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Conserved domains on  [gi|1950452754|ref|XP_038259156|]
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probable ATP-dependent RNA helicase DDX4 isoform X1 [Dermochelys coriacea]

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 ...
211-474 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: 573.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 211 YVPPPPPDNEEAIFAHYQTGINFDKYDTILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG 290
Cdd:cd18052     1 YIPPPPPEDEDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 291 RDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQT 370
Cdd:cd18052    81 RDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 371 GHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFP 450
Cdd:cd18052   161 GHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFP 240
                         250       260
                  ....*....|....*....|....
gi 1950452754 451 EEIQRLAGEFLKPEYLFVAVGQVG 474
Cdd:cd18052   241 EEIQRLAAEFLKEDYLFLTVGRVG 264
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
480-609 1.61e-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: 193.49  E-value: 1.61e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 480 VQQTILQVSQYSKREKL-VEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPV 558
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1950452754 559 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 609
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 ...
211-474 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: 573.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 211 YVPPPPPDNEEAIFAHYQTGINFDKYDTILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG 290
Cdd:cd18052     1 YIPPPPPEDEDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 291 RDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQT 370
Cdd:cd18052    81 RDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 371 GHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFP 450
Cdd:cd18052   161 GHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFP 240
                         250       260
                  ....*....|....*....|....
gi 1950452754 451 EEIQRLAGEFLKPEYLFVAVGQVG 474
Cdd:cd18052   241 EEIQRLAAEFLKEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
254-610 3.01e-153

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 449.98  E-value: 3.01e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGvtashfreQQEPEC 333
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR--------PRAPQA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 334 IIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEA 413
Cdd:COG0513    75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 414 DRMLDMGFGPEMKKLIS-CPgmpskDRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVGQVGGACSDVQQTILQVSQYSK 492
Cdd:COG0513   155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 493 REKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIE 572
Cdd:COG0513   229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1950452754 573 NVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 610
Cdd:COG0513   309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT 346
PTZ00110 PTZ00110
helicase; Provisional
151-653 1.68e-116

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 360.24  E-value: 1.68e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 151 SRRGEFGGPTGDNDSNRNRGFGSKGGYR-GYNEEViAGSGRSSWKLHGETASGDNQGP----KVTYVPppppdNEEAIFA 225
Cdd:PTZ00110   22 NSYGPYPDSSNPYGNYQANHQDNYGGFRpGYGNYS-GGYGGFGMNSYGSSTLGKRLQPidwkSINLVP-----FEKNFYK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 226 HYQ--TGINFDKYDTILVE-----VSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQ 298
Cdd:PTZ00110   96 EHPevSALSSKEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 299 TGSGKTAAFLLPILAHmmkdgVTASH-FREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQI 377
Cdd:PTZ00110  176 TGSGKTLAFLLPAIVH-----INAQPlLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYAL 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 378 MQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPEMKKLIScpgmPSKDRRQTLMFSATFPEEIQRLA 457
Cdd:PTZ00110  251 RRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLA 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 458 GEFLKPEYLFVAVGQVG-GACSDVQQTILQVSQYSKREKLVEILQSIRDE--RTMVFVETKKKADFIATFLCQEKIPTTS 534
Cdd:PTZ00110  327 RDLCKEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALC 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 535 IHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFDSvSD 614
Cdd:PTZ00110  407 IHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP-DK 485
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1950452754 615 SHIAQPLLKVLSDAQQEVPLWLEEIAFSAHGTGFSNPRG 653
Cdd:PTZ00110  486 YRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWG 524
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
277-456 9.26e-61

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: 200.93  E-value: 9.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 277 TPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfrEQQEPECIIVAPTRELINQIFLEARKFSYG 356
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK---------LDNGPQALVLAPTRELAEQIYEELKKLGKG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 357 TCIRPVVIYGGTQTGHSIRQImQGCNILCATPGRLMDIIGKEKiGLREVRYLVLDEADRMLDMGFGPEMKKLISCpgMPS 436
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LPK 147
                         170       180
                  ....*....|....*....|
gi 1950452754 437 KdrRQTLMFSATFPEEIQRL 456
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 ...
480-609 1.61e-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: 193.49  E-value: 1.61e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 480 VQQTILQVSQYSKREKL-VEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPV 558
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1950452754 559 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 609
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
268-468 1.27e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 177.68  E-value: 1.27e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754  268 IAKAGYLKLTPVQKYSIPIILAG-RDLMACAQTGSGKTAAFLLPILAHmmkdgvtashFREQQEPECIIVAPTRELINQI 346
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA----------LKRGKGGRVLVLVPTRELAEQW 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754  347 FLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGC-NILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPEM 425
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1950452754  426 KKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKPEYLFV 468
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLNDPVFID 189
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
491-600 1.37e-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: 141.19  E-value: 1.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 491 SKREKLVEILQSIRDERTMVFVETKKKADfIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLD 570
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1950452754 571 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 600
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
519-600 6.08e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 109.99  E-value: 6.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754  519 DFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 598
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1950452754  599 CG 600
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
489-606 1.13e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 96.72  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 489 QYSKREKLVEILQSIR----DERTMVFVETKKKADFIATFLCQEKIPTTSIHG--DRE------QREREEALGDFRSGKC 556
Cdd:COG1111   333 EHPKLSKLREILKEQLgtnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGEF 412
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1950452754 557 PVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNIGKAI 606
Cdd:COG1111   413 NVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
PRK13766 PRK13766
Hef nuclease; Provisional
492-606 5.70e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.76  E-value: 5.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 492 KREKLVEILQSI----RDERTMVFVETKKKADFIATFLCQEKIPTTSIHG--DRE------QREREEALGDFRSGKCPVL 559
Cdd:PRK13766  348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaSKDgdkgmsQKEQIEILDKFRAGEFNVL 427
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1950452754 560 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNIGKAI 606
Cdd:PRK13766  428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
292-600 3.92e-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: 55.92  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 292 DLMACAQTGSGKTAAFLLpILAHMMKdgvtashfrEQQEPECIIVAPTRELINQIFLEARK-FSYGTcirpVVIYGGTQT 370
Cdd:TIGR01587   1 LLVIEAPTGYGKTEAALL-WALHSIK---------SQKADRVIIALPTRATINAMYRRAKElFGSEL----VGLHHSSSF 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 371 -------------------GHSIRQIMQGCNILCaTPGRLMDIIGKE----KIGLREVRY--LVLDEADRMLdmgfgPEM 425
Cdd:TIGR01587  67 srikemgdseefehlfplyIHSNDKLFLDPITVC-TIDQVLKSVFGEfghyEFTLASIANslLIFDEVHFYD-----EYT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 426 KKLISCPGMPSKDRRQTLM-FSATFPEEIQRlagEFLKPEYLFVAVGQV--GGACSDVQQTILQVSQY-SKREKLVEILQ 501
Cdd:TIGR01587 141 LALILAVLEVLKDNDVPILlMSATLPKFLKE---YAEKIGYVEFNEPLDlkEERRFENHRFILIESDKvGEISSLERLLE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 502 SIRDE-RTMVFVETKKKADFIATFLcQEKIPTTSI---HG-----DREQREREEALGDFRSGKCPVLVATSVAARGLDie 572
Cdd:TIGR01587 218 FIKKGgSIAIIVNTVDRAQEFYQQL-KEKAPEEEIilyHSrftekDRAKKEAELLREMKKSNEKFVIVATQVIEASLD-- 294
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1950452754 573 nvqhvINFDL----PSTIDEYVHRIGRTGRCG 600
Cdd:TIGR01587 295 -----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 ...
211-474 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: 573.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 211 YVPPPPPDNEEAIFAHYQTGINFDKYDTILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG 290
Cdd:cd18052     1 YIPPPPPEDEDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 291 RDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQT 370
Cdd:cd18052    81 RDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 371 GHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFP 450
Cdd:cd18052   161 GHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFP 240
                         250       260
                  ....*....|....*....|....
gi 1950452754 451 EEIQRLAGEFLKPEYLFVAVGQVG 474
Cdd:cd18052   241 EEIQRLAAEFLKEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
254-610 3.01e-153

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 449.98  E-value: 3.01e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGvtashfreQQEPEC 333
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR--------PRAPQA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 334 IIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEA 413
Cdd:COG0513    75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 414 DRMLDMGFGPEMKKLIS-CPgmpskDRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVGQVGGACSDVQQTILQVSQYSK 492
Cdd:COG0513   155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 493 REKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIE 572
Cdd:COG0513   229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1950452754 573 NVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 610
Cdd:COG0513   309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT 346
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
254-474 5.61e-143

