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Conserved domains on  [gi|312077716|ref|XP_003141426|]
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DEAD/DEAH box helicase [Loa loa]

Protein Classification

DEAD/DEAH box helicase domain-containing protein( domain architecture ID 1000559)

DEAD/DEAH box helicase domain-containing protein may function as an RNA helicase

EC:  3.6.4.-
Gene Ontology:  GO:0005524|GO:0004386|GO:0003676
PubMed:  20206133

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB super family cl33924
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
219-590 1.93e-61

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


The actual alignment was detected with superfamily member COG0513:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 209.23  E-value: 1.93e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHAKGVVLVPTHALRMQTS 298
Cdd:COG0513    9 LSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILAPTRELALQVA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 299 LMISKLAEGTNIK---IVGG----SERWRSEEDWDILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSFLNDIIR 366
Cdd:COG0513   89 EELRKLAKYLGLRvatVYGGvsigRQIRALKRGVDIVVATPGrlldlIERGALDLSGVETLVLDEADRMLDMGFIEDIER 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 367 LLgplkirhsvidkNATDGVR--LIFSsATYPDQLQLIAESIV-DYEYlycVKTENLHRIMPHIKQTFIRIREIDKLEKl 443
Cdd:COG0513  169 IL------------KLLPKERqtLLFS-ATMPPEIRKLAKRYLkNPVR---IEVAPENATAETIEQRYYLVDKRDKLEL- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 444 kellekgL-----SFPHGQTLIFCKNLKNVGLVSRSLREMGIEHTSLSGGR----RiEQLIDELRSGAVRIIIATDVASR 514
Cdd:COG0513  232 -------LrrllrDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLsqgqR-ERALDAFRNGKIRVLVATDVAAR 303
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312077716 515 GLDLPQLRHIINYDFPRQISDYVHRCGRIGRIGSLHKCLmtSFVRRAwEVKHVNSIELAARLHRPLQDVELNDPAR 590
Cdd:COG0513  304 GIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAI--SLVTPD-ERRLLRAIEKLIGQKIEEEELPGFEPVE 376
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
219-590 1.93e-61

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 209.23  E-value: 1.93e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHAKGVVLVPTHALRMQTS 298
Cdd:COG0513    9 LSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILAPTRELALQVA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 299 LMISKLAEGTNIK---IVGG----SERWRSEEDWDILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSFLNDIIR 366
Cdd:COG0513   89 EELRKLAKYLGLRvatVYGGvsigRQIRALKRGVDIVVATPGrlldlIERGALDLSGVETLVLDEADRMLDMGFIEDIER 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 367 LLgplkirhsvidkNATDGVR--LIFSsATYPDQLQLIAESIV-DYEYlycVKTENLHRIMPHIKQTFIRIREIDKLEKl 443
Cdd:COG0513  169 IL------------KLLPKERqtLLFS-ATMPPEIRKLAKRYLkNPVR---IEVAPENATAETIEQRYYLVDKRDKLEL- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 444 kellekgL-----SFPHGQTLIFCKNLKNVGLVSRSLREMGIEHTSLSGGR----RiEQLIDELRSGAVRIIIATDVASR 514
Cdd:COG0513  232 -------LrrllrDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLsqgqR-ERALDAFRNGKIRVLVATDVAAR 303
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312077716 515 GLDLPQLRHIINYDFPRQISDYVHRCGRIGRIGSLHKCLmtSFVRRAwEVKHVNSIELAARLHRPLQDVELNDPAR 590
Cdd:COG0513  304 GIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAI--SLVTPD-ERRLLRAIEKLIGQKIEEEELPGFEPVE 376
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
223-406 1.67e-41

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: 148.74  E-value: 1.67e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHAKGV---VLVPTHALRMQTSL 299
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPqalVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 300 MISKLAEGTNIK---IVGGSERWRSEEDW----DILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSFLNDIIRL 367
Cdd:cd00268   81 VARKLGKGTGLKvaaIYGGAPIKKQIEALkkgpDIVVGTPGrlldlIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 312077716 368 LGPLKIRHsvidknatdgvRLIFSSATYPDQLQLIAESI 406
Cdd:cd00268  161 LSALPKDR-----------QTLLFSATLPEEVKELAKKF 188
PTZ00110 PTZ00110
helicase; Provisional
223-548 5.92e-33

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 132.97  E-value: 5.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVN-RHAKG---VVLVPTHALRMQTS 298
Cdd:PTZ00110 141 ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLlRYGDGpivLVLAPTRELAEQIR 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 299 LMISKLAEGTNIK---IVGG----SERWRSEEDWDILVSTPSFSPEFFTPH-----NIDYIVLDEADMLLDDSFLNDIIR 366
Cdd:PTZ00110 221 EQCNKFGASSKIRntvAYGGvpkrGQIYALRRGVEILIACPGRLIDFLESNvtnlrRVTYLVLDEADRMLDMGFEPQIRK 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 367 LLGplKIRhsvidknaTDGVRLIFSsATYPDQLQLIAESIVDYEYLYcVKTENLHRIMPH-IKQTFIRIREIDKLEKLKE 445
Cdd:PTZ00110 301 IVS--QIR--------PDRQTLMWS-ATWPKEVQSLARDLCKEEPVH-VNVGSLDLTACHnIKQEVFVVEEHEKRGKLKM 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 446 LLEKgLSFPHGQTLIFCKNLKNVGLVSRSLREMGIEHTSLSGGRRIEQ---LIDELRSGAVRIIIATDVASRGLDLPQLR 522
Cdd:PTZ00110 369 LLQR-IMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEErtwVLNEFKTGKSPIMIATDVASRGLDVKDVK 447
                        330       340
                 ....*....|....*....|....*.
gi 312077716 523 HIINYDFPRQISDYVHRCGRIGRIGS 548
Cdd:PTZ00110 448 YVINFDFPNQIEDYVHRIGRTGRAGA 473
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
236-402 1.01e-29

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: 115.03  E-value: 1.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716  236 TVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNrHAKGVVLVPTHALRMQTSLMISKLAEGTNIK---I 312
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN-GPQALVLAPTRELAEQIYEELKKLGKGLGLKvasL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716  313 VGGSERWRSEEDW---DILVSTP----SFSPEFFTPHNIDYIVLDEADMLLDDSFLNDIIRLLGPLKIrhsvidknatdG 385
Cdd:pfam00270  80 LGGDSRKEQLEKLkgpDILVGTPgrllDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-----------K 148
                         170
                  ....*....|....*..
gi 312077716  386 VRLIFSSATYPDQLQLI 402
Cdd:pfam00270 149 RQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
228-423 2.00e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.81  E-value: 2.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716   228 RKLGFRVPTVIQRRAFRAFKSDA-HLLIAAETGSGKTAAYAAPLLSALLRNVNRHAkgVVLVPTHALRMQTSLMISKLAE 306
Cdd:smart00487   2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKGGRV--LVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716   307 GTNIKIV---GGSERWRSEEDW-----DILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSFLNDIIRLLGPLKi 373
Cdd:smart00487  80 SLGLKVVglyGGDSKREQLRKLesgktDILVTTPGrlldlLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP- 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 312077716   374 rhsvidknatDGVRLIFSSATYPDQLQLIAESIVDYEYLYCVKTENLHRI 423
Cdd:smart00487 159 ----------KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPI 198
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
219-590 1.93e-61

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 209.23  E-value: 1.93e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHAKGVVLVPTHALRMQTS 298
Cdd:COG0513    9 LSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILAPTRELALQVA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 299 LMISKLAEGTNIK---IVGG----SERWRSEEDWDILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSFLNDIIR 366
Cdd:COG0513   89 EELRKLAKYLGLRvatVYGGvsigRQIRALKRGVDIVVATPGrlldlIERGALDLSGVETLVLDEADRMLDMGFIEDIER 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 367 LLgplkirhsvidkNATDGVR--LIFSsATYPDQLQLIAESIV-DYEYlycVKTENLHRIMPHIKQTFIRIREIDKLEKl 443
Cdd:COG0513  169 IL------------KLLPKERqtLLFS-ATMPPEIRKLAKRYLkNPVR---IEVAPENATAETIEQRYYLVDKRDKLEL- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 444 kellekgL-----SFPHGQTLIFCKNLKNVGLVSRSLREMGIEHTSLSGGR----RiEQLIDELRSGAVRIIIATDVASR 514
Cdd:COG0513  232 -------LrrllrDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLsqgqR-ERALDAFRNGKIRVLVATDVAAR 303
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312077716 515 GLDLPQLRHIINYDFPRQISDYVHRCGRIGRIGSLHKCLmtSFVRRAwEVKHVNSIELAARLHRPLQDVELNDPAR 590
Cdd:COG0513  304 GIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAI--SLVTPD-ERRLLRAIEKLIGQKIEEEELPGFEPVE 376
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
223-406 1.67e-41

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: 148.74  E-value: 1.67e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHAKGV---VLVPTHALRMQTSL 299
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPqalVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 300 MISKLAEGTNIK---IVGGSERWRSEEDW----DILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSFLNDIIRL 367
Cdd:cd00268   81 VARKLGKGTGLKvaaIYGGAPIKKQIEALkkgpDIVVGTPGrlldlIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 312077716 368 LGPLKIRHsvidknatdgvRLIFSSATYPDQLQLIAESI 406
Cdd:cd00268  161 LSALPKDR-----------QTLLFSATLPEEVKELAKKF 188
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
223-433 4.82e-39

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: 143.28  E-value: 4.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLR------NVNRHAKGVVLVPTHALRMQ 296
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRykllaeGPFNAPRGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 297 TSLMISKLAEGTNIK---IVGGSERWR----SEEDWDILVSTPSFSPEFFTPHNID-----YIVLDEADMLLDDSFLNDI 364
Cdd:cd17948   81 IGSVAQSLTEGLGLKvkvITGGRTKRQirnpHFEEVDILVATPGALSKLLTSRIYSleqlrHLVLDEADTLLDDSFNEKL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312077716 365 IRLLG--PLKIRHSVIDKNATDGVRLIFSSATYPDQLQLIAESIVDYEYLYCVKTENLHRIMPHIKQTFIR 433
Cdd:cd17948  161 SHFLRrfPLASRRSENTDGLDPGTQLVLVSATMPSGVGEVLSKVIDVDSIETVTSDKLHRLMPHVKQKFLR 231
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
427-558 8.15e-34

