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Conserved domains on  [gi|1040698459|ref|XP_017213195|]
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DEAD-box helicase 3 X-linked a isoform X12 [Danio rerio]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030640)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

EC:  3.6.4.-
PubMed:  20206133
SCOP:  3002019

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
223-477 0e+00

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: 578.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 223 FEKYDDIPVEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVL 302
Cdd:cd18051     1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 303 SQIYSEGPGEALQatkastQENGKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLER 382
Cdd:cd18051    81 SQIYEQGPGESLP------SESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLER 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 383 GCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGSRQTMMFSATFPKEIQILARD 462
Cdd:cd18051   155 GCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARD 234
                         250
                  ....*....|....*
gi 1040698459 463 FLEEYIFLAVGRVGS 477
Cdd:cd18051   235 FLDNYIFLAVGRVGS 249
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
482-612 3.35e-60

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: 198.50  E-value: 3.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 482 ITQKVVWVEENDKRSFLLDLLNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPI 561
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1040698459 562 MVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFY 612
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
223-477 0e+00

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: 578.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 223 FEKYDDIPVEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVL 302
Cdd:cd18051     1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 303 SQIYSEGPGEALQatkastQENGKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLER 382
Cdd:cd18051    81 SQIYEQGPGESLP------SESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLER 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 383 GCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGSRQTMMFSATFPKEIQILARD 462
Cdd:cd18051   155 GCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARD 234
                         250
                  ....*....|....*
gi 1040698459 463 FLEEYIFLAVGRVGS 477
Cdd:cd18051   235 FLDNYIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
244-684 1.23e-168

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 490.81  E-value: 1.23e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 244 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIySEGPGEALQAtkastqe 323
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-DPSRPRAPQA------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 324 ngkyvrrkqypisLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 403
Cdd:COG0513    75 -------------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGAL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 404 GLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENIT 483
Cdd:COG0513   142 DLSGVETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 484 QKVVWVEENDKRSFLLDLLNATGKDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMV 563
Cdd:COG0513   218 QRYYLVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLV 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 564 ATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNITKD---LLDILVEaKQEVPSWLEN 640
Cdd:COG0513   297 ATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAiekLIGQKIE-EEELPGFEPV 375
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1040698459 641 LAYEHQH-KSTNRGRPKRFSGGFGARDYRQMPGGGNTfGNRGARN 684
Cdd:COG0513   376 EEKRLERlKPKIKEKLKGKKAGRGGRPGPKGERKARR-GKRRRRK 419
PTZ00110 PTZ00110
helicase; Provisional
125-675 3.32e-133

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 404.54  E-value: 3.32e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 125 HNAGYGTYENKDGGWNSVVNRDAYASFGGRSDRGKSAFFNDRGASSRGRY---ERGGFGGGTGGNSRWVEESRD---EED 198
Cdd:PTZ00110    1 MRSTDGSSSNGSVSSGPSNNYNSYGPYPDSSNPYGNYQANHQDNYGGFRPgygNYSGGYGGFGMNSYGSSTLGKrlqPID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 199 WSK----PMPPNERLEHELFSASNTginfEKYDDIPVE-----ATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPV 269
Cdd:PTZ00110   81 WKSinlvPFEKNFYKEHPEVSALSS----KEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 270 QKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgealqatkastqengKYVRRKQYPISLVLAPTRELALQI 349
Cdd:PTZ00110  157 QVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQ-----------------PLLRYGDGPIVLVLAPTRELAEQI 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 350 YDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIR 429
Cdd:PTZ00110  220 REQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIR 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 430 RIVEQdtmpPKGSRQTMMFSATFPKEIQILARDFL-EEYIFLAVGRVG-STSENITQKVVWVEENDKRSFLLDLLNATGK 507
Cdd:PTZ00110  300 KIVSQ----IRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMR 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 508 D-SLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLP 586
Cdd:PTZ00110  376 DgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFP 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 587 SDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNITKDLLDILVEAKQEVPSWLENLAYEHqhkSTNRGRPKRFSGGFGARD 666
Cdd:PTZ00110  456 NQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNER---SNGTERRRWGGYGRFSNN 532

                  ....*....
gi 1040698459 667 YRQMPGGGN 675
Cdd:PTZ00110  533 VNNIPLGGS 541
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
482-612 3.35e-60

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: 198.50  E-value: 3.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 482 ITQKVVWVEENDKRSFLLDLLNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPI 561
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1040698459 562 MVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFY 612
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
267-459 8.17e-60

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: 199.01  E-value: 8.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 267 TPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGealqatkastqengkyvrrkqyPISLVLAPTRELA 346
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG----------------------PQALVLAPTRELA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 347 LQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDYCKYLVLDEADRMLDMGFEP 426
Cdd:pfam00270  59 EQIYEELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGP 136
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1040698459 427 QIRRIVEQdtMPPKgsRQTMMFSATFPKEIQIL 459
Cdd:pfam00270 137 DLEEILRR--LPKK--RQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
258-485 1.26e-54

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 186.16  E-value: 1.26e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459  258 ITLSRYTRPTPVQKYAIP-IIKTKRDLMACAQTGSGKTAAFLLPVLsqiysegpgealqatkastqengKYVRRKQYPIS 336
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-----------------------EALKRGKGGRV 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459  337 LVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDYCKYLVLDE 415
Cdd:smart00487  58 LVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDE 137
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459  416 ADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAVGRvgSTSENITQK 485
Cdd:smart00487 138 AHRLLDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
493-603 1.27e-37

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: 135.80  E-value: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 493 DKRSFLLDLLNaTGKDSLTLVFVETKKGADAlEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGL 572
Cdd:pfam00271   1 EKLEALLELLK-KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1040698459 573 DISNVKHVINFDLPSDIEEYVHRIGRTGRVG 603
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
522-603 3.93e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 110.76  E-value: 3.93e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459  522 DALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 601
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1040698459  602 VG 603
Cdd:smart00490  81 AG 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
371-613 3.71e-22

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 100.60  E-value: 3.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 371 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdyckyLVLDEA--------DrmldmgFEP---QIRRIVE 433
Cdd:COG0514    94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 434 QDTMPPkgsrqTMMFSATFPKEIQ--ILARDFLEE-YIFLA-VGRvgstsENITQKVVWVEENDKRSFLLDLLNATGKDS 509
Cdd:COG0514   163 RLPNVP-----VLALTATATPRVRadIAEQLGLEDpRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPGGS 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 510 lTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATaVA-ARGLDISNVKHVINFDLPSD 588
Cdd:COG0514   233 -GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKS 310
                         250       260
                  ....*....|....*....|....*
gi 1040698459 589 IEEYVHRIGRTGRVGNLGLATSFYN 613
Cdd:COG0514   311 IEAYYQEIGRAGRDGLPAEALLLYG 335
PRK13766 PRK13766
Hef nuclease; Provisional
490-601 3.33e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 63.35  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 490 EENDKRSFLLDLLNAT---GKDSLTLVFVETKKGADALEDFLYREGYAC------TSIHGDR--SQRDREEALHQFRSGR 558
Cdd:PRK13766  344 IEHPKLEKLREIVKEQlgkNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGE 423
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1040698459 559 CPIMVATAVAARGLDISNVKHVINFD-LPSDIeEYVHRIGRTGR 601
Cdd:PRK13766  424 FNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR 466
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
446-603 6.18e-03

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: 39.36  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 446 MMFSATFPKEIQILARDFleEYIFLAVGRVGSTSENITQKVVWVEENDKR---SFLLDLLNATGKDSLTLVFVETKKGAD 522
Cdd:TIGR01587 159 LLMSATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILIESDKVgeiSSLERLLEFIKKGGSIAIIVNTVDRAQ 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 523 ALEDFLYREGYACTSI--HGDRSQRDRE----EALHQFRSGRCP-IMVATAVAARGLDISnvkhvinFDL----PSDIEE 591
Cdd:TIGR01587 237 EFYQQLKEKAPEEEIIlyHSRFTEKDRAkkeaELLREMKKSNEKfVIVATQVIEASLDIS-------ADVmiteLAPIDS 309
                         170
                  ....*....|..
gi 1040698459 592 YVHRIGRTGRVG 603
Cdd:TIGR01587 310 LIQRLGRLHRYG 321
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
223-477 0e+00

