.31e-09

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 61.39  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 515 SKRDQLLELLR--ATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGH-CPV-LVATSVAA 590
Cdd:COG0553 533 AKLEALLELLEelLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLKAGG 612

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 18859541 591 RGLDIEQVQHVVNFDMP-------SSIDEyVHRIGRT 620
Cdd:COG0553 613 EGLNLTAADHVIHYDLWwnpaveeQAIDR-AHRIGQT 648
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 311-437 4.62e-09

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: 56.44  E-value: 4.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 311 ISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvaaskfseiQEPEAIIVAPTRELINQIYLEARKFAYGtCVRPVVV-- 388
Cdd:cd17923  12 ARAGRSVVVTTGTASGKSLCYQLPILEALLRD----------PGSRALYLYPTKALAQDQLRSLRELLEQ-LGLGIRVat 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18859541 389 YGGiNTGYTIREVL--KGCNVLCATPGRLHDLIGRGKIG----LSKVRYLVLDEA 437
Cdd:cd17923  81 YDG-DTPREERRAIirNPPRILLTNPDMLHYALLPHHDRwarfLRNLRYVVLDEA 134
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
300-630 6.88e-09

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 59.35  E-value: 6.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 300 PTPVQKHGIPIISAGRDLMACAQTGSGKT-AAFlLPILQRFMTDGVAASKFSEIQepeAIIVAPTRELINQIY------L 372
Cdd:COG1201  25 PTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGLR---VLYISPLKALANDIErnlrapL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 373 EARKFAYGTCVRPVVVygGINTGYT-----IREVLKGCNVLCATPGRLHDLIG--RGKIGLSKVRYLVLDE----AD--R 439
Cdd:COG1201 101 EEIGEAAGLPLPEIRV--GVRTGDTpaserQRQRRRPPHILITTPESLALLLTspDARELLRGVRTVIVDEihalAGskR 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 440 --MLDMGFEpEMRKLVASP----GMpskeerqtlmfSATY--PEDiqrmAADFLkvdyiflavgvvGGACSDVEQTVVQV 511
Cdd:COG1201 179 gvHLALSLE-RLRALAPRPlqriGL-----------SATVgpLEE----VARFL------------VGYEDPRPVTIVDA 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 512 DqYSKR---------------------------DQLLELLRATGNerTMVFVETKRSADFIATFLCQEKISTTSI----H 560
Cdd:COG1201 231 G-AGKKpdlevlvpvedlierfpwaghlwphlyPRVLDLIEAHRT--TLVFTNTRSQAERLFQRLNELNPEDALPiaahH 307

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859541 561 G--DREQRER-EKALSDFRLghcPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTG-RCGNTGRAV 630
Cdd:COG1201 308 GslSREQRLEvEEALKAGEL---RAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVSKGR 378
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 511-656 7.62e-09

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 58.96  E-value: 7.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  511 VDQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAA 590
Cdd:PRK11057 218 VEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFG 297

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18859541  591 RGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPESDTPLARSLVKVLSGAQQVV 656
Cdd:PRK11057 298 MGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDI 363
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 582-634 1.29e-07

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 49.24  E-value: 1.29e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 18859541 582 VLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFN 634
Cdd:cd18785  25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 518-622 1.48e-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: 51.11  E-value: 1.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 518 DQLLELLRATGNerTMVFVETKRSADFIAT---FLCQEKISTTSI---HG--DREQRER-EKALSDfrlGHCPVLVATSV 588
Cdd:cd18796  29 AEVIFLLERHKS--TLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAALKR---GDLKVVVATSS 103

                        90       100       110
                ....*....|....*....|....*....|....
gi 18859541 589 AARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGR 622
Cdd:cd18796 104 LELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 515-630 2.68e-07

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB 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: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 51.09  E-value: 2.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 515 SKRDQLLELL-----RATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVA 589
Cdd:cd18790   8 PTEGQVDDLLgeirkRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLL 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 18859541 590 ARGLDIEQVQHVVNFD-----MPSSIDEYVHRIGRTGRCGNtGRAV 630
Cdd:cd18790  88 REGLDLPEVSLVAILDadkegFLRSETSLIQTIGRAARNVN-GKVI 132
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 299-472 4.93e-07

DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 50.49  E-value: 4.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 299 KPTPVQKHGI-PIISA-----GRDLMACAQTGSGKTAAFLLPILqrfmtDGVAASKfseiqepEAIIVAPTRELINQIYL 372
Cdd:cd17918  15 SLTKDQAQAIkDIEKDlhspePMDRLLSGDVGSGKTLVALGAAL-----LAYKNGK-------QVAILVPTEILAHQHYE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 373 EARKFaygtcvrpvvvYGGIN----TGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLskvryLVLDEADRmldmgFEPE 448
Cdd:cd17918  83 EARKF-----------LPFINvelvTGGTKAQILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHR-----FGVA 141

                       170       180
                ....*....|....*....|....
gi 18859541 449 MRKLVASPGMPSkeerqTLMFSAT 472
Cdd:cd17918 142 QREALYNLGATH-----FLEATAT 160
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 530-619 4.94e-06

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: 46.01  E-value: 4.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 530 ERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKA---LSDFRLGHCPVLVATSVAARGLDIEQVQHVVnFDM 606
Cdd:cd18799   7 IKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV-FLR 85

                        90
                ....*....|....*
gi 18859541 607 P--SSIdEYVHRIGR 619
Cdd:cd18799  86 PteSRT-LFLQMLGR 99
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 314-436 8.22e-06

DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 46.42  E-value: 8.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 314 GRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKfseiqepeAIIVAPTRELINQIYLEARKFAYGTCV-RPVVVYGGI 392
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------VLYISPLKALINDQERRLEEPLDEIDLeIPVAVRHGD 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18859541 393 NTGYTIREVLKGC-NVLCATPGRLHDLIGRGKIG--LSKVRYLVLDE 436
Cdd:cd17922  73 TSQSEKAKQLKNPpGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 315-437 5.12e-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: 5.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 315 RDLMACAQTGSGKT--AAFLLPILqrfmtdgvaASKFSEIQEPEAIIV--APTRELINQIYLEARKFaygTCVRPVVVYG 390
Cdd:cd18034  17 RNTIVVLPTGSGKTliAVMLIKEM---------GELNRKEKNPKKRAVflVPTVPLVAQQAEAIRSH---TDLKVGEYSG 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18859541 391 GINTGYTIREVLKGC----NVLCATPGRLHDLIGRGKIGLSKVRYLVLDEA 437
Cdd:cd18034  85 EMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK13767 PRK13767
ATP-dependent helicase; Provisional
 294-371 6.82e-05

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 46.42  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541  294 KSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKT-AAFLLPI---LQRFMTDGVAASKFseiqepeAIIVAPTRELINQ 369
Cdd:PRK13767  27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAIIdelFRLGREGELEDKVY-------CLYVSPLRALNND 99


                 ..
gi 18859541  370 IY 371
Cdd:PRK13767 100 IH 101
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 318-457 6.07e-04

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 41.35  E-value: 6.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 318 MACAQTGSGKTAAFLLPILQRFMTDGvaaskfseiqePEAIIVAPTRELINQIYLEARKFAygTCVRPVVVYGGINTGYT 397
Cdd:cd18035  20 LIVLPTGLGKTIIAILVAADRLTKKG-----------GKVLILAPSRPLVEQHAENLKRVL--NIPDKITSLTGEVKPEE 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18859541 398 IREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADR--------MLDMGFEPEMRK-----LVASPG 457
Cdd:cd18035  87 RAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHHavgnyayvYIAHRYKREANNplilgLTASPG 159
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 314-436 6.08e-04

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 41.17  E-value: 6.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 314 GRDLMACAQTGSGKTAAFLLPILQRFMTDGvaaskfseiqepEAIIVAPTRELINQIYLEARKFaygtcvRPVVVYGGIN 393
Cdd:cd18028  17 GENLLISIPTASGKTLIAEMAMVNTLLEGG------------KALYLVPLRALASEKYEEFKKL------EEIGLKVGIS 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18859541 394 TG-YTIR-EVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDE 436
Cdd:cd18028  79 TGdYDEDdEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 315-487 8.03e-04

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 41.19  E-value: 8.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 315 RDLMACAQTGSGKTAAFLLPILQRFMTDGVAASkfseiQEPEAIIVAPTRELINQIYLEAR-KFA-YGTCVRPVVvygGI 392
Cdd:cd18023  18 KNFVVSAPTGSGKTVLFELAILRLLKERNPLPW-----GNRKVVYIAPIKALCSEKYDDWKeKFGpLGLSCAELT---GD 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 393 NTGYTIREvLKGCNVLCATPGRLHDLIGRGKIG---LSKVRYLVLDE---------------ADRMLDMGFEPEMRKLVA 454
Cdd:cd18023  90 TEMDDTFE-IQDADIILTTPEKWDSMTRRWRDNgnlVQLVALVLIDEvhiikenrgatlevvVSRMKTLSSSSELRGSTV 168

                       170       180       190
                ....*....|....*....|....*....|....*
gi 18859541 455 SPgmpskeeRQTLMFSATYP--EDIqrmaADFLKV 487
Cdd:cd18023 169 RP-------MRFVAVSATIPniEDL----AEWLGD 192
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 528-633 2.93e-03

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 38.77  E-value: 2.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 528 GNERTMVFVETKRSADFIAtflcqEKISTTSIHGDREQREREKALSDFRLGHCPVLVATSVAARGLDIEQ----VQHVVN 603
Cdd:cd18789  48 QGDKIIVFTDNVEALYRYA-----KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEanvaIQISGH 122

                        90       100       110
                ....*....|....*....|....*....|
gi 18859541 604 FdmpSSIDEYVHRIGRTGRCGNTGRAVSFF 633
Cdd:cd18789 123 G---GSRRQEAQRLGRILRPKKGGGKNAFF 149
ResIII pfam04851
Type III restriction enzyme, res subunit;
323-439 3.45e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.81  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541   323 TGSGKT--AAFLlpilqrfmtdgvAASKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGTcvrpvVVYGGINTGYTIRE 400
Cdd:pfam04851  32 TGSGKTltAAKL------------IARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNY-----VEIGEIISGDKKDE 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18859541   401 VLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVL--DEADR 439
Cdd:pfam04851  95 SVDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHR 135
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
 531-625 6.79e-03

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: 37.62  E-value: 6.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859541 531 RTMVFVETKRSADFIATFLCQEKIST----TSIHGDR---EQREREKALSDFRLGHCPVLVATSVAARGLDIEQVQHVVN 603
Cdd:cd18797  37 KTIVFCRSRKLAELLLRYLKARLVEEgplaSKVASYRagyLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116

                        90       100
                ....*....|....*....|..
gi 18859541 604 FDMPSSIDEYVHRIGRTGRCGN 625
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGK 138
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 559-595 9.68e-03

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 37.63  E-value: 9.68e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 18859541 559 IHGDREQREREKALSDFRLGHCPVLVATSVAARGLDI 595
Cdd:cd18792  66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDV 102
 
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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