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Conserved domains on  [gi|2092326298|ref|XP_043402850|]
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probable ATP-dependent RNA helicase DDX4 isoform X9 [Chelonia mydas]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030645)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
153-416 0e+00

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


:

Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 573.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 153 YVPPPPPDNEEAIFAHYQTGINFDKYDTILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG 232
Cdd:cd18052     1 YIPPPPPEDEDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 233 RDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQT 312
Cdd:cd18052    81 RDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 313 GHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFP 392
Cdd:cd18052   161 GHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFP 240
                         250       260
                  ....*....|....*....|....
gi 2092326298 393 EEIQRLAGEFLKPEYLFVAVGQVG 416
Cdd:cd18052   241 EEIQRLAAEFLKEDYLFLTVGRVG 264
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
422-551 1.19e-58

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: 192.72  E-value: 1.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 422 VQQTILQVSQYSKREKL-VEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPV 500
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2092326298 501 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 551
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
153-416 0e+00

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 573.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 153 YVPPPPPDNEEAIFAHYQTGINFDKYDTILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG 232
Cdd:cd18052     1 YIPPPPPEDEDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 233 RDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQT 312
Cdd:cd18052    81 RDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 313 GHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFP 392
Cdd:cd18052   161 GHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFP 240
                         250       260
                  ....*....|....*....|....
gi 2092326298 393 EEIQRLAGEFLKPEYLFVAVGQVG 416
Cdd:cd18052   241 EEIQRLAAEFLKEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
196-552 1.39e-154

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 451.52  E-value: 1.39e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 196 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGvtashfreQQEPEC 275
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR--------PRAPQA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 276 IIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEA 355
Cdd:COG0513    75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 356 DRMLDMGFGPEMKKLIS-CPgmpskDRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVGQVGGACSDVQQTILQVSQYSK 434
Cdd:COG0513   155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 435 REKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIE 514
Cdd:COG0513   229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2092326298 515 NVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 552
Cdd:COG0513   309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT 346
PTZ00110 PTZ00110
helicase; Provisional
59-595 1.36e-119

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 366.41  E-value: 1.36e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298  59 GGFGTGRSFGNRASLGNKFEERRSSGFERESTEDGQSRalSRRGGDNDSNRSRGFGSkGGYRgyNEEVIAGSGRSSWKph 138
Cdd:PTZ00110   10 NGSVSSGPSNNYNSYGPYPDSSNPYGNYQANHQDNYGG--FRPGYGNYSGGYGGFGM-NSYG--SSTLGKRLQPIDWK-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 139 getesgdnqgpKVTYVPppppdNEEAIFAHYQ--TGINFDKYDTILVE-----VSGLDPPPAILTFEEANLCQTLNKNIA 211
Cdd:PTZ00110   83 -----------SINLVP-----FEKNFYKEHPevSALSSKEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 212 KAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmkdgVTASH-FREQQEPECIIVAPTRELINQIFL 290
Cdd:PTZ00110  147 NAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INAQPlLRYGDGPIVLVLAPTRELAEQIRE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 291 EARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKL 370
Cdd:PTZ00110  222 QCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKI 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 371 IScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKPEYLFVAVGQVG-GACSDVQQTILQVSQYSKREKLVEILQSIRDE- 448
Cdd:PTZ00110  302 VS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDg 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 449 -RTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDLPST 527
Cdd:PTZ00110  378 dKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQ 457
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2092326298 528 IDEYVHRIGRTGRCGNIGKAISFFDSvSDSHIAQPLLKVLSDAQQEVPSWLEEIAFSAHGTGFSNPRG 595
Cdd:PTZ00110  458 IEDYVHRIGRTGRAGAKGASYTFLTP-DKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWG 524
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
219-398 8.81e-62

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: 202.47  E-value: 8.81e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 219 TPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfrEQQEPECIIVAPTRELINQIFLEARKFSYG 298
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK---------LDNGPQALVLAPTRELAEQIYEELKKLGKG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 299 TCIRPVVIYGGTQTGHSIRQIKqGCNILCATPGRLMDIIGKEKiGLRKVRYLVLDEADRMLDMGFGPEMKKLISCpgMPS 378
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LPK 147
                         170       180
                  ....*....|....*....|
gi 2092326298 379 KdrRQTLMFSATFPEEIQRL 398
Cdd:pfam00270 148 K--RQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
422-551 1.19e-58

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: 192.72  E-value: 1.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 422 VQQTILQVSQYSKREKL-VEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPV 500
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2092326298 501 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 551
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
210-410 2.43e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 178.45  E-value: 2.43e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298  210 IAKAGYLKLTPVQKYSIPIILAG-RDLMACAQTGSGKTAAFLLPILAHmmkdgvtashFREQQEPECIIVAPTRELINQI 288
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA----------LKRGKGGRVLVLVPTRELAEQW 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298  289 FLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGC-NILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEM 367
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2092326298  368 KKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKPEYLFV 410
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLNDPVFID 189
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
433-542 1.06e-39

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: 140.81  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 433 SKREKLVEILQSIRDERTMVFVETKKKADfIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLD 512
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 2092326298 513 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 542
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
461-542 5.22e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 109.99  E-value: 5.22e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298  461 DFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 540
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 2092326298  541 CG 542
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
431-548 1.24e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 96.34  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 431 QYSKREKLVEILQSIR----DERTMVFVETKKKADFIATFLCQEKIPTTSIHG--DRE------QREREEALGDFRSGKC 498
Cdd:COG1111   333 EHPKLSKLREILKEQLgtnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGEF 412
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2092326298 499 PVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNIGKAI 548
Cdd:COG1111   413 NVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
PRK13766 PRK13766
Hef nuclease; Provisional
434-548 5.55e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.38  E-value: 5.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 434 KREKLVEILQSI----RDERTMVFVETKKKADFIATFLCQEKIPTTSIHG--DRE------QREREEALGDFRSGKCPVL 501
Cdd:PRK13766  348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaSKDgdkgmsQKEQIEILDKFRAGEFNVL 427
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2092326298 502 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNIGKAI 548
Cdd:PRK13766  428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
234-542 4.43e-08

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 55.54  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 234 DLMACAQTGSGKTAAFLLpILAHMMKdgvtashfrEQQEPECIIVAPTRELINQIFLEARK-FSYGTcirpvviyGGTQT 312
Cdd:TIGR01587   1 LLVIEAPTGYGKTEAALL-WALHSIK---------SQKADRVIIALPTRATINAMYRRAKElFGSEL--------VGLHH 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 313 GHSIRQIK----------------QGCNILCATPGRL--MDIIGKEKIGLRKVRY----------LVLDEADRMLdmgfg 364
Cdd:TIGR01587  63 SSSFSRIKemgdseefehlfplyiHSNDKLFLDPITVctIDQVLKSVFGEFGHYEftlasianslLIFDEVHFYD----- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 365 PEMKKLISCPGMPSKDRRQTLM-FSATFPEEIQRlagEFLKPEYLFVAVGQV--GGACSDVQQTILQVSQY-SKREKLVE 440
Cdd:TIGR01587 138 EYTLALILAVLEVLKDNDVPILlMSATLPKFLKE---YAEKIGYVEFNEPLDlkEERRFENHRFILIESDKvGEISSLER 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 441 ILQSIRDE-RTMVFVETKKKADFIATFLcQEKIPTTSI---HG-----DREQREREEALGDFRSGKCPVLVATSVAARGL 511
Cdd:TIGR01587 215 LLEFIKKGgSIAIIVNTVDRAQEFYQQL-KEKAPEEEIilyHSrftekDRAKKEAELLREMKKSNEKFVIVATQVIEASL 293
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2092326298 512 DienvqhvINFDL----PSTIDEYVHRIGRTGRCG 542
Cdd:TIGR01587 294 D-------ISADVmiteLAPIDSLIQRLGRLHRYG 321
 
Name Accession Description Interval E-value
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
153-416 0e+00

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 573.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 153 YVPPPPPDNEEAIFAHYQTGINFDKYDTILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG 232
Cdd:cd18052     1 YIPPPPPEDEDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 233 RDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQT 312
Cdd:cd18052    81 RDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 313 GHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFP 392
Cdd:cd18052   161 GHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFP 240
                         250       260
                  ....*....|....*....|....
gi 2092326298 393 EEIQRLAGEFLKPEYLFVAVGQVG 416
Cdd:cd18052   241 EEIQRLAAEFLKEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
196-552 1.39e-154

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 451.52  E-value: 1.39e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 196 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGvtashfreQQEPEC 275
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR--------PRAPQA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 276 IIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEA 355
Cdd:COG0513    75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 356 DRMLDMGFGPEMKKLIS-CPgmpskDRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVGQVGGACSDVQQTILQVSQYSK 434
Cdd:COG0513   155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 435 REKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIE 514
Cdd:COG0513   229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2092326298 515 NVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 552
Cdd:COG0513   309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT 346
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
196-416 8.41e-144

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 416.12  E-value: 8.41e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 196 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAS-HFREQQEPE 274
Cdd:cd17967     1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgRGRRKAYPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 275 CIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDE 354
Cdd:cd17967    81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092326298 355 ADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVGQVG 416
Cdd:cd17967   161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
PTZ00110 PTZ00110
helicase; Provisional
59-595 1.36e-119