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: 5.61e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAS-HFREQQEPE 332
Cdd:cd17967     1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgRGRRKAYPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 333 CIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDE 412
Cdd:cd17967    81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950452754 413 ADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVGQVG 474
Cdd:cd17967   161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
PTZ00110 PTZ00110
helicase; Provisional
151-653 1.68e-116

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 360.24  E-value: 1.68e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 151 SRRGEFGGPTGDNDSNRNRGFGSKGGYR-GYNEEViAGSGRSSWKLHGETASGDNQGP----KVTYVPppppdNEEAIFA 225
Cdd:PTZ00110   22 NSYGPYPDSSNPYGNYQANHQDNYGGFRpGYGNYS-GGYGGFGMNSYGSSTLGKRLQPidwkSINLVP-----FEKNFYK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 226 HYQ--TGINFDKYDTILVE-----VSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQ 298
Cdd:PTZ00110   96 EHPevSALSSKEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 299 TGSGKTAAFLLPILAHmmkdgVTASH-FREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQI 377
Cdd:PTZ00110  176 TGSGKTLAFLLPAIVH-----INAQPlLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYAL 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 378 MQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPEMKKLIScpgmPSKDRRQTLMFSATFPEEIQRLA 457
Cdd:PTZ00110  251 RRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLA 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 458 GEFLKPEYLFVAVGQVG-GACSDVQQTILQVSQYSKREKLVEILQSIRDE--RTMVFVETKKKADFIATFLCQEKIPTTS 534
Cdd:PTZ00110  327 RDLCKEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALC 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 535 IHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFDSvSD 614
Cdd:PTZ00110  407 IHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP-DK 485
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1950452754 615 SHIAQPLLKVLSDAQQEVPLWLEEIAFSAHGTGFSNPRG 653
Cdd:PTZ00110  486 YRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWG 524
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
233-474 3.28e-112

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: 338.17  E-value: 3.28e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 233 FDKYDTILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPIL 312
Cdd:cd18051     1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 313 AHMMKDG-------VTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILC 385
Cdd:cd18051    81 SQIYEQGpgeslpsESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 386 ATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFPEEIQRLAGEFLKpEY 465
Cdd:cd18051   161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLD-NY 239

                  ....*....
gi 1950452754 466 LFVAVGQVG 474
Cdd:cd18051   240 IFLAVGRVG 248
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
255-609 1.22e-100

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 315.97  E-value: 1.22e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmkdgVTASHFREQqepeCI 334
Cdd:PRK11776    6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK-----LDVKRFRVQ----AL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 335 IVAPTRELINQIFLEARKFSYGT-CIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEA 413
Cdd:PRK11776   77 VLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 414 DRMLDMGFGPEMKKLIS-CPGmpskdRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVGQVGGAcSDVQQTILQVSQYSK 492
Cdd:PRK11776  157 DRMLDMGFQDAIDAIIRqAPA-----RRQTLLFSATYPEGIAAISQRFQR-DPVEVKVESTHDL-PAIEQRFYEVSPDER 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 493 REKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIE 572
Cdd:PRK11776  230 LPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1950452754 573 NVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 609
Cdd:PRK11776  310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLV 346
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
254-608 1.01e-91

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 291.85  E-value: 1.01e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashFREQQE--P 331
Cdd:PRK11192    2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLD-------FPRRKSgpP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 332 ECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLD 411
Cdd:PRK11192   75 RILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 412 EADRMLDMGFGPEMKKL-ISCPGmpskdRRQTLMFSATFP-EEIQRLAGEFLK-PEYLFVAvgqvggACSDVQQTILQV- 487
Cdd:PRK11192  155 EADRMLDMGFAQDIETIaAETRW-----RKQTLLFSATLEgDAVQDFAERLLNdPVEVEAE------PSRRERKKIHQWy 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 488 ----SQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATS 563
Cdd:PRK11192  224 yradDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATD 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1950452754 564 VAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 608
Cdd:PRK11192  304 VAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
238-633 9.89e-87

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 281.68  E-value: 9.89e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 238 TILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMK 317
Cdd:PLN00206  106 KLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCT 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 318 dgVTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGK 397
Cdd:PLN00206  186 --IRSGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSK 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 398 EKIGLREVRYLVLDEADRMLDMGFGPEMKKLISCPGMPskdrrQTLMFSATFPEEIQRLAGEFLKpEYLFVAVGQVGGAC 477
Cdd:PLN00206  264 HDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAK-DIILISIGNPNRPN 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 478 SDVQQTILQVSQYSKREKLVEILQSIRDER--TMVFVETKKKADFIAtflcqEKIPTT------SIHGDREQREREEALG 549
Cdd:PLN00206  338 KAVKQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLA-----NAITVVtglkalSIHGEKSMKERREVMK 412
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 550 DFRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFDSvSDSHIAQPLLKVLSDAQ 629
Cdd:PLN00206  413 SFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNE-EDRNLFPELVALLKSSG 491

                  ....
gi 1950452754 630 QEVP 633
Cdd:PLN00206  492 AAIP 495
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
253-607 5.22e-86

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 277.84  E-value: 5.22e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 253 LTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtASHFREQQEPE 332
Cdd:PRK10590    1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITR---QPHAKGRRPVR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 333 CIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDE 412
Cdd:PRK10590   78 ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 413 ADRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLAGEFLK-PEYlfVAVGQVGGACSDVQQTILQVSQYS 491
Cdd:PRK10590  158 ADRMLDMGFIHDIRRVLA--KLPAK--RQNLLFSATFSDDIKALAEKLLHnPLE--IEVARRNTASEQVTQHVHFVDKKR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 492 KREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDI 571
Cdd:PRK10590  232 KRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDI 311
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1950452754 572 ENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAIS 607
Cdd:PRK10590  312 EELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALS 347
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
264-462 1.31e-83

DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 261.99  E-value: 1.31e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVtashfREQQEPECIIVAPTRELI 343
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-----KKGRGPQALVLAPTRELA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 344 NQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGP 423
Cdd:cd00268    76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEE 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1950452754 424 EMKKLIS-CPgmpskDRRQTLMFSATFPEEIQRLAGEFLK 462
Cdd:cd00268   156 DVEKILSaLP-----KDRQTLLFSATLPEEVKELAKKFLK 190
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
246-608 1.02e-79

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 261.77  E-value: 1.02e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 246 LDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHF 325
Cdd:PRK01297   80 VEPQEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERY 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 326 ReqQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQI-MQGCNILCATPGRLMDIIGKEKIGLRE 404
Cdd:PRK01297  160 M--GEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDM 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 405 VRYLVLDEADRMLDMGFGPEMKKLIScpGMPSKDRRQTLMFSATFPEEIQRLAGEFL-KPEYLFVAVGQVggACSDVQQT 483
Cdd:PRK01297  238 VEVMVLDEADRMLDMGFIPQVRQIIR--QTPRKEERQTLLFSATFTDDVMNLAKQWTtDPAIVEIEPENV--ASDTVEQH 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 484 ILQVSQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATS 563
Cdd:PRK01297  314 VYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATD 393
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1950452754 564 VAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 608
Cdd:PRK01297  394 VAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
247-608 9.15e-77

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 256.80  E-value: 9.15e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 247 DPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAShfR 326
Cdd:PRK04537    3 DKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALAD--R 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 327 EQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKI-GLREV 405
Cdd:PRK04537   81 KPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHAC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 406 RYLVLDEADRMLDMGFGPEMKKLIScpGMPSKDRRQTLMFSATFPEEIQRLAGEFL-KPEYLFVAVGQVGGAcsDVQQTI 484
Cdd:PRK04537  161 EICVLDEADRMFDLGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMnEPEKLVVETETITAA--RVRQRI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 485 LQVSQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSV 564
Cdd:PRK04537  237 YFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDV 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1950452754 565 AARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 608
Cdd:PRK04537  317 AARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
268-608 3.50e-72

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 240.26  E-value: 3.50e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 268 IAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvTASHFREQQEPECIIVAPTRELINQIF 347
Cdd:PRK04837   23 LEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSH--PAPEDRKVNQPRALIMAPTRELAVQIH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 348 LEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPEMKK 427
Cdd:PRK04837  101 ADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRW 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 428 LIScpGMPSKDRRQTLMFSATFPEEIQRLAGEFL-KPEYLFVAVGQVGGacSDVQQTILQVSQYSKREKLVEILQSIRDE 506
Cdd:PRK04837  181 LFR--RMPPANQRLNMLFSATLSYRVRELAFEHMnNPEYVEVEPEQKTG--HRIKEELFYPSNEEKMRLLQTLIEEEWPD 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 507 RTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTI 586
Cdd:PRK04837  257 RAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDC 336
                         330       340
                  ....*....|....*....|..
gi 1950452754 587 DEYVHRIGRTGRCGNIGKAISF 608
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 ...
266-468 8.38e-66

DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 215.31  E-value: 8.38e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtaSHFREQQEPECIIVAPTRELINQ 345
Cdd:cd17966     3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQ----PPLERGDGPIVLVLAPTRELAQQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 346 IFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPEM 425
Cdd:cd17966    79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1950452754 426 KKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKpEYLFV 468
Cdd:cd17966   159 RKIVD----QIRPDRQTLMWSATWPKEVRRLAEDFLK-DYIQV 196
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
254-611 1.67e-64

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 225.11  E-value: 1.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILaHMMKDGVTAshfreqqePEC 333
Cdd:PRK11634    7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLL-HNLDPELKA--------PQI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 334 IIVAPTRELINQIFLEARKFS-YGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDE 412
Cdd:PRK11634   78 LVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 413 ADRMLDMGFGPEMKKLIScpGMPskDRRQTLMFSATFPEEIQRLAGEFLK-PEYlfVAVGQVGGACSDVQQTILQVSQYS 491
Cdd:PRK11634  158 ADEMLRMGFIEDVETIMA--QIP--EGHQTALFSATMPEAIRRITRRFMKePQE--VRIQSSVTTRPDISQSYWTVWGMR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 492 KREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDI 571
Cdd:PRK11634  232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1950452754 572 ENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFDS 611
Cdd:PRK11634  312 ERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVEN 351
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
277-456 9.26e-61

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: 200.93  E-value: 9.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 277 TPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfrEQQEPECIIVAPTRELINQIFLEARKFSYG 356
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK---------LDNGPQALVLAPTRELAEQIYEELKKLGKG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 357 TCIRPVVIYGGTQTGHSIRQImQGCNILCATPGRLMDIIGKEKiGLREVRYLVLDEADRMLDMGFGPEMKKLISCpgMPS 436
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LPK 147
                         170       180
                  ....*....|....*....|
gi 1950452754 437 KdrRQTLMFSATFPEEIQRL 456
Cdd:pfam00270 148 K--RQILLLSATLPRNLEDL 165
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
266-468 3.53e-60

DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 200.89  E-value: 3.53e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 266 KNIAKAGYLKLTPVQKYSIPIILA-GRDLMACAQTGSGKTAAFLLPILAHMMKDgvtasHFREQQEP-ECIIVAPTRELI 343
Cdd:cd17964     7 KALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNT-----KPAGRRSGvSALIISPTRELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 344 NQIFLEARKF-SYGTCIRPVVIYGGTQTGHSIRQIM-QGCNILCATPGRLMDIIGKEKIG--LREVRYLVLDEADRMLDM 419
Cdd:cd17964    82 LQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLDM 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1950452754 420 GFGPEMKKLISCPGMPSKDRRQTLMFSATFPEEIQRLAGEFLKPEYLFV 468
Cdd:cd17964   162 GFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
264-461 8.55e-60

DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 199.56  E-value: 8.55e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtaSHFREQQEPECIIVAPTRELI 343
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ----RELEKGEGPIAVIVAPTRELA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 344 NQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGP 423
Cdd:cd17952    77 QQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEY 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1950452754 424 EMKKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFL 461
Cdd:cd17952   157 QVRSIVG----HVRPDRQTLLFSATFKKKIEQLARDIL 190
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
480-609 1.61e-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: 193.49  E-value: 1.61e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 480 VQQTILQVSQYSKREKL-VEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPV 558
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1950452754 559 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 609
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
243-462 4.06e-58

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: 195.67  E-value: 4.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 243 VSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMkdgvtA 322
Cdd:cd17953     2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIK-----D 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 323 SHFREQQE-PECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDII---GKE 398
Cdd:cd17953    77 QRPVKPGEgPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGR 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1950452754 399 KIGLREVRYLVLDEADRMLDMGFGPEMKKLIscpgMPSKDRRQTLMFSATFPEEIQRLAGEFLK 462
Cdd:cd17953   157 VTNLRRVTYVVLDEADRMFDMGFEPQIMKIV----NNIRPDRQTVLFSATFPRKVEALARKVLH 216
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
264-471 5.02e-57

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


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 192.03  E-value: 5.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtashfREQQEPECIIVAPTRELI 343
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP-------RKKKGLRALILAPTRELA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 344 NQIFLEARKFSYGTCIRPVVIYGGTQTG-HSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFG 422
Cdd:cd17957    74 SQIYRELLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFR 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1950452754 423 PEMKKLI-SCPGmPSKdrrQTLMFSATFPEEIQRLAGEFLKPeYLFVAVG 471
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 ...
268-462 6.13e-57

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 192.53  E-value: 6.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 268 IAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMK----DGVTashfrEQQEPECIIVAPTRELI 343
Cdd:cd17945     5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpplDEET-----KDDGPYALILAPTRELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 344 NQIFLEARKFSYGTCIRPVVIYGGtqtgHSIR----QIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDM 419
Cdd:cd17945    80 QQIEEETQKFAKPLGIRVVSIVGG----HSIEeqafSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDM 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950452754 420 GFGPEMKKLIScpGMPS------------------KDRRQTLMFSATFPEEIQRLAGEFLK 462
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, ...
241-471 1.62e-56

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: 192.15  E-value: 1.62e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 241 VEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmkdgV 320
Cdd:cd18049    12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH-----I 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 321 TASHFREQQE-PECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEK 399
Cdd:cd18049    87 NHQPFLERGDgPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950452754 400 IGLREVRYLVLDEADRMLDMGFGPEMKKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVG 471
Cdd:cd18049   167 TNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLK-DYIHINIG 233
PTZ00424 PTZ00424
helicase 45; Provisional
254-608 3.53e-54

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 191.19  E-value: 3.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAshfreqqepEC 333
Cdd:PTZ00424   29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNAC---------QA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 334 IIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEA 413
Cdd:PTZ00424  100 LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 414 DRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLAGEFLK-PEYLFVAVGQVggACSDVQQTILQVSQYS- 491
Cdd:PTZ00424  180 DEMLSRGFKGQIYDVFK--KLPPD--VQVALFSATMPNEILELTTKFMRdPKRILVKKDEL--TLEGIRQFYVAVEKEEw 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 492 KREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDI 571
Cdd:PTZ00424  254 KFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDV 333
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1950452754 572 ENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 608
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 ...
266-462 4.88e-52

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: 178.43  E-value: 4.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMmkdgVTASHFREQQE-PECIIVAPTRELIN 344
Cdd:cd17958     3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL----DLQPIPREQRNgPGVLVLTPTRELAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 345 QIFLEARKFSYGTcIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPE 424
Cdd:cd17958    79 QIEAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1950452754 425 MKKLIscpgMPSKDRRQTLMFSATFPEEIQRLAGEFLK 462
Cdd:cd17958   158 IRKIL----LDIRPDRQTIMTSATWPDGVRRLAQSYLK 191
DEXDc smart00487
DEAD-like helicases superfamily;
268-468 1.27e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 177.68  E-value: 1.27e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754  268 IAKAGYLKLTPVQKYSIPIILAG-RDLMACAQTGSGKTAAFLLPILAHmmkdgvtashFREQQEPECIIVAPTRELINQI 346
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA----------LKRGKGGRVLVLVPTRELAEQW 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754  347 FLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGC-NILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPEM 425
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1950452754  426 KKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKPEYLFV 468
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 ...
241-471 7.00e-51

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: 177.90  E-value: 7.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 241 VEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgv 320
Cdd:cd18050    50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQ-- 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 321 taSHFREQQEPECIIVAPTRELINQIflEARKFSYGTC--IRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKE 398
Cdd:cd18050   128 --PYLERGDGPICLVLAPTRELAQQV--QQVADDYGKSsrLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAG 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950452754 399 KIGLREVRYLVLDEADRMLDMGFGPEMKKLIScpgmPSKDRRQTLMFSATFPEEIQRLAGEFLKpEYLFVAVG 471
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 ...
255-468 1.84e-50

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: 174.33  E-value: 1.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVtaSHFreqqepeCI 334
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPY--GIF-------AL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 335 IVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQtghSIRQ---IMQGCNILCATPGRLMDII---GKEKIGLREVRYL 408
Cdd:cd17955    72 VLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMD---MVKQaleLSKRPHIVVATPGRLADHLrssDDTTKVLSRVKFL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 409 VLDEADRMLDMGFGPEMKKLISCpgMPSKdrRQTLMFSATFPEEIQRLAGEFLKPEYLFV 468
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) ...
270-466 1.48e-49