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: 578.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 223 FEKYDDIPVEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVL 302
Cdd:cd18051     1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 303 SQIYSEGPGEALQatkastQENGKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLER 382
Cdd:cd18051    81 SQIYEQGPGESLP------SESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLER 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 383 GCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGSRQTMMFSATFPKEIQILARD 462
Cdd:cd18051   155 GCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARD 234
                         250
                  ....*....|....*
gi 1040698459 463 FLEEYIFLAVGRVGS 477
Cdd:cd18051   235 FLDNYIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
244-684 1.23e-168

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 490.81  E-value: 1.23e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 244 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIySEGPGEALQAtkastqe 323
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-DPSRPRAPQA------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 324 ngkyvrrkqypisLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 403
Cdd:COG0513    75 -------------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGAL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 404 GLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENIT 483
Cdd:COG0513   142 DLSGVETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 484 QKVVWVEENDKRSFLLDLLNATGKDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMV 563
Cdd:COG0513   218 QRYYLVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLV 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 564 ATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNITKD---LLDILVEaKQEVPSWLEN 640
Cdd:COG0513   297 ATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAiekLIGQKIE-EEELPGFEPV 375
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1040698459 641 LAYEHQH-KSTNRGRPKRFSGGFGARDYRQMPGGGNTfGNRGARN 684
Cdd:COG0513   376 EEKRLERlKPKIKEKLKGKKAGRGGRPGPKGERKARR-GKRRRRK 419
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
244-476 1.07e-156

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: 452.33  E-value: 1.07e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 244 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPgealqatkastqE 323
Cdd:cd17967     1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGP------------P 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 324 NGKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 403
Cdd:cd17967    69 SVGRGRRKAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRI 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040698459 404 GLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGSRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVG 476
Cdd:cd17967   149 SLSSIKFLVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
202-476 1.79e-148

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: 433.24  E-value: 1.79e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 202 PMPPNErlEHELFSASNTGINFEKYDDIPVEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKR 281
Cdd:cd18052     4 PPPPED--EDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 282 DLMACAQTGSGKTAAFLLPVLSQIYSEGpgealqaTKASTQENGkyvrrkQYPISLVLAPTRELALQIYDEARKFAYRSR 361
Cdd:cd18052    82 DLMACAQTGSGKTAAFLLPVLTGMMKEG-------LTASSFSEV------QEPQALIVAPTRELANQIFLEARKFSYGTC 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 362 VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKG 441
Cdd:cd18052   149 IRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKE 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1040698459 442 SRQTMMFSATFPKEIQILARDFL-EEYIFLAVGRVG 476
Cdd:cd18052   229 DRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVGRVG 264
PTZ00110 PTZ00110
helicase; Provisional
125-675 3.32e-133

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 404.54  E-value: 3.32e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 125 HNAGYGTYENKDGGWNSVVNRDAYASFGGRSDRGKSAFFNDRGASSRGRY---ERGGFGGGTGGNSRWVEESRD---EED 198
Cdd:PTZ00110    1 MRSTDGSSSNGSVSSGPSNNYNSYGPYPDSSNPYGNYQANHQDNYGGFRPgygNYSGGYGGFGMNSYGSSTLGKrlqPID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 199 WSK----PMPPNERLEHELFSASNTginfEKYDDIPVE-----ATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPV 269
Cdd:PTZ00110   81 WKSinlvPFEKNFYKEHPEVSALSS----KEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 270 QKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgealqatkastqengKYVRRKQYPISLVLAPTRELALQI 349
Cdd:PTZ00110  157 QVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQ-----------------PLLRYGDGPIVLVLAPTRELAEQI 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 350 YDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIR 429
Cdd:PTZ00110  220 REQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIR 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 430 RIVEQdtmpPKGSRQTMMFSATFPKEIQILARDFL-EEYIFLAVGRVG-STSENITQKVVWVEENDKRSFLLDLLNATGK 507
Cdd:PTZ00110  300 KIVSQ----IRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMR 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 508 D-SLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLP 586
Cdd:PTZ00110  376 DgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFP 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 587 SDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNITKDLLDILVEAKQEVPSWLENLAYEHqhkSTNRGRPKRFSGGFGARD 666
Cdd:PTZ00110  456 NQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNER---SNGTERRRWGGYGRFSNN 532

                  ....*....
gi 1040698459 667 YRQMPGGGN 675
Cdd:PTZ00110  533 VNNIPLGGS 541
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
263-615 1.88e-101

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 319.44  E-value: 1.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQiysegpgeaLQATKASTQengkyvrrkqypiSLVLAPT 342
Cdd:PRK11776   24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK---------LDVKRFRVQ-------------ALVLCPT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 343 RELALQIYDEARKFAyrsRVRP-------CvvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDE 415
Cdd:PRK11776   82 RELADQVAKEIRRLA---RFIPnikvltlC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 416 ADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYifLAVgRVGSTSEN--ITQKVVWVEEND 493
Cdd:PRK11776  156 ADRMLDMGFQDAIDAIIRQ--APAR--RQTLLFSATYPEGIAAISQRFQRDP--VEV-KVESTHDLpaIEQRFYEVSPDE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 494 KRSFLLDLLNATGKDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLD 573
Cdd:PRK11776  229 RLPALQRLLLHHQPES-CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLD 307
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1040698459 574 ISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDK 615
Cdd:PRK11776  308 IKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
263-683 3.04e-93

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 297.88  E-value: 3.04e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPgealqatkastQENGkyvRRkqyPI-SLVLAP 341
Cdd:PRK10590   21 YREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQP-----------HAKG---RR---PVrALILTP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 342 TRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLD 421
Cdd:PRK10590   84 TRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 422 MGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENITQKVVWVEENDKRSfLLDL 501
Cdd:PRK10590  164 MGFIHDIRRVLAK--LPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRE-LLSQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 502 LNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVI 581
Cdd:PRK10590  239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 582 NFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNITKDLLDILveaKQEVPSwLENLAYEH----QHKSTNRGRPKR 657
Cdd:PRK10590  319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL---KKEIPR-IAIPGYEPdpsiKAEPIQNGRQQR 394
                         410       420
                  ....*....|....*....|....*.
gi 1040698459 658 FSGGFGARDYRQMPGGGNTFGNRGAR 683
Cdd:PRK10590  395 GGGGRGQGGGRGQQQGQPRRGEGGAK 420
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
229-657 4.59e-92

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 296.70  E-value: 4.59e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 229 IPVEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLS---QI 305
Cdd:PLN00206  107 LEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTI 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 306 YSEGPGEalqatkastqengkyvRRKqyPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCH 385
Cdd:PLN00206  187 RSGHPSE----------------QRN--PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVE 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 386 LLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPpkgsrQTMMFSATFPKEIQILARDFLE 465
Cdd:PLN00206  249 LIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAK 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 466 EYIFLAVGRVGSTSENITQKVVWVEENDKRSFLLDLLnaTGKDSLT---LVFVETKKGADALEDFLYR-EGYACTSIHGD 541
Cdd:PLN00206  324 DIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDIL--KSKQHFKppaVVFVSSRLGADLLANAITVvTGLKALSIHGE 401
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 542 RSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNITK 621
Cdd:PLN00206  402 KSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFP 481
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1040698459 622 DLLDILVEAKQEVPSWLENLAYEHQHKSTNRGRPKR 657
Cdd:PLN00206  482 ELVALLKSSGAAIPRELANSRYLGSGRKRKKKRRYG 517
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
254-470 6.11e-92

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: 284.72  E-value: 6.11e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 254 IMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPgealqatkastqengkyvRRKQY 333
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK------------------KKGRG 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 334 PISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVL 413
Cdd:cd00268    63 PQALVLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVL 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1040698459 414 DEADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFL 470
Cdd:cd00268   143 DEADRMLDMGFEEDVEKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
245-617 5.56e-90