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 366.41  E-value: 1.36e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298  59 GGFGTGRSFGNRASLGNKFEERRSSGFERESTEDGQSRalSRRGGDNDSNRSRGFGSkGGYRgyNEEVIAGSGRSSWKph 138
Cdd:PTZ00110   10 NGSVSSGPSNNYNSYGPYPDSSNPYGNYQANHQDNYGG--FRPGYGNYSGGYGGFGM-NSYG--SSTLGKRLQPIDWK-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 139 getesgdnqgpKVTYVPppppdNEEAIFAHYQ--TGINFDKYDTILVE-----VSGLDPPPAILTFEEANLCQTLNKNIA 211
Cdd:PTZ00110   83 -----------SINLVP-----FEKNFYKEHPevSALSSKEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 212 KAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmkdgVTASH-FREQQEPECIIVAPTRELINQIFL 290
Cdd:PTZ00110  147 NAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INAQPlLRYGDGPIVLVLAPTRELAEQIRE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 291 EARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKL 370
Cdd:PTZ00110  222 QCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKI 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 371 IScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKPEYLFVAVGQVG-GACSDVQQTILQVSQYSKREKLVEILQSIRDE- 448
Cdd:PTZ00110  302 VS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDg 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 449 -RTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDLPST 527
Cdd:PTZ00110  378 dKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQ 457
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2092326298 528 IDEYVHRIGRTGRCGNIGKAISFFDSvSDSHIAQPLLKVLSDAQQEVPSWLEEIAFSAHGTGFSNPRG 595
Cdd:PTZ00110  458 IEDYVHRIGRTGRAGAKGASYTFLTP-DKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWG 524
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
175-416 3.69e-113

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: 338.94  E-value: 3.69e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 175 FDKYDTILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPIL 254
Cdd:cd18051     1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 255 AHMMKDG-------VTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILC 327
Cdd:cd18051    81 SQIYEQGpgeslpsESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 328 ATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFPEEIQRLAGEFLKpEY 407
Cdd:cd18051   161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLD-NY 239

                  ....*....
gi 2092326298 408 LFVAVGQVG 416
Cdd:cd18051   240 IFLAVGRVG 248
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
197-551 3.87e-101

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 315.59  E-value: 3.87e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 197 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmkdgVTASHFREQqepeCI 276
Cdd:PRK11776    6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK-----LDVKRFRVQ----AL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 277 IVAPTRELINQIFLEARKFSYGT-CIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEA 355
Cdd:PRK11776   77 VLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 356 DRMLDMGFGPEMKKLIS-CPGmpskdRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVGQVGGAcSDVQQTILQVSQYSK 434
Cdd:PRK11776  157 DRMLDMGFQDAIDAIIRqAPA-----RRQTLLFSATYPEGIAAISQRFQR-DPVEVKVESTHDL-PAIEQRFYEVSPDER 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 435 REKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIE 514
Cdd:PRK11776  230 LPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2092326298 515 NVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 551
Cdd:PRK11776  310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLV 346
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
196-550 3.04e-92

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 291.85  E-value: 3.04e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 196 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashFREQQE--P 273
Cdd:PRK11192    2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLD-------FPRRKSgpP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 274 ECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLD 353
Cdd:PRK11192   75 RILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 354 EADRMLDMGFGPEMKKL-ISCPGmpskdRRQTLMFSATFP-EEIQRLAGEFLK-PEYLFVAvgqvggACSDVQQTILQV- 429
Cdd:PRK11192  155 EADRMLDMGFAQDIETIaAETRW-----RKQTLLFSATLEgDAVQDFAERLLNdPVEVEAE------PSRRERKKIHQWy 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 430 ----SQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATS 505
Cdd:PRK11192  224 yradDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATD 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2092326298 506 VAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 550
Cdd:PRK11192  304 VAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
180-575 5.06e-88

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 283.60  E-value: 5.06e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 180 TILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMK 259
Cdd:PLN00206  106 KLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCT 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 260 dgVTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGK 339
Cdd:PLN00206  186 --IRSGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSK 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 340 EKIGLRKVRYLVLDEADRMLDMGFGPEMKKLISCPGMPskdrrQTLMFSATFPEEIQRLAGEFLKpEYLFVAVGQVGGAC 419
Cdd:PLN00206  264 HDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAK-DIILISIGNPNRPN 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 420 SDVQQTILQVSQYSKREKLVEILQSIRDER--TMVFVETKKKADFIAtflcqEKIPTT------SIHGDREQREREEALG 491
Cdd:PLN00206  338 KAVKQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLA-----NAITVVtglkalSIHGEKSMKERREVMK 412
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 492 DFRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFDSvSDSHIAQPLLKVLSDAQ 571
Cdd:PLN00206  413 SFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNE-EDRNLFPELVALLKSSG 491

                  ....
gi 2092326298 572 QEVP 575
Cdd:PLN00206  492 AAIP 495
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
195-549 7.57e-88

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 280.93  E-value: 7.57e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 195 LTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtASHFREQQEPE 274
Cdd:PRK10590    1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITR---QPHAKGRRPVR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 275 CIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDE 354
Cdd:PRK10590   78 ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 355 ADRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLAGEFLK-PEYlfVAVGQVGGACSDVQQTILQVSQYS 433
Cdd:PRK10590  158 ADRMLDMGFIHDIRRVLA--KLPAK--RQNLLFSATFSDDIKALAEKLLHnPLE--IEVARRNTASEQVTQHVHFVDKKR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 434 KREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDI 513
Cdd:PRK10590  232 KRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDI 311
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2092326298 514 ENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAIS 549
Cdd:PRK10590  312 EELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALS 347
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
206-404 3.23e-85

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: 264.69  E-value: 3.23e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 206 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVtashfREQQEPECIIVAPTRELI 285
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-----KKGRGPQALVLAPTRELA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 286 NQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGP 365
Cdd:cd00268    76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEE 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2092326298 366 EMKKLIS-CPgmpskDRRQTLMFSATFPEEIQRLAGEFLK 404
Cdd:cd00268   156 DVEKILSaLP-----KDRQTLLFSATLPEEVKELAKKFLK 190
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
188-550 4.45e-80

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 261.39  E-value: 4.45e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 188 LDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHF 267
Cdd:PRK01297   80 VEPQEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERY 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 268 ReqQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIK-QGCNILCATPGRLMDIIGKEKIGLRK 346
Cdd:PRK01297  160 M--GEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDM 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 347 VRYLVLDEADRMLDMGFGPEMKKLIScpGMPSKDRRQTLMFSATFPEEIQRLAGEFL-KPEYLFVAVGQVggACSDVQQT 425
Cdd:PRK01297  238 VEVMVLDEADRMLDMGFIPQVRQIIR--QTPRKEERQTLLFSATFTDDVMNLAKQWTtDPAIVEIEPENV--ASDTVEQH 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 426 ILQVSQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATS 505
Cdd:PRK01297  314 VYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATD 393
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2092326298 506 VAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 550
Cdd:PRK01297  394 VAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
189-550 1.27e-77

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 257.57  E-value: 1.27e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 189 DPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAShfR 268
Cdd:PRK04537    3 DKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALAD--R 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 269 EQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKI-GLRKV 347
Cdd:PRK04537   81 KPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHAC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 348 RYLVLDEADRMLDMGFGPEMKKLIScpGMPSKDRRQTLMFSATFPEEIQRLAGEFL-KPEYLFVAVGQVGGAcsDVQQTI 426
Cdd:PRK04537  161 EICVLDEADRMFDLGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMnEPEKLVVETETITAA--RVRQRI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 427 LQVSQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSV 506
Cdd:PRK04537  237 YFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDV 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2092326298 507 AARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 550
Cdd:PRK04537  317 AARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
210-550 6.51e-73

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 240.64  E-value: 6.51e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 210 IAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvTASHFREQQEPECIIVAPTRELINQIF 289
Cdd:PRK04837   23 LEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSH--PAPEDRKVNQPRALIMAPTRELAVQIH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 290 LEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKK 369
Cdd:PRK04837  101 ADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRW 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 370 LIScpGMPSKDRRQTLMFSATFPEEIQRLAGEFL-KPEYLFVAVGQVGGacSDVQQTILQVSQYSKREKLVEILQSIRDE 448
Cdd:PRK04837  181 LFR--RMPPANQRLNMLFSATLSYRVRELAFEHMnNPEYVEVEPEQKTG--HRIKEELFYPSNEEKMRLLQTLIEEEWPD 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 449 RTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTI 528
Cdd:PRK04837  257 RAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDC 336
                         330       340
                  ....*....|....*....|..
gi 2092326298 529 DEYVHRIGRTGRCGNIGKAISF 550
Cdd:PRK04837  337 EDYVHRIGRTGRAGASGHSISL 358
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
208-410 3.00e-67

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: 218.01  E-value: 3.00e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 208 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtaSHFREQQEPECIIVAPTRELINQ 287
Cdd:cd17966     3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQ----PPLERGDGPIVLVLAPTRELAQQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 288 IFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEM 367
Cdd:cd17966    79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2092326298 368 KKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKpEYLFV 410
Cdd:cd17966   159 RKIVD----QIRPDRQTLMWSATWPKEVRRLAEDFLK-DYIQV 196
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
196-553 3.99e-66