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: 125.31  E-value: 8.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 427 IKQTFIRIREIDKLEKLKELLEKGLSFphGQTLIFCKNLKNVGLVSRSLREMGIEHTSLSGGRRIEQ---LIDELRSGAV 503
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKP--GKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEErerALKKFRSGKV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 312077716 504 RIIIATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGRIGRIGslHKCLMTSFV 558
Cdd:cd18787   79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAG--RKGTAITFV 131
PTZ00110 PTZ00110
helicase; Provisional
223-548 5.92e-33

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 132.97  E-value: 5.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVN-RHAKG---VVLVPTHALRMQTS 298
Cdd:PTZ00110 141 ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLlRYGDGpivLVLAPTRELAEQIR 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 299 LMISKLAEGTNIK---IVGG----SERWRSEEDWDILVSTPSFSPEFFTPH-----NIDYIVLDEADMLLDDSFLNDIIR 366
Cdd:PTZ00110 221 EQCNKFGASSKIRntvAYGGvpkrGQIYALRRGVEILIACPGRLIDFLESNvtnlrRVTYLVLDEADRMLDMGFEPQIRK 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 367 LLGplKIRhsvidknaTDGVRLIFSsATYPDQLQLIAESIVDYEYLYcVKTENLHRIMPH-IKQTFIRIREIDKLEKLKE 445
Cdd:PTZ00110 301 IVS--QIR--------PDRQTLMWS-ATWPKEVQSLARDLCKEEPVH-VNVGSLDLTACHnIKQEVFVVEEHEKRGKLKM 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 446 LLEKgLSFPHGQTLIFCKNLKNVGLVSRSLREMGIEHTSLSGGRRIEQ---LIDELRSGAVRIIIATDVASRGLDLPQLR 522
Cdd:PTZ00110 369 LLQR-IMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEErtwVLNEFKTGKSPIMIATDVASRGLDVKDVK 447
                        330       340
                 ....*....|....*....|....*.
gi 312077716 523 HIINYDFPRQISDYVHRCGRIGRIGS 548
Cdd:PTZ00110 448 YVINFDFPNQIEDYVHRIGRTGRAGA 473
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
219-547 1.07e-32

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 130.45  E-value: 1.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRH---AKGVVLVPTHALRM 295
Cdd:PRK11192   8 LDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKsgpPRILILTPTRELAM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 296 QTSLMISKLAEGTNIKIV---GG----SERWRSEEDWDILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSFLND 363
Cdd:PRK11192  88 QVADQARELAKHTHLDIAtitGGvaymNHAEVFSENQDIVVATPGrllqyIKEENFDCRAVETLILDEADRMLDMGFAQD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 364 IIRLLGPLKIRHSVIDKNAT---DGVRLiFSSATYPDQLQLIAES-------IVDYEYL---YCVKTENLHRImphIKQt 430
Cdd:PRK11192 168 IETIAAETRWRKQTLLFSATlegDAVQD-FAERLLNDPVEVEAEPsrrerkkIHQWYYRaddLEHKTALLCHL---LKQ- 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 431 firireidkleklkellekglsfPH-GQTLIFCKNLKNVGLVSRSLREMGIEHTSLSG----GRRiEQLIDELRSGAVRI 505
Cdd:PRK11192 243 -----------------------PEvTRSIVFVRTRERVHELAGWLRKAGINCCYLEGemvqAKR-NEAIKRLTDGRVNV 298
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 312077716 506 IIATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGRIGRIG 547
Cdd:PRK11192 299 LVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAG 340
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
219-545 3.04e-31

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 126.85  E-value: 3.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSaLLRNVNRHAKG------VVLVPTHA 292
Cdd:PRK10590   8 LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQ-HLITRQPHAKGrrpvraLILTPTRE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 293 LRMQTSLMISKLAEGTNIK---IVGG----SERWRSEEDWDILVSTPSFSPEFftPH-------NIDYIVLDEADMLLDD 358
Cdd:PRK10590  87 LAAQIGENVRDYSKYLNIRslvVFGGvsinPQMMKLRGGVDVLVATPGRLLDL--EHqnavkldQVEILVLDEADRMLDM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 359 SFLNDIIRLLGPLKIRHSvidknatdgvRLIFSsATYPDQLQLIAESIVDYEYLYCVKTENL--HRIMPHIKqtFI---R 433
Cdd:PRK10590 165 GFIHDIRRVLAKLPAKRQ----------NLLFS-ATFSDDIKALAEKLLHNPLEIEVARRNTasEQVTQHVH--FVdkkR 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 434 IREIdkleklkellekgLSFPHG-----QTLIFCKNLKNVGLVSRSLREMGIE----HTSLSGGRRIEQLIDeLRSGAVR 504
Cdd:PRK10590 232 KREL-------------LSQMIGkgnwqQVLVFTRTKHGANHLAEQLNKDGIRsaaiHGNKSQGARTRALAD-FKSGDIR 297
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 312077716 505 IIIATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGRIGR 545
Cdd:PRK10590 298 VLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
209-591 8.09e-31

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 125.68  E-value: 8.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 209 SFSwdenvSL-LDPVIIENARKLGFRVPTVIQRRAFRAFKsDAHLLIA-AETGSGKTAAYAAPLLSALlrNVNRHA-KGV 285
Cdd:PRK11776   5 AFS-----TLpLPPALLANLNELGYTEMTPIQAQSLPAIL-AGKDVIAqAKTGSGKTAAFGLGLLQKL--DVKRFRvQAL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 286 VLVPTHALRMQTSLMISKLAEGT-NIKIV---GGS----ERWRSEEDWDILVSTPS-----FSPEFFTPHNIDYIVLDEA 352
Cdd:PRK11776  77 VLCPTRELADQVAKEIRRLARFIpNIKVLtlcGGVpmgpQIDSLEHGAHIIVGTPGrildhLRKGTLDLDALNTLVLDEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 353 DMLLDDSFLNDIirllgplkirHSVIDKNATDGVRLIFSsATYPDQLQLIAESIvdyeyLY---CVKTENLHrIMPHIKQ 429
Cdd:PRK11776 157 DRMLDMGFQDAI----------DAIIRQAPARRQTLLFS-ATYPEGIAAISQRF-----QRdpvEVKVESTH-DLPAIEQ 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 430 TFIrirEIDKLEKLKELLEKGLSFPHGQTLIFCKNLKNVGLVSRSLREMGIEHTSLSGG---RRIEQLIDELRSGAVRII 506
Cdd:PRK11776 220 RFY---EVSPDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDleqRDRDQVLVRFANRSCSVL 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 507 IATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGRIGRIGSlhKCLMTSFVRRAwEVKHVNSIELAarLHRPLQDVELN 586
Cdd:PRK11776 297 VATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGS--KGLALSLVAPE-EMQRANAIEDY--LGRKLNWEPLP 371

                 ....*
gi 312077716 587 DPARL 591
Cdd:PRK11776 372 SLSPL 376
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
236-402 1.01e-29

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: 115.03  E-value: 1.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716  236 TVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNrHAKGVVLVPTHALRMQTSLMISKLAEGTNIK---I 312
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN-GPQALVLAPTRELAEQIYEELKKLGKGLGLKvasL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716  313 VGGSERWRSEEDW---DILVSTP----SFSPEFFTPHNIDYIVLDEADMLLDDSFLNDIIRLLGPLKIrhsvidknatdG 385
Cdd:pfam00270  80 LGGDSRKEQLEKLkgpDILVGTPgrllDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-----------K 148
                         170
                  ....*....|....*..
gi 312077716  386 VRLIFSSATYPDQLQLI 402
Cdd:pfam00270 149 RQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
228-423 2.00e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.81  E-value: 2.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716   228 RKLGFRVPTVIQRRAFRAFKSDA-HLLIAAETGSGKTAAYAAPLLSALLRNVNRHAkgVVLVPTHALRMQTSLMISKLAE 306
Cdd:smart00487   2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKGGRV--LVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716   307 GTNIKIV---GGSERWRSEEDW-----DILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSFLNDIIRLLGPLKi 373
Cdd:smart00487  80 SLGLKVVglyGGDSKREQLRKLesgktDILVTTPGrlldlLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP- 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 312077716   374 rhsvidknatDGVRLIFSSATYPDQLQLIAESIVDYEYLYCVKTENLHRI 423
Cdd:smart00487 159 ----------KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPI 198
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
223-596 8.00e-25

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 109.17  E-value: 8.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSallrNVNRHAKG---VVLVPTHALRMQTSL 299
Cdd:PRK11634  17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLH----NLDPELKApqiLVLAPTRELAVQVAE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 300 MI---SKLAEGTNIKIVGGSERWRSE-----EDWDILVSTPSFSPEFFTPHNIDY-----IVLDEADMLLDDSFLNDIIR 366
Cdd:PRK11634  93 AMtdfSKHMRGVNVVALYGGQRYDVQlralrQGPQIVVGTPGRLLDHLKRGTLDLsklsgLVLDEADEMLRMGFIEDVET 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 367 LLGPLKIRHSVIDKNAT----------------DGVRLIFSSATYPDqlqlIAESivdYEYLYCV-KTENLHRimphikq 429
Cdd:PRK11634 173 IMAQIPEGHQTALFSATmpeairritrrfmkepQEVRIQSSVTTRPD----ISQS---YWTVWGMrKNEALVR------- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 430 tFIRIREIDKleklkellekglsfphgqTLIFCKNlKNVGL-VSRSLREMGIEHTSLSGGRRI---EQLIDELRSGAVRI 505
Cdd:PRK11634 239 -FLEAEDFDA------------------AIIFVRT-KNATLeVAEALERNGYNSAALNGDMNQalrEQTLERLKDGRLDI 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 506 IIATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGRIGRIGSLHKCLMtsFVRRAwEVKHVNSIELAARLHRPlqDVEL 585
Cdd:PRK11634 299 LIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALL--FVENR-ERRLLRNIERTMKLTIP--EVEL 373
                        410
                 ....*....|.
gi 312077716 586 NDpARLLGLQR 596
Cdd:PRK11634 374 PN-AELLGKRR 383
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
219-548 1.39e-23

