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Conserved domains on  [gi|528483637|ref|XP_005168847|]
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DEAD-box helicase 3 X-linked b isoform X3 [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 ...
188-442 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: 581.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 188 FEKYDDIPVEATGHNGPQPIDRFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVL 267
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 268 SQIYTDGPGEALQaaknsaQENGKYGRRKQYPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLER 347
Cdd:cd18051   81 SQIYEQGPGESLP------SESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLER 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 348 GCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGLRQTMMFSATFPKEIQILARD 427
Cdd:cd18051  155 GCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARD 234
                        250
                 ....*....|....*
gi 528483637 428 FLEDYIFLAVGRVGS 442
Cdd:cd18051  235 FLDNYIFLAVGRVGS 249
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
447-594 1.83e-57

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 190.80  E-value: 1.83e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 447 ITQKVVWVEENDKRSFLLDLLNatvipsevqestgeSVEKPGKdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQ 526
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLL--------------EKLKPGK---AIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQ 63
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528483637 527 RDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 594
Cdd:cd18787   64 EERERALKKFRSGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 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 ...
188-442 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: 581.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 188 FEKYDDIPVEATGHNGPQPIDRFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVL 267
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 268 SQIYTDGPGEALQaaknsaQENGKYGRRKQYPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLER 347
Cdd:cd18051   81 SQIYEQGPGESLP------SESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLER 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 348 GCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGLRQTMMFSATFPKEIQILARD 427
Cdd:cd18051  155 GCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARD 234
                        250
                 ....*....|....*
gi 528483637 428 FLEDYIFLAVGRVGS 442
Cdd:cd18051  235 FLDNYIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
209-651 5.07e-168

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 488.50  E-value: 5.07e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 209 RFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDGPGEAlQAaknsaqe 288
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP-QA------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 289 ngkygrrkqypisLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 368
Cdd:COG0513   75 -------------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGAL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 369 GLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFLAVGRVGSTSENIT 448
Cdd:COG0513  142 DLSGVETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIE 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 449 QKVVWVEENDKRSFLLDLLNatvipsevqestgesVEKPGKdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRD 528
Cdd:COG0513  218 QRYYLVDKRDKLELLRRLLR---------------DEDPER---AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQ 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 529 REEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNDKNGNITKD---L 605
Cdd:COG0513  280 RERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAiekL 359
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 528483637 606 LDILVEaKQEVPSWLESLAYEHQH-KSSSRGRSKRFSGGFGARDYRQ 651
Cdd:COG0513  360 IGQKIE-EEELPGFEPVEEKRLERlKPKIKEKLKGKKAGRGGRPGPK 405
PTZ00110 PTZ00110
helicase; Provisional
163-652 9.18e-130

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 394.91  E-value: 9.18e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 163 DWSK----PLPPNERLEHELFSGSNTginfEKYDDIPVE-----ATGHNGPQPIDRFHDLEMGEIIMGNINLSRYTRPTP 233
Cdd:PTZ00110  80 DWKSinlvPFEKNFYKEHPEVSALSS----KEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 234 VQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIytdgpgealqaaknSAQENGKYGrrkQYPISLVLAPTRELALQ 313
Cdd:PTZ00110 156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI--------------NAQPLLRYG---DGPIVLVLAPTRELAEQ 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 314 IYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLDMGFEPQI 393
Cdd:PTZ00110 219 IREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQI 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 394 RRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFL-EDYIFLAVGRVG-STSENITQKVVWVEENDKRSFLLDLLNATV 471
Cdd:PTZ00110 299 RKIVSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIM 374
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 472 IPSevqestgesvekpgkdSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVATAVAA 551
Cdd:PTZ00110 375 RDG----------------DKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVAS 438
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 552 RGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNDKNGNITKDLLDILVEAKQEVPSWLESLAYEHqhks 631
Cdd:PTZ00110 439 RGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNER---- 514
                        490       500
                 ....*....|....*....|.
gi 528483637 632 sSRGRSKRFSGGFGARDYRQN 652
Cdd:PTZ00110 515 -SNGTERRRWGGYGRFSNNVN 534
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
232-424 2.75e-59