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 228.19  E-value: 3.99e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 196 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILaHMMKDGVTAshfreqqePEC 275
Cdd:PRK11634    7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLL-HNLDPELKA--------PQI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 276 IIVAPTRELINQIFLEARKFS-YGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDE 354
Cdd:PRK11634   78 LVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 355 ADRMLDMGFGPEMKKLIScpGMPskDRRQTLMFSATFPEEIQRLAGEFLK-PEYlfVAVGQVGGACSDVQQTILQVSQYS 433
Cdd:PRK11634  158 ADEMLRMGFIEDVETIMA--QIP--EGHQTALFSATMPEAIRRITRRFMKePQE--VRIQSSVTTRPDISQSYWTVWGMR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 434 KREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDI 513
Cdd:PRK11634  232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2092326298 514 ENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFDS 553
Cdd:PRK11634  312 ERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVEN 351
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
219-398 8.81e-62

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: 202.47  E-value: 8.81e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 219 TPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfrEQQEPECIIVAPTRELINQIFLEARKFSYG 298
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK---------LDNGPQALVLAPTRELAEQIYEELKKLGKG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 299 TCIRPVVIYGGTQTGHSIRQIKqGCNILCATPGRLMDIIGKEKiGLRKVRYLVLDEADRMLDMGFGPEMKKLISCpgMPS 378
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LPK 147
                         170       180
                  ....*....|....*....|
gi 2092326298 379 KdrRQTLMFSATFPEEIQRL 398
Cdd:pfam00270 148 K--RQILLLSATLPRNLEDL 165
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
206-403 2.63e-61

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: 202.26  E-value: 2.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 206 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtaSHFREQQEPECIIVAPTRELI 285
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ----RELEKGEGPIAVIVAPTRELA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 286 NQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGP 365
Cdd:cd17952    77 QQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEY 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2092326298 366 EMKKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFL 403
Cdd:cd17952   157 QVRSIVG----HVRPDRQTLLFSATFKKKIEQLARDIL 190
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
208-410 8.43e-61

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: 201.66  E-value: 8.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 208 KNIAKAGYLKLTPVQKYSIPIILA-GRDLMACAQTGSGKTAAFLLPILAHMMKDgvtasHFREQQEP-ECIIVAPTRELI 285
Cdd:cd17964     7 KALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNT-----KPAGRRSGvSALIISPTRELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 286 NQIFLEARKF-SYGTCIRPVVIYGGTQTGHSI-RQIKQGCNILCATPGRLMDIIGKEKIG--LRKVRYLVLDEADRMLDM 361
Cdd:cd17964    82 LQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELnRLRRGRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLDM 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2092326298 362 GFGPEMKKLISCPGMPSKDRRQTLMFSATFPEEIQRLAGEFLKPEYLFV 410
Cdd:cd17964   162 GFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
185-404 8.98e-60

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: 199.14  E-value: 8.98e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 185 VSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMkdgvtA 264
Cdd:cd17953     2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIK-----D 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 265 SHFREQQE-PECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDII---GKE 340
Cdd:cd17953    77 QRPVKPGEgPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGR 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092326298 341 KIGLRKVRYLVLDEADRMLDMGFGPEMKKLIscpgMPSKDRRQTLMFSATFPEEIQRLAGEFLK 404
Cdd:cd17953   157 VTNLRRVTYVVLDEADRMFDMGFEPQIMKIV----NNIRPDRQTVLFSATFPRKVEALARKVLH 216
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
422-551 1.19e-58

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: 192.72  E-value: 1.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 422 VQQTILQVSQYSKREKL-VEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPV 500
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2092326298 501 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 551
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
206-413 1.55e-58

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 195.12  E-value: 1.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 206 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtashfREQQEPECIIVAPTRELI 285
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP-------RKKKGLRALILAPTRELA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 286 NQIFLEARKFSYGTCIRPVVIYGGTQTG-HSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFG 364
Cdd:cd17957    74 SQIYRELLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFR 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2092326298 365 PEMKKLI-SCPGmPSKdrrQTLMFSATFPEEIQRLAGEFLKPeYLFVAVG 413
Cdd:cd17957   154 EQTDEILaACTN-PNL---QRSLFSATIPSEVEELARSVMKD-PIRIIVG 198
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
210-404 8.13e-58

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: 194.08  E-value: 8.13e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 210 IAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMK----DGVTashfrEQQEPECIIVAPTRELI 285
Cdd:cd17945     5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpplDEET-----KDDGPYALILAPTRELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 286 NQIFLEARKFSYGTCIRPVVIYGGtqtgHSIR----QIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDM 361
Cdd:cd17945    80 QQIEEETQKFAKPLGIRVVSIVGG----HSIEeqafSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDM 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2092326298 362 GFGPEMKKLIScpGMPS------------------KDRRQTLMFSATFPEEIQRLAGEFLK 404
Cdd:cd17945   156 GFEPQVTKILD--AMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLR 214
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
183-413 1.01e-57

DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 194.07  E-value: 1.01e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 183 VEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmkdgV 262
Cdd:cd18049    12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH-----I 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 263 TASHFREQQE-PECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEK 341
Cdd:cd18049    87 NHQPFLERGDgPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092326298 342 IGLRKVRYLVLDEADRMLDMGFGPEMKKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVG 413
Cdd:cd18049   167 TNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLK-DYIHINIG 233
PTZ00424 PTZ00424
helicase 45; Provisional
196-550 6.19e-56

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 194.66  E-value: 6.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 196 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAshfreqqepEC 275
Cdd:PTZ00424   29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNAC---------QA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 276 IIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEA 355
Cdd:PTZ00424  100 LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 356 DRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLAGEFLK-PEYLFVAVGQVggACSDVQQTILQVSQYS- 433
Cdd:PTZ00424  180 DEMLSRGFKGQIYDVFK--KLPPD--VQVALFSATMPNEILELTTKFMRdPKRILVKKDEL--TLEGIRQFYVAVEKEEw 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 434 KREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDI 513
Cdd:PTZ00424  254 KFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDV 333
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2092326298 514 ENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 550
Cdd:PTZ00424  334 QQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINF 370
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
208-404 7.52e-53

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 179.97  E-value: 7.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 208 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMmkdgVTASHFREQQE-PECIIVAPTRELIN 286
Cdd:cd17958     3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL----DLQPIPREQRNgPGVLVLTPTRELAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 287 QIFLEARKFSYGTcIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPE 366
Cdd:cd17958    79 QIEAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2092326298 367 MKKLIscpgMPSKDRRQTLMFSATFPEEIQRLAGEFLK 404
Cdd:cd17958   158 IRKIL----LDIRPDRQTIMTSATWPDGVRRLAQSYLK 191
DEXDc smart00487
DEAD-like helicases superfamily;
210-410 2.43e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 178.45  E-value: 2.43e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298  210 IAKAGYLKLTPVQKYSIPIILAG-RDLMACAQTGSGKTAAFLLPILAHmmkdgvtashFREQQEPECIIVAPTRELINQI 288
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA----------LKRGKGGRVLVLVPTRELAEQW 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298  289 FLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGC-NILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEM 367
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2092326298  368 KKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKPEYLFV 410
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLNDPVFID 189
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
183-413 5.95e-52

DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 180.21  E-value: 5.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 183 VEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgv 262
Cdd:cd18050    50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQ-- 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 263 taSHFREQQEPECIIVAPTRELINQIflEARKFSYGTC--IRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKE 340
Cdd:cd18050   128 --PYLERGDGPICLVLAPTRELAQQV--QQVADDYGKSsrLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAG 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2092326298 341 KIGLRKVRYLVLDEADRMLDMGFGPEMKKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVG 413
Cdd:cd18050   204 KTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLR-DYVQINIG 271
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
197-410 6.01e-51

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: 175.11  E-value: 6.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 197 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVtaSHFreqqepeCI 276
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPY--GIF-------AL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 277 IVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQtghSIRQIK---QGCNILCATPGRLMDII---GKEKIGLRKVRYL 350
Cdd:cd17955    72 VLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMD---MVKQALelsKRPHIVVATPGRLADHLrssDDTTKVLSRVKFL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 351 VLDEADRMLDMGFGPEMKKLISCpgMPSKdrRQTLMFSATFPEEIQRLAGEFLKPEYLFV 410
Cdd:cd17955   149 VLDEADRLLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
212-408 1.25e-50

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: 174.31  E-value: 1.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 212 KAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtASHFREQQEPECIIVAPTRELINQIFLE 291
Cdd:cd17949     8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSL---EPRVDRSDGTLALVLVPTRELALQIYEV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 292 ARKF-SYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEK-IGLRKVRYLVLDEADRMLDMGFGPEMKK 369
Cdd:cd17949    85 LEKLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEKDITK 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2092326298 370 LIS--------CPGMPSKD-RRQTLMFSATFPEEIQRLAGEFLK-PEYL 408
Cdd:cd17949   165 ILEllddkrskAGGEKSKPsRRQTVLVSATLTDGVKRLAGLSLKdPVYI 213
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
208-404 4.67e-50