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: 172.39  E-value: 1.48e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 270 KAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtASHFREQQEPECIIVAPTRELINQIFLE 349
Cdd:cd17949     8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSL---EPRVDRSDGTLALVLVPTRELALQIYEV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 350 ARKF-SYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEK-IGLREVRYLVLDEADRMLDMGFGPEMKK 427
Cdd:cd17949    85 LEKLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEKDITK 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1950452754 428 LIS--------CPGMPSKD-RRQTLMFSATFPEEIQRLAGEFLK-PEYL 466
Cdd:cd17949   165 ILEllddkrskAGGEKSKPsRRQTVLVSATLTDGVKRLAGLSLKdPVYI 213
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
266-462 5.57e-49

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: 170.13  E-value: 5.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMkdgvtashFREQQEPEC--IIVAPTRELI 343
Cdd:cd17947     3 RALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLL--------YRPKKKAATrvLVLVPTRELA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 344 NQIFLEARKFSYGTCIRPVVIYGGTqtghSIRQ----IMQGCNILCATPGRLMDIIGKEK-IGLREVRYLVLDEADRMLD 418
Cdd:cd17947    75 MQCFSVLQQLAQFTDITFALAVGGL----SLKAqeaaLRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLE 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1950452754 419 MGFGPEMKKLI-SCPGmpskdRRQTLMFSATFPEEIQRLAGEFLK 462
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 ...
254-451 3.35e-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: 168.25  E-value: 3.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPIL----AHMMKDGVTAshfreqq 329
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIeklkAHSPTVGARA------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 330 epecIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLV 409
Cdd:cd17959    75 ----LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVV 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1950452754 410 LDEADRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPE 451
Cdd:cd17959   151 FDEADRLFEMGFAEQLHEILS--RLPEN--RQTLLFSATLPK 188
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
268-457 1.38e-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: 166.60  E-value: 1.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 268 IAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfREQQEPE----CIIVAPTRELI 343
Cdd:cd17960     5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLK--------RKANLKKgqvgALIISPTRELA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 344 NQIFLEARKF--SYGTCIRPVVIYGGTQTGHSIRQIM-QGCNILCATPGRLMDIIG--KEKIGLREVRYLVLDEADRMLD 418
Cdd:cd17960    77 TQIYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLD 156
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1950452754 419 MGFGPEMKKLISCpgMPsKDRRqTLMFSATFPEEIQRLA 457
Cdd:cd17960   157 LGFEADLNRILSK--LP-KQRR-TGLFSATQTDAVEELI 191
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
254-456 1.49e-47

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: 1.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtashfreQQEPEC 333
Cdd:cd17954     1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---------PQRFFA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 334 IIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEK-IGLREVRYLVLDE 412
Cdd:cd17954    72 LVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDE 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1950452754 413 ADRMLDMGFGPEMKKLISCpgMPSkdRRQTLMFSATFPEEIQRL 456
Cdd:cd17954   152 ADRLLNMDFEPEIDKILKV--IPR--ERTTYLFSATMTTKVAKL 191
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
266-468 3.38e-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: 3.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMmkdgvtashFREQQEPE----CIIVAPTRE 341
Cdd:cd17941     3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL---------YRERWTPEdglgALIISPTRE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 342 LINQIFLEARKFSYGTCIRPVVIYGGTQTGHSiRQIMQGCNILCATPGRL---MDiigkEKIGL--REVRYLVLDEADRM 416
Cdd:cd17941    74 LAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE-KERINRMNILVCTPGRLlqhMD----ETPGFdtSNLQMLVLDEADRI 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1950452754 417 LDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLAGEFLK-PEYLFV 468
Cdd:cd17941   149 LDMGFKETLDAIVE--NLPKS--RQTLLFSATQTKSVKDLARLSLKnPEYISV 197
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
266-468 5.72e-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: 159.45  E-value: 5.72e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmmkDGVTASHFREQQEPECIIVAPTRELINQ 345
Cdd:cd17942     3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-----ELLYKLKFKPRNGTGVIIISPTRELALQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 346 IFLEARKF------SYGTCIrpvviyGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGL-REVRYLVLDEADRMLD 418
Cdd:cd17942    78 IYGVAKELlkyhsqTFGIVI------GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILE 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1950452754 419 MGFGPEMKKLISCpgMPSkdRRQTLMFSATFPEEIQRLAGEFLKPEYLFV 468
Cdd:cd17942   152 IGFEEEMRQIIKL--LPK--RRQTMLFSATQTRKVEDLARISLKKKPLYV 197
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
255-465 5.97e-45

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: 159.39  E-value: 5.97e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPIL--AHMMKDGVTAshfreqqepe 332
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILekIDPKKDVIQA---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 333 cIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDE 412
Cdd:cd17940    71 -LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1950452754 413 ADRMLDMGFGPEMKKLIS-CPgmpskDRRQTLMFSATFPEEIQRLAGEFLKPEY 465
Cdd:cd17940   150 ADKLLSQDFQPIIEKILNfLP-----KERQILLFSATFPLTVKNFMDRHMHNPY 198
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
255-457 2.21e-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: 2.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmmkdgvtashfreqQEPECI 334
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------QIVVAL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 335 IVAPTRELINQIFLEARKFSY---GTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLD 411
Cdd:cd17938    65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1950452754 412 EADRMLDMGFGPEMKKLIS-CPGMPSKDRR-QTLMFSATF-PEEIQRLA 457
Cdd:cd17938   145 EADRLLSQGNLETINRIYNrIPKITSDGKRlQVIVCSATLhSFEVKKLA 193
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
266-457 7.41e-43

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: 153.65  E-value: 7.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAShFREQQEPECIIVAPTRELINQ 345
Cdd:cd17951     3 KGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLP-FIKGEGPYGLIVCPSRELARQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 346 IF---------LEARKFSYgtcIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRM 416
Cdd:cd17951    82 THevieyyckaLQEGGYPQ---LRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1950452754 417 LDMGFGPEMKKLISCpgmpSKDRRQTLMFSATFPEEIQRLA 457
Cdd:cd17951   159 IDMGFEEDIRTIFSY----FKGQRQTLLFSATMPKKIQNFA 195
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
264-462 6.89e-42

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: 150.78  E-value: 6.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfrEQQEPECIIVAPTRELI 343
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT---------EHRNPSALILTPTRELA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 344 NQIFLEARKFSYGTC-IRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFG 422
Cdd:cd17962    72 VQIEDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQ 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1950452754 423 PE-MKKLISCPGMPskdrrQTLMFSATFPEEIQRLAGEFLK 462
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 ...
266-449 1.26e-40

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: 148.54  E-value: 1.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 266 KNIAKAGYLKLTPVQKYSIP-IILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHFREQQEPECIIVAPTRELIN 344
Cdd:cd17946     3 RALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTRELAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 345 QI---FLEARKFsygTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGK--EKIG-LREVRYLVLDEADRMLD 418
Cdd:cd17946    83 QVkdhLKAIAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEgnEHLAnLKSLRFLVLDEADRMLE 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1950452754 419 MGFGPEMKKLISC---PGMPSKDRRQTLMFSATF 449
Cdd:cd17946   160 KGHFAELEKILELlnkDRAGKKRKRQTFVFSATL 193
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
491-600 1.37e-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: 141.19  E-value: 1.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 491 SKREKLVEILQSIRDERTMVFVETKKKADfIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLD 570
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1950452754 571 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 600
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 ...
264-462 5.22e-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: 134.63  E-value: 5.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAshfREQQEPECIIVAPTRELI 343
Cdd:cd17961     5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAES---GEEQGTRALILVPTRELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 344 NQIFLEARKFSYGTC--IRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRE-VRYLVLDEADRMLDMG 420
Cdd:cd17961    82 QQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLSYG 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1950452754 421 FGPEMKKLIScpGMPSkdRRQTLMFSATFPEEIQRLAGEFLK 462
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 ...
266-465 7.64e-34

DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 128.43  E-value: 7.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtASHFREQQEPECIIVAPTRELINQ 345
Cdd:cd17944     3 KLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQED---QQPRKRGRAPKVLVLAPTRELANQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 346 IFLE----ARKFSYgTCIrpvviYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGF 421
Cdd:cd17944    80 VTKDfkdiTRKLSV-ACF-----YGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGF 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1950452754 422 GPEMKKLISCP-GMPSKDRRQTLMFSATFPEEIQRLAGEFLKPEY 465
Cdd:cd17944   154 AEQVEEILSVSyKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQY 198
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
264-463 8.40e-34