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: 197.08  E-value: 2.75e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637  232 TPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDGPGealqaaknsaqengkygrrkqyPISLVLAPTRELA 311
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG----------------------PQALVLAPTRELA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637  312 LQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDYCNYLVLDEADRMLDMGFEP 391
Cdd:pfam00270  59 EQIYEELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGP 136
                         170       180       190
                  ....*....|....*....|....*....|...
gi 528483637  392 QIRRIVEQdtMPPKglRQTMMFSATFPKEIQIL 424
Cdd:pfam00270 137 DLEEILRR--LPKK--RQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
447-594 1.83e-57

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 190.80  E-value: 1.83e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 447 ITQKVVWVEENDKRSFLLDLLNatvipsevqestgeSVEKPGKdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQ 526
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLL--------------EKLKPGK---AIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQ 63
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528483637 527 RDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 594
Cdd:cd18787   64 EERERALKKFRSGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
223-450 2.85e-55

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 187.70  E-value: 2.85e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637   223 INLSRYTRPTPVQKHAIP-IIKSKRDLMACAQTGSGKTAAFLLPVLsqiytdgpgealqaaknsaqengKYGRRKQYPIS 301
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-----------------------EALKRGKGGRV 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637   302 LVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDYCNYLVLDE 380
Cdd:smart00487  58 LVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDE 137
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637   381 ADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFLAVGRvgSTSENITQK 450
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, ...
486-585 6.19e-36

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: 130.79  E-value: 6.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637  486 KPGKDSLTLVFVETKKGADAlEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINF 565
Cdd:pfam00271  11 KKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINY 89
                          90       100
                  ....*....|....*....|
gi 528483637  566 DLPSDIEEYVHRIGRTGRVG 585
Cdd:pfam00271  90 DLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
504-585 1.11e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 112.31  E-value: 1.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637   504 DALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 583
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 528483637   584 VG 585
Cdd:smart00490  81 AG 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
336-595 1.65e-19

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 92.13  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 336 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdycnyLVLDEA--------DrmldmgFEP---QIRRIVE 398
Cdd:COG0514   94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 399 QDTMPPkglrqTMMFSATFPKEIQ--ILARDFLED-YIFLA-VGRvgstsENITQKVVWVEENDKRSFLLDLLnatvips 474
Cdd:COG0514  163 RLPNVP-----VLALTATATPRVRadIAEQLGLEDpRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFL------- 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 475 evQESTGESvekpgkdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVATaVA-ARG 553
Cdd:COG0514  226 --KEHPGGS---------GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMG 293
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 528483637 554 LDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFN 595
Cdd:COG0514  294 IDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYG 335
PRK13766 PRK13766
Hef nuclease; Provisional
489-583 2.60e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 63.74  E-value: 2.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 489 KDSLTLVFVETKKGADALEDFLYREGYAC------TSIHGDR--SQRDREEALHQFRSGRCPILVATAVAARGLDISNVK 560
Cdd:PRK13766 364 PDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVD 443
                         90       100
                 ....*....|....*....|....
gi 528483637 561 HVINFD-LPSDIeEYVHRIGRTGR 583
Cdd:PRK13766 444 LVIFYEpVPSEI-RSIQRKGRTGR 466
 
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 ...
188-442 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: 581.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 188 FEKYDDIPVEATGHNGPQPIDRFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVL 267
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 268 SQIYTDGPGEALQaaknsaQENGKYGRRKQYPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLER 347
Cdd:cd18051   81 SQIYEQGPGESLP------SESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLER 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 348 GCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGLRQTMMFSATFPKEIQILARD 427
Cdd:cd18051  155 GCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARD 234
                        250
                 ....*....|....*
gi 528483637 428 FLEDYIFLAVGRVGS 442
Cdd:cd18051  235 FLDNYIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
209-651 5.07e-168