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 172.44  E-value: 4.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 208 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMkdgvtashFREQQEPEC--IIVAPTRELI 285
Cdd:cd17947     3 RALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLL--------YRPKKKAATrvLVLVPTRELA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 286 NQIFLEARKFSYGTCIRPVVIYGGTqtghSIRQ----IKQGCNILCATPGRLMDIIGKEK-IGLRKVRYLVLDEADRMLD 360
Cdd:cd17947    75 MQCFSVLQQLAQFTDITFALAVGGL----SLKAqeaaLRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLE 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2092326298 361 MGFGPEMKKLI-SCPGmpskdRRQTLMFSATFPEEIQRLAGEFLK 404
Cdd:cd17947   151 EGFADELKEILrLCPR-----TRQTMLFSATMTDEVKDLAKLSLN 190
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
196-393 2.64e-48

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: 167.87  E-value: 2.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 196 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPIL----AHMMKDGVTAshfreqq 271
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIeklkAHSPTVGARA------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 272 epecIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLV 351
Cdd:cd17959    75 ----LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVV 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2092326298 352 LDEADRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPE 393
Cdd:cd17959   151 FDEADRLFEMGFAEQLHEILS--RLPEN--RQTLLFSATLPK 188
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
196-398 6.19e-48

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: 166.72  E-value: 6.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 196 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtashfreQQEPEC 275
Cdd:cd17954     1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---------PQRFFA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 276 IIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEK-IGLRKVRYLVLDE 354
Cdd:cd17954    72 LVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDE 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2092326298 355 ADRMLDMGFGPEMKKLISCpgMPSkdRRQTLMFSATFPEEIQRL 398
Cdd:cd17954   152 ADRLLNMDFEPEIDKILKV--IPR--ERTTYLFSATMTTKVAKL 191
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
210-399 1.53e-47

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: 165.83  E-value: 1.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 210 IAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfREQQEPE----CIIVAPTRELI 285
Cdd:cd17960     5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLK--------RKANLKKgqvgALIISPTRELA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 286 NQIFLEARKF--SYGTCIRPVVIYGGTQTGHSIRQIK-QGCNILCATPGRLMDIIGKEKiGLRKVR---YLVLDEADRML 359
Cdd:cd17960    77 TQIYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRKA-DKVKVKsleVLVLDEADRLL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2092326298 360 DMGFGPEMKKLISCpgMPsKDRRqTLMFSATFPEEIQRLA 399
Cdd:cd17960   156 DLGFEADLNRILSK--LP-KQRR-TGLFSATQTDAVEELI 191
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
208-410 1.71e-47

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: 165.54  E-value: 1.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 208 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMmkdgvtashFREQQEPE----CIIVAPTRE 283
Cdd:cd17941     3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL---------YRERWTPEdglgALIISPTRE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 284 LINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQgCNILCATPGRL---MDiigkEKIGL--RKVRYLVLDEADRM 358
Cdd:cd17941    74 LAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLlqhMD----ETPGFdtSNLQMLVLDEADRI 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2092326298 359 LDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLAGEFLK-PEYLFV 410
Cdd:cd17941   149 LDMGFKETLDAIVE--NLPKS--RQTLLFSATQTKSVKDLARLSLKnPEYISV 197
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
197-407 5.11e-46

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 161.70  E-value: 5.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 197 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPIL--AHMMKDGVTAshfreqqepe 274
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILekIDPKKDVIQA---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 275 cIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDE 354
Cdd:cd17940    71 -LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2092326298 355 ADRMLDMGFGPEMKKLIS-CPgmpskDRRQTLMFSATFPEEIQRLAGEFLKPEY 407
Cdd:cd17940   150 ADKLLSQDFQPIIEKILNfLP-----KERQILLFSATFPLTVKNFMDRHMHNPY 198
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
208-410 1.30e-45

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: 160.22  E-value: 1.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 208 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmmkDGVTASHFREQQEPECIIVAPTRELINQ 287
Cdd:cd17942     3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-----ELLYKLKFKPRNGTGVIIISPTRELALQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 288 IFLEARKF------SYGTCIrpvviyGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRK-VRYLVLDEADRMLD 360
Cdd:cd17942    78 IYGVAKELlkyhsqTFGIVI------GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILE 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2092326298 361 MGFGPEMKKLISCpgMPSkdRRQTLMFSATFPEEIQRLAGEFLKPEYLFV 410
Cdd:cd17942   152 IGFEEEMRQIIKL--LPK--RRQTMLFSATQTRKVEDLARISLKKKPLYV 197
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
208-399 5.09e-44

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: 156.35  E-value: 5.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 208 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAShFREQQEPECIIVAPTRELINQ 287
Cdd:cd17951     3 KGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLP-FIKGEGPYGLIVCPSRELARQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 288 IF---------LEARKFSYgtcIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRM 358
Cdd:cd17951    82 THevieyyckaLQEGGYPQ---LRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2092326298 359 LDMGFGPEMKKLISCpgmpSKDRRQTLMFSATFPEEIQRLA 399
Cdd:cd17951   159 IDMGFEEDIRTIFSY----FKGQRQTLLFSATMPKKIQNFA 195
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
197-399 1.37e-43

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: 155.17  E-value: 1.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 197 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmmkdgvtashfreqQEPECI 276
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------QIVVAL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 277 IVAPTRELINQIFLEARKFSY---GTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLD 353
Cdd:cd17938    65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2092326298 354 EADRMLDMGFGPEMKKLIS-CPGMPSKDRR-QTLMFSATF-PEEIQRLA 399
Cdd:cd17938   145 EADRLLSQGNLETINRIYNrIPKITSDGKRlQVIVCSATLhSFEVKKLA 193
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
206-404 8.96e-43

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: 152.32  E-value: 8.96e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 206 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfrEQQEPECIIVAPTRELI 285
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT---------EHRNPSALILTPTRELA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 286 NQIFLEARKFSYGTC-IRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFG 364
Cdd:cd17962    72 VQIEDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQ 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2092326298 365 PE-MKKLISCPGMPskdrrQTLMFSATFPEEIQRLAGEFLK 404
Cdd:cd17962   152 QQvLDILENISHDH-----QTILVSATIPRGIEQLAGQLLQ 187
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
208-391 2.98e-42

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: 152.39  E-value: 2.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 208 KNIAKAGYLKLTPVQKYSIP-IILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHFREQQEPECIIVAPTRELIN 286
Cdd:cd17946     3 RALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTRELAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 287 QI---FLEARKFsygTCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGK--EKIG-LRKVRYLVLDEADRMLD 360
Cdd:cd17946    83 QVkdhLKAIAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEgnEHLAnLKSLRFLVLDEADRMLE 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2092326298 361 MGFGPEMKKLISC---PGMPSKDRRQTLMFSATF 391
Cdd:cd17946   160 KGHFAELEKILELlnkDRAGKKRKRQTFVFSATL 193
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
433-542 1.06e-39

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: 140.81  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 433 SKREKLVEILQSIRDERTMVFVETKKKADfIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLD 512
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 2092326298 513 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 542
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
206-404 8.60e-36

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: 133.48  E-value: 8.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 206 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAshfREQQEPECIIVAPTRELI 285
Cdd:cd17961     5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAES---GEEQGTRALILVPTRELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 286 NQIFLEARKFSYGTC--IRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDII-GKEKIGLRKVRYLVLDEADRMLDMG 362
Cdd:cd17961    82 QQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLeSGSLLLLSTLKYLVIDEADLVLSYG 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2092326298 363 FGPEMKKLIScpGMPSkdRRQTLMFSATFPEEIQRLAGEFLK 404
Cdd:cd17961   162 YEEDLKSLLS--YLPK--NYQTFLMSATLSEDVEALKKLVLH 199
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
208-407 3.55e-35

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: 131.89  E-value: 3.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 208 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtASHFREQQEPECIIVAPTRELINQ 287
Cdd:cd17944     3 KLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQED---QQPRKRGRAPKVLVLAPTRELANQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 288 IFLE----ARKFSYgTCIrpvviYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGF 363
Cdd:cd17944    80 VTKDfkdiTRKLSV-ACF-----YGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGF 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2092326298 364 GPEMKKLISCP-GMPSKDRRQTLMFSATFPEEIQRLAGEFLKPEY 407
Cdd:cd17944   154 AEQVEEILSVSyKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQY 198
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
206-405 8.63e-35

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: 130.39  E-value: 8.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 206 LNKNIAKAGYLKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILAHMmkDgvtashfREQQEPECIIVAPTRE 283
Cdd:cd17963     5 LLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV--D-------PTLKSPQALCLAPTRE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 284 LINQIFLEARKFSYGT------CIRPVVIYGGTQ-TGHsirqikqgcnILCATPGRLMDIIGKEKIGLRKVRYLVLDEAD 356
Cdd:cd17963    76 LARQIGEVVEKMGKFTgvkvalAVPGNDVPRGKKiTAQ----------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEAD 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2092326298 357 RMLDM-GFGPE---MKKLIscpgmpsKDRRQTLMFSATFPEEIQRLAGEFLKP 405
Cdd:cd17963   146 VMLDTqGHGDQsirIKRML-------PRNCQILLFSATFPDSVRKFAEKIAPN 191
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
206-398 7.06e-33