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: 128.08  E-value: 8.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 264 LNKNIAKAGYLKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILAHMmkDgvtashfREQQEPECIIVAPTRE 341
Cdd:cd17963     5 LLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV--D-------PTLKSPQALCLAPTRE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 342 LINQIFLEARKFSYGT------CIRPVVIYGGTQ-TGHsirqimqgcnILCATPGRLMDIIGKEKIGLREVRYLVLDEAD 414
Cdd:cd17963    76 LARQIGEVVEKMGKFTgvkvalAVPGNDVPRGKKiTAQ----------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEAD 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1950452754 415 RMLDM-GFGPE---MKKLIscpgmpsKDRRQTLMFSATFPEEIQRLAGEFLKP 463
Cdd:cd17963   146 VMLDTqGHGDQsirIKRML-------PRNCQILLFSATFPDSVRKFAEKIAPN 191
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
264-456 1.96e-32

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: 125.44  E-value: 1.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 264 LNKNIAKAGYLKLTPVQKYSIPIILAG---------RDLMACAQTGSGKTAAFLLPILAhMMKDGVtASHFReqqepeCI 334
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQ-ALSKRV-VPRLR------AL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 335 IVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGC--------NILCATPGRLMD-IIGKEKIGLREV 405
Cdd:cd17956    73 IVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDhLNSTPGFTLKHL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 406 RYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRR----------------QTLMFSATF---PEEIQRL 456
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 ...
264-468 2.40e-30

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: 118.60  E-value: 2.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILaHMMKDgvtashfrEQQEPECIIVAPTRELI 343
Cdd:cd17950    13 LLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL-QQLEP--------VDGQVSVLVICHTRELA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 344 NQIFLEARKFS-YGTCIRPVVIYGGTQTGHSIRQIMQGC-NILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDmgf 421
Cdd:cd17950    84 FQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE--- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1950452754 422 GPEMKKLI-----SCPgmpsKDrRQTLMFSATFPEEIQRLAGEFLK-PEYLFV 468
Cdd:cd17950   161 QLDMRRDVqeifrATP----HD-KQVMMFSATLSKEIRPVCKKFMQdPLEIFV 208
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
267-451 6.43e-30

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 118.24  E-value: 6.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 267 NIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAShfREQQEPECIIVAPTRELINQI 346
Cdd:cd17948     4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAE--GPFNAPRGLVITPSRELAEQI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 347 FLEARKFSYGTCIRPVVIYGgtqtGHSIRQIM----QGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFG 422
Cdd:cd17948    82 GSVAQSLTEGLGLKVKVITG----GRTKRQIRnphfEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1950452754 423 PEMKKLIS-CP--GMPSKDRR------QTLMFSATFPE 451
Cdd:cd17948   158 EKLSHFLRrFPlaSRRSENTDgldpgtQLVLVSATMPS 195
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
266-451 5.06e-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: 114.28  E-value: 5.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLlpILAHMMKDgvtashfREQQEPECIIVAPTRELINQ 345
Cdd:cd17943     3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFV--VIALESLD-------LERRHPQVLILAPTREIAVQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 346 IFLEARKF-SYGTCIRPVVIYGGTQTGHSiRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADRMLDMGFGPE 424
Cdd:cd17943    74 IHDVFKKIgKKLEGLKCEVFIGGTPVKED-KKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKD 152
                         170       180
                  ....*....|....*....|....*..
gi 1950452754 425 MKKLIScpGMPSkdRRQTLMFSATFPE 451
Cdd:cd17943   153 VNWIFS--SLPK--NKQVIAFSATYPK 175
HELICc smart00490
helicase superfamily c-terminal domain;
519-600 6.08e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 109.99  E-value: 6.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754  519 DFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 598
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1950452754  599 CG 600
Cdd:smart00490  81 AG 82
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
257-461 4.42e-28

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: 111.65  E-value: 4.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 257 EANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMkdgvtashfREQQEPECIIV 336
Cdd:cd17939     1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRID---------TTVRETQALVL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 337 APTRELINQI---------FLEARKFsygTCIrpvviyGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRY 407
Cdd:cd17939    72 APTRELAQQIqkvvkalgdYMGVKVH---ACI------GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKM 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1950452754 408 LVLDEADRMLDMGFGPEMKKLISCpgMPSKdrRQTLMFSATFPEEIQRLAGEFL 461
Cdd:cd17939   143 FVLDEADEMLSRGFKDQIYDIFQF--LPPE--TQVVLFSATMPHEVLEVTKKFM 192
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
255-461 5.90e-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: 108.71  E-value: 5.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILaHMMKDGVtashfreqQEPECI 334
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQV--------RETQAL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 335 IVAPTRELINQI---FLEARKF---SYGTCIrpvviyGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYL 408
Cdd:cd18045    72 ILSPTRELAVQIqkvLLALGDYmnvQCHACI------GGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKML 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1950452754 409 VLDEADRMLDMGFgpemKKLISCPGMPSKDRRQTLMFSATFPEEIQRLAGEFL 461
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 ...
255-462 2.57e-25

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: 104.06  E-value: 2.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfrEQQEPECI 334
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDT---------SLKATQAL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 335 IVAPTRELINQI---------FLEARKFSygtCIrpvviyGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREV 405
Cdd:cd18046    72 VLAPTRELAQQIqkvvmalgdYMGIKCHA---CI------GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYI 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1950452754 406 RYLVLDEADRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLAGEFLK 462
Cdd:cd18046   143 KMFVLDEADEMLSRGFKDQIYDIFQ--KLPPD--TQVVLLSATMPNDVLEVTTKFMR 195
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
241-457 2.66e-21

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


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 93.16  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 241 VEVSGLDPPP---AILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILAHm 315
Cdd:cd18048     3 VEVLQRDPTSplfSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 316 mkdgVTAshfrEQQEPECIIVAPTRELINQ---IFLEARKFsygtCIRPVVIYG--GTQTGHSIRQIMQgcnILCATPGR 390
Cdd:cd18048    82 ----VDA----LKLYPQCLCLSPTFELALQtgkVVEEMGKF----CVGIQVIYAirGNRPGKGTDIEAQ---IVIGTPGT 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950452754 391 LMDIIGKEK-IGLREVRYLVLDEADRMLDM-GFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLA 457
Cdd:cd18048   147 VLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKR--SMPKE--CQMLLFSATFEDSVWAFA 211
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
289-630 7.70e-21

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 97.02  E-value: 7.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 289 AGRDLMACAQTGSGKTAAFLLpILAHMMKDGVTashfreqqepecIIVAPTRELINQIFLEARKFsygtcirpvviYGGT 368
Cdd:COG1061    99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGKRV------------LVLVPRRELLEQWAEELRRF-----------LGDP 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 369 QTGHSIRQImqGCNILCATPGRLMDIIGKEKIGlREVRYLVLDEADRmldmGFGPEMKKLIScpGMPSKDRrqtLMFSAT 448
Cdd:COG1061   155 LAGGGKKDS--DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILE--AFPAAYR---LGLTAT 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 449 ------FPEEIQRLAG-------------EFLKP-EYLFVAVG-----QVGGACSDVQQTILQVSQYSKREKLVEILQSI 503
Cdd:COG1061   223 pfrsdgREILLFLFDGivyeyslkeaiedGYLAPpEYYGIRVDltderAEYDALSERLREALAADAERKDKILRELLREH 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 504 RD-ERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFDL 582
Cdd:COG1061   303 PDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP 382
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1950452754 583 PSTIDEYVHRIGRTGRCGNIGKAISFFDSVSDSHiaqPLLKVLSDAQQ 630
Cdd:COG1061   383 TGSPREFIQRLGRGLRPAPGKEDALVYDFVGNDV---PVLEELAKDLR 427
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
489-606 1.13e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 96.72  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 489 QYSKREKLVEILQSIR----DERTMVFVETKKKADFIATFLCQEKIPTTSIHG--DRE------QREREEALGDFRSGKC 556
Cdd:COG1111   333 EHPKLSKLREILKEQLgtnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGEF 412
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1950452754 557 PVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNIGKAI 606
Cdd:COG1111   413 NVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
266-460 7.77e-20

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


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 89.36  E-value: 7.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 266 KNIAKAGYLKL------TPVQKYSIPIILAGR----------------DLMACAQTGSGKTAAFLLPILAHMMKDGVTAS 323
Cdd:cd17965    15 IKEILKGSNKTdeeikpSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 324 HFREQQE--------PECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGH--SIRQIMQGCNILCATPGRLMD 393
Cdd:cd17965    95 EEAEEEYesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYqrLQLAFKGRIDILVTTPGKLAS 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1950452754 394 IIGKEKIGLREVRYLVLDEADRMLDMGFGPEMKKLIScPGMPSKDrrqtLMF-SATFPEEIQRLAGEF 460
Cdd:cd17965   175 LAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIK-RAPKLKH----LILcSATIPKEFDKTLRKL 237
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
287-610 6.91e-19