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 289.89  E-value: 5.56e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 245 FHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGEAlqatkastqen 324
Cdd:PRK01297   89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKE----------- 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 325 gkyvRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLE-RGCHLLVATPGRLVDMMERGKI 403
Cdd:PRK01297  158 ----RYMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEV 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 404 GLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmPPKGSRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENIT 483
Cdd:PRK01297  234 HLDMVEVMVLDEADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVE 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 484 QKVVWVEENDKRSFLLDLLNATGKDSLtLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMV 563
Cdd:PRK01297  312 QHVYAVAGSDKYKLLYNLVTQNPWERV-MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLV 390
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1040698459 564 ATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNS 617
Cdd:PRK01297  391 ATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDA 444
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
254-470 3.71e-84

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: 264.62  E-value: 3.71e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 254 IMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkaSTQEngkYVRRKQY 333
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI--------------NAQP---PLERGDG 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 334 PISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVL 413
Cdd:cd17966    64 PIVLVLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVL 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1040698459 414 DEADRMLDMGFEPQIRRIVEQdTMPpkgSRQTMMFSATFPKEIQILARDFLEEYIFL 470
Cdd:cd17966   144 DEADRMLDMGFEPQIRKIVDQ-IRP---DRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
244-636 2.82e-82

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 272.59  E-value: 2.82e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 244 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgPGEAlqatkastqe 323
Cdd:PRK04537   10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSR-PALA---------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 324 ngkyVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 403
Cdd:PRK04537   79 ----DRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 404 -GLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGSRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENI 482
Cdd:PRK04537  155 vSLHACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 483 TQKVVWVEENDKRSFLLDLLNATgKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIM 562
Cdd:PRK04537  233 RQRIYFPADEEKQTLLLGLLSRS-EGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEIL 311
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040698459 563 VATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSnitKDLLDILVEAKQEVPS 636
Cdd:PRK04537  312 VATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYA---MSLPDIEAYIEQKIPV 382
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
263-611 1.61e-80

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 263.34  E-value: 1.61e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSegpgealqatkastqengkYVRRKQYPIS-LVLAP 341
Cdd:PRK11192   21 YTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLD-------------------FPRRKSGPPRiLILTP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 342 TRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLD 421
Cdd:PRK11192   82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 422 MGFEPQIRRIVEQdtmpPKGSRQTMMFSATFPKE-IQILARDFLEEYIFLAVGrvGSTSE--NITQkvvWVEEND----K 494
Cdd:PRK11192  162 MGFAQDIETIAAE----TRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAE--PSRRErkKIHQ---WYYRADdlehK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 495 RSFLLDLLNATGKDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDI 574
Cdd:PRK11192  233 TALLCHLLKQPEVTR-SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDI 311
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1040698459 575 SNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSF 611
Cdd:PRK11192  312 DDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
267-611 8.06e-76

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 250.66  E-value: 8.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 267 TPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGEAlqatkastqengkyvRRKQYPISLVLAPTRELA 346
Cdd:PRK04837   32 TPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPED---------------RKVNQPRALIMAPTRELA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 347 LQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEP 426
Cdd:PRK04837   97 VQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIK 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 427 QIRRIVEQdtMPPKGSRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENITQKVVWVEENDKRSFLLDLLNATG 506
Cdd:PRK04837  177 DIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEW 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 507 KDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLP 586
Cdd:PRK04837  255 PDR-AIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLP 333
                         330       340
                  ....*....|....*....|....*
gi 1040698459 587 SDIEEYVHRIGRTGRVGNLGLATSF 611
Cdd:PRK04837  334 DDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
231-473 1.34e-70

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: 230.28  E-value: 1.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 231 VEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgp 310
Cdd:cd18049    12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQ-- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 311 gealqatkastqengKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVAT 390
Cdd:cd18049    90 ---------------PFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIAT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 391 PGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtmpPKGSRQTMMFSATFPKEIQILARDFLEEYIFL 470
Cdd:cd18049   155 PGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230

                  ...
gi 1040698459 471 AVG 473
Cdd:cd18049   231 NIG 233
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
244-615 2.53e-69

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 238.98  E-value: 2.53e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 244 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgeaLQAtkastqe 323
Cdd:PRK11634    7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE-----LKA------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 324 ngkyvrrkqyPISLVLAPTRELALQIYDEARKFAYRSR-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK 402
Cdd:PRK11634   75 ----------PQILVLAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGT 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 403 IGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPpkGSRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENI 482
Cdd:PRK11634  145 LDLSKLSGLVLDEADEMLRMGFIEDVETIMAQ--IP--EGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDI 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 483 TQKVVWVEENDKRSFLLDLLNATGKDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIM 562
Cdd:PRK11634  221 SQSYWTVWGMRKNEALVRFLEAEDFDA-AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDIL 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1040698459 563 VATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDK 615
Cdd:PRK11634  300 IATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENR 352
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
235-473 3.26e-69

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: 227.97  E-value: 3.26e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 235 GTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgeal 314
Cdd:cd18050    54 GVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQ------ 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 315 qatkastqengKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRL 394
Cdd:cd18050   128 -----------PYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRL 196
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040698459 395 VDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtmpPKGSRQTMMFSATFPKEIQILARDFLEEYIFLAVG 473
Cdd:cd18050   197 IDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
233-464 7.32e-69

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: 225.33  E-value: 7.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 233 ATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpge 312
Cdd:cd17953     2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 313 alQATKASTQENGkyvrrkqyPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPG 392
Cdd:cd17953    75 --KDQRPVKPGEG--------PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPG 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040698459 393 RLVDM--MERGKI-GLDYCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPkgSRQTMMFSATFPKEIQILARDFL 464
Cdd:cd17953   145 RMIDIltANNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIV--NNIRP--DRQTVLFSATFPRKVEALARKVL 215
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
254-468 2.74e-68

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: 222.68  E-value: 2.74e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 254 IMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgealqatkastqengKYVRRKQY 333
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ-----------------RELEKGEG 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 334 PISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVL 413
Cdd:cd17952    64 PIAVIVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVL 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1040698459 414 DEADRMLDMGFEPQIRRIVEQdTMPpkgSRQTMMFSATFPKEIQILARDFLEEYI 468
Cdd:cd17952   144 DEADRMFDMGFEYQVRSIVGH-VRP---DRQTLLFSATFKKKIEQLARDILSDPI 194
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
262-464 1.31e-64

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: 213.72  E-value: 1.31e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 262 RYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSegpgeaLQATKASTQENGkyvrrkqyPISLVLAP 341
Cdd:cd17945     9 GYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISR------LPPLDEETKDDG--------PYALILAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 342 TRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLD 421
Cdd:cd17945    75 TRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMID 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040698459 422 MGFEPQIRRIVeqDTMPP------------------KGSRQTMMFSATFPKEIQILARDFL 464
Cdd:cd17945   155 MGFEPQVTKIL--DAMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYL 213
PTZ00424 PTZ00424
helicase 45; Provisional
203-623 5.00e-64

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 218.54  E-value: 5.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 203 MPPNERLEHELFSASNTGINfEKYDDIpveatgtnspghIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRD 282
Cdd:PTZ00424    1 MATSEQKNQSEQVASTGTIE-SNYDEI------------VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 283 LMACAQTGSGKTAAFLLPVLSQI-YSegpgeaLQATKAstqengkyvrrkqypisLVLAPTRELALQIYDEARKFAYRSR 361
Cdd:PTZ00424   68 TIGQAQSGTGKTATFVIAALQLIdYD------LNACQA-----------------LILAPTRELAQQIQKVVLALGDYLK 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 362 VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkg 441
Cdd:PTZ00424  125 VRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKK--LPP-- 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 442 SRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENITQKVVWVEEND-KRSFLLDLLnatgkDSLTLV----FVE 516
Cdd:PTZ00424  201 DVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEwKFDTLCDLY-----ETLTITqaiiYCN 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 517 TKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRI 596
Cdd:PTZ00424  276 TRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRI 355
                         410       420
                  ....*....|....*....|....*..
gi 1040698459 597 GRTGRVGNLGLATSFYNDKNSNITKDL 623
Cdd:PTZ00424  356 GRSGRFGRKGVAINFVTPDDIEQLKEI 382
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
482-612 3.35e-60