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: 126.21  E-value: 7.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 206 LNKNIAKAGYLKLTPVQKYSIPIILAG---------RDLMACAQTGSGKTAAFLLPILAhMMKDGVtASHFReqqepeCI 276
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQ-ALSKRV-VPRLR------AL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 277 IVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIKQGC--------NILCATPGRLMD-IIGKEKIGLRKV 347
Cdd:cd17956    73 IVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDhLNSTPGFTLKHL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 348 RYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRR----------------QTLMFSATF---PEEIQRL 398
Cdd:cd17956   153 RFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLgsfgdanllersvrplQKLLFSATLtrdPEKLSSL 222
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
206-410 4.07e-32

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 123.22  E-value: 4.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 206 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILaHMMKDgvtashfrEQQEPECIIVAPTRELI 285
Cdd:cd17950    13 LLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL-QQLEP--------VDGQVSVLVICHTRELA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 286 NQIFLEARKFS-YGTCIRPVVIYGGTQTGHSIRQIKQGC-NILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDmgf 363
Cdd:cd17950    84 FQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE--- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2092326298 364 GPEMKKLI-----SCPgmpsKDrRQTLMFSATFPEEIQRLAGEFLK-PEYLFV 410
Cdd:cd17950   161 QLDMRRDVqeifrATP----HD-KQVMMFSATLSKEIRPVCKKFMQdPLEIFV 208
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
208-393 1.58e-29

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: 115.44  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 208 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLlpILAHMMKDgvtashfREQQEPECIIVAPTRELINQ 287
Cdd:cd17943     3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFV--VIALESLD-------LERRHPQVLILAPTREIAVQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 288 IFLEARKF-SYGTCIRPVVIYGGTQTGHSIRQIKqGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPE 366
Cdd:cd17943    74 IHDVFKKIgKKLEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKD 152
                         170       180
                  ....*....|....*....|....*..
gi 2092326298 367 MKKLIScpGMPSkdRRQTLMFSATFPE 393
Cdd:cd17943   153 VNWIFS--SLPK--NKQVIAFSATYPK 175
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
199-403 1.74e-29

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: 115.50  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 199 EANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMkdgvtashfREQQEPECIIV 278
Cdd:cd17939     1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRID---------TTVRETQALVL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 279 APTRELINQI---------FLEARKFsygTCIrpvviyGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRY 349
Cdd:cd17939    72 APTRELAQQIqkvvkalgdYMGVKVH---ACI------GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKM 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2092326298 350 LVLDEADRMLDMGFGPEMKKLISCpgMPSKdrRQTLMFSATFPEEIQRLAGEFL 403
Cdd:cd17939   143 FVLDEADEMLSRGFKDQIYDIFQF--LPPE--TQVVLFSATMPHEVLEVTKKFM 192
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
209-393 2.47e-29

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: 116.31  E-value: 2.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 209 NIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAShfREQQEPECIIVAPTRELINQI 288
Cdd:cd17948     4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAE--GPFNAPRGLVITPSRELAEQI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 289 FLEARKFSYGTCIRPVVIYGGtQTGHSIRQIKQG-CNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEM 367
Cdd:cd17948    82 GSVAQSLTEGLGLKVKVITGG-RTKRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2092326298 368 KKLIS-CP--GMPSKDRR------QTLMFSATFPE 393
Cdd:cd17948   161 SHFLRrFPlaSRRSENTDgldpgtQLVLVSATMPS 195
HELICc smart00490
helicase superfamily c-terminal domain;
461-542 5.22e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 109.99  E-value: 5.22e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298  461 DFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 540
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 2092326298  541 CG 542
Cdd:smart00490  81 AG 82
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
197-403 2.55e-27

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: 109.48  E-value: 2.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 197 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILaHMMKDGVtashfreqQEPECI 276
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQV--------RETQAL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 277 IVAPTRELINQI---FLEARKF---SYGTCIrpvviyGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYL 350
Cdd:cd18045    72 ILSPTRELAVQIqkvLLALGDYmnvQCHACI------GGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKML 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2092326298 351 VLDEADRMLDMGFgpemKKLISCPGMPSKDRRQTLMFSATFPEEIQRLAGEFL 403
Cdd:cd18045   146 VLDEADEMLNKGF----KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFM 194
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
197-404 2.53e-26

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: 106.76  E-value: 2.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 197 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfrEQQEPECI 276
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDT---------SLKATQAL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 277 IVAPTRELINQI---------FLEARKFSygtCIrpvviyGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKV 347
Cdd:cd18046    72 VLAPTRELAQQIqkvvmalgdYMGIKCHA---CI------GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYI 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2092326298 348 RYLVLDEADRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLAGEFLK 404
Cdd:cd18046   143 KMFVLDEADEMLSRGFKDQIYDIFQ--KLPPD--TQVVLLSATMPNDVLEVTTKFMR 195
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
183-399 2.45e-22

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 96.24  E-value: 2.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 183 VEVSGLDPPP---AILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILAHm 257
Cdd:cd18048     3 VEVLQRDPTSplfSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 258 mkdgVTAshfrEQQEPECIIVAPTRELINQ---IFLEARKFsygtCIRPVVIYG--GTQTGHSIRQIKQgcnILCATPGR 332
Cdd:cd18048    82 ----VDA----LKLYPQCLCLSPTFELALQtgkVVEEMGKF----CVGIQVIYAirGNRPGKGTDIEAQ---IVIGTPGT 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092326298 333 LMDIIGKEK-IGLRKVRYLVLDEADRMLDM-GFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLA 399
Cdd:cd18048   147 VLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKR--SMPKE--CQMLLFSATFEDSVWAFA 211
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
208-402 2.01e-21

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 93.98  E-value: 2.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 208 KNIAKAGYLKL------TPVQKYSIPIILAGR----------------DLMACAQTGSGKTAAFLLPILAHMMKDGVTAS 265
Cdd:cd17965    15 IKEILKGSNKTdeeikpSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 266 HFREQQE--------PECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGH--SIRQIKQGCNILCATPGRLMD 335
Cdd:cd17965    95 EEAEEEYesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYqrLQLAFKGRIDILVTTPGKLAS 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2092326298 336 IIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLIScPGMPSKDrrqtLMF-SATFPEEIQRLAGEF 402
Cdd:cd17965   175 LAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIK-RAPKLKH----LILcSATIPKEFDKTLRKL 237
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
231-572 6.77e-21

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 96.63  E-value: 6.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 231 AGRDLMACAQTGSGKTAAFLLpILAHMMKDGVTashfreqqepecIIVAPTRELINQIFLEARKFsygtcirpvviYGGT 310
Cdd:COG1061    99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGKRV------------LVLVPRRELLEQWAEELRRF-----------LGDP 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 311 QTGHSIRQIkqGCNILCATPGRLMDIIGKEKIGlRKVRYLVLDEADRmldmGFGPEMKKLIScpGMPSKDRrqtLMFSAT 390
Cdd:COG1061   155 LAGGGKKDS--DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILE--AFPAAYR---LGLTAT 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 391 ------FPEEIQRLAG-------------EFLKP-EYLFVAVG-----QVGGACSDVQQTILQVSQYSKREKLVEILQSI 445
Cdd:COG1061   223 pfrsdgREILLFLFDGivyeyslkeaiedGYLAPpEYYGIRVDltderAEYDALSERLREALAADAERKDKILRELLREH 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 446 RD-ERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDL 524
Cdd:COG1061   303 PDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP 382
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2092326298 525 PSTIDEYVHRIGRTGRCGNIGKAISFFDSVSDSHiaqPLLKVLSDAQQ 572
Cdd:COG1061   383 TGSPREFIQRLGRGLRPAPGKEDALVYDFVGNDV---PVLEELAKDLR 427
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
431-548 1.24e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 96.34  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 431 QYSKREKLVEILQSIR----DERTMVFVETKKKADFIATFLCQEKIPTTSIHG--DRE------QREREEALGDFRSGKC 498
Cdd:COG1111   333 EHPKLSKLREILKEQLgtnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGEF 412
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2092326298 499 PVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNIGKAI 548
Cdd:COG1111   413 NVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
229-552 1.49e-18

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 89.04  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 229 ILAGRDLMACAQTGSGKTAAFLLPILahmMKDGVTashfreqqepecIIVAPtreLI----NQI-FLEARKfsygtcIRP 303
Cdd:COG0514    29 VLAGRDALVVMPTGGGKSLCYQLPAL---LLPGLT------------LVVSP---LIalmkDQVdALRAAG------IRA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 304 VVIYGgTQTGHSIRQIKQGCN-----ILCATPGRLM-----DIIGKEKIGLrkvryLVLDEA--------DrmldmgFGP 365
Cdd:COG0514    85 AFLNS-SLSAEERREVLRALRagelkLLYVAPERLLnprflELLRRLKISL-----FAIDEAhcisqwghD------FRP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 366 E---MKKLI-SCPGMPskdrrqTLMFSATFPEE-----IQRLAGE--------FLKPEyLFVAVgqvggacsdvqqtiLQ 428
Cdd:COG0514   153 DyrrLGELReRLPNVP------VLALTATATPRvradiAEQLGLEdprvfvgsFDRPN-LRLEV--------------VP 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 429 VSQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSvaA 508
Cdd:COG0514   212 KPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--A 289
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2092326298 509 RGL--DIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 552
Cdd:COG0514   290 FGMgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYG 335
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
432-537 5.83e-16