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 104.22  E-value: 1.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFrAFKSDAHLLIA-AETGSGKTAAYAAPLLSALLRN---VNRH---AKGVVLVPTH 291
Cdd:PRK01297  94 LAPELMHAIHDLGFPYCTPIQAQVL-GYTLAGHDAIGrAQTGTGKTAAFLISIINQLLQTpppKERYmgePRALIIAPTR 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 292 ALRMQTSLMISKLAEGTNIKI---VGGSE-----RWRSEEDWDILVSTPSFSPEFFTPHN-----IDYIVLDEADMLLDD 358
Cdd:PRK01297 173 ELVVQIAKDAAALTKYTGLNVmtfVGGMDfdkqlKQLEARFCDILVATPGRLLDFNQRGEvhldmVEVMVLDEADRMLDM 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 359 SFL---NDIIRLLGPLKIRHSvidknatdgvrLIFSsATYPDQLQLIAE------SIVDYE-----------YLYCVKTE 418
Cdd:PRK01297 253 GFIpqvRQIIRQTPRKEERQT-----------LLFS-ATFTDDVMNLAKqwttdpAIVEIEpenvasdtveqHVYAVAGS 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 419 NLHRIMphikQTFIRIREIDkleklkellekglsfphgQTLIFCKNLKNVGLVSRSLREMGIEHTSLSGG----RRIEQL 494
Cdd:PRK01297 321 DKYKLL----YNLVTQNPWE------------------RVMVFANRKDEVRRIEERLVKDGINAAQLSGDvpqhKRIKTL 378
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 312077716 495 iDELRSGAVRIIIATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGRIGRIGS 548
Cdd:PRK01297 379 -EGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGA 431
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
223-408 1.69e-23

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: 98.43  E-value: 1.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLR-NVNRHAKGVVLVPTHALRMQTSLMI 301
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKpRKKKGLRALILAPTRELASQIYREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 302 SKLAEGTNIKIV--------GGSERWRSEEDWDILVSTP------------SFSpefftphNIDYIVLDEADMLLDDSFL 361
Cdd:cd17957   81 LKLSKGTGLRIVllsksleaKAKDGPKSITKYDILVSTPlrlvfllkqgpiDLS-------SVEYLVLDEADKLFEPGFR 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 312077716 362 N---DIIRLLGPLKIRhsvidknatdgvRLIFsSATYPDQLQLIAESIVD 408
Cdd:cd17957  154 EqtdEILAACTNPNLQ------------RSLF-SATIPSEVEELARSVMK 190
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
219-547 3.36e-23

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 103.88  E-value: 3.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRN---VNRHA---KGVVLVPTHA 292
Cdd:PRK04537  16 LHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRpalADRKPedpRALILAPTRE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 293 LRMQTSLMISKLAEGTNIK---IVGG----SERWRSEEDWDILVSTPSFSPEFFTPHNI------DYIVLDEADMLLDDS 359
Cdd:PRK04537  96 LAIQIHKDAVKFGADLGLRfalVYGGvdydKQRELLQQGVDVIIATPGRLIDYVKQHKVvslhacEICVLDEADRMFDLG 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 360 FLNDIIRLLGPLKIRhsvidknatdGVR--LIFSSATYPDQLQLIAESIVDYEYLyCVKTENlhrimphIKQTFIRIREI 437
Cdd:PRK04537 176 FIKDIRFLLRRMPER----------GTRqtLLFSATLSHRVLELAYEHMNEPEKL-VVETET-------ITAARVRQRIY 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 438 DKLEKLKELLEKGL-SFPHG-QTLIFCKNLKNVGLVSRSLREMGIEHTSLSGG---RRIEQLIDELRSGAVRIIIATDVA 512
Cdd:PRK04537 238 FPADEEKQTLLLGLlSRSEGaRTMVFVNTKAFVERVARTLERHGYRVGVLSGDvpqKKRESLLNRFQKGQLEILVATDVA 317
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 312077716 513 SRGLDLPQLRHIINYDFPRQISDYVHRCGRIGRIG 547
Cdd:PRK04537 318 ARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLG 352
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
230-368 1.40e-22

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: 95.78  E-value: 1.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 230 LGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHA--KGVVLVPTHALRMQTSLMISKLAEG 307
Cdd:cd17947    8 LGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAatRVLVLVPTRELAMQCFSVLQQLAQF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 308 TNIK---IVGGSERwRSEEDW-----DILVSTP---------SFSpefFTPHNIDYIVLDEADMLLDDSF---LNDIIRL 367
Cdd:cd17947   88 TDITfalAVGGLSL-KAQEAAlrarpDIVIATPgrlidhlrnSPS---FDLDSIEILVLDEADRMLEEGFadeLKEILRL 163

                 .
gi 312077716 368 L 368
Cdd:cd17947  164 C 164
PTZ00424 PTZ00424
helicase 45; Provisional
231-571 2.19e-22

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 99.52  E-value: 2.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 231 GFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNrHAKGVVLVPTHALRMQTSLMISKLAEGTNI 310
Cdd:PTZ00424  47 GFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN-ACQALILAPTRELAQQIQKVVLALGDYLKV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 311 KI---VGGS----ERWRSEEDWDILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSF---LNDIIRLLGPlkirh 375
Cdd:PTZ00424 126 RChacVGGTvvrdDINKLKAGVHMVVGTPGrvydmIDKRHLRVDDLKLFILDEADEMLSRGFkgqIYDVFKKLPP----- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 376 svidknatdGVRLIFSSATYPDQ-LQLIAESIVDYEYLYcVKTENLhrIMPHIKQTFIRIREIDKLEKLKELLEKGLSFP 454
Cdd:PTZ00424 201 ---------DVQVALFSATMPNEiLELTTKFMRDPKRIL-VKKDEL--TLEGIRQFYVAVEKEEWKFDTLCDLYETLTIT 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 455 hgQTLIFCKNLKNVGLVSRSLREMGIEHTSLSGG---RRIEQLIDELRSGAVRIIIATDVASRGLDLPQLRHIINYDFPR 531
Cdd:PTZ00424 269 --QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDmdqKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPA 346
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 312077716 532 QISDYVHRCGRIGRIGslHKCLMTSFVRRAwEVKHVNSIE 571
Cdd:PTZ00424 347 SPENYIHRIGRSGRFG--RKGVAINFVTPD-DIEQLKEIE 383
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
219-547 2.19e-22

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 101.02  E-value: 2.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLS--ALLR----NVNRHAKGVVLVPTHA 292
Cdd:PLN00206 128 LPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcCTIRsghpSEQRNPLAMVLTPTRE 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 293 LRMQTSLMISKLAEGTNIK---IVGGS----ERWRSEEDWDILVSTPSFSPEFFTPHNIDY-----IVLDEADMLLDDSF 360
Cdd:PLN00206 208 LCVQVEDQAKVLGKGLPFKtalVVGGDampqQLYRIQQGVELIVGTPGRLIDLLSKHDIELdnvsvLVLDEVDCMLERGF 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 361 LNDIIRLLGPLkirhsvidknATDGVrLIFSsATYPDQLQLIAESIVDYEYLYCVKTENlhRIMPHIKQTFIRIREIDKL 440
Cdd:PLN00206 288 RDQVMQIFQAL----------SQPQV-LLFS-ATVSPEVEKFASSLAKDIILISIGNPN--RPNKAVKQLAIWVETKQKK 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 441 EKLKELLEKGLSF-PHGqtLIFCKNLKNVGLVSRSLREM-GIEHTSLSGGRRIEQLIDELRS---GAVRIIIATDVASRG 515
Cdd:PLN00206 354 QKLFDILKSKQHFkPPA--VVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSflvGEVPVIVATGVLGRG 431
                        330       340       350
                 ....*....|....*....|....*....|..
gi 312077716 516 LDLPQLRHIINYDFPRQISDYVHRCGRIGRIG 547
Cdd:PLN00206 432 VDLLRVRQVIIFDMPNTIKEYIHQIGRASRMG 463
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
219-403 8.14e-22

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: 94.09  E-value: 8.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRN-------VNRHAK--GVVLVP 289
Cdd:cd17967    7 LRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDgppsvgrGRRKAYpsALILAP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 290 THALRMQTSLMISKLAEGTNIKIV---GGSE----RWRSEEDWDILVSTP------------SFSpefftphNIDYIVLD 350
Cdd:cd17967   87 TRELAIQIYEEARKFSYRSGVRSVvvyGGADvvhqQLQLLRGCDILVATPgrlvdfiergriSLS-------SIKFLVLD 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 312077716 351 EADMLLDDSFLNDIIRLlgplkIRHSVIDKNatdGVR--LIFsSATYPDQLQLIA 403
Cdd:cd17967  160 EADRMLDMGFEPQIRKI-----VEHPDMPPK---GERqtLMF-SATFPREIQRLA 205
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
454-547 1.23e-21

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: 89.96  E-value: 1.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716  454 PHGQTLIFCKNLKNVGLvSRSLREMGIEHTSLSGGRRIEQ---LIDELRSGAVRIIIATDVASRGLDLPQLRHIINYDFP 530
Cdd:pfam00271  14 RGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEreeILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLP 92
                          90
                  ....*....|....*..
gi 312077716  531 RQISDYVHRCGRIGRIG 547
Cdd:pfam00271  93 WNPASYIQRIGRAGRAG 109
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
214-422 1.30e-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: 94.37  E-value: 1.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 214 ENVSLLDPV---IIENARK-----LGFRVPTVIQRRAFRAF-----------------KSDAHLlIAAETGSGKTAAYAA 268
Cdd:cd17965    2 DQLKLLPSVreaIIKEILKgsnktDEEIKPSPIQTLAIKKLlktlmrkvtkqtsneepKLEVFL-LAAETGSGKTLAYLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 269 PLLSALLR-----------NVNRHAK-----GVVLVPTHALRMQTSLMISKLAEGTNIKIvgGSERW-----------RS 321
Cdd:cd17965   81 PLLDYLKRqeqepfeeaeeEYESAKDtgrprSVILVPTHELVEQVYSVLKKLSHTVKLGI--KTFSSgfgpsyqrlqlAF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 322 EEDWDILVSTPSFSPEFFTPHN-----IDYIVLDEADMLLDDSFLNDIirllgplkirHSVIdKNATDGVRLIFSSATYP 396
Cdd:cd17965  159 KGRIDILVTTPGKLASLAKSRPkilsrVTHLVVDEADTLFDRSFLQDT----------TSII-KRAPKLKHLILCSATIP 227
                        250       260
                 ....*....|....*....|....*.
gi 312077716 397 DQLQLIAESIvdYEYLYCVKTENLHR 422
Cdd:cd17965  228 KEFDKTLRKL--FPDVVRIATPRLHA 251
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
219-399 2.24e-21

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: 92.37  E-value: 2.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNR-HAKGVVLVPTHALRMQT 297
Cdd:cd17959    8 LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTvGARALILSPTRELALQT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 298 SLMISKLAEGTNIK---IVGGSerwRSEEDW-------DILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSF-- 360
Cdd:cd17959   88 LKVTKELGKFTDLRtalLVGGD---SLEEQFealasnpDIIIATPGrllhlLVEMNLKLSSVEYVVFDEADRLFEMGFae 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 312077716 361 -LNDIIRLLGPLKirhsvidknatdgVRLIFsSATYPDQL 399
Cdd:cd17959  165 qLHEILSRLPENR-------------QTLLF-SATLPKLL 190
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
229-412 3.19e-21