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: 198.50  E-value: 3.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 482 ITQKVVWVEENDKRSFLLDLLNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPI 561
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1040698459 562 MVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFY 612
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
267-459 8.17e-60

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: 199.01  E-value: 8.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 267 TPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGealqatkastqengkyvrrkqyPISLVLAPTRELA 346
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG----------------------PQALVLAPTRELA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 347 LQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDYCKYLVLDEADRMLDMGFEP 426
Cdd:pfam00270  59 EQIYEELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGP 136
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1040698459 427 QIRRIVEQdtMPPKgsRQTMMFSATFPKEIQIL 459
Cdd:pfam00270 137 DLEEILRR--LPKK--RQILLLSATLPRNLEDL 165
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
258-461 2.89e-59

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: 198.96  E-value: 2.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 258 ITLSRYTRPTPVQKYAI-PIIKTKRDLMACAQTGSGKTAAFLLPVLsqiysegpgEALQATKAstqengkyvRRKQYPIS 336
Cdd:cd17964     9 LTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAI---------QSLLNTKP---------AGRRSGVS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 337 -LVLAPTRELALQIYDEARKFAYRSR-VRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMME--RGKIGLDYCKYL 411
Cdd:cd17964    71 aLIISPTRELALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1040698459 412 VLDEADRMLDMGFEPQIRRIVeqDTMPPKGS--RQTMMFSATFPKEIQILAR 461
Cdd:cd17964   151 VLDEADRLLDMGFRPDLEQIL--RHLPEKNAdpRQTLLFSATVPDEVQQIAR 200
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
263-461 8.86e-58

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: 194.40  E-value: 8.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLsqiysegpgEALQATKastqengkyvRRKQYPISLVLAPT 342
Cdd:cd17947    10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPIL---------ERLLYRP----------KKKAATRVLVLVPT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 343 RELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDYCKYLVLDEADRMLD 421
Cdd:cd17947    71 RELAMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLE 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1040698459 422 MGFEPQIRRIVEqdtMPPKgSRQTMMFSATFPKEIQILAR 461
Cdd:cd17947   151 EGFADELKEILR---LCPR-TRQTMLFSATMTDEVKDLAK 186
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
254-466 4.74e-56

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: 189.98  E-value: 4.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 254 IMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgeaLQATKASTQENGkyvrrkqy 333
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL--------DLQPIPREQRNG-------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 334 PISLVLAPTRELALQIYDEARKFAYRSRVRPCVvYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVL 413
Cdd:cd17958    65 PGVLVLTPTRELALQIEAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVL 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1040698459 414 DEADRMLDMGFEPQIRRIVeQDTMPpkgSRQTMMFSATFPKEIQILARDFLEE 466
Cdd:cd17958   144 DEADRMLDMGFEPQIRKIL-LDIRP---DRQTIMTSATWPDGVRRLAQSYLKD 192
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
265-464 1.19e-55

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: 189.09  E-value: 1.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 265 RPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQiysegpgeALQatkastQENGKYVRRKQYPISLVLAPTRE 344
Cdd:cd17951    12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMF--------ALE------QEKKLPFIKGEGPYGLIVCPSRE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 345 LALQIYDEARKFAYR------SRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADR 418
Cdd:cd17951    78 LARQTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADR 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1040698459 419 MLDMGFEPQIRRIVEQDtmppKGSRQTMMFSATFPKEIQILARDFL 464
Cdd:cd17951   158 MIDMGFEEDIRTIFSYF----KGQRQTLLFSATMPKKIQNFAKSAL 199
DEXDc smart00487
DEAD-like helicases superfamily;
258-485 1.26e-54

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 186.16  E-value: 1.26e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459  258 ITLSRYTRPTPVQKYAIP-IIKTKRDLMACAQTGSGKTAAFLLPVLsqiysegpgealqatkastqengKYVRRKQYPIS 336
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-----------------------EALKRGKGGRV 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459  337 LVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDYCKYLVLDE 415
Cdd:smart00487  58 LVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDE 137
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459  416 ADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAVGRvgSTSENITQK 485
Cdd:smart00487 138 AHRLLDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
254-473 1.68e-53

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: 183.17  E-value: 1.68e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 254 IMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYsegpgealqatkasTQENGKYVRrkqy 333
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLG--------------KPRKKKGLR---- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 334 piSLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGG-ADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLV 412
Cdd:cd17957    63 --ALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLV 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040698459 413 LDEADRMLDMGFEPQIRRIVEQDTMPPKgsrQTMMFSATFPKEIQILARDFLEEYIFLAVG 473
Cdd:cd17957   141 LDEADKLFEPGFREQTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
263-469 5.41e-52

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 179.34  E-value: 5.41e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLsQIYSEGPgealqatkastqengkyvrrkqYPI-SLVLAP 341
Cdd:cd17955    19 IKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-QRLSEDP----------------------YGIfALVLTP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 342 TRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMME---RGKIGLDYCKYLVLDEADR 418
Cdd:cd17955    76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1040698459 419 MLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIF 469
Cdd:cd17955   156 LLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
259-470 1.14e-50

DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 175.85  E-value: 1.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 259 TLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastQENGKYVRRKQYPISLV 338
Cdd:cd17949     7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL----------------LSLEPRVDRSDGTLALV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 339 LAPTRELALQIYDEARKFAYRSR-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDYCKYLVLDEA 416
Cdd:cd17949    71 LVPTRELALQIYEVLEKLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEA 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040698459 417 DRMLDMGFEPQIRRIVE---------QDTMPPKGSRQTMMFSATFPKEIQILARDFLEEYIFL 470
Cdd:cd17949   151 DRLLDMGFEKDITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
245-468 4.54e-50

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: 173.64  E-value: 4.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 245 FHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGeaLQAtkastqen 324
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV--IQA-------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 325 gkyvrrkqypisLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIG 404
Cdd:cd17940    71 ------------LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVAD 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040698459 405 LDYCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPKgsRQTMMFSATFPKEIQilarDFLEEYI 468
Cdd:cd17940   139 LSHCKTLVLDEADKLLSQDFQPIIEKIL--NFLPKE--RQILLFSATFPLTVK----NFMDRHM 194
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
263-461 1.13e-49

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 172.89  E-value: 1.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastqengkyVRRKQYPISLVLAPT 342
Cdd:cd17954    20 WKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL----------------------LENPQRFFALVLAPT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 343 RELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDYCKYLVLDEADRMLD 421
Cdd:cd17954    78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLN 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1040698459 422 MGFEPQIRRIVEqdTMPPKgsRQTMMFSATFPKEIQILAR 461
Cdd:cd17954   158 MDFEPEIDKILK--VIPRE--RTTYLFSATMTTKVAKLQR 193
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
244-470 2.84e-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: 169.02  E-value: 2.84e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 244 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatKASTQE 323
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL------------KAHSPT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 324 NGkyVRrkqypiSLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 403
Cdd:cd17959    70 VG--AR------ALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNL 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040698459 404 GLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgSRQTMMFSATFPKEIQILARDFLEEYIFL 470
Cdd:cd17959   142 KLSSVEYVVFDEADRLFEMGFAEQLHEILSR--LPE--NRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
263-464 1.70e-46

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: 163.90  E-value: 1.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYsegpgealqatKASTQENGKYVRrkqypiSLVLAPT 342
Cdd:cd17960    10 FTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILL-----------KRKANLKKGQVG------ALIISPT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 343 RELALQIYDEARKFA--YRSRVRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMMERGKIGLDY--CKYLVLDEAD 417
Cdd:cd17960    73 RELATQIYEVLQSFLehHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKVksLEVLVLDEAD 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1040698459 418 RMLDMGFEPQIRRIVEQdtmPPKgSRQTMMFSATFPKEIQILARDFL 464
Cdd:cd17960   153 RLLDLGFEADLNRILSK---LPK-QRRTGLFSATQTDAVEELIKAGL 195
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
261-472 6.40e-46