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: 74.94  E-value: 5.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 432 YSKREKLVEILQSIRDE----RTMVFVETKKKADFIATFLCQEKIPTTSIHGD---------------REQREREEALGD 492
Cdd:cd18802     6 IPKLQKLIEILREYFPKtpdfRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDK 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2092326298 493 FRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGR 537
Cdd:cd18802    86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
196-399 1.44e-15

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 75.91  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 196 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILAHMmkDGVTashfreqQEP 273
Cdd:cd18047     2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPAN-------KYP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 274 ECIIVAPTRELINQ---IFLEARKFSygtcirPVVIYGGTQTGHSI-RQIKQGCNILCATPGRLMDIIGKEK-IGLRKVR 348
Cdd:cd18047    73 QCLCLSPTYELALQtgkVIEQMGKFY------PELKLAYAVRGNKLeRGQKISEQIVIGTPGTVLDWCSKLKfIDPKKIK 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2092326298 349 YLVLDEADRMLDMGfGPEMKKLISCPGMPSKdrRQTLMFSATFPEEIQRLA 399
Cdd:cd18047   147 VFVLDEADVMIATQ-GHQDQSIRIQRMLPRN--CQMLLFSATFEDSVWKFA 194
PRK13766 PRK13766
Hef nuclease; Provisional
434-548 5.55e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.38  E-value: 5.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 434 KREKLVEILQSI----RDERTMVFVETKKKADFIATFLCQEKIPTTSIHG--DRE------QREREEALGDFRSGKCPVL 501
Cdd:PRK13766  348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaSKDgdkgmsQKEQIEILDKFRAGEFNVL 427
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2092326298 502 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNIGKAI 548
Cdd:PRK13766  428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
199-548 1.72e-14

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 76.80  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 199 EANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKD-GVTAshfreqqepecII 277
Cdd:COG1205    38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDpGATA-----------LY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 278 VAPTRELIN-QifLEA-RKF--SYGTCIRPVVIYGGTqTGHSIRQIKQGCNILCATPgrlmDII------GKEKIG--LR 345
Cdd:COG1205   107 LYPTKALARdQ--LRRlRELaeALGLGVRVATYDGDT-PPEERRWIREHPDIVLTNP----DMLhygllpHHTRWArfFR 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 346 KVRYLVLDEAD--RmldmG-FGPEMKKLIscpgmpskdRR------------QTLMFSATF--PEEI-QRLAGEflkPey 407
Cdd:COG1205   180 NLRYVVIDEAHtyR----GvFGSHVANVL---------RRlrricrhygsdpQFILASATIgnPAEHaERLTGR---P-- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 408 lFVAVGQVGGACSDVQQTILQVSQYSKREKLVEILQSIR--------DERTMVFVETKKKADFIATFL---CQEKIPTTS 476
Cdd:COG1205   242 -VTVVDEDGSPRGERTFVLWNPPLVDDGIRRSALAEAARlladlvreGLRTLVFTRSRRGAELLARYArraLREPDLADR 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2092326298 477 IHGDR------EQREREEALgdfRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAI 548
Cdd:COG1205   321 VAAYRagylpeERREIERGL---RSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
434-540 4.69e-14

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 69.69  E-value: 4.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 434 KREKLVEIL-------QSIRDERTMVFVETKKKADFIATFLCQEKI---PTTSI-HGDRE------QREREEALGDFRSG 496
Cdd:cd18801    10 KLEKLEEIVkehfkkkQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPgirATRFIgQASGKsskgmsQKEQKEVIEQFRKG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2092326298 497 KCPVLVATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGR 540
Cdd:cd18801    90 GYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
210-540 3.48e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 72.24  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 210 IAKAGYLKLTPVQKYSIP-IILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGvtashfreqqepECIIVAPTRELINQI 288
Cdd:COG1204    15 LKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------KALYIVPLRALASEK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 289 FLEARKF--SYGtcIRPVVIYGGTQtghSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEAdRML-DMGFGP 365
Cdd:COG1204    83 YREFKRDfeELG--IKVGVSTGDYD---SDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLIdDESRGP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 366 --EM---KKLISCPGMpskdrrQTLMFSATF--PEEIQR-LAGEFLKPEYlfVAVGQVGGACSDVQQTILQVSQYSKREK 437
Cdd:COG1204   157 tlEVllaRLRRLNPEA------QIVALSATIgnAEEIAEwLDAELVKSDW--RPVPLNEGVLYDGVLRFDDGSRRSKDPT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 438 LVEILQSIRDE-RTMVFVETKKKA-----------------------DFIATFLCQEKIPTTSI--------------HG 479
Cdd:COG1204   229 LALALDLLEEGgQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELLEVSEETHTNekladclekgvafhHA 308
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2092326298 480 D--REQREREEALgdFRSGKCPVLVATSVAARGLdieN--VQHVI------NFDLPSTIDEYVHRIGRTGR 540
Cdd:COG1204   309 GlpSELRRLVEDA--FREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGR 374
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
438-551 6.13e-13

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


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 66.08  E-value: 6.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 438 LVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQ 517
Cdd:cd18794    21 LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVR 100
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2092326298 518 HVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 551
Cdd:cd18794   101 FVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
433-536 9.93e-13

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 65.58  E-value: 9.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 433 SKREKLVEILQSIRD--ERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSG-KCPV-LVATSVAA 508
Cdd:cd18793    11 GKLEALLELLEELREpgEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGG 90
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2092326298 509 RGLDIENVQHVINFDLP--STIDEY----VHRIG 536
Cdd:cd18793    91 VGLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
418-538 1.18e-11

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 67.94  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 418 ACSDVQQTILQVSQY----SKREKLVEILQSI--RDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALG 491
Cdd:COG0553   514 ICSHPALLLEEGAELsgrsAKLEALLELLEELlaEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVD 593
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2092326298 492 DFRSGK-CPV-LVATSVAARGLdieNVQ---HVINFDLP-------STIDEyVHRIGRT 538
Cdd:COG0553   594 RFQEGPeAPVfLISLKAGGEGL---NLTaadHVIHYDLWwnpaveeQAIDR-AHRIGQT 648
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
222-355 4.14e-10

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: 59.14  E-value: 4.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 222 QKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKD-GVTAshfreqqepecIIVAPTRELINQIFLEARKF--SYG 298
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDpGSRA-----------LYLYPTKALAQDQLRSLRELleQLG 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2092326298 299 TCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDII----GKEKIGLRKVRYLVLDEA 355
Cdd:cd17923    74 LGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
218-355 8.82e-10

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: 58.43  E-value: 8.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 218 LTPVQKYSI-PIILAGRDLMACAQTGSGKTAAFLLPILAHmmkdgvtashfREQQEPECIIVAPTRELINQIFLEARKFS 296
Cdd:cd17921     2 LNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRA-----------LATSGGKAVYIAPTRALVNQKEADLRERF 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 297 YGTCIRPVVIYGGTQtgHSIRQIKQgCNILCATPGRLMDIIGKEKI-GLRKVRYLVLDEA 355
Cdd:cd17921    71 GPLGKNVGLLTGDPS--VNKLLLAE-ADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
446-557 1.22e-09

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 57.64  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 446 RDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFD-- 523
Cdd:cd18790    26 RGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDad 105
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2092326298 524 ----LPSTiDEYVHRIGRTGRCGNiGKAISFFDSVSDS 557
Cdd:cd18790   106 kegfLRSE-TSLIQTIGRAARNVN-GKVILYADKITDS 141
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
232-390 1.24e-09

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: 57.03  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 232 GRDLMACAQTGSGKTAAFLLPILAHMmkdgvtashfrEQQEPECIIVAPTRELINQIFLEARKFsYGTCIRPVVIYGGTQ 311
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLL-----------LKKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 312 TGHSIRQIKQGCNILCATPGRL-MDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLISCPGMPsKDRRQTLMfSAT 390
Cdd:cd00046    69 AEEREKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGL-KNAQVILL-SAT 146
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
214-552 1.61e-09

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 60.88  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 214 GYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmMKDGVTashfreqqepecIIVAPTREL----INQif 289
Cdd:PRK11057   22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL---VLDGLT------------LVVSPLISLmkdqVDQ-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 290 LEARKFSyGTCIrpvviyGGTQTGHSIRQIKQGCN-----ILCATPGRLM--DIIgkEKIGLRKVRYLVLDEADRMLDMG 362
Cdd:PRK11057   85 LLANGVA-AACL------NSTQTREQQLEVMAGCRtgqikLLYIAPERLMmdNFL--EHLAHWNPALLAVDEAHCISQWG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 363 --FGPEMKKL----ISCPGMPskdrrqTLMFSATFPE----EIQRL---------AGEFLKPeylfvavgqvggacsDVQ 423
Cdd:PRK11057  156 hdFRPEYAALgqlrQRFPTLP------FMALTATADDttrqDIVRLlglndpliqISSFDRP---------------NIR 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 424 QTIlqVSQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVA 503
Cdd:PRK11057  215 YTL--VEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVA 292
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2092326298 504 TSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 552
Cdd:PRK11057  293 TVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
218-539 4.50e-09