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: 92.26  E-value: 3.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 229 KLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHAK-----GVVLVPTHALRMQTSLMISK 303
Cdd:cd17949    8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRsdgtlALVLVPTRELALQIYEVLEK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 304 LAEG-TNI---KIVGG----SERWRSEEDWDILVSTP-----------SFSPEfftphNIDYIVLDEADMLLDDSFLNDI 364
Cdd:cd17949   88 LLKPfHWIvpgYLIGGekrkSEKARLRKGVNILIATPgrlldhlkntqSFDVS-----NLRWLVLDEADRLLDMGFEKDI 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 312077716 365 IRLLGPLKIRHSVIDKNATDGVRL--IFSSATYPDQLQLIAE-SIVDYEYL 412
Cdd:cd17949  163 TKILELLDDKRSKAGGEKSKPSRRqtVLVSATLTDGVKRLAGlSLKDPVYI 213
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
219-413 3.87e-21

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: 91.88  E-value: 3.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAH-LLIAAETGSGKTAAYAAPLLSALLRN----VNRHAKGVVLVPTHAL 293
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGDdVLARAKTGTGKTLAFLLPAIQSLLNTkpagRRSGVSALIISPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 294 RMQTSLMISKLAEG-TNIKI---VGGSERWRSEEDW-----DILVSTP---------SFSPEFFTphNIDYIVLDEADML 355
Cdd:cd17964   81 ALQIAAEAKKLLQGlRKLRVqsaVGGTSRRAELNRLrrgrpDILVATPgrlidhlenPGVAKAFT--DLDYLVLDEADRL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 312077716 356 LDDSFLNDIIRLLGPLKirhsviDKNATDGVRLIFsSATYPDQLQLIAESIVDYEYLY 413
Cdd:cd17964  159 LDMGFRPDLEQILRHLP------EKNADPRQTLLF-SATVPDEVQQIARLTLKKDYKF 209
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
219-413 6.20e-21

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: 92.72  E-value: 6.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRN--------VNRHAKGVVLVPT 290
Cdd:cd18052   50 LCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfsEVQEPQALIVAPT 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 291 HALRMQTSLMISKLAEGTNIKIV---GG-----SERwRSEEDWDILVSTPSFSPEFFTP-----HNIDYIVLDEADMLLD 357
Cdd:cd18052  130 RELANQIFLEARKFSYGTCIRPVvvyGGvsvghQIR-QIEKGCHILVATPGRLLDFIGRgkislSKLKYLILDEADRMLD 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312077716 358 DSFLNDIIRLL-----GPLKIRHSvidknatdgvrLIFsSATYPDQLQLIAESIVDYEYLY 413
Cdd:cd18052  209 MGFGPEIRKLVsepgmPSKEDRQT-----------LMF-SATFPEEIQRLAAEFLKEDYLF 257
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
219-383 7.09e-21

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: 91.11  E-value: 7.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLR----NVNRHA-KGVVLVPTHAL 293
Cdd:cd17961    1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKakaeSGEEQGtRALILVPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 294 RMQTSLMISKLAEGTN--IKIV-----GGSERWRS--EEDWDILVSTPS------FSPEFFTPHNIDYIVLDEADMLLDD 358
Cdd:cd17961   81 AQQVSKVLEQLTAYCRkdVRVVnlsasSSDSVQRAllAEKPDIVVSTPArllshlESGSLLLLSTLKYLVIDEADLVLSY 160
                        170       180
                 ....*....|....*....|....*
gi 312077716 359 SFLNDIIRLLGPLKIRHSVIDKNAT 383
Cdd:cd17961  161 GYEEDLKSLLSYLPKNYQTFLMSAT 185
HELICc smart00490
helicase superfamily c-terminal domain;
471-547 7.14e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 86.88  E-value: 7.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716   471 VSRSLREMGIEHTSLSGGRRIEQ---LIDELRSGAVRIIIATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGRIGRIG 547
Cdd:smart00490   3 LAELLKELGIKVARLHGGLSQEEreeILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
223-394 3.62e-20

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: 89.61  E-value: 3.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLI-AAETGSGKTAAYAAPLLSALLR--------NVNRHAKGVVLVPTHAL 293
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPAAIRDGKDVIgAAETGSGKTLAFGIPILERLLSqkssngvgGKQKPLRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 294 RMQTSLMISKLAEGTNIK---IVGG-----SERWRSEEDwDILVSTP-------SFSPEFFTP-HNIDYIVLDEAD-MLL 356
Cdd:cd17946   81 AVQVKDHLKAIAKYTNIKiasIVGGlavqkQERLLKKRP-EIVVATPgrlweliQEGNEHLANlKSLRFLVLDEADrMLE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 312077716 357 DDSF--LNDIIRLLGplKIRHSVIDKNATdgvrLIFsSAT 394
Cdd:cd17946  160 KGHFaeLEKILELLN--KDRAGKKRKRQT----FVF-SAT 192
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
252-394 3.46e-19

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: 86.92  E-value: 3.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 252 LLIAAETGSGKTAAYAAPLLSALLRNVNRHAKGVVLVPTHALRMQTSLMISKLAEGTNIKIV---GGSERWRSEEDW--- 325
Cdd:cd17956   39 LCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKVVslsGQKSFKKEQKLLlvd 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 326 ---------DILVSTPS------FSPEFFTPHNIDYIVLDEADMLLDDSFLNDIIRLLGPLKIRHSVIDKNATDG----- 385
Cdd:cd17956  119 tsgrylsrvDILVATPGrlvdhlNSTPGFTLKHLRFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLGSFGDAnller 198
                        170
                 ....*....|...
gi 312077716 386 ----VRLIFSSAT 394
Cdd:cd17956  199 svrpLQKLLFSAT 211
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
223-403 7.85e-19

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: 85.45  E-value: 7.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLR-------NVNRHAKGVVLVPTHALRM 295
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppldeeTKDDGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 296 QTSLMISKLAEGTNIK---IVGGserwRSEEDW--------DILVSTP-----SFSPEFFTPHNIDYIVLDEADMLLDDS 359
Cdd:cd17945   81 QIEEETQKFAKPLGIRvvsIVGG----HSIEEQafslrngcEILIATPgrlldCLERRLLVLNQCTYVVLDEADRMIDMG 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 312077716 360 F---LNDIIRLLGP--LKIRHSVIDKNATDGVR-----LIFsSATYPDQLQLIA 403
Cdd:cd17945  157 FepqVTKILDAMPVsnKKPDTEEAEKLAASGKHryrqtMMF-TATMPPAVEKIA 209
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
219-400 1.64e-18

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: 84.20  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHAkGVVLVPTHALRMQTS 298
Cdd:cd17955    6 LSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIF-ALVLTPTRELAYQIA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 299 LMISKLAEGTNIK---IVGGSERWRSEEDWD----ILVSTP--------SFSPEFFTPHNIDYIVLDEADMLLDDSF--- 360
Cdd:cd17955   85 EQFRALGAPLGLRccvIVGGMDMVKQALELSkrphIVVATPgrladhlrSSDDTTKVLSRVKFLVLDEADRLLTGSFedd 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 312077716 361 LNDIIRLLGPlkirhsvidKNATdgvrLIFsSATYPDQLQ 400
Cdd:cd17955  165 LATILSALPP---------KRQT----LLF-SATLTDALK 190
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
219-547 7.47e-18

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 86.18  E-value: 7.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALL-------RNVNrHAKGVVLVPTH 291
Cdd:PRK04837  15 LHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLshpapedRKVN-QPRALIMAPTR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 292 ALRMQTSLMISKLAEGTNIK--IVGGSERWRS-----EEDWDILVSTpsfspeffTPHNIDY-------------IVLDE 351
Cdd:PRK04837  94 ELAVQIHADAEPLAQATGLKlgLAYGGDGYDKqlkvlESGVDILIGT--------TGRLIDYakqnhinlgaiqvVVLDE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 352 ADMLLDDSFLNDIIRLLGPLKirhsvidkNATDGVRLIFSsATYPDQLQLIA-ESIVDYEYLycvktenlhRIMPHIKqT 430
Cdd:PRK04837 166 ADRMFDLGFIKDIRWLFRRMP--------PANQRLNMLFS-ATLSYRVRELAfEHMNNPEYV---------EVEPEQK-T 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 431 FIRIREidkleklkellekGLSFPHG-------QTLI----------F------CKNL--------KNVGLvsrslremg 479
Cdd:PRK04837 227 GHRIKE-------------ELFYPSNeekmrllQTLIeeewpdraiiFantkhrCEEIwghlaadgHRVGL--------- 284
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312077716 480 iehtsLSGG---RRIEQLIDELRSGAVRIIIATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGRIGRIG 547
Cdd:PRK04837 285 -----LTGDvaqKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAG 350
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
223-405 9.69e-18

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: 81.74  E-value: 9.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAP----LLSALLRNVNRHAKGV-VLVPTHALRMQT 297
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgfihLDLQPIPREQRNGPGVlVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 298 SLMISKLAEgTNIKIV---GGSERWRSEEDW----DILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSFLNDII 365
Cdd:cd17958   81 EAECSKYSY-KGLKSVcvyGGGNRNEQIEDLskgvDIIIATPGrlndlQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 312077716 366 RLLgpLKIRHsviDKnatdgvRLIFSSATYPDQLQLIAES 405
Cdd:cd17958  160 KIL--LDIRP---DR------QTIMTSATWPDGVRRLAQS 188
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
219-407 2.85e-17

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: 80.31  E-value: 2.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSD--AHLLIAAETGSGKTAAYAAPLLSALLRNvNRHAKGVVLVPTHALRMQ 296
Cdd:cd17963    1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPT-LKSPQALCLAPTRELARQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 297 TSLMISKLAEGTNIKI---VGGSERWRSEE-DWDILVSTP-----SFSPEFFTPHNIDYIVLDEAD-MLLDDSFLNDIIR 366
Cdd:cd17963   80 IGEVVEKMGKFTGVKValaVPGNDVPRGKKiTAQIVIGTPgtvldWLKKRQLDLKKIKILVLDEADvMLDTQGHGDQSIR 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 312077716 367 LlgplkirhsvidKNA-TDGVRLIFSSATYPDQLQLIAESIV 407
Cdd:cd17963  160 I------------KRMlPRNCQILLFSATFPDSVRKFAEKIA 189
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
219-369 6.84e-17