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: 162.46  E-value: 6.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 261 SRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSE--GPGEALQAtkastqengkyvrrkqypisLV 338
Cdd:cd17941     8 AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRErwTPEDGLGA--------------------LI 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 339 LAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQirdLER--GCHLLVATPGRLVDMMERgKIGLDY--CKYLVLD 414
Cdd:cd17941    68 ISPTRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE---KERinRMNILVCTPGRLLQHMDE-TPGFDTsnLQMLVLD 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1040698459 415 EADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAV 472
Cdd:cd17941   144 EADRILDMGFKETLDAIVEN--LPKS--RQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
250-451 3.97e-44

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 157.48  E-value: 3.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 250 MGEIIMGnITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLsQIYSegpgealqatkastqengkyvr 329
Cdd:cd17938     7 MPELIKA-VEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QIVV---------------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 330 rkqypiSLVLAPTRELALQIYDEARKFAY---RSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 406
Cdd:cd17938    63 ------ALILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLS 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1040698459 407 YCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGSR----QTMMFSAT 451
Cdd:cd17938   137 SVRFFVLDEADRLLSQGNLETINRIYNR--IPKITSDgkrlQVIVCSAT 183
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
257-468 9.20e-44

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: 156.17  E-value: 9.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 257 NITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgealqatkastqengkyvrrKQYPIS 336
Cdd:cd17962     4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTE----------------------HRNPSA 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 337 LVLAPTRELALQIYDEARKFAY-RSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDE 415
Cdd:cd17962    62 LILTPTRELAVQIEDQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDE 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1040698459 416 ADRMLDMGFEPQIRRIVEQDTMPPkgsrQTMMFSATFPKEIQILARDFLEEYI 468
Cdd:cd17962   142 ADTMLKMGFQQQVLDILENISHDH----QTILVSATIPRGIEQLAGQLLQNPV 190
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
262-457 2.12e-41

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: 150.85  E-value: 2.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 262 RYTRPTPVQKYAIP-IIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgealqatkasTQENGKYVRRKqYPISLVLA 340
Cdd:cd17946     9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQ------------KSSNGVGGKQK-PLRALILT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 341 PTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL---DYCKYLVLDEAD 417
Cdd:cd17946    76 PTRELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLanlKSLRFLVLDEAD 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1040698459 418 RMLDMG-FEP--QIRRIVEQDTMPPKGSRQTMMFSATFPKEIQ 457
Cdd:cd17946   156 RMLEKGhFAEleKILELLNKDRAGKKRKRQTFVFSATLTLDHQ 198
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
263-461 9.35e-41

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: 147.89  E-value: 9.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGpgealqatkaSTQENGKYVrrkqypisLVLAPT 342
Cdd:cd17942    10 FTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLK----------FKPRNGTGV--------IIISPT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 343 RELALQIYDEARKF-AYRSRVRPCVVyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKiGLDY--CKYLVLDEADRM 419
Cdd:cd17942    72 RELALQIYGVAKELlKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTK-GFLYknLQCLIIDEADRI 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1040698459 420 LDMGFEPQIRRIVEqdtMPPKgSRQTMMFSATFPKEIQILAR 461
Cdd:cd17942   150 LEIGFEEEMRQIIK---LLPK-RRQTMLFSATQTRKVEDLAR 187
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
263-468 1.09e-39

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: 144.64  E-value: 1.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAIPII--KTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastqengkyVRRKQYPISLVLA 340
Cdd:cd17963    14 FNKPSKIQETALPLIlsDPPENLIAQSQSGTGKTAAFVLAMLSRV----------------------DPTLKSPQALCLA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 341 PTRELALQIYDEARKFA------YRSRVRPCVVYGGADIGQQIrdlergchlLVATPGRLVDMMERGKIGLDYCKYLVLD 414
Cdd:cd17963    72 PTRELARQIGEVVEKMGkftgvkVALAVPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQLDLKKIKILVLD 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1040698459 415 EADRMLDM-GFEPQIRRIveQDTMPPkgSRQTMMFSATFPKEIqilaRDFLEEYI 468
Cdd:cd17963   143 EADVMLDTqGHGDQSIRI--KRMLPR--NCQILLFSATFPDSV----RKFAEKIA 189
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
263-464 1.82e-39

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: 144.39  E-value: 1.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAI-PIIKtKRDLMACAQTGSGKTAAFLLPVLSQIYSegpgealqaTKASTQengkyvrrkqypiSLVLAP 341
Cdd:cd17939    17 FEKPSAIQQRAIvPIIK-GRDVIAQAQSGTGKTATFSIGALQRIDT---------TVRETQ-------------ALVLAP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 342 TRELALQIYD--EARKFAYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRM 419
Cdd:cd17939    74 TRELAQQIQKvvKALGDYMGVKVHACI--GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEM 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1040698459 420 LDMGFEPQIRRIVEQdtMPPKGsrQTMMFSATFPKEIQILARDFL 464
Cdd:cd17939   152 LSRGFKDQIYDIFQF--LPPET--QVVLFSATMPHEVLEVTKKFM 192
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
493-603 1.27e-37

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: 135.80  E-value: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 493 DKRSFLLDLLNaTGKDSLTLVFVETKKGADAlEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGL 572
Cdd:pfam00271   1 EKLEALLELLK-KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1040698459 573 DISNVKHVINFDLPSDIEEYVHRIGRTGRVG 603
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
263-464 6.51e-37

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: 137.33  E-value: 6.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgeaLQATKAStqengkyvRRKQYPISLVLAPT 342
Cdd:cd17961    14 WEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKI--------LKAKAES--------GEEQGTRALILVPT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 343 RELALQIYDEARKFAY--RSRVRpCV-VYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL-DYCKYLVLDEADR 418
Cdd:cd17961    78 RELAQQVSKVLEQLTAycRKDVR-VVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1040698459 419 MLDMGFEPQIRRIVEqdtMPPKGSrQTMMFSATFPKEIQILARDFL 464
Cdd:cd17961   157 VLSYGYEEDLKSLLS---YLPKNY-QTFLMSATLSEDVEALKKLVL 198
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
245-468 8.32e-37

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: 136.81  E-value: 8.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 245 FHDVDMGEIIMGNITLSRYTRPTPVQKYAI-PIIKtKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgeaLQATKAstqe 323
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAImPCIK-GYDVIAQAQSGTGKTATFSISILQQIDTS-----LKATQA---- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 324 ngkyvrrkqypisLVLAPTRELALQIYD--EARKFAYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERG 401
Cdd:cd18046    71 -------------LVLAPTRELAQQIQKvvMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRR 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040698459 402 KIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgSRQTMMFSATFPKEIQILARDFLEEYI 468
Cdd:cd18046   136 YLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQK--LPP--DTQVVLLSATMPNDVLEVTTKFMRDPI 198
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
244-464 1.09e-35

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


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 134.01  E-value: 1.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 244 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgPGEalqatkastqe 323
Cdd:cd17950     3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPV-DGQ----------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 324 ngkyvrrkqypIS-LVLAPTRELALQIYDEARKFA-YRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMER 400
Cdd:cd17950    71 -----------VSvLVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVRE 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040698459 401 GKIGLDYCKYLVLDEADRM---LDMgfepqiRRIVeQD--TMPPKgSRQTMMFSATFPKEIQILARDFL 464
Cdd:cd17950   140 KKLKLSHVKHFVLDECDKMleqLDM------RRDV-QEifRATPH-DKQVMMFSATLSKEIRPVCKKFM 200
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
263-469 2.57e-35

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: 132.39  E-value: 2.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLsqiysegpgEALQATKASTQengkyvrrkqypiSLVLAPT 342
Cdd:cd17943    10 FQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL---------ESLDLERRHPQ-------------VLILAPT 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 343 RELALQIYDEARKFA-YRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLD 421
Cdd:cd17943    68 REIAVQIHDVFKKIGkKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLME 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1040698459 422 MGFEPQIRRIveqDTMPPKgSRQTMMFSATFPKE-IQILARdFLEEYIF 469
Cdd:cd17943   147 GSFQKDVNWI---FSSLPK-NKQVIAFSATYPKNlDNLLAR-YMRKPVL 190
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
263-466 8.54e-32