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 90.20  E-value: 6.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 287 ILAGRDLMACAQTGSGKTAAFLLPILahmMKDGVTashfreqqepecIIVAPtreLI----NQI-FLEARKfsygtcIRP 361
Cdd:COG0514    29 VLAGRDALVVMPTGGGKSLCYQLPAL---LLPGLT------------LVVSP---LIalmkDQVdALRAAG------IRA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 362 VVIYGgTQTGHSIRQIMQGCN-----ILCATPGRLM-----DIIGKEKIGLrevryLVLDEA--------DrmldmgFGP 423
Cdd:COG0514    85 AFLNS-SLSAEERREVLRALRagelkLLYVAPERLLnprflELLRRLKISL-----FAIDEAhcisqwghD------FRP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 424 E---MKKLI-SCPGMPskdrrqTLMFSATFPEE-----IQRLAGE--------FLKPEyLFVAVgqvggacsdvqqtiLQ 486
Cdd:COG0514   153 DyrrLGELReRLPNVP------VLALTATATPRvradiAEQLGLEdprvfvgsFDRPN-LRLEV--------------VP 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 487 VSQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSvaA 566
Cdd:COG0514   212 KPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--A 289
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1950452754 567 RGL--DIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 610
Cdd:COG0514   290 FGMgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYG 335
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
490-595 6.26e-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: 6.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 490 YSKREKLVEILQSIRDE----RTMVFVETKKKADFIATFLCQEKIPTTSIHGD---------------REQREREEALGD 550
Cdd:cd18802     6 IPKLQKLIEILREYFPKtpdfRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDK 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1950452754 551 FRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGR 595
Cdd:cd18802    86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
PRK13766 PRK13766
Hef nuclease; Provisional
492-606 5.70e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.76  E-value: 5.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 492 KREKLVEILQSI----RDERTMVFVETKKKADFIATFLCQEKIPTTSIHG--DRE------QREREEALGDFRSGKCPVL 559
Cdd:PRK13766  348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaSKDgdkgmsQKEQIEILDKFRAGEFNVL 427
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1950452754 560 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNIGKAI 606
Cdd:PRK13766  428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
254-457 1.57e-14

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: 72.83  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILAHMmkDGVTashfreqQEP 331
Cdd:cd18047     2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPAN-------KYP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 332 ECIIVAPTRELINQ---IFLEARKFSygtcirPVVIYGGTQTGHSI-RQIMQGCNILCATPGRLMDIIGKEK-IGLREVR 406
Cdd:cd18047    73 QCLCLSPTYELALQtgkVIEQMGKFY------PELKLAYAVRGNKLeRGQKISEQIVIGTPGTVLDWCSKLKfIDPKKIK 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1950452754 407 YLVLDEADRMLDMGfGPEMKKLISCPGMPSKdrRQTLMFSATFPEEIQRLA 457
Cdd:cd18047   147 VFVLDEADVMIATQ-GHQDQSIRIQRMLPRN--CQMLLFSATFEDSVWKFA 194
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
492-598 5.71e-14

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 69.69  E-value: 5.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 492 KREKLVEIL-------QSIRDERTMVFVETKKKADFIATFLCQEKI---PTTSI-HGDRE------QREREEALGDFRSG 554
Cdd:cd18801    10 KLEKLEEIVkehfkkkQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPgirATRFIgQASGKsskgmsQKEQKEVIEQFRKG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1950452754 555 KCPVLVATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGR 598
Cdd:cd18801    90 GYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
257-606 1.01e-13

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: 74.87  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 257 EANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKD-GVTAshfreqqepecII 335
Cdd:COG1205    38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDpGATA-----------LY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 336 VAPTRELIN-QifLEA-RKF--SYGTCIRPVVIYGGTqTGHSIRQIMQGCNILCATPgrlmDII------GKEKIG--LR 403
Cdd:COG1205   107 LYPTKALARdQ--LRRlRELaeALGLGVRVATYDGDT-PPEERRWIREHPDIVLTNP----DMLhygllpHHTRWArfFR 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 404 EVRYLVLDEAD--RmldmG-FGPEMKKLIscpgmpskdRR------------QTLMFSATF--PEEI-QRLAGEflkPey 465
Cdd:COG1205   180 NLRYVVIDEAHtyR----GvFGSHVANVL---------RRlrricrhygsdpQFILASATIgnPAEHaERLTGR---P-- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 466 lFVAVGQVGGACSDVQQTILQVSQYSKREKLVEILQSIR--------DERTMVFVETKKKADFIATFL---CQEKIPTTS 534
Cdd:COG1205   242 -VTVVDEDGSPRGERTFVLWNPPLVDDGIRRSALAEAARlladlvreGLRTLVFTRSRRGAELLARYArraLREPDLADR 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1950452754 535 IHGDR------EQREREEALgdfRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAI 606
Cdd:COG1205   321 VAAYRagylpeERREIERGL---RSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
268-598 4.66e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 72.24  E-value: 4.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 268 IAKAGYLKLTPVQKYSIP-IILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGvtashfreqqepECIIVAPTRELINQI 346
Cdd:COG1204    15 LKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------KALYIVPLRALASEK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 347 FLEARKF--SYGtcIRPVVIYGGTQtghSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEAdRML-DMGFGP 423
Cdd:COG1204    83 YREFKRDfeELG--IKVGVSTGDYD---SDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLIdDESRGP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 424 --EM---KKLISCPGMpskdrrQTLMFSATF--PEEIQR-LAGEFLKPEYlfVAVGQVGGACSDVQQTILQVSQYSKREK 495
Cdd:COG1204   157 tlEVllaRLRRLNPEA------QIVALSATIgnAEEIAEwLDAELVKSDW--RPVPLNEGVLYDGVLRFDDGSRRSKDPT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 496 LVEILQSIRDE-RTMVFVETKKKA-----------------------DFIATFLCQEKIPTTSI--------------HG 537
Cdd:COG1204   229 LALALDLLEEGgQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELLEVSEETHTNekladclekgvafhHA 308
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950452754 538 D--REQREREEALgdFRSGKCPVLVATSVAARGLdieN--VQHVI------NFDLPSTIDEYVHRIGRTGR 598
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 ...
496-609 6.64e-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: 6.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 496 LVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQ 575
Cdd:cd18794    21 LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVR 100
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1950452754 576 HVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 609
Cdd:cd18794   101 FVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
491-594 1.10e-12

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 65.58  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 491 SKREKLVEILQSIRD--ERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSG-KCPV-LVATSVAA 566
Cdd:cd18793    11 GKLEALLELLEELREpgEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGG 90
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1950452754 567 RGLDIENVQHVINFDLP--STIDEY----VHRIG 594
Cdd:cd18793    91 VGLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
476-596 1.37e-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: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 476 ACSDVQQTILQVSQY----SKREKLVEILQSI--RDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALG 549
Cdd:COG0553   514 ICSHPALLLEEGAELsgrsAKLEALLELLEELlaEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVD 593
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1950452754 550 DFRSGK-CPV-LVATSVAARGLdieNVQ---HVINFDLP-------STIDEyVHRIGRT 596
Cdd:COG0553   594 RFQEGPeAPVfLISLKAGGEGL---NLTaadHVIHYDLWwnpaveeQAIDR-AHRIGQT 648
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
272-610 2.04e-10

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 63.96  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 272 GYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmMKDGVTashfreqqepecIIVAPTREL----INQif 347
Cdd:PRK11057   22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL---VLDGLT------------LVVSPLISLmkdqVDQ-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 348 LEARKFSyGTCIrpvviyGGTQTGHSIRQIMQGCN-----ILCATPGRLM--DIIgkEKIGLREVRYLVLDEADRMLDMG 420
Cdd:PRK11057   85 LLANGVA-AACL------NSTQTREQQLEVMAGCRtgqikLLYIAPERLMmdNFL--EHLAHWNPALLAVDEAHCISQWG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 421 --FGPEMKKL----ISCPGMPskdrrqTLMFSATFPE----EIQRL---------AGEFLKPeylfvavgqvggacsDVQ 481
Cdd:PRK11057  156 hdFRPEYAALgqlrQRFPTLP------FMALTATADDttrqDIVRLlglndpliqISSFDRP---------------NIR 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 482 QTIlqVSQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVA 561
Cdd:PRK11057  215 YTL--VEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVA 292
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1950452754 562 TSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 610
Cdd:PRK11057  293 TVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
504-615 1.09e-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: 58.03  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 504 RDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVINFD-- 581
Cdd:cd18790    26 RGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDad 105
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1950452754 582 ----LPSTiDEYVHRIGRTGRCGNiGKAISFFDSVSDS 615
Cdd:cd18790   106 kegfLRSE-TSLIQTIGRAARNVN-GKVILYADKITDS 141
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
276-413 1.13e-09