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: 79.28  E-value: 6.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFrAFKSDAHLLIA-AETGSGKTAAYAAPLLSALLRNVNR-HAkgVVLVPTHALRMQ 296
Cdd:cd17954    7 VCEELCEACEKLGWKKPTKIQEEAI-PVALQGRDIIGlAETGSGKTAAFALPILQALLENPQRfFA--LVLAPTRELAQQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 297 TSLMISKLAEGTNIK---IVGG----SERWRSEEDWDILVSTPSF------SPEFFTPHNIDYIVLDEADMLLDDSFLND 363
Cdd:cd17954   84 ISEQFEALGSSIGLKsavLVGGmdmmAQAIALAKKPHVIVATPGRlvdhleNTKGFSLKSLKFLVMDEADRLLNMDFEPE 163

                 ....*.
gi 312077716 364 IIRLLG 369
Cdd:cd17954  164 IDKILK 169
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
221-409 8.77e-17

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: 79.29  E-value: 8.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 221 PVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALlrnvnrhaKGVVLVPTHALRMQTSLM 300
Cdd:cd17938    8 PELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV--------VALILEPSRELAEQTYNC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 301 ISKLA-EGTNIKI-----VGG----SERWRSEEDWDILVSTPSFSPEFFTPHNID-----YIVLDEADMLLDDSFLNDII 365
Cdd:cd17938   80 IENFKkYLDNPKLrvallIGGvkarEQLKRLESGVDIVVGTPGRLEDLIKTGKLDlssvrFFVLDEADRLLSQGNLETIN 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 312077716 366 RLlgplkirHSVIDKNATDGVRL--IFSSAT-YPDQLQLIAESIVDY 409
Cdd:cd17938  160 RI-------YNRIPKITSDGKRLqvIVCSATlHSFEVKKLADKIMHF 199
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
161-543 1.70e-16

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 82.77  E-value: 1.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 161 EYNHYEGMRYPPGNILLASTYWVKSKYKNDWFTIHPVMRKNPSFNRDESFSWDENVSLLDPVIIENARKLGFRVPTVI-- 238
Cdd:COG1061    1 VLLRGIAERGADKLRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSfe 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 239 ----QRRAFRAFKSDA-----HLLIAAETGSGKTAayaapLLSALLRNVNRHAKGVVLVPTHALRMQTslmISKLAEGTN 309
Cdd:COG1061   81 lrpyQQEALEALLAALergggRGLVVAPTGTGKTV-----LALALAAELLRGKRVLVLVPRRELLEQW---AEELRRFLG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 310 IKIVGGSERwrsEEDWDILVST-PSFSPEFF---TPHNIDYIVLDEADMLLDDSFLnDIIRLLGPLKI--------Rhsv 377
Cdd:COG1061  153 DPLAGGGKK---DSDAPITVATyQSLARRAHldeLGDRFGLVIIDEAHHAGAPSYR-RILEAFPAAYRlgltatpfR--- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 378 idknaTDGVRLIFS-------SATYPDQLQliAESIVDYEYL------------YCVKTENL-HRIMPHIKQTFIRIREI 437
Cdd:COG1061  226 -----SDGREILLFlfdgivyEYSLKEAIE--DGYLAPPEYYgirvdltderaeYDALSERLrEALAADAERKDKILREL 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 438 DKLEKLKEllekglsfphgQTLIFCKNLKNVGLVSRSLREMGIEHTSLSGG---RRIEQLIDELRSGAVRIIIATDVASR 514
Cdd:COG1061  299 LREHPDDR-----------KTLVFCSSVDHAEALAELLNEAGIRAAVVTGDtpkKEREEILEAFRDGELRILVTVDVLNE 367
                        410       420       430
                 ....*....|....*....|....*....|..
gi 312077716 515 GLDLPQLRHII---NYDFPRQisdYVHRCGRI 543
Cdd:COG1061  368 GVDVPRLDVAIllrPTGSPRE---FIQRLGRG 396
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
251-394 3.17e-16

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 75.90  E-value: 3.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 251 HLLIAAETGSGKTAAYaapLLSALLRNVNRHAKGVVLVPTHALRMQTSLMISKLA-EGTNIKIVGGSE-----RWRSEED 324
Cdd:cd00046    3 NVLITAPTGSGKTLAA---LLAALLLLLKKGKKVLVLVPTKALALQTAERLRELFgPGIRVAVLVGGSsaeerEKNKLGD 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312077716 325 WDILVSTPSF------SPEFFTPHNIDYIVLDEADMLLDDSFLNDIIRLLgplkirhsvIDKNATDGVRLIFSSAT 394
Cdd:cd00046   80 ADIIIATPDMllnlllREDRLFLKDLKLIIVDEAHALLIDSRGALILDLA---------VRKAGLKNAQVILLSAT 146
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
229-371 1.15e-15

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: 75.69  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 229 KLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLR----NVNRHAKGVVLVPTHALRMQTSLMISKL 304
Cdd:cd17960    7 ELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKrkanLKKGQVGALIISPTRELATQIYEVLQSF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 305 AEGTNIKI-----VGGSE-----RWRSEEDWDILVSTPSFSPEFFT-------PHNIDYIVLDEADMLLDDSFLNDIIRL 367
Cdd:cd17960   87 LEHHLPKLkcqllIGGTNveedvKKFKRNGPNILVGTPGRLEELLSrkadkvkVKSLEVLVLDEADRLLDLGFEADLNRI 166

                 ....
gi 312077716 368 LGPL 371
Cdd:cd17960  167 LSKL 170
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
231-414 1.03e-14

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: 73.09  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 231 GFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHAKG---VVLVPTHALRMQTSLMISKLAEG 307
Cdd:cd17941    9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGlgaLIISPTRELAMQIFEVLRKVGKY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 308 TNIK---IVGGS----ERWRSEEdWDILVSTPSF-------SPEFFTPhNIDYIVLDEADMLLDDSF---LNDIIRLLGP 370
Cdd:cd17941   89 HSFSaglIIGGKdvkeEKERINR-MNILVCTPGRllqhmdeTPGFDTS-NLQMLVLDEADRILDMGFketLDAIVENLPK 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 312077716 371 lkirhsvidKNATdgvrLIFsSATYPDQLQLIAE-SIVDYEYLYC 414
Cdd:cd17941  167 ---------SRQT----LLF-SATQTKSVKDLARlSLKNPEYISV 197
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
223-408 2.39e-14

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: 72.06  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHAK----GVVLVPTHALRMQTS 298
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGegpiAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 299 LMISKLAEGTNIKIV---GGSERWRS----EEDWDILVSTPSFSPEFF-----TPHNIDYIVLDEADMLLDDSFlndiir 366
Cdd:cd17952   81 LEAKKFGKAYNLRVVavyGGGSKWEQakalQEGAEIVVATPGRLIDMVkkkatNLQRVTYLVLDEADRMFDMGF------ 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 312077716 367 llGPlKIRhSVIDKNATDGVRLIFsSATYPDQLQLIAESIVD 408
Cdd:cd17952  155 --EY-QVR-SIVGHVRPDRQTLLF-SATFKKKIEQLARDILS 191
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
231-406 2.80e-14

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: 71.59  E-value: 2.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 231 GFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRhAKGVVLVPTHALRMQTSLMISKLAEGTNI 310
Cdd:cd17939   16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRE-TQALVLAPTRELAQQIQKVVKALGDYMGV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 311 KI---VGGS----ERWRSEEDWDILVSTP-----SFSPEFFTPHNIDYIVLDEADMLLDDSF---LNDIIRLLgPLKIrh 375
Cdd:cd17939   95 KVhacIGGTsvreDRRKLQYGPHIVVGTPgrvfdMLQRRSLRTDKIKMFVLDEADEMLSRGFkdqIYDIFQFL-PPET-- 171
                        170       180       190
                 ....*....|....*....|....*....|.
gi 312077716 376 svidknatdgvRLIFSSATYPDQLQLIAESI 406
Cdd:cd17939  172 -----------QVVLFSATMPHEVLEVTKKF 191
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
228-368 3.33e-14

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: 71.62  E-value: 3.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 228 RKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSAL--LRNVNRHAKGV-VLVPTHALRMQT-----SL 299
Cdd:cd17942    6 EEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLykLKFKPRNGTGViIISPTRELALQIygvakEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 300 MisKLAEGTNIKIVGGSERwRSEED-----WDILVSTP-------SFSPEFFTpHNIDYIVLDEADMLLDDSF---LNDI 364
Cdd:cd17942   86 L--KYHSQTFGIVIGGANR-KAEAEklgkgVNILVATPgrlldhlQNTKGFLY-KNLQCLIIDEADRILEIGFeeeMRQI 161

                 ....
gi 312077716 365 IRLL 368
Cdd:cd17942  162 IKLL 165
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
228-406 4.49e-14

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: 71.64  E-value: 4.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 228 RKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLsallrnvnRHAK------------GVVLVPTHALRM 295
Cdd:cd17953   28 KKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMF--------RHIKdqrpvkpgegpiGLIMAPTRELAL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 296 QTSLMISKLAEGTNIKIV---GGS-------ERWRSEEdwdILVSTPSFSPEFFTPHN--------IDYIVLDEADMLLD 357
Cdd:cd17953  100 QIYVECKKFSKALGLRVVcvyGGSgiseqiaELKRGAE---IVVCTPGRMIDILTANNgrvtnlrrVTYVVLDEADRMFD 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 312077716 358 DSFLNDIIRllgplkirhsvIDKNATDGVRLIFSSATYPDQLQLIAESI 406
Cdd:cd17953  177 MGFEPQIMK-----------IVNNIRPDRQTVLFSATFPRKVEALARKV 214
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
219-396 8.30e-14

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: 70.40  E-value: 8.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALlRNVNRHAKGVVLVPTHALRMQTS 298
Cdd:cd17940    6 LKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-DPKKDVIQALILVPTRELALQTS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 299 LMISKLAEGTNIKI---VGGS----ERWRSEEDWDILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSFLNDIIR 366
Cdd:cd17940   85 QVCKELGKHMGVKVmvtTGGTslrdDIMRLYQTVHVLVGTPGrildlAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEK 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 312077716 367 LLGPLKIRHSVidknatdgvrLIFsSATYP 396
Cdd:cd17940  165 ILNFLPKERQI----------LLF-SATFP 183
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
223-405 3.11e-13