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: 122.58  E-value: 8.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 263 YTRPTPVQKYAI-PIIKTkRDLMACAQTGSGKTAAFLLPVLSqiysegpgeALQATKASTQengkyvrrkqypiSLVLAP 341
Cdd:cd18045    19 FEKPSAIQQRAIkPIIKG-RDVIAQSQSGTGKTATFSISVLQ---------CLDIQVRETQ-------------ALILSP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 342 TRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLD 421
Cdd:cd18045    76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1040698459 422 MGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEE 466
Cdd:cd18045   156 KGFKEQIYDVYRY--LPPA--TQVVLVSATLPQDILEMTNKFMTD 196
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
268-464 2.70e-31

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: 121.11  E-value: 2.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 268 PVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastQENGKYVRRKQYPISLVLAPTRELAL 347
Cdd:cd17944    15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKL----------------QEDQQPRKRGRAPKVLVLAPTRELAN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 348 QIYDEARKFAYRSRVrpCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQ 427
Cdd:cd17944    79 QVTKDFKDITRKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQ 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1040698459 428 IRRIV-EQDTMPPKGSRQTMMFSATFPKEIQILARDFL 464
Cdd:cd17944   157 VEEILsVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
259-461 3.34e-29

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 116.31  E-value: 3.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 259 TLSRY--TRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQI--YSEGPGEALQAtkastqengkyvrrkqyP 334
Cdd:cd17948     4 ILQRQgiTKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAEGPFNA-----------------P 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 335 ISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIgQQIRDLERG-CHLLVATPGRLVDMMERGKIGLDYCKYLVL 413
Cdd:cd17948    67 RGLVITPSRELAEQIGSVAQSLTEGLGLKVKVITGGRTK-RQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVL 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 414 DEADRMLDMGFEPQIRRIVEQ-----------DTMPPKGsrQTMMFSATFPKEI-QILAR 461
Cdd:cd17948   146 DEADTLLDDSFNEKLSHFLRRfplasrrsentDGLDPGT--QLVLVSATMPSGVgEVLSK 203
HELICc smart00490
helicase superfamily c-terminal domain;
522-603 3.93e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 110.76  E-value: 3.93e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459  522 DALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 601
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1040698459  602 VG 603
Cdd:smart00490  81 AG 82
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
254-461 3.08e-27

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: 110.41  E-value: 3.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 254 IMGNITLSRYTRPTPVQKYAIP-IIKT--------KRDLMACAQTGSGKTAAFLLPVLsQIYSEGPGEALQAtkastqen 324
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPwLLPSskstppyrPGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVPRLRA-------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 325 gkyvrrkqypisLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHL--------LVATPGRLVD 396
Cdd:cd17956    72 ------------LIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGrylsrvdiLVATPGRLVD 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 397 MMERGK-IGLDYCKYLVLDEADRMLDMGFE---PQIRRIVEQDTMPPKGSR-------------QTMMFSATFPKEIQIL 459
Cdd:cd17956   140 HLNSTPgFTLKHLRFLVIDEADRLLNQSFQdwlETVMKALGRPTAPDLGSFgdanllersvrplQKLLFSATLTRDPEKL 219

                  ..
gi 1040698459 460 AR 461
Cdd:cd17956   220 SS 221
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
250-463 2.99e-22

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: 96.68  E-value: 2.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 250 MGEIIMGNITLSRYTRPTPVQKYAIPII-----------------KTKRDLMAcAQTGSGKTAAFLLPVLSQIYSEgpgE 312
Cdd:cd17965    15 IKEILKGSNKTDEEIKPSPIQTLAIKKLlktlmrkvtkqtsneepKLEVFLLA-AETGSGKTLAYLAPLLDYLKRQ---E 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 313 ALQATKASTQENGKyvRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVV-YGGADIGQQIRDLERG-CHLLVAT 390
Cdd:cd17965    91 QEPFEEAEEEYESA--KDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLAFKGrIDILVTT 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040698459 391 PGRLVDMME-RGKIgLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgSRQTMMFSATFPKEIQILARDF 463
Cdd:cd17965   169 PGKLASLAKsRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APK--LKHLILCSATIPKEFDKTLRKL 237
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
371-613 3.71e-22

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 100.60  E-value: 3.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 371 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdyckyLVLDEA--------DrmldmgFEP---QIRRIVE 433
Cdd:COG0514    94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 434 QDTMPPkgsrqTMMFSATFPKEIQ--ILARDFLEE-YIFLA-VGRvgstsENITQKVVWVEENDKRSFLLDLLNATGKDS 509
Cdd:COG0514   163 RLPNVP-----VLALTATATPRVRadIAEQLGLEDpRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPGGS 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 510 lTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATaVA-ARGLDISNVKHVINFDLPSD 588
Cdd:COG0514   233 -GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKS 310
                         250       260
                  ....*....|....*....|....*
gi 1040698459 589 IEEYVHRIGRTGRVGNLGLATSFYN 613
Cdd:COG0514   311 IEAYYQEIGRAGRDGLPAEALLLYG 335
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
269-598 9.15e-21

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 96.63  E-value: 9.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 269 VQKYAIPIIKTKRDLMACAQTGSGKT--AAFLLpvlsqiysegpGEALQATKAstqengkyvrrkqypisLVLAPTRELA 346
Cdd:COG1061    89 LEALLAALERGGGRGLVVAPTGTGKTvlALALA-----------AELLRGKRV-----------------LVLVPRRELL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 347 LQIYDEARKFayrsrvrpcvvYGGADIGQQIRDleRGCHLLVATPGRLVDMMERGKIGlDYCKYLVLDEADRmldmGFEP 426
Cdd:COG1061   141 EQWAEELRRF-----------LGDPLAGGGKKD--SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 427 QIRRIVEQdtMPPKgsrQTMMFSAT------FPKEI-------------QILARDFLEEYIFLAV--------GRVGSTS 479
Cdd:COG1061   203 SYRRILEA--FPAA---YRLGLTATpfrsdgREILLflfdgivyeyslkEAIEDGYLAPPEYYGIrvdltderAEYDALS 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 480 ENITQKVVWVEENdKRSFLLDLLNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRC 559
Cdd:COG1061   278 ERLREALAADAER-KDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGEL 356
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1040698459 560 PIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGR 598
Cdd:COG1061   357 RILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
242-452 1.43e-18

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: 85.46  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 242 IESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPII--KTKRDLMACAQTGSGKTAAFLLPVLSQIYSegpgealqatka 319
Cdd:cd18048    17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMlaDPPQNLIAQSQSGTGKTAAFVLAMLSRVDA------------ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 320 stqengkyvrRKQYPISLVLAPTRELALQ---IYDEARKFAYRSRV----RPCVVYGGADIGQQIrdlergchlLVATPG 392
Cdd:cd18048    85 ----------LKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQViyaiRGNRPGKGTDIEAQI---------VIGTPG 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040698459 393 RLVDMMERGK-IGLDYCKYLVLDEADRMLDM-GFEPQIRRIveQDTMPPkgSRQTMMFSATF 452
Cdd:cd18048   146 TVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRV--KRSMPK--ECQMLLFSATF 203
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
490-601 6.84e-16

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 81.70  E-value: 6.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 490 EENDKRSFLLDLLN---ATGKDSLTLVFVETKKGADALEDFLYREGYACT------SIHGDR--SQRDREEALHQFRSGR 558
Cdd:COG1111   332 IEHPKLSKLREILKeqlGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGE 411
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1040698459 559 CPIMVATAVAARGLDISNVKHVINFDL-PSDIeEYVHRIGRTGR 601
Cdd:COG1111   412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR 454
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
498-598 1.56e-14

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: 71.08  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 498 LLDLLNAT---GKDSLTLVFVETKKGADALEDFL-----YREGYACTSIHG----------DRSQRDREEALHQFRSGRC 559
Cdd:cd18802    12 LIEILREYfpkTPDFRGIIFVERRATAVVLSRLLkehpsTLAFIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGEL 91
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1040698459 560 PIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGR 598
Cdd:cd18802    92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
479-612 7.18e-14