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 488.50  E-value: 5.07e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 209 RFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDGPGEAlQAaknsaqe 288
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP-QA------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 289 ngkygrrkqypisLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 368
Cdd:COG0513   75 -------------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGAL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 369 GLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFLAVGRVGSTSENIT 448
Cdd:COG0513  142 DLSGVETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIE 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 449 QKVVWVEENDKRSFLLDLLNatvipsevqestgesVEKPGKdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRD 528
Cdd:COG0513  218 QRYYLVDKRDKLELLRRLLR---------------DEDPER---AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQ 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 529 REEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNDKNGNITKD---L 605
Cdd:COG0513  280 RERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAiekL 359
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 528483637 606 LDILVEaKQEVPSWLESLAYEHQH-KSSSRGRSKRFSGGFGARDYRQ 651
Cdd:COG0513  360 IGQKIE-EEELPGFEPVEEKRLERlKPKIKEKLKGKKAGRGGRPGPK 405
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
210-441 3.33e-157

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: 453.10  E-value: 3.33e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 210 FHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDGPgealqaaknsaqEN 289
Cdd:cd17967    2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGP------------PS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 290 GKYGRRKQYPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIG 369
Cdd:cd17967   70 VGRGRRKAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRIS 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528483637 370 LDYCNYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGLRQTMMFSATFPKEIQILARDFLEDYIFLAVGRVG 441
Cdd:cd17967  150 LSSIKFLVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
167-441 2.80e-147

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: 429.39  E-value: 2.80e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 167 PLPPNErlEHELFSGSNTGINFEKYDDIPVEATGHNGPQPIDRFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKR 246
Cdd:cd18052    4 PPPPED--EDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 247 DLMACAQTGSGKTAAFLLPVLSQIYTDGpgeaLQAAKNSAQengkygrrkQYPISLVLAPTRELALQIYDEARKFSYRSH 326
Cdd:cd18052   82 DLMACAQTGSGKTAAFLLPVLTGMMKEG----LTASSFSEV---------QEPQALIVAPTRELANQIFLEARKFSYGTC 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 327 VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKG 406
Cdd:cd18052  149 IRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKE 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 528483637 407 LRQTMMFSATFPKEIQILARDFL-EDYIFLAVGRVG 441
Cdd:cd18052  229 DRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVGRVG 264
PTZ00110 PTZ00110
helicase; Provisional
163-652 9.18e-130

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 394.91  E-value: 9.18e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 163 DWSK----PLPPNERLEHELFSGSNTginfEKYDDIPVE-----ATGHNGPQPIDRFHDLEMGEIIMGNINLSRYTRPTP 233
Cdd:PTZ00110  80 DWKSinlvPFEKNFYKEHPEVSALSS----KEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 234 VQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIytdgpgealqaaknSAQENGKYGrrkQYPISLVLAPTRELALQ 313
Cdd:PTZ00110 156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI--------------NAQPLLRYG---DGPIVLVLAPTRELAEQ 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 314 IYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLDMGFEPQI 393
Cdd:PTZ00110 219 IREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQI 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 394 RRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFL-EDYIFLAVGRVG-STSENITQKVVWVEENDKRSFLLDLLNATV 471
Cdd:PTZ00110 299 RKIVSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIM 374
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 472 IPSevqestgesvekpgkdSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVATAVAA 551
Cdd:PTZ00110 375 RDG----------------DKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVAS 438
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 552 RGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNDKNGNITKDLLDILVEAKQEVPSWLESLAYEHqhks 631
Cdd:PTZ00110 439 RGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNER---- 514
                        490       500
                 ....*....|....*....|.
gi 528483637 632 sSRGRSKRFSGGFGARDYRQN 652
Cdd:PTZ00110 515 -SNGTERRRWGGYGRFSNNVN 534
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
228-597 1.45e-100