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 58.04  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 276 LTPVQKYSI-PIILAGRDLMACAQTGSGKTAAFLLPILAHmmkdgvtashfREQQEPECIIVAPTRELINQIFLEARKFS 354
Cdd:cd17921     2 LNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRA-----------LATSGGKAVYIAPTRALVNQKEADLRERF 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 355 YGTCIRPVVIYGGTQTGhsiRQIMQGCNILCATPGRLMDIIGKEKI-GLREVRYLVLDEA 413
Cdd:cd17921    71 GPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
290-448 3.47e-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: 55.87  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 290 GRDLMACAQTGSGKTAAFLLPILAHMmkdgvtashfrEQQEPECIIVAPTRELINQIFLEARKFsYGTCIRPVVIYGGTQ 369
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLL-----------LKKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 370 TGHSIRQIMQGCNILCATPGRL-MDIIGKEKIGLREVRYLVLDEADRMLDMGFGPEMKKLISCPGMPsKDRRQTLMfSAT 448
Cdd:cd00046    69 AEEREKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGL-KNAQVILL-SAT 146
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
280-413 7.60e-09

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 55.67  E-value: 7.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 280 QKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKD-GVTAshfreqqepecIIVAPTRELINQIFLEARKF--SYG 356
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDpGSRA-----------LYLYPTKALAQDQLRSLRELleQLG 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950452754 357 TCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDII----GKEKIGLREVRYLVLDEA 413
Cdd:cd17923    74 LGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
276-597 1.08e-08

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 58.58  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 276 LTPVQKYSIPIILAGRDLMACAQTGSGKT-AAFlLPILAHMMKDGVTASHfreQQEPECIIVAPTRELINQI------FL 348
Cdd:COG1201    25 PTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGEL---PDGLRVLYISPLKALANDIernlraPL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 349 EARKFSYGTCIRPVVIygGTQTG---HSIRQIM--QGCNILCATPGRLMDII----GKEKigLREVRYLVLDEA------ 413
Cdd:COG1201   101 EEIGEAAGLPLPEIRV--GVRTGdtpASERQRQrrRPPHILITTPESLALLLtspdAREL--LRGVRTVIVDEIhalags 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 414 -------------DRMLDMGFgpemkkliscpgmpskdRRQTLmfSATF--PEEIQR-LAGEFLKPEYLFVAVGqvGGAC 477
Cdd:COG1201   177 krgvhlalslerlRALAPRPL-----------------QRIGL--SATVgpLEEVARfLVGYEDPRPVTIVDAG--AGKK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 478 SDVqQTILQVSQYSKR--------EKLVE-ILQSIRDER-TMVFVETKKKADFIATFLCqEKIPTTSI-----HG--DRE 540
Cdd:COG1201   236 PDL-EVLVPVEDLIERfpwaghlwPHLYPrVLDLIEAHRtTLVFTNTRSQAERLFQRLN-ELNPEDALpiaahHGslSRE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1950452754 541 QRER-EEALgdfRSGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTG 597
Cdd:COG1201   314 QRLEvEEAL---KAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
558-610 3.81e-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: 3.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1950452754 558 VLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 610
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
292-600 3.92e-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: 55.92  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 292 DLMACAQTGSGKTAAFLLpILAHMMKdgvtashfrEQQEPECIIVAPTRELINQIFLEARK-FSYGTcirpVVIYGGTQT 370
Cdd:TIGR01587   1 LLVIEAPTGYGKTEAALL-WALHSIK---------SQKADRVIIALPTRATINAMYRRAKElFGSEL----VGLHHSSSF 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 371 -------------------GHSIRQIMQGCNILCaTPGRLMDIIGKE----KIGLREVRY--LVLDEADRMLdmgfgPEM 425
Cdd:TIGR01587  67 srikemgdseefehlfplyIHSNDKLFLDPITVC-TIDQVLKSVFGEfghyEFTLASIANslLIFDEVHFYD-----EYT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 426 KKLISCPGMPSKDRRQTLM-FSATFPEEIQRlagEFLKPEYLFVAVGQV--GGACSDVQQTILQVSQY-SKREKLVEILQ 501
Cdd:TIGR01587 141 LALILAVLEVLKDNDVPILlMSATLPKFLKE---YAEKIGYVEFNEPLDlkEERRFENHRFILIESDKvGEISSLERLLE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 502 SIRDE-RTMVFVETKKKADFIATFLcQEKIPTTSI---HG-----DREQREREEALGDFRSGKCPVLVATSVAARGLDie 572
Cdd:TIGR01587 218 FIKKGgSIAIIVNTVDRAQEFYQQL-KEKAPEEEIilyHSrftekDRAKKEAELLREMKKSNEKFVIVATQVIEASLD-- 294
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1950452754 573 nvqhvINFDL----PSTIDEYVHRIGRTGRCG 600
Cdd:TIGR01587 295 -----ISADVmiteLAPIDSLIQRLGRLHRYG 321
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
275-448 5.10e-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: 53.19  E-value: 5.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 275 KLTPVQKYSIPIILAG------RDLMACAQTGSGKTAAFLLPILAhmmkdgVTASHFReqqepeCIIVAPTRELINQIFL 348
Cdd:cd17918    15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL------AYKNGKQ------VAILVPTEILAHQHYE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 349 EARKFSygTCIRPVVIYGGTQTghsirQIMQGCNILCATPGRLMDIIGKEKIGLrevryLVLDEADRmldmgFGPEMKKL 428
Cdd:cd17918    83 EARKFL--PFINVELVTGGTKA-----QILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHR-----FGVAQREA 145
                         170       180
                  ....*....|....*....|
gi 1950452754 429 ISCPGMPSkdrrqTLMFSAT 448
Cdd:cd17918   146 LYNLGATH-----FLEATAT 160
PRK13767 PRK13767
ATP-dependent helicase; Provisional
273-412 3.24e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 53.74  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 273 YLKLTPVQKYSIPIILAGRDLMACAQTGSGKT-AAFLlpilahmmkdGVTASHFREQQEPE------CIIVAPTRELINQ 345
Cdd:PRK13767   30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL----------AIIDELFRLGREGEledkvyCLYVSPLRALNND 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 346 IF--LE---------ARKFSYG-TCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIG----KEKigLREVRYLV 409
Cdd:PRK13767  100 IHrnLEeplteireiAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLNspkfREK--LRTVKWVI 177

                  ...
gi 1950452754 410 LDE 412
Cdd:PRK13767  178 VDE 180
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
297-595 3.25e-07

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: 53.55  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 297 AQTGSGKTAAFLLPILAHMmkdgvtashfREQQEPECIIVAPTRELINQIFLEARKFSYGTcirpVVIYGGTQTGHSIRQ 376
Cdd:COG1203   154 APTGGGKTEAALLFALRLA----------AKHGGRRIIYALPFTSIINQTYDRLRDLFGED----VLLHHSLADLDLLEE 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 377 IMQGCN---------------ILCATPGRLMD-IIGKEKIglREVRY-------LVLDEADrMLDmgfgPEMKKLIscpg 433
Cdd:COG1203   220 EEEYESearwlkllkelwdapVVVTTIDQLFEsLFSNRKG--QERRLhnlansvIILDEVQ-AYP----PYMLALL---- 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 434 mpskdrRQTLMF-----------SATFPEEIQrlagEFLKPEYLFVavgqvggaCSDVQQTILQVSQYSKR--------- 493
Cdd:COG1203   289 ------LRLLEWlknlggsvilmTATLPPLLR----EELLEAYELI--------PDEPEELPEYFRAFVRKrvelkegpl 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 494 ------EKLVEILQSirDERTMVFVETKKKAdfIATF-LCQEKIPTTSIH--------GDREQRErEEALGDFRSGKCPV 558
Cdd:COG1203   351 sdeelaELILEALHK--GKSVLVIVNTVKDA--QELYeALKEKLPDEEVYllhsrfcpADRSEIE-KEIKERLERGKPCI 425
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1950452754 559 LVATSVAARGLDienvqhvINFDL----PSTIDEYVHRIGR 595
Cdd:COG1203   426 LVSTQVVEAGVD-------IDFDVvirdLAPLDSLIQRAGR 459
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
504-598 6.05e-07

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 49.57  E-value: 6.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 504 RDERTMVFVETKKKADFIAT---FLCQEKIPTTSI---HG--DREQREREEAlgDFRSGKCPVLVATSVAARGLDIENVQ 575
Cdd:cd18796    37 RHKSTLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEVEA--ALKRGDLKVVVATSSLELGIDIGDVD 114
                          90       100
                  ....*....|....*....|...
gi 1950452754 576 HVINFDLPSTIDEYVHRIGRTGR 598
Cdd:cd18796   115 LVIQIGSPKSVARLLQRLGRSGH 137
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
290-412 1.13e-06