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: 68.55  E-value: 3.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAP-LLSALLRNVNRHAKG---VVLVPTHALRMQTS 298
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPaIVHINAQPPLERGDGpivLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 299 LMISKLAEGTNIK---IVGGSERWRSEEDW----DILVSTPSFSPEFF-----TPHNIDYIVLDEADMLLDDSFLNDIIR 366
Cdd:cd17966   81 QEANKFGGSSRLRntcVYGGAPKGPQIRDLrrgvEICIATPGRLIDFLdqgktNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 312077716 367 LLGplKIRhsvidknaTDGVRLIFsSATYPDQLQLIAES 405
Cdd:cd17966  161 IVD--QIR--------PDRQTLMW-SATWPKEVRRLAED 188
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
226-383 1.15e-12

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: 66.80  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 226 NARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVnRHAKGVVLVPTHALRMQTSLMISKLA 305
Cdd:cd17962    4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEH-RNPSALILTPTRELAVQIEDQAKELM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 306 EGT-NIK---IVGG----SERWRSEEDWDILVSTPSFSPEFFTPH-----NIDYIVLDEADMLLDDSFLNDIIRLLGPLK 372
Cdd:cd17962   83 KGLpPMKtalLVGGlplpPQLYRLQQGVKVIIATPGRLLDILKQSsveldNIKIVVVDEADTMLKMGFQQQVLDILENIS 162
                        170
                 ....*....|.
gi 312077716 373 IRHSVIDKNAT 383
Cdd:cd17962  163 HDHQTILVSAT 173
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
219-545 1.35e-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: 70.63  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRnvNRHAKGVVLVPTHAL----- 293
Cdd:COG1205   41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE--DPGATALYLYPTKALardql 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 294 -RMQTslMISKLAEGTNIKIVGG----SERWRSEEDWDILVSTP-----SFSP------EFFTphNIDYIVLDEAD---- 353
Cdd:COG1205  119 rRLRE--LAEALGLGVRVATYDGdtppEERRWIREHPDIVLTNPdmlhyGLLPhhtrwaRFFR--NLRYVVIDEAHtyrg 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 354 -------MLLDDsfLNDIIRLLG--PlkirhsvidknatdgvRLIFSSATY--PDQLqliAESIVDYEYLycVKTEN--- 419
Cdd:COG1205  195 vfgshvaNVLRR--LRRICRHYGsdP----------------QFILASATIgnPAEH---AERLTGRPVT--VVDEDgsp 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 420 ---LHRIM--PHIKQTFIR------IREIdklekLKELLEKGLsfphgQTLIFCKNLKNVGLVSRSLREMGIEH------ 482
Cdd:COG1205  252 rgeRTFVLwnPPLVDDGIRrsalaeAARL-----LADLVREGL-----RTLVFTRSRRGAELLARYARRALREPdladrv 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312077716 483 TSLSGG------RRIEQlidELRSGAVRIIIATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGRIGR 545
Cdd:COG1205  322 AAYRAGylpeerREIER---GLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGR 387
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
238-397 1.88e-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: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 238 IQRRAFR-AFKSDAHLLIAAETGSGKT-AAYAapllsALLRNVNRHAKGVV-LVPTHALRMQtslMISKLAE-----GTN 309
Cdd:cd17921    5 IQREALRaLYLSGDSVLVSAPTSSGKTlIAEL-----AILRALATSGGKAVyIAPTRALVNQ---KEADLRErfgplGKN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 310 IKIVGGSERWRSEE--DWDILVSTP-------SFSPEFFTPHnIDYIVLDEADMLLDDS---FLNDIIRLLgplkirhsv 377
Cdd:cd17921   77 VGLLTGDPSVNKLLlaEADILVATPekldlllRNGGERLIQD-VRLVVVDEAHLIGDGErgvVLELLLSRL--------- 146
                        170       180
                 ....*....|....*....|
gi 312077716 378 idKNATDGVRLIFSSATYPD 397
Cdd:cd17921  147 --LRINKNARFVGLSATLPN 164
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
223-413 2.37e-11

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: 64.29  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLG-FRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLS---------ALLRNVNRHAK------GVV 286
Cdd:cd18051   31 IIRNNIELArYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSqiyeqgpgeSLPSESGYYGRrkqyplALV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 287 LVPTHALRMQTSLMISKLAEGTNIK---IVGGSERWRSEEDWD----ILVSTPSFSPEFFTP-----HNIDYIVLDEADM 354
Cdd:cd18051  111 LAPTRELASQIYDEARKFAYRSRVRpcvVYGGADIGQQMRDLErgchLLVATPGRLVDMLERgkiglDYCKYLVLDEADR 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312077716 355 LLDDSFLNDIIRllgplkirhsVIDKNAT--DGVR--LIFsSATYPDQLQLIAESIVDyEYLY 413
Cdd:cd18051  191 MLDMGFEPQIRR----------IVEQDTMppTGERqtLMF-SATFPKEIQMLARDFLD-NYIF 241
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
227-411 6.12e-11

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: 62.17  E-value: 6.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 227 ARKLGFRVPtvIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHAKG-----VVLVPTHALRMQTSLMI 301
Cdd:cd17944    7 ARGVTYLFP--IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGrapkvLVLAPTRELANQVTKDF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 302 SKLAEGTNIKIVGGSERWRSEEDW-----DILVSTPSFSPEFFTPHNID-----YIVLDEADMLLDDSFLNDIIRLLgpl 371
Cdd:cd17944   85 KDITRKLSVACFYGGTPYQQQIFAirngiDILVGTPGRIKDHLQNGRLDltklkHVVLDEVDQMLDMGFAEQVEEIL--- 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 312077716 372 kirHSVIDKNATDGVRLIFSSATYPDQLQLIAESIVDYEY 411
Cdd:cd17944  162 ---SVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQY 198
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
223-399 6.84e-11

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: 61.90  E-value: 6.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNvNRHAKGVVLVPTHALRMQTSLMIS 302
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE-RRHPQVLILAPTREIAVQIHDVFK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 303 KLAE-GTNIKI---VGGSERWRSEEDWD---ILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSFLNDIirllgp 370
Cdd:cd17943   80 KIGKkLEGLKCevfIGGTPVKEDKKKLKgchIAVGTPGrikqlIELGALNVSHVRLFVLDEADKLMEGSFQKDV------ 153
                        170       180
                 ....*....|....*....|....*....
gi 312077716 371 lkirhSVIDKNATDGVRLIFSSATYPDQL 399
Cdd:cd17943  154 -----NWIFSSLPKNKQVIAFSATYPKNL 177
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
231-396 1.77e-10

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: 60.92  E-value: 1.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 231 GFRVPTVIQRRAFRAFkSDAHLLIA-AETGSGKTAAYAAPLLSALLRNVnRHAKGVVLVPTHALRMQTSLMISKLAEGTN 309
Cdd:cd18046   18 GFEKPSAIQQRAIMPC-IKGYDVIAqAQSGTGKTATFSISILQQIDTSL-KATQALVLAPTRELAQQIQKVVMALGDYMG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 310 IKI---VGGS----ERWRSEEDWDILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLDDSF---LNDIIRLLGPlkir 374
Cdd:cd18046   96 IKChacIGGTsvrdDAQKLQAGPHIVVGTPGrvfdmINRRYLRTDYIKMFVLDEADEMLSRGFkdqIYDIFQKLPP---- 171
                        170       180
                 ....*....|....*....|..
gi 312077716 375 hsvidknatdGVRLIFSSATYP 396
Cdd:cd18046  172 ----------DTQVVLLSATMP 183
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
231-370 1.79e-10

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: 60.56  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 231 GFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVnRHAKGVVLVPTHALRMQTSLMISKLAEGTNI 310
Cdd:cd18045   18 GFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQV-RETQALILSPTRELAVQIQKVLLALGDYMNV 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312077716 311 KI---VGGS----ERWRSEEDWDILVSTPSFSPEFFT-----PHNIDYIVLDEADMLLDDSF---LNDIIRLLGP 370
Cdd:cd18045   97 QChacIGGTsvgdDIRKLDYGQHIVSGTPGRVFDMIRrrslrTRHIKMLVLDEADEMLNKGFkeqIYDVYRYLPP 171
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
217-394 3.05e-10

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 62.99  E-value: 3.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 217 SLLDPVIIENARKLGFRVPTVIQRRAFRA-FKSDAHLLIAAETGSGKTA-AYaapllSALLRNVNRHAKGVVLVPTHALR 294
Cdd:COG1204    5 ELPLEKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLiAE-----LAILKALLNGGKALYIVPLRALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 295 MQTSLMISKLAEGTNIKIVGGSERWRSEEDW----DILVSTP-------SFSPEFFTphNIDYIVLDEADMLLDDSflnd 363
Cdd:COG1204   80 SEKYREFKRDFEELGIKVGVSTGDYDSDDEWlgryDILVATPekldsllRNGPSWLR--DVDLVVVDEAHLIDDES---- 153
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 312077716 364 iiRllGPL------KIRHSVidknatDGVRLIFSSAT 394
Cdd:COG1204  154 --R--GPTlevllaRLRRLN------PEAQIVALSAT 180
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
230-420 4.08e-10

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: 60.42  E-value: 4.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 230 LGFRVPTVIQRRAFRAFKSD--AHLLIAAETGSGKTAAYAAPLLSALLRNvNRHAKGVVLVPTHALRMQTSLMISKLAEG 307
Cdd:cd18048   36 MGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAL-KLYPQCLCLSPTFELALQTGKVVEEMGKF 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 308 TN-IKIV----GGSERWRSEEDWDILVSTPS------FSPEFFTPHNIDYIVLDEADMLLDDSFLNDiirllgplkirHS 376
Cdd:cd18048  115 CVgIQVIyairGNRPGKGTDIEAQIVIGTPGtvldwcFKLRLIDVTNISVFVLDEADVMINVQGHSD-----------HS 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 312077716 377 V-IDKNATDGVRLIFSSATYPDQLQLIAESIVDYEYLYCVKTENL 420
Cdd:cd18048  184 VrVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEEL 228
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
505-548 1.51e-09

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 54.63  E-value: 1.51e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 312077716 505 IIIATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGRIGRIGS 548
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
223-409 4.20e-09

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: 57.33  E-value: 4.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYaapLLSALLrNVN-----RHAKG---VVLVPTHALR 294
Cdd:cd18049   35 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSY---LLPAIV-HINhqpflERGDGpicLVLAPTRELA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 295 MQTSLMISKLAEGTNIK---IVGGSERWRSEEDW----DILVSTPSFSPEFFTPHNID-----YIVLDEADMLLDDSFLN 362
Cdd:cd18049  111 QQVQQVAAEYGRACRLKstcIYGGAPKGPQIRDLergvEICIATPGRLIDFLEAGKTNlrrctYLVLDEADRMLDMGFEP 190
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 312077716 363 DIirllgplkirHSVIDKNATDGVRLIFsSATYPDQLQLIAESIV-DY 409
Cdd:cd18049  191 QI----------RKIVDQIRPDRQTLMW-SATWPKEVRQLAEDFLkDY 227
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
232-409 7.49e-09