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 316.36  E-value: 1.45e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 228 YTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQiytdgpgeaLQAAKNSAQengkygrrkqypiSLVLAPT 307
Cdd:PRK11776  24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK---------LDVKRFRVQ-------------ALVLCPT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 308 RELALQIYDEARKFSYRSH-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLD 386
Cdd:PRK11776  82 RELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 387 MGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYifLAVgRVGSTSEN--ITQKVVWVEENDKRSFLL 464
Cdd:PRK11776 162 MGFQDAIDAIIRQ--APAR--RQTLLFSATYPEGIAAISQRFQRDP--VEV-KVESTHDLpaIEQRFYEVSPDERLPALQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 465 DLLnatvipsevqestgeSVEKPgkDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIL 544
Cdd:PRK11776 235 RLL---------------LHHQP--ES-CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVL 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528483637 545 VATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNDK 597
Cdd:PRK11776 297 VATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
219-435 2.60e-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: 285.10  E-value: 2.60e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 219 IMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDGPgealqaaknsaqengkygRRKQY 298
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK------------------KKGRG 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 299 PISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVL 378
Cdd:cd00268   63 PQALVLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVL 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528483637 379 DEADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFL 435
Cdd:cd00268  143 DEADRMLDMGFEEDVEKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLKNPVRI 195
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
194-637 4.81e-91

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 293.23  E-value: 4.81e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 194 IPVEATGHNGPQPIDRFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLS---QI 270
Cdd:PLN00206 107 LEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTI 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 271 YTDGPGEalqaaknsaqengkygRRKqyPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCH 350
Cdd:PLN00206 187 RSGHPSE----------------QRN--PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVE 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 351 LLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQDTMPpkglrQTMMFSATFPKEIQILARDFLE 430
Cdd:PLN00206 249 LIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAK 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 431 DYIFLAVGRVGSTSENITQKVVWVEENDKRSFLLDLLNATVipsevqestgeSVEKPGkdsltLVFVETKKGADALEDFL 510
Cdd:PLN00206 324 DIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQ-----------HFKPPA-----VVFVSSRLGADLLANAI 387
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 511 YR-EGYACTSIHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGL 589
Cdd:PLN00206 388 TVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGT 467
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528483637 590 ATSFFNDKNGNITKDLLDILVEAKQEVPSWL---ESLAYEHQHKSSSRGRS 637
Cdd:PLN00206 468 AIVFVNEEDRNLFPELVALLKSSGAAIPRELansRYLGSGRKRKKKRRYGS 518
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
228-617 5.25e-91

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 291.33  E-value: 5.25e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 228 YTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDGPgealqAAKnsaqengkyGRRkqyPI-SLVLAP 306
Cdd:PRK10590  21 YREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQP-----HAK---------GRR---PVrALILTP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 307 TRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLD 386
Cdd:PRK10590  84 TRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 387 MGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFLAVGRVGSTSENITQKVVWVEENDKRSFLLDL 466
Cdd:PRK10590 164 MGFIHDIRRVLAK--LPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 467 LnatvipsevqestGEsvekpGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVA 546
Cdd:PRK10590 240 I-------------GK-----GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVA 301
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528483637 547 TAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNDKNGNITKDLLDILveaKQEVP 617
Cdd:PRK10590 302 TDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL---KKEIP 369
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
190-593 3.00e-89

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 287.19  E-value: 3.00e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 190 KYDDIPVEatghngPQPI-DRFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLS 268
Cdd:PRK01297  74 KLEDFVVE------PQEGkTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIIN 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 269 QIYTDGPGEAlqaaknsaqengkygRRKQYPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLE-R 347
Cdd:PRK01297 148 QLLQTPPPKE---------------RYMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaR 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 348 GCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQDtmPPKGLRQTMMFSATFPKEIQILARD 427
Cdd:PRK01297 213 FCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQ 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 428 FLEDYIFLAVGRVGSTSENITQKVVWVEENDKRSFLLDLLnatvipsevqesTGESVEKpgkdslTLVFVETKKGADALE 507
Cdd:PRK01297 291 WTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLV------------TQNPWER------VMVFANRKDEVRRIE 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 508 DFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNL 587
Cdd:PRK01297 353 ERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGAS 432