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


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 69.16  E-value: 7.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 479 SENITQKVVWVEENDKRSFLLDLLNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGR 558
Cdd:cd18794     1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1040698459 559 CPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFY 612
Cdd:cd18794    81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
285-451 2.59e-13

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: 67.81  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 285 ACAQTGSGKTAAFLLPVLSQIYSEGPGealqatkastqengkyvrrkqypiSLVLAPTRELALQIYDEARKFAYRS-RVR 363
Cdd:cd00046     6 ITAPTGSGKTLAALLAALLLLLKKGKK------------------------VLVLVPTKALALQTAERLRELFGPGiRVA 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 364 pcVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMER-GKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGs 442
Cdd:cd00046    62 --VLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNA- 138

                  ....*....
gi 1040698459 443 rQTMMFSAT 451
Cdd:cd00046   139 -QVILLSAT 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
243-456 4.18e-13

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: 68.98  E-value: 4.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 243 ESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPII--KTKRDLMACAQTGSGKTAAFLLPVLSQIYSegpgealqATKAS 320
Cdd:cd18047     1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMlaEPPQNLIAQSQSGTGKTAAFVLAMLSQVEP--------ANKYP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 321 TqengkyvrrkqypiSLVLAPTRELALQIydeARKFAYRSRVRPCVVYGGADIGQQirdLERGC----HLLVATPGRLVD 396
Cdd:cd18047    73 Q--------------CLCLSPTYELALQT---GKVIEQMGKFYPELKLAYAVRGNK---LERGQkiseQIVIGTPGTVLD 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040698459 397 MMERGK-IGLDYCKYLVLDEADRML-DMGFEPQIRRIveqDTMPPKGSrQTMMFSATFPKEI 456
Cdd:cd18047   133 WCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRI---QRMLPRNC-QMLLFSATFEDSV 190
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
495-597 1.47e-11

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: 62.49  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 495 RSFLLDLLNATGKdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSG-RCPIM-VATAVAARGL 572
Cdd:cd18793    17 LELLEELREPGEK---VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVFlLSTKAGGVGL 93
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1040698459 573 DISNVKHVINFDL---PSDIE---EYVHRIG 597
Cdd:cd18793    94 NLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
264-608 1.04e-10

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: 65.24  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 264 TRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYsEGPGealqATkastqengkyvrrkqypiSLVLAPTR 343
Cdd:COG1205    55 ERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL-EDPG----AT------------------ALYLYPTK 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 344 ELAlqiYDEARKF-----AYRSRVRPCVVYGgaDIGQQIRD--LERGcHLLVATPgrlvDMMERGkIgLDY--------- 407
Cdd:COG1205   112 ALA---RDQLRRLrelaeALGLGVRVATYDG--DTPPEERRwiREHP-DIVLTNP----DMLHYG-L-LPHhtrwarffr 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 408 -CKYLVLDEA---------------DRMldmgfepqiRRIVEQdtmppKGSRQTMMF-SATF--PKEiqiLARDFLEEYi 468
Cdd:COG1205   180 nLRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRH-----YGSDPQFILaSATIgnPAE---HAERLTGRP- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 469 FLAVGRVGSTSENITQkVVW----VEENDKRSFLLD----LLNATGKDSLTLVFVETKKGA--------DALEDFL---- 528
Cdd:COG1205   242 VTVVDEDGSPRGERTF-VLWnpplVDDGIRRSALAEaarlLADLVREGLRTLVFTRSRRGAellaryarRALREPDladr 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 529 ---YREGYactsihgdrSQRDREEALHQFRSGRCPIMVAT-AVAArGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGN 604
Cdd:COG1205   321 vaaYRAGY---------LPEERREIERGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQ 390

                  ....
gi 1040698459 605 LGLA 608
Cdd:COG1205   391 DSLV 394
PRK13766 PRK13766
Hef nuclease; Provisional
490-601 3.33e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 63.35  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 490 EENDKRSFLLDLLNAT---GKDSLTLVFVETKKGADALEDFLYREGYAC------TSIHGDR--SQRDREEALHQFRSGR 558
Cdd:PRK13766  344 IEHPKLEKLREIVKEQlgkNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGE 423
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1040698459 559 CPIMVATAVAARGLDISNVKHVINFD-LPSDIeEYVHRIGRTGR 601
Cdd:PRK13766  424 FNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR 466
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
543-601 4.41e-09

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: 55.44  E-value: 4.41e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 543 SQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFD-LPSDIeEYVHRIGRTGR 601
Cdd:cd18801    75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
485-602 5.15e-09

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 59.47  E-value: 5.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 485 KVVWVEEndkrsFLLDLLNATGKdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGR-CP-IM 562
Cdd:COG0553   534 KLEALLE-----LLEELLAEGEK---VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPvFL 605
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1040698459 563 VATAVAARGLDISNVKHVINFDLP--SDIEEY----VHRIGRTGRV 602
Cdd:COG0553   606 ISLKAGGEGLNLTAADHVIHYDLWwnPAVEEQaidrAHRIGQTRDV 651
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
561-601 3.58e-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: 3.58e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1040698459 561 IMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 601
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
261-315 2.77e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 53.95  E-value: 2.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1040698459 261 SRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKT-AAFlLPVLSQIYSEGPGEALQ 315
Cdd:COG1201    20 ARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELP 74
PRK13767 PRK13767
ATP-dependent helicase; Provisional
260-391 1.64e-06

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 51.43  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 260 LSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGEALqatkastqENGKYVrrkqypisLVL 339
Cdd:PRK13767   27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGEL--------EDKVYC--------LYV 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040698459 340 APTRELA----------LQ-IYDEARKFAYR-SRVRPCVVYGGADIGQQIRDLERGCHLLVATP 391
Cdd:PRK13767   91 SPLRALNndihrnleepLTeIREIAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTP 154
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
267-416 4.10e-06

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 49.89  E-value: 4.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 267 TPVQKYAIP-IIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastQENGKyvrrkqypiSLVLAPTREL 345
Cdd:COG1204    24 YPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKAL----------------LNGGK---------ALYIVPLRAL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040698459 346 ALQIYDEARKFAYRSRVRPCVVYGGADIGqqIRDLERgCHLLVATPGRLvDMMERGKIG-LDYCKYLVLDEA 416
Cdd:COG1204    79 ASEKYREFKRDFEELGIKVGVSTGDYDSD--DEWLGR-YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA 146
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
265-389 4.80e-06

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: 47.41  E-value: 4.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 265 RPTPVQKYAIPII------KTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastqENGKYVrrkqypisLV 338
Cdd:cd17918    15 SLTKDQAQAIKDIekdlhsPEPMDRLLSGDVGSGKTLVALGAALLAY-----------------KNGKQV--------AI 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1040698459 339 LAPTRELALQIYDEARKFAyrSRVRPCVVYGG--ADIGQQIrDLERGCHLLVA 389
Cdd:cd17918    70 LVPTEILAHQHYEEARKFL--PFINVELVTGGtkAQILSGI-SLLVGTHALLH 119
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
267-416 4.66e-05

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: 44.56  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 267 TPVQKYAI-PIIKTKRDLMACAQTGSGKTAAFLLPVLsqiysegpgealqatKASTQENGKyvrrkqypiSLVLAPTREL 345
Cdd:cd17921     3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAIL---------------RALATSGGK---------AVYIAPTRAL 58
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040698459 346 ALQIYDEARKFAYRSRVRPCVVYGGADIGqqiRDLERGCHLLVATPGRLvDMMER--GKIGLDYCKYLVLDEA 416
Cdd:cd17921    59 VNQKEADLRERFGPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKL-DLLLRngGERLIQDVRLVVVDEA 127
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
270-416 4.66e-05

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: 44.88  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 270 QKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgPGealqaTKAstqengkyvrrkqypisLVLAPTRELAlqi 349
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD-PG-----SRA-----------------LYLYPTKALA--- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 350 YDEARKF-----AYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPgrlvDMMERGKI-----------GLdycKYLVL 413
Cdd:cd17923    59 QDQLRSLrelleQLGLGIRVATYDGDTPREERRAIIRNPPRILLTNP----DMLHYALLphhdrwarflrNL---RYVVL 131