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


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 49.12  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 290 GRDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHfreqqepeCIIVAPTRELINQIF--LEArkfsYGTCI---RPVVI 364
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------VLYISPLKALINDQErrLEE----PLDEIdleIPVAV 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1950452754 365 YGGtQTGHSIRQIM--QGCNILCATPGRLMDIIGKEKIG--LREVRYLVLDE 412
Cdd:cd17922    69 RHG-DTSQSEKAKQlkNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
502-595 1.48e-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: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 502 SIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQRERE-EALGDFRSG--KCPVLVATSVAARGLDIENVQHVI 578
Cdd:cd18799     3 KYVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
                          90
                  ....*....|....*....
gi 1950452754 579 nFDLP--STIdEYVHRIGR 595
Cdd:cd18799    83 -FLRPteSRT-LFLQMLGR 99
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
491-612 3.65e-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: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 491 SKREKLVEILQSIRD-ERTMVFVETKKKADFIATFLcqeKIPttSIHGDREQREREEALGDFRSGKCPVLVATSVAARGL 569
Cdd:cd18789    34 NKLRALEELLKRHEQgDKIIVFTDNVEALYRYAKRL---LKP--FITGETPQSEREEILQNFREGEYNTLVVSKVGDEGI 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1950452754 570 DI--ENVQHVINFDLPSTiDEYVHRIGRTGRCGNIGKAISFFDSV 612
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 ...
272-455 2.15e-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: 45.99  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 272 GYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmMKDGVTashfreqqepecIIVAPTRELIN--QIFLE 349
Cdd:cd17920     9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL---LLDGVT------------LVVSPLISLMQdqVDRLQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 350 ARkfsygtCIRPVVIyGGTQTGHSIRQIMQGC-----NILCATPGRLMDIIGKEKIG----LREVRYLVLDEADRMLDMG 420
Cdd:cd17920    74 QL------GIRAAAL-NSTLSPEEKREVLLRIkngqyKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHCVSQWG 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1950452754 421 --FGPEMKKLIS----CPGMPskdrrqTLMFSATFPEEIQR 455
Cdd:cd17920   147 hdFRPDYLRLGRlrraLPGVP------ILALTATATPEVRE 181
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
291-412 7.59e-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: 7.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 291 RDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHfreqqEPECIIVAPTRELINQIFLEAR-KFSyGTCIRPVVIYGGTQ 369
Cdd:cd18023    18 KNFVVSAPTGSGKTVLFELAILRLLKERNPLPWG-----NRKVVYIAPIKALCSEKYDDWKeKFG-PLGLSCAELTGDTE 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1950452754 370 TGhSIRQImQGCNILCATPGR--LMDIIGKEKIGL-REVRYLVLDE 412
Cdd:cd18023    92 MD-DTFEI-QDADIILTTPEKwdSMTRRWRDNGNLvQLVALVLIDE 135
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
291-413 8.62e-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: 44.18  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 291 RDLMACAQTGSGKT--AAFLLPILAHMmkdgvtashFREQQEPECIIV--APTRELINQIFLEARKFSYGTCIrpvVIYG 366
Cdd:cd18034    17 RNTIVVLPTGSGKTliAVMLIKEMGEL---------NRKEKNPKKRAVflVPTVPLVAQQAEAIRSHTDLKVG---EYSG 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1950452754 367 GTQTGHSIRQIMQGC----NILCATPGRLMDIIGKEKIGLREVRYLVLDEA 413
Cdd:cd18034    85 EMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
286-415 9.75e-05

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: 43.66  E-value: 9.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 286 IILAGRDL----MACAQTGSGKTAAFLLPILAHMMKDGvtashfreqqePECIIVAPTRELINQIFLEARKFSygTCIRP 361
Cdd:cd18035     8 VLIAAVALngntLIVLPTGLGKTIIAILVAADRLTKKG-----------GKVLILAPSRPLVEQHAENLKRVL--NIPDK 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1950452754 362 VVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLREVRYLVLDEADR 415
Cdd:cd18035    75 ITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
535-595 2.17e-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: 2.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1950452754 535 IHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIEN-----VQHVINFDLpSTIDEYVHRIGR 595
Cdd:cd18811    67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGL-SQLHQLRGRVGR 131
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
535-574 5.81e-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: 5.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1950452754 535 IHGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENV 574
Cdd:cd18792    66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA 105
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
507-601 1.05e-03

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 39.93  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 507 RTMVFVETKKKADFIATFLCQEKIPT----TSIHGDR-----EQREREEAlgDFRSGKCPVLVATSVAARGLDIENVQHV 577
Cdd:cd18797    37 KTIVFCRSRKLAELLLRYLKARLVEEgplaSKVASYRagylaEDRREIEA--ELFNGELLGVVATNALELGIDIGGLDAV 114
                          90       100
                  ....*....|....*....|....
gi 1950452754 578 INFDLPSTIDEYVHRIGRTGRCGN 601
Cdd:cd18797   115 VLAGYPGSLASLWQQAGRAGRRGK 138
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
296-430 1.43e-03

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


Pssm-ID: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 40.32  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 296 CAQTGSGKTAAFLLPILAhmmkdgvtasHFREQQEPECIIVAPTRELINQIFLE-ARKFSYGTCIRPVVIYGGTQTghSI 374
Cdd:cd18021    25 GAPTGSGKTVCAELALLR----------HWRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLGKKVVKLTGETST--DL 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1950452754 375 RQIMQGcNILCATPGRLmDIIG---KEKIGLREVRYLVLDEAdRMLDMGFGPEMKKLIS 430
Cdd:cd18021    93 KLLAKS-DVILATPEQW-DVLSrrwKQRKNVQSVELFIADEL-HLIGGENGPVYEVVVS 148
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
290-353 1.58e-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: 1.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1950452754 290 GRDLMACAQTGSGKTAAFLLPILahmmkdgvtaSHFREQQEPECIIVAPTRELINQIFLEARKF 353
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 ...
272-412 1.70e-03

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


Pssm-ID: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 40.43  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 272 GYLKLTPVQKYSIPIILAGRD-LMACAQTGSGKTAAFLLPILAHMMKD-----GVTASHFReqqepeCIIVAPTRELINQ 345
Cdd:cd18019    14 GFKSLNRIQSKLFPAAFETDEnLLLCAPTGAGKTNVALLTILREIGKHrnpdgTINLDAFK------IVYIAPMKALVQE 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1950452754 346 IF--LEARKFSYGTCIRPVviyggtqTG-HSI--RQIMQgCNILCATPGRlMDII---GKEKIGLREVRYLVLDE 412
Cdd:cd18019    88 MVgnFSKRLAPYGITVAEL-------TGdQQLtkEQISE-TQIIVTTPEK-WDIItrkSGDRTYTQLVRLIIIDE 153
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
288-415 3.29e-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: 39.34  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 288 LAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashFREQQEPECIIVAPTRELINQiflEARKFSYGTCIRP---VVI 364
Cdd:cd17927    15 LKGKNTIICLPTGSGKTFVAVLICEHHLKK-------FPAGRKGKVVFLANKVPLVEQ---QKEVFRKHFERPGykvTGL 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1950452754 365 YGGTQTGHSIRQIMQGCNILCATPGRLM-DIIGKEKIGLREVRYLVLDEADR 415
Cdd:cd17927    85 SGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
530-600 5.30e-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: 5.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950452754 530 IPTTSI---HGDREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQHVI-----NFDLpSTIDEYVHRIGRTGRCG 600
Cdd:cd18810    49 VPEARIaiaHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGL-AQLYQLRGRVGRSKERA 126
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
467-606 8.68e-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: 37.53  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950452754 467 FVAVGQVGGACSDVQQTILQVSQYskrEKLVEILQSIRDERTMVFVETKKKADFIATFLcqekiptTSI---HGDREQRE 543
Cdd:cd18795     8 YVLGFNGLGIKLRVDVMNKFDSDI---IVLLKIETVSEGKPVLVFCSSRKECEKTAKDL-------AGIafhHAGLTRED 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1950452754 544 REEALGDFRSGKCPVLVATSVAARGLD-------IENVQHVINF---DLPSTidEYVHRIGRTGRCG--NIGKAI 606
Cdd:cd18795    78 RELVEELFREGLIKVLVATSTLAAGVNlpartviIKGTQRYDGKgyrELSPL--EYLQMIGRAGRPGfdTRGEAI 150
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
504-575 9.26e-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: 9.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950452754 504 RDERTMVFVETKKKADFIATFLcQEKIPTTSIHG-DREQREREEALGDFRSGKCPVLVATSVAARGLDIENVQ 575
Cdd:COG4098   318 EGRQLLIFVPTIELLEQLVALL-QKLFPEERIAGvHAEDPERKEKVQAFRDGEIPILVTTTILERGVTFPNVD 389
 
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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