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: 56.94  E-value: 7.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 232 FRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYaapLLSALLrNVNRHA---KG-----VVLVPTHALRMQTSLMISK 303
Cdd:cd18050   82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAY---LLPAIV-HINHQPyleRGdgpicLVLAPTRELAQQVQQVADD 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 304 LAEGTNIK---IVGGSERWRSEEDW----DILVSTPSFSPEFFTPHNID-----YIVLDEADMLLDDSFLNDIirllgpl 371
Cdd:cd18050  158 YGKSSRLKstcIYGGAPKGPQIRDLergvEICIATPGRLIDFLEAGKTNlrrctYLVLDEADRMLDMGFEPQI------- 230
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 312077716 372 kirHSVIDKNATDGVRLIFsSATYPDQLQLIAESIV-DY 409
Cdd:cd18050  231 ---RKIVDQIRPDRQTLMW-SATWPKEVRQLAEDFLrDY 265
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
239-394 8.70e-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: 55.28  E-value: 8.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 239 QRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRnvNRHAKGVVLVPTHAL-RMQTSLM---ISKLAEGTNIKIVG 314
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLR--DPGSRALYLYPTKALaQDQLRSLrelLEQLGLGIRVATYD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 315 GSERWRSEEDW-----DILVSTP-----------SFSPEFFTphNIDYIVLDEADMlLDDSFLNDIIRLLGPLKIRHSVI 378
Cdd:cd17923   83 GDTPREERRAIirnppRILLTNPdmlhyallphhDRWARFLR--NLRYVVLDEAHT-YRGVFGSHVALLLRRLRRLCRRY 159
                        170
                 ....*....|....*.
gi 312077716 379 DKNatdgVRLIFSSAT 394
Cdd:cd17923  160 GAD----PQFILTSAT 171
ResIII pfam04851
Type III restriction enzyme, res subunit;
239-352 1.34e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 54.22  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716  239 QRRAFRAFKS-----DAHLLIAAETGSGKTAAYAAplLSALLRNVNRHAKGVVLVPTHALRMQTSLMISKLAEGT--NIK 311
Cdd:pfam04851   8 QIEAIENLLEsikngQKRGLIVMATGSGKTLTAAK--LIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYveIGE 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 312077716  312 IVGGSERWRSEEDWDILVSTP-SFSPEF------FTPHNIDYIVLDEA 352
Cdd:pfam04851  86 IISGDKKDESVDDNKIVVTTIqSLYKALelasleLLPDFFDVIIIDEA 133
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
219-407 2.27e-08

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: 54.73  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 219 LDPVIIENARKLGFRVPTVIQRRAFRAFKSD--AHLLIAAETGSGKTAAYAAPLLSAlLRNVNRHAKGVVLVPTHALRMQ 296
Cdd:cd18047    8 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ-VEPANKYPQCLCLSPTYELALQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 297 TSLMISKLA----EGTNIKIVGGSERWRSEEDWD-ILVSTPS------FSPEFFTPHNIDYIVLDEADMLLDDSFLNDii 365
Cdd:cd18047   87 TGKVIEQMGkfypELKLAYAVRGNKLERGQKISEqIVIGTPGtvldwcSKLKFIDPKKIKVFVLDEADVMIATQGHQD-- 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 312077716 366 rllgpLKIRhsvIDKNATDGVRLIFSSATYPDQLQLIAESIV 407
Cdd:cd18047  165 -----QSIR---IQRMLPRNCQMLLFSATFEDSVWKFAQKVV 198
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
453-554 1.17e-07

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: 51.06  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 453 FPHGQTLIFCKNLKNVGLVSRSLREMGIE----HTSL-SGGRRIEQ---LIDELRsgavrIIIATDVASRGLDLPQLRHI 524
Cdd:cd18794   28 HLGGSGIIYCLSRKECEQVAARLQSKGISaaayHAGLePSDRRDVQrkwLRDKIQ-----VIVATVAFGMGIDKPDVRFV 102
                         90       100       110
                 ....*....|....*....|....*....|
gi 312077716 525 INYDFPRQISDYVHRCGRIGRIGSLHKCLM 554
Cdd:cd18794  103 IHYSLPKSMESYYQESGRAGRDGLPSECIL 132
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
223-351 1.34e-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: 52.03  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRvPTVIQRRAFRAFKSDAH------LLIAAETGSGKTAAYaapLLSALLrNVNRHAKGVVLVPTHALRMQ 296
Cdd:cd17918    5 IQELCKSLPFS-LTKDQAQAIKDIEKDLHspepmdRLLSGDVGSGKTLVA---LGAALL-AYKNGKQVAILVPTEILAHQ 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 312077716 297 TSLMISKLAEGTNIKIVGGSERWRSEEDWDILVSTPSFSPEFFTPHNIDYIVLDE 351
Cdd:cd17918   80 HYEEARKFLPFINVELVTGGTKAQILSGISLLVGTHALLHLDVKFKNLDLVIVDE 134
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
228-394 1.74e-07

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 51.56  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 228 RKLGFRvPTVIQRR-AFRAFKSDAHLLIAAeTGSGKTAAyaapLLSALLRNVNRHAKGVVLVPTHALRMQTSLMISKLAE 306
Cdd:cd17924   12 KKTGFP-PWGAQRTwAKRLLRGKSFAIIAP-TGVGKTTF----GLATSLYLASKGKRSYLIFPTKSLVKQAYERLSKYAE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 307 --GTNIKIV---GGSERWRSEE--------DWDILVSTPSFSPEFF---TPHNIDYIVLDEADMLLDDSflNDIIRLLGP 370
Cdd:cd17924   86 kaGVEVKILvyhSRLKKKEKEEllekiekgDFDILVTTNQFLSKNFdllSNKKFDFVFVDDVDAVLKSS--KNIDRLLKL 163
                        170       180
                 ....*....|....*....|....
gi 312077716 371 LKIRhsvidknatdgvRLIFSSAT 394
Cdd:cd17924  164 LGFG------------QLVVSSAT 175
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
489-542 3.51e-07

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: 49.90  E-value: 3.51e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 312077716 489 RRIEQLIDELRSGAVRIIIATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGR 542
Cdd:cd18802   77 RKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
241-352 3.75e-07

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 49.61  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 241 RAFRAFKSDAHLLIAAETGSGKTAAYAAplLSALLRNvnrhAKGVVLVPTHALRMQTSlmiSKLAEGTNIKIVG--GSER 318
Cdd:cd17926   10 EAWLAHKNNRRGILVLPTGSGKTLTALA--LIAYLKE----LRTLIVVPTDALLDQWK---ERFEDFLGDSSIGliGGGK 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 312077716 319 WRSEEDWDILVSTPS-----FSPEFFTPHNIDYIVLDEA 352
Cdd:cd17926   81 KKDFDDANVVVATYQslsnlAEEEKDLFDQFGLLIVDEA 119
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
252-547 6.25e-07

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 51.66  E-value: 6.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 252 LLIAAETGSGKT---AAYAAPLLSALLRNvnrhaKGVVLVPTHAL------RMQTSL----MISKLAEGTNIKIVGGSER 318
Cdd:cd09639    2 LVIEAPTGYGKTeaaLLWALHSLKSQKAD-----RVIIALPTRATinamyrRAKEAFgetgLYHSSILSSRIKEMGDSEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 319 WRSEEDW------------------DILVS--TPSFSPEFFTPHNIDY--IVLDEADmLLDDSFLNDIIRLLGPLKirhs 376
Cdd:cd09639   77 FEHLFPLyihsndtlfldpitvctiDQVLKsvFGEFGHYEFTLASIANslLIFDEVH-FYDEYTLALILAVLEVLK---- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 377 viDKnatdGVRLIFSSATYPDQLQLIAESIvdyeyLYCVKTENLHRImpHIKQTFIRIREIDKLEKLKELLEKGLSFPH- 455
Cdd:cd09639  152 --DN----DVPILLMSATLPKFLKEYAEKI-----GYVEENEPLDLK--PNERAPFIKIESDKVGEISSLERLLEFIKKg 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 456 GQTLIFCKNLKNVGLVSRSLREMGIE------HTSLSGGRRIE---QLIDELRSGAVRIIIATDVASRGLDlpqlrhiIN 526
Cdd:cd09639  219 GSVAIIVNTVDRAQEFYQQLKEKGPEeeimliHSRFTEKDRAKkeaELLLEFKKSEKFVIVATQVIEASLD-------IS 291
                        330       340
                 ....*....|....*....|....*
gi 312077716 527 YDF----PRQISDYVHRCGRIGRIG 547
Cdd:cd09639  292 VDVmiteLAPIDSLIQRLGRLHRYG 316
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
238-545 1.05e-06

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 51.62  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 238 IQRRAFRAFKSDAHL-----LIAAETGSGKT-AA-----------------YAAPLLSALLRNVNRhakgVVLVPTHALR 294
Cdd:COG1203  131 LQNEALELALEAAEEepglfILTAPTGGGKTeAAllfalrlaakhggrriiYALPFTSIINQTYDR----LRDLFGEDVL 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 295 MQTSLmiSKLAEGTNIKIVGGSERWRSE--EDWD--ILVSTP------SFSP--EFFTP-HNIDY--IVLDEADMLlDDS 359
Cdd:COG1203  207 LHHSL--ADLDLLEEEEEYESEARWLKLlkELWDapVVVTTIdqlfesLFSNrkGQERRlHNLANsvIILDEVQAY-PPY 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 360 FLNDIIRLLGPLKIRhsvidknatdGVRLIFSSATYPdqlQLIAESIVDYEYLYCVKTENLHRIMPHIKQTFIRIREIDK 439
Cdd:COG1203  284 MLALLLRLLEWLKNL----------GGSVILMTATLP---PLLREELLEAYELIPDEPEELPEYFRAFVRKRVELKEGPL 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 440 LEKLKELLEKGLSFPHGQTLIFCKNLKNVGLVSRSLREMGIE------HTSLSGGRR---IEQLIDELRSGAVRIIIATD 510
Cdd:COG1203  351 SDEELAELILEALHKGKSVLVIVNTVKDAQELYEALKEKLPDeevyllHSRFCPADRseiEKEIKERLERGKPCILVSTQ 430
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 312077716 511 VASRGLDLpqlrhiinyDFPRQISDY------VHRCGRIGR 545
Cdd:COG1203  431 VVEAGVDI---------DFDVVIRDLapldslIQRAGRCNR 462
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
457-545 4.52e-06