                  ...
gi 1040698459 414 DEA 416
Cdd:cd17923   132 DEA 134
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
511-601 5.57e-05

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: 43.79  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 511 TLVFVETKKGA--------DALEDFLYREGYACTsiHG--DRSQRDR-EEALhqfRSGRCPIMVATAVAARGLDISNVKH 579
Cdd:cd18796    41 TLVFTNTRSQAerlaqrlrELCPDRVPPDFIALH--HGslSRELREEvEAAL---KRGDLKVVVATSSLELGIDIGDVDL 115
                          90       100
                  ....*....|....*....|..
gi 1040698459 580 VINFDLPSDIEEYVHRIGRTGR 601
Cdd:cd18796   116 VIQIGSPKSVARLLQRLGRSGH 137
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
561-613 9.17e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 45.86  E-value: 9.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1040698459 561 IMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYN 613
Cdd:PRK11057  289 IVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
538-629 1.07e-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: 43.10  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 538 IHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISN-----VKHVINFDLPSdieeyVHRI-GRTGRVGNLGLATSF 611
Cdd:cd18811    67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGRGDHQSYCLLV 141
                          90
                  ....*....|....*...
gi 1040698459 612 YNDKNSNITKDLLDILVE 629
Cdd:cd18811   142 YKDPLTETAKQRLRVMTE 159
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
511-598 5.96e-04

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: 40.24  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 511 TLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDRE-EALHQFRSG--RCPIMVATAVAARGLDISNVKHVInFDLP- 586
Cdd:cd18799     9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV-FLRPt 87
                          90
                  ....*....|...
gi 1040698459 587 -SDIeEYVHRIGR 598
Cdd:cd18799    88 eSRT-LFLQMLGR 99
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
278-452 8.03e-04

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 40.37  E-value: 8.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 278 KTKRDLMACAQTGSGKTA-AFLLPVLsqiysegpgealqatkastqengkyvrRKQYPIsLVLAPTRELALQIYDEARKF 356
Cdd:cd17926    16 KNNRRGILVLPTGSGKTLtALALIAY---------------------------LKELRT-LIVVPTDALLDQWKERFEDF 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 357 AYRSRVrpCVVYGGADIGQqirdleRGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRmldmGFEPQIRRIVEQDT 436
Cdd:cd17926    68 LGDSSI--GLIGGGKKKDF------DDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEILKELN 135
                         170
                  ....*....|....*.
gi 1040698459 437 MPPKgsrqtMMFSATF 452
Cdd:cd17926   136 AKYR-----LGLTATP 146
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
269-400 1.19e-03

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: 40.80  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 269 VQKYAIP-IIKTKRDLMACAQTGSGKTAAFLLPVLsQIYSEGPGEALQATKAstqengkyvrrkqypisLVLAPTRELAL 347
Cdd:cd18023     5 IQSEVFPdLLYSDKNFVVSAPTGSGKTVLFELAIL-RLLKERNPLPWGNRKV-----------------VYIAPIKALCS 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1040698459 348 QIYDEAR-KFayrSRVRPCVVYGGADigQQIRDLE--RGCHLLVATPGRLvDMMER 400
Cdd:cd18023    67 EKYDDWKeKF---GPLGLSCAELTGD--TEMDDTFeiQDADIILTTPEKW-DSMTR 116
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
279-416 2.68e-03

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: 39.56  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 279 TKRDLMACAQTGSGKT--AAFLLPVLSQIYSEgpgealqatkasTQENGKyvrrkqypISLVLAPTRELALQIYDEARKF 356
Cdd:cd18034    15 LKRNTIVVLPTGSGKTliAVMLIKEMGELNRK------------EKNPKK--------RAVFLVPTVPLVAQQAEAIRSH 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040698459 357 AYrSRVRPCvvYGGADIGQQIRDLERGC----HLLVATPGRLVDMMERGKIGLDYCKYLVLDEA 416
Cdd:cd18034    75 TD-LKVGEY--SGEMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
538-603 3.25e-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: 38.86  E-value: 3.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040698459 538 IHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVI-----NFDLpSDIEEYVHRIGRTGRVG 603
Cdd:cd18810    57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGL-AQLYQLRGRVGRSKERA 126
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
537-645 3.53e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.06  E-value: 3.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459  537 SIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTG-RVGnlGLATSFYNDK 615
Cdd:PRK09751   306 SHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGLFFPR 383
                           90       100       110
                   ....*....|....*....|....*....|
gi 1040698459  616 NSnitKDLLDILVEAKQEVPSWLENLAYEH 645
Cdd:PRK09751   384 TR---RDLVDSAVIVECMFAGRLENLTPPH 410
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
538-603 3.57e-03

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 38.79  E-value: 3.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040698459 538 IHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVI-----NFDLpSDIEEYVHRIGRTGRVG 603
Cdd:cd18792    66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIiedadRFGL-SQLHQLRGRVGRGKHQS 135
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
337-418 4.29e-03

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: 39.03  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 337 LVLAPTRELALQIYDEARKFAyrSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEA 416
Cdd:cd18035    49 LILAPSRPLVEQHAENLKRVL--NIPDKITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126

                  ..
gi 1040698459 417 DR 418
Cdd:cd18035   127 HH 128
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
278-465 4.30e-03

N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 38.95  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 278 KTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkASTQENGKYVRRKQYPISLVlAPTRELALQIYDearKFA 357
Cdd:cd18020    15 KTNENMLICAPTGAGKTNIAMLTILHEI-------------RQHVNQGGVIKKDDFKIVYI-APMKALAAEMVE---KFS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 358 yrSRVRPcvvyggadIGQQIRDLE----------RGCHLLVATPGRLvDMMERGKIG----LDYCKYLVLDEAdRMLDMG 423
Cdd:cd18020    78 --KRLAP--------LGIKVKELTgdmqltkkeiAETQIIVTTPEKW-DVVTRKSSGdvalSQLVRLLIIDEV-HLLHDD 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1040698459 424 FEPQIRRIVEQdTMPPKGSRQTMM----FSATFPKEIQIlaRDFLE 465
Cdd:cd18020   146 RGPVIESLVAR-TLRQVESTQSMIrivgLSATLPNYLDV--ADFLR 188
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
281-310 4.93e-03

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: 38.33  E-value: 4.93e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1040698459 281 RDLMACAQTGSGKTAAFLLPVLSQIYSEGP 310
Cdd:cd17922     2 RNVLIAAPTGSGKTEAAFLPALSSLADEPE 31
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
497-601 5.68e-03

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 38.00  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 497 FLLDLLNATGKdslTLVFVETKKGADAL-EDFLYregYActsIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDI- 574
Cdd:cd18789    41 ELLKRHEQGDK---IIVFTDNVEALYRYaKRLLK---PF---ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLp 111
                          90       100
                  ....*....|....*....|....*...
gi 1040698459 575 -SNVKHVINFDLPSDiEEYVHRIGRTGR 601
Cdd:cd18789   112 eANVAIQISGHGGSR-RQEAQRLGRILR 138
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
446-603 6.18e-03

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: 39.36  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 446 MMFSATFPKEIQILARDFleEYIFLAVGRVGSTSENITQKVVWVEENDKR---SFLLDLLNATGKDSLTLVFVETKKGAD 522
Cdd:TIGR01587 159 LLMSATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILIESDKVgeiSSLERLLEFIKKGGSIAIIVNTVDRAQ 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040698459 523 ALEDFLYREGYACTSI--HGDRSQRDRE----EALHQFRSGRCP-IMVATAVAARGLDISnvkhvinFDL----PSDIEE 591
Cdd:TIGR01587 237 EFYQQLKEKAPEEEIIlyHSRFTEKDRAkkeaELLREMKKSNEKfVIVATQVIEASLDIS-------ADVmiteLAPIDS 309
                         170
                  ....*....|..
gi 1040698459 592 YVHRIGRTGRVG 603
Cdd:TIGR01587 310 LIQRLGRLHRYG 321
 
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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