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 59.73  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 218 LTPVQKYSIPIILAGRDLMACAQTGSGKT-AAFlLPILAHMMKDGVTASHfreQQEPECIIVAPTRELINQI------FL 290
Cdd:COG1201    25 PTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGEL---PDGLRVLYISPLKALANDIernlraPL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 291 EARKFSYGTCIRPVVIygGTQTGHS-----IRQIKQGCNILCATPGRLMDII----GKEKigLRKVRYLVLDEA------ 355
Cdd:COG1201   101 EEIGEAAGLPLPEIRV--GVRTGDTpaserQRQRRRPPHILITTPESLALLLtspdAREL--LRGVRTVIVDEIhalags 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 356 -------------DRMLDMGFgpemkkliscpgmpskdRRQTLmfSATF--PEEIQR-LAGEFLKPEYLFVAVGqvGGAC 419
Cdd:COG1201   177 krgvhlalslerlRALAPRPL-----------------QRIGL--SATVgpLEEVARfLVGYEDPRPVTIVDAG--AGKK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 420 SDVqQTILQVSQYSKR--------EKLVE-ILQSIRDER-TMVFVETKKKADFIATFLCqEKIPTTSI-----HG--DRE 482
Cdd:COG1201   236 PDL-EVLVPVEDLIERfpwaghlwPHLYPrVLDLIEAHRtTLVFTNTRSQAERLFQRLN-ELNPEDALpiaahHGslSRE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2092326298 483 QRER-EEALgdfRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTG 539
Cdd:COG1201   314 QRLEvEEAL---KAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
217-390 1.95e-08

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: 54.34  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 217 KLTPVQKYSIPIILAG------RDLMACAQTGSGKTAAFLLPILAhmmkdgVTASHFReqqepeCIIVAPTRELINQIFL 290
Cdd:cd17918    15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL------AYKNGKQ------VAILVPTEILAHQHYE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 291 EARKFSygTCIRPVVIYGGTQTghsirQIKQGCNILCATPGRLMDIIGKEKIGLrkvryLVLDEADRmldmgFGPEMKKL 370
Cdd:cd17918    83 EARKFL--PFINVELVTGGTKA-----QILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHR-----FGVAQREA 145
                         170       180
                  ....*....|....*....|
gi 2092326298 371 ISCPGMPSkdrrqTLMFSAT 390
Cdd:cd17918   146 LYNLGATH-----FLEATAT 160
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
500-552 3.72e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 50.78  E-value: 3.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2092326298 500 VLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 552
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
234-542 4.43e-08

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 55.54  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 234 DLMACAQTGSGKTAAFLLpILAHMMKdgvtashfrEQQEPECIIVAPTRELINQIFLEARK-FSYGTcirpvviyGGTQT 312
Cdd:TIGR01587   1 LLVIEAPTGYGKTEAALL-WALHSIK---------SQKADRVIIALPTRATINAMYRRAKElFGSEL--------VGLHH 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 313 GHSIRQIK----------------QGCNILCATPGRL--MDIIGKEKIGLRKVRY----------LVLDEADRMLdmgfg 364
Cdd:TIGR01587  63 SSSFSRIKemgdseefehlfplyiHSNDKLFLDPITVctIDQVLKSVFGEFGHYEftlasianslLIFDEVHFYD----- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 365 PEMKKLISCPGMPSKDRRQTLM-FSATFPEEIQRlagEFLKPEYLFVAVGQV--GGACSDVQQTILQVSQY-SKREKLVE 440
Cdd:TIGR01587 138 EYTLALILAVLEVLKDNDVPILlMSATLPKFLKE---YAEKIGYVEFNEPLDlkEERRFENHRFILIESDKvGEISSLER 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 441 ILQSIRDE-RTMVFVETKKKADFIATFLcQEKIPTTSI---HG-----DREQREREEALGDFRSGKCPVLVATSVAARGL 511
Cdd:TIGR01587 215 LLEFIKKGgSIAIIVNTVDRAQEFYQQL-KEKAPEEEIilyHSrftekDRAKKEAELLREMKKSNEKFVIVATQVIEASL 293
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2092326298 512 DienvqhvINFDL----PSTIDEYVHRIGRTGRCG 542
Cdd:TIGR01587 294 D-------ISADVmiteLAPIDSLIQRLGRLHRYG 321
PRK13767 PRK13767
ATP-dependent helicase; Provisional
215-354 4.87e-08

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 56.43  E-value: 4.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 215 YLKLTPVQKYSIPIILAGRDLMACAQTGSGKT-AAFLlpilahmmkdGVTASHFREQQEPE------CIIVAPTRELINQ 287
Cdd:PRK13767   30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL----------AIIDELFRLGREGEledkvyCLYVSPLRALNND 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 288 IF--LE---------ARKFSYG-TCIRPVVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIG----KEKigLRKVRYLV 351
Cdd:PRK13767  100 IHrnLEeplteireiAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLNspkfREK--LRTVKWVI 177

                  ...
gi 2092326298 352 LDE 354
Cdd:PRK13767  178 VDE 180
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
239-537 6.92e-08

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: 55.47  E-value: 6.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 239 AQTGSGKTAAFLLPILAHMmkdgvtashfREQQEPECIIVAPTRELINQIFLEARKFSYGTcirpVVIYGGTQTGHSIRQ 318
Cdd:COG1203   154 APTGGGKTEAALLFALRLA----------AKHGGRRIIYALPFTSIINQTYDRLRDLFGED----VLLHHSLADLDLLEE 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 319 IKQGCN---------------ILCATPGRLMDII-----GKEKIGLR---KVryLVLDEADrMLDmgfgPEMKKLIscpg 375
Cdd:COG1203   220 EEEYESearwlkllkelwdapVVVTTIDQLFESLfsnrkGQERRLHNlanSV--IILDEVQ-AYP----PYMLALL---- 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 376 mpskdrRQTLMF-----------SATFPEEIQrlagEFLKPEYLFVavgqvggaCSDVQQTILQVSQYSKR--------- 435
Cdd:COG1203   289 ------LRLLEWlknlggsvilmTATLPPLLR----EELLEAYELI--------PDEPEELPEYFRAFVRKrvelkegpl 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 436 ------EKLVEILQSirDERTMVFVETKKKAdfIATF-LCQEKIPTTSIH--------GDREQRErEEALGDFRSGKCPV 500
Cdd:COG1203   351 sdeelaELILEALHK--GKSVLVIVNTVKDA--QELYeALKEKLPDEEVYllhsrfcpADRSEIE-KEIKERLERGKPCI 425
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2092326298 501 LVATSVAARGLDienvqhvINFDL----PSTIDEYVHRIGR 537
Cdd:COG1203   426 LVSTQVVEAGVD-------IDFDVvirdLAPLDSLIQRAGR 459
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
232-354 2.28e-07

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


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 51.04  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 232 GRDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHfreqqepeCIIVAPTRELINQIF--LEArkfsYGTCI---RPVVI 306
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------VLYISPLKALINDQErrLEE----PLDEIdleIPVAV 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2092326298 307 YGGtQTGHSIR--QIKQGCNILCATPGRLMDIIGKEKIG--LRKVRYLVLDE 354
Cdd:cd17922    69 RHG-DTSQSEKakQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
440-540 6.02e-07

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 49.18  E-value: 6.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 440 EILQSIRDERTM-VFVETKKKADFIAT---FLCQEKIPTTSI---HG--DREQREREEAlgDFRSGKCPVLVATSVAARG 510
Cdd:cd18796    30 EVIFLLERHKSTlVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEVEA--ALKRGDLKVVVATSSLELG 107
                          90       100       110
                  ....*....|....*....|....*....|
gi 2092326298 511 LDIENVQHVINFDLPSTIDEYVHRIGRTGR 540
Cdd:cd18796   108 IDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
444-537 1.35e-06

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 47.55  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 444 SIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQRERE-EALGDFRSG--KCPVLVATSVAARGLDIENVQHVI 520
Cdd:cd18799     3 KYVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
                          90
                  ....*....|....*....
gi 2092326298 521 nFDLP--STIdEYVHRIGR 537
Cdd:cd18799    83 -FLRPteSRT-LFLQMLGR 99
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
433-554 3.33e-06

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 47.24  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 433 SKREKLVEILQSIRD-ERTMVFVETKKKADFIATFLcqeKIPttSIHGDREQREREEALGDFRSGKCPVLVATSVAARGL 511
Cdd:cd18789    34 NKLRALEELLKRHEQgDKIIVFTDNVEALYRYAKRL---LKP--FITGETPQSEREEILQNFREGEYNTLVVSKVGDEGI 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2092326298 512 DI--ENVQHVINFDLPSTiDEYVHRIGRTGRCGNIGKAISFFDSV 554
Cdd:cd18789   109 DLpeANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFFYSL 152
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
214-397 2.81e-05

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 45.60  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 214 GYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmMKDGVTashfreqqepecIIVAPTRELIN--QIFLE 291
Cdd:cd17920     9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL---LLDGVT------------LVVSPLISLMQdqVDRLQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 292 ARkfsygtCIRPVVIyGGTQTGHSIRQIKQGC-----NILCATPGRLMDIIGKEKIG----LRKVRYLVLDEADRMLDMG 362
Cdd:cd17920    74 QL------GIRAAAL-NSTLSPEEKREVLLRIkngqyKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHCVSQWG 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2092326298 363 --FGPEMKKLIS----CPGMPskdrrqTLMFSATFPEEIQR 397
Cdd:cd17920   147 hdFRPDYLRLGRlrraLPGVP------ILALTATATPEVRE 181
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
233-355 4.92e-05