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: 46.48  E-value: 4.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 457 QTLIFCKNLKNVGLVSRSLREMGIEHTSLS-------GG------RRIEqliDELRSGAVRIIIATDVASRGLDLPQLRH 523
Cdd:cd18797   37 KTIVFCRSRKLAELLLRYLKARLVEEGPLAskvasyrAGylaedrREIE---AELFNGELLGVVATNALELGIDIGGLDA 113
                         90       100
                 ....*....|....*....|..
gi 312077716 524 IINYDFPRQISDYVHRCGRIGR 545
Cdd:cd18797  114 VVLAGYPGSLASLWQQAGRAGR 135
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
223-405 5.34e-06

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: 47.72  E-value: 5.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 223 IIENARKLGFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHA-------KGVVLVPTHALRM 295
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPfikgegpYGLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 296 QTSLMIS----KLAEGTNIKI-----VGG---SERWRS-EEDWDILVSTPS-----FSPEFFTPHNIDYIVLDEADMLLD 357
Cdd:cd17951   81 QTHEVIEyyckALQEGGYPQLrcllcIGGmsvKEQLEViRKGVHIVVATPGrlmdmLNKKKINLDICRYLCLDEADRMID 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 312077716 358 DSFLNDIIRLLGPLKirhsvidknatdGVR--LIFsSATYPDQLQLIAES 405
Cdd:cd17951  161 MGFEEDIRTIFSYFK------------GQRqtLLF-SATMPKKIQNFAKS 197
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
211-293 6.21e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 49.33  E-value: 6.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 211 SWDENVSLLDPVIIE--NARklgFRVPTVIQRRAFRAFKSDAHLLIAAETGSGKTaaYAApLLSALLRNVNRHAKGVVLV 288
Cdd:COG1201    2 SAEDVLSLLHPAVRAwfAAR---FGAPTPPQREAWPAIAAGESTLLIAPTGSGKT--LAA-FLPALDELARRPRPGELPD 75

                 ....*
gi 312077716 289 PTHAL 293
Cdd:COG1201   76 GLRVL 80
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
240-352 7.90e-06

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 46.40  E-value: 7.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 240 RRAFRAFKSDA--HLLIAAeTGSGKTaaYAAPLLSALLRNVNRHAKGVVLVPTHALRMQTSLMISKLAEGTNIKIVGGSE 317
Cdd:cd18032   10 EALEEAREKGQrrALLVMA-TGTGKT--YTAAFLIKRLLEANRKKRILFLAHREELLEQAERSFKEVLPDGSFGNLKGGK 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 312077716 318 rwRSEEDWDILVST-PS---------FSPEFFtphniDYIVLDEA 352
Cdd:cd18032   87 --KKPDDARVVFATvQTlnkrkrlekFPPDYF-----DLIIIDEA 124
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
239-358 1.45e-05

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 45.79  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 239 QRRAFRA-FKSDAHLLIAAETGSGKTaayaapLLS--ALLRNVNRHAKGVVLVPTHALRMQTSLMISKLAE-GTNIKIVG 314
Cdd:cd18028    6 QAEAVRAgLLKGENLLISIPTASGKT------LIAemAMVNTLLEGGKALYLVPLRALASEKYEEFKKLEEiGLKVGIST 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 312077716 315 GSerWRSEEDW----DILVSTPS-------FSPEFFtpHNIDYIVLDEADMLLDD 358
Cdd:cd18028   80 GD--YDEDDEWlgdyDIIVATYEkfdsllrHSPSWL--RDVGVVVVDEIHLISDE 130
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
459-547 5.40e-05

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 46.37  E-value: 5.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 459 LIFCKNLKNVGLVSRSLREMGIEHTSLSGG----RRiEQLIDELRSG--AVRIIIATDVASRGLDLPQLRHIINYDFP-- 530
Cdd:COG0553  553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGtsaeER-DELVDRFQEGpeAPVFLISLKAGGEGLNLTAADHVIHYDLWwn 631
                         90       100
                 ....*....|....*....|.
gi 312077716 531 ----RQisdyvhRCGRIGRIG 547
Cdd:COG0553  632 paveEQ------AIDRAHRIG 646
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
251-410 1.15e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 42.75  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716   251 HLLIAAETGSGKTAayaapLLSALLRNVNRHAKGVVLVPTHALRMQTSLMISKLAEGTNIKIVGGSERwrsEEDWDILVS 330
Cdd:smart00382   4 VILIVGPPGSGKTT-----LARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELR---LRLALALAR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716   331 TpsfspefftpHNIDYIVLDEADMLLDDSFLNDIIRLLgplkIRHSVIDKNATDGVRLIFSSATYPDQLQLIAESIVDYE 410
Cdd:smart00382  76 K----------LKPDVLILDEITSLLDAEQEALLLLLE----ELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRR 141
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
459-547 2.68e-04

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: 41.31  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 459 LIFCKNLKNVGLVSRSLREMGIEHTSLSGGRRIEQ---LIDELR--SGAVRIIIATDVASRGLDLPQLRHIINYDFP--- 530
Cdd:cd18793   31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKErqkLVDRFNedPDIRVFLLSTKAGGVGLNLTAANRVILYDPWwnp 110
                         90       100
                 ....*....|....*....|
gi 312077716 531 ---RQisdyvhRCGRIGRIG 547
Cdd:cd18793  111 aveEQ------AIDRAHRIG 124
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
239-352 3.36e-04

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: 42.25  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 239 QRRAFRAFKsDAHLLIAAETGSGKTAAyAAPLLSALLRNVNRHAKG----VVLVPTHAL--------RMQTSLMISKLAE 306
Cdd:cd18034    7 QLELFEAAL-KRNTIVVLPTGSGKTLI-AVMLIKEMGELNRKEKNPkkraVFLVPTVPLvaqqaeaiRSHTDLKVGEYSG 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 312077716 307 GTNIKIvGGSERWRSE-EDWDILVSTP-----SFSPEFFTPHNIDYIVLDEA 352
Cdd:cd18034   85 EMGVDK-WTKERWKEElEKYDVLVMTAqilldALRHGFLSLSDINLLIFDEC 135
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
459-547 3.38e-04

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 43.55  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 459 LIFCKNLKNVGLVSRSLREMGIE----HTSLSGGRRiEQLIDELRSGAVRIIIATDVASRGLDLPQLRHIINYDFPRQIS 534
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISaaayHAGLDNDVR-ADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIE 318
                         90
                 ....*....|...
gi 312077716 535 DYVHRCGRIGRIG 547
Cdd:PRK11057 319 SYYQETGRAGRDG 331
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
492-548 7.01e-04

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 42.79  E-value: 7.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 312077716 492 EQLIDELRSGAVRIIIATDVASRGLDLPQLRHIINYD-FPRQISdYVHRCGRIGRIGS 548
Cdd:COG1111  401 IEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPSEIR-SIQRKGRTGRKRE 457
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
454-547 8.10e-04

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 40.23  E-value: 8.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 454 PHGQTLIFCKNLKNVGLVSRSLREMGIEHTSLSggrRIE-QLIDEL-RSGAVRIIIATDVASRGLDLPQLRHII------ 525
Cdd:cd18795   42 EGKPVLVFCSSRKECEKTAKDLAGIAFHHAGLT---REDrELVEELfREGLIKVLVATSTLAAGVNLPARTVIIkgtqry 118
                         90       100
                 ....*....|....*....|....
gi 312077716 526 NYDFPRQIS--DYVHRCGRIGRIG 547
Cdd:cd18795  119 DGKGYRELSplEYLQMIGRAGRPG 142
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
484-545 1.25e-03

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: 39.65  E-value: 1.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312077716 484 SLSGGRRIEQL--IDELRSGAVRIIIATDVASRGLDLPQLRHIINYDFPRQISDYVHRCGRIGR 545
Cdd:cd18801   70 SSKGMSQKEQKevIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
455-545 1.48e-03

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: 39.55  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 455 HGQTLIFCKNLKNVGLVSRSLREM----------GIEHTSLSGGRRiEQLIDELRSGAVRIIIATDVASRGLDLPQLRHI 524
Cdd:cd18796   38 HKSTLVFTNTRSQAERLAQRLRELcpdrvppdfiALHHGSLSRELR-EEVEAALKRGDLKVVVATSSLELGIDIGDVDLV 116
                         90       100
                 ....*....|....*....|.
gi 312077716 525 INYDFPRQISDYVHRCGRIGR 545
Cdd:cd18796  117 IQIGSPKSVARLLQRLGRSGH 137
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
238-397 1.56e-03

N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 40.43  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 238 IQRRAFR-AFKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNRHA-------KGVVLVPTHALRMQTSLMISKLAEGTN 309
Cdd:cd18019   21 IQSKLFPaAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGtinldafKIVYIAPMKALVQEMVGNFSKRLAPYG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312077716 310 IKI---VGGSERWRSE-EDWDILVSTPS-------FSPEFFTPHNIDYIVLDEADMLLDDSflndiirllGPL------- 371
Cdd:cd18019  101 ITVaelTGDQQLTKEQiSETQIIVTTPEkwdiitrKSGDRTYTQLVRLIIIDEIHLLHDDR---------GPVlesivar 171
                        170       180
                 ....*....|....*....|....*.
gi 312077716 372 KIRHSvidKNATDGVRLIFSSATYPD 397
Cdd:cd18019  172 TIRQI---EQTQEYVRLVGLSATLPN 194
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
472-541 3.85e-03

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 39.45  E-value: 3.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312077716 472 SRSLREMGIEHTSLSGGRRIEQLI--DELRSGAVRIIIATDVASRGL--DLPQLrhiINYDFPRQISDYVHRCG 541
Cdd:cd06218  117 AKQLAERGIKVTVLLGFRSADDLFlvEEFEALGAEVYVATDDGSAGTkgFVTDL---LKELLAEARPDVVYACG 187
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
458-525 5.15e-03

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 37.15  E-value: 5.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312077716 458 TLIFCKNLKNVGLVSRSLREMGIEHTSLSGG-----RRIEQLI-DELRSGAVRIIIATDVASRGLDLPQLRHII 525
Cdd:cd18799    9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysdreRGDEALIlLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
238-293 8.30e-03

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 38.01  E-value: 8.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 312077716 238 IQRRAFRA-FKSDAHLLIAAETGSGKTAAYAAPLLSALLRNVNrhAKGVVLVPTHAL 293
Cdd:cd18021    7 IQTQVFNSlYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPK--GRAVYIAPMQEL 61
 
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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