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 44.56  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 233 RDLMACAQTGSGKT--AAFLLPILAHMmkdgvtashFREQQEPECIIV--APTRELINQIFLEARKFSYGTCIrpvVIYG 308
Cdd:cd18034    17 RNTIVVLPTGSGKTliAVMLIKEMGEL---------NRKEKNPKKRAVflVPTVPLVAQQAEAIRSHTDLKVG---EYSG 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2092326298 309 GTQTGHSIRQIKQGC----NILCATPGRLMDIIGKEKIGLRKVRYLVLDEA 355
Cdd:cd18034    85 EMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
233-354 7.28e-05

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 44.27  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 233 RDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHfreqqEPECIIVAPTRELINQIFLEAR-KFSyGTCIRPVVIYGGTQ 311
Cdd:cd18023    18 KNFVVSAPTGSGKTVLFELAILRLLKERNPLPWG-----NRKVVYIAPIKALCSEKYDDWKeKFG-PLGLSCAELTGDTE 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2092326298 312 TGhSIRQIkQGCNILCATPGR--LMDIIGKEKIGL-RKVRYLVLDE 354
Cdd:cd18023    92 MD-DTFEI-QDADIILTTPEKwdSMTRRWRDNGNLvQLVALVLIDE 135
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
477-537 1.96e-04

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 42.33  E-value: 1.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092326298 477 IHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIEN-----VQHVINFDLpSTIDEYVHRIGR 537
Cdd:cd18811    67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGL-SQLHQLRGRVGR 131
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
228-357 4.82e-04

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 41.35  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 228 IILAGRDL----MACAQTGSGKTAAFLLPILAHMMKDGvtashfreqqePECIIVAPTRELINQIFLEARKFSygTCIRP 303
Cdd:cd18035     8 VLIAAVALngntLIVLPTGLGKTIIAILVAADRLTKKG-----------GKVLILAPSRPLVEQHAENLKRVL--NIPDK 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2092326298 304 VVIYGGTQTGHSIRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADR 357
Cdd:cd18035    75 ITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
238-372 4.88e-04

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: 41.48  E-value: 4.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 238 CAQTGSGKTAAFLLPILAhmmkdgvtasHFREQQEPECIIVAPTRELINQIFLE-ARKFSYGTCIRPVVIYGGTQTghSI 316
Cdd:cd18021    25 GAPTGSGKTVCAELALLR----------HWRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLGKKVVKLTGETST--DL 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2092326298 317 RQIKQGcNILCATPGRLmDIIG---KEKIGLRKVRYLVLDEAdRMLDMGFGPEMKKLIS 372
Cdd:cd18021    93 KLLAKS-DVILATPEQW-DVLSrrwKQRKNVQSVELFIADEL-HLIGGENGPVYEVVVS 148
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
477-516 5.25e-04

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 41.10  E-value: 5.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2092326298 477 IHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENV 516
Cdd:cd18792    66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA 105
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
217-395 6.16e-04

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 41.17  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 217 KLTPVQKYSI-PIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGvtashfreqqepECIIVAPTRELINQIFLEARKF 295
Cdd:cd18028     1 ELYPPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG------------KALYLVPLRALASEKYEEFKKL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 296 SygtcirPVVIYGGTQTGHSIRQIKQ--GCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLIsc 373
Cdd:cd18028    69 E------EIGLKVGISTGDYDEDDEWlgDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIV-- 140
                         170       180
                  ....*....|....*....|....*....
gi 2092326298 374 pgmpSKDRR-----QTLMFSATF--PEEI 395
Cdd:cd18028   141 ----ARLRRlnpntQIIGLSATIgnPDEL 165
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
449-543 9.33e-04

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 39.93  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 449 RTMVFVETKKKADFIATFLCQEKIPT----TSIHGDR-----EQREREEAlgDFRSGKCPVLVATSVAARGLDIENVQHV 519
Cdd:cd18797    37 KTIVFCRSRKLAELLLRYLKARLVEEgplaSKVASYRagylaEDRREIEA--ELFNGELLGVVATNALELGIDIGGLDAV 114
                          90       100
                  ....*....|....*....|....
gi 2092326298 520 INFDLPSTIDEYVHRIGRTGRCGN 543
Cdd:cd18797   115 VLAGYPGSLASLWQQAGRAGRRGK 138
ResIII pfam04851
Type III restriction enzyme, res subunit;
216-393 1.32e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 39.96  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 216 LKLTPVQKYSIPIILAGRDL--------MAcaqTGSGKTAafllpILAHMMkdgvtASHFREQQEPECIIVAPTRELINQ 287
Cdd:pfam04851   2 LELRPYQIEAIENLLESIKNgqkrglivMA---TGSGKTL-----TAAKLI-----ARLFKKGPIKKVLFLVPRKDLLEQ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 288 IFLEARKFSYGTCIRPVVIYGGTQtghsiRQIKQGCNILCATPGRLMDIIGKEKIGLRKVRYLVL--DEADRmldmGFGP 365
Cdd:pfam04851  69 ALEEFKKFLPNYVEIGEIISGDKK-----DESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHR----SGAS 139
                         170       180
                  ....*....|....*....|....*...
gi 2092326298 366 EMKKLISCpgmpSKDRRQtLMFSATFPE 393
Cdd:pfam04851 140 SYRNILEY----FKPAFL-LGLTATPER 162
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
232-295 1.43e-03

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 39.97  E-value: 1.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092326298 232 GRDLMACAQTGSGKTAAFLLPILahmmkdgvtaSHFREQQEPECIIVAPTRELINQIFLEARKF 295
Cdd:cd17930     1 PGLVILEAPTGSGKTEAALLWAL----------KLAARGGKRRIIYALPTRATINQMYERIREI 54
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
214-354 3.54e-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: 39.28  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 214 GYLKLTPVQKYSIPIILAGRD-LMACAQTGSGKTAAFLLPILAHMMKD-----GVTASHFReqqepeCIIVAPTRELINQ 287
Cdd:cd18019    14 GFKSLNRIQSKLFPAAFETDEnLLLCAPTGAGKTNVALLTILREIGKHrnpdgTINLDAFK------IVYIAPMKALVQE 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092326298 288 IF--LEARKFSYGTCIRPVviyggtqTG-HSI--RQIKQgCNILCATPGRlMDII---GKEKIGLRKVRYLVLDE 354
Cdd:cd18019    88 MVgnFSKRLAPYGITVAEL-------TGdQQLtkEQISE-TQIIVTTPEK-WDIItrkSGDRTYTQLVRLIIIDE 153
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
472-542 4.16e-03

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


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 38.09  E-value: 4.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092326298 472 IPTTSI---HGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVI-----NFDLpSTIDEYVHRIGRTGRCG 542
Cdd:cd18810    49 VPEARIaiaHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGL-AQLYQLRGRVGRSKERA 126
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
230-357 7.50e-03

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 38.18  E-value: 7.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 230 LAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashFREQQEPECIIVAPTRELINQiflEARKFSYGTCIRP---VVI 306
Cdd:cd17927    15 LKGKNTIICLPTGSGKTFVAVLICEHHLKK-------FPAGRKGKVVFLANKVPLVEQ---QKEVFRKHFERPGykvTGL 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2092326298 307 YGGTQTGHSIRQIKQGCNILCATPGRLM-DIIGKEKIGLRKVRYLVLDEADR 357
Cdd:cd17927    85 SGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
220-355 8.17e-03

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


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 38.01  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 220 PVQKYSIPIILAGRDLMACAQTGSGKTAAFLLP--ILAHmMKDGVTashfreqqepecIIVAPTREL-INQI-FLEARkf 295
Cdd:cd18018    15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPalLLRR-RGPGLT------------LVVSPLIALmKDQVdALPRA-- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092326298 296 sygtcIRPVVIYGG---TQTGHSIRQIKQG-CNILCATPGRLMDIIGKEKIGLRK-VRYLVLDEA 355
Cdd:cd18018    80 -----IKAAALNSSltrEERRRILEKLRAGeVKILYVSPERLVNESFRELLRQTPpISLLVVDEA 139
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
446-517 8.29e-03

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 39.09  E-value: 8.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2092326298 446 RDERTMVFVETKKKADFIATFLcQEKIPTTSIHG-DREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQ 517
Cdd:COG4098   318 EGRQLLIFVPTIELLEQLVALL-QKLFPEERIAGvHAEDPERKEKVQAFRDGEIPILVTTTILERGVTFPNVD 389
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
409-548 8.89e-03

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: 37.15  E-value: 8.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092326298 409 FVAVGQVGGACSDVQQTILQVSQYskrEKLVEILQSIRDERTMVFVETKKKADFIATFLcqekiptTSI---HGDREQRE 485
Cdd:cd18795     8 YVLGFNGLGIKLRVDVMNKFDSDI---IVLLKIETVSEGKPVLVFCSSRKECEKTAKDL-------AGIafhHAGLTRED 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092326298 486 REEALGDFRSGKCPVLVATSVAARGLD-------IENVQHVINF---DLPSTidEYVHRIGRTGRCG--NIGKAI 548
Cdd:cd18795    78 RELVEELFREGLIKVLVATSTLAAGVNlpartviIKGTQRYDGKgyrELSPL--EYLQMIGRAGRPGfdTRGEAI 150
 
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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