                 ....*.
gi 528483637 588 GLATSF 593
Cdd:PRK01297 433 GVSISF 438
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
219-435 9.27e-85

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: 265.77  E-value: 9.27e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 219 IMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIytdgpgealqaaknSAQEngkYGRRKQY 298
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI--------------NAQP---PLERGDG 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 299 PISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVL 378
Cdd:cd17966   64 PIVLVLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVL 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528483637 379 DEADRMLDMGFEPQIRRIVEQdTMPPkglRQTMMFSATFPKEIQILARDFLEDYIFL 435
Cdd:cd17966  144 DEADRMLDMGFEPQIRKIVDQ-IRPD---RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
210-593 1.63e-83

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 270.66  E-value: 1.63e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 210 FHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLsQIYTDGPgealqaaknsaqen 289
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAL-QHLLDFP-------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 290 gkygRRKQYPIS-LVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 368
Cdd:PRK11192  68 ----RRKSGPPRiLILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 369 GLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtmpPKGLRQTMMFSATFPKE-IQILARDFLEDYIFLAVGrvGSTSE-- 445
Cdd:PRK11192 144 DCRAVETLILDEADRMLDMGFAQDIETIAAE----TRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAE--PSRRErk 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 446 NITQkvvWVEEND----KRSFLLDLLnatvipsevqesTGESVEKpgkdslTLVFVETKKGADALEDFLYREGYACTSIH 521
Cdd:PRK11192 218 KIHQ---WYYRADdlehKTALLCHLL------------KQPEVTR------SIVFVRTRERVHELAGWLRKAGINCCYLE 276
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528483637 522 GDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSF 593
Cdd:PRK11192 277 GEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
210-618 1.15e-78

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 262.19  E-value: 1.15e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 210 FHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDgPGEAlqaaknsaqen 289
Cdd:PRK04537  11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSR-PALA----------- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 290 gkyGRRKQYPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI- 368
Cdd:PRK04537  79 ---DRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVv 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 369 GLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGLRQTMMFSATFPKEIQILARDFLEDYIFLAVGRVGSTSENIT 448
Cdd:PRK04537 156 SLHACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 449 QKVVWVEENDKRSFLLDLLNatvipsevqESTGesvekpgkdSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRD 528
Cdd:PRK04537 234 QRIYFPADEEKQTLLLGLLS---------RSEG---------ARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKK 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 529 REEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNDKngnITKDLLDI 608
Cdd:PRK04537 296 RESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACER---YAMSLPDI 372
                        410
                 ....*....|
gi 528483637 609 LVEAKQEVPS 618
Cdd:PRK04537 373 EAYIEQKIPV 382
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
209-593 6.56e-76

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 250.27  E-value: 6.56e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 209 RFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTdgpgealqaakNSAQE 288
Cdd:PRK04837   9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLS-----------HPAPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 289 ngkyGRRKQYPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 368
Cdd:PRK04837  78 ----DRKVNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 369 GLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGLRQTMMFSATFPKEIQILARDFLEDYIFLAVGRVGSTSENIT 448
Cdd:PRK04837 154 NLGAIQVVVLDEADRMFDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 449 QKVVWVEENDKRSFLLDLLnatvipsevQEstgesvEKPGKdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRD 528
Cdd:PRK04837 232 EELFYPSNEEKMRLLQTLI---------EE------EWPDR---AIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKK 293
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528483637 529 REEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSF 593
Cdd:PRK04837 294 RLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
196-438 8.44e-73

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: 235.67  E-value: 8.44e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 196 VEATGHNGPQPIDRFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIytdgp 275
Cdd:cd18049   12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI----- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 276 gealqaaknsaqENGKYGRRKQYPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVAT 355
Cdd:cd18049   87 ------------NHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIAT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 356 PGRLVDMMERGKIGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFL 435
Cdd:cd18049  155 PGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLKDYIHI 230

                 ...
gi 528483637 436 AVG 438
Cdd:cd18049  231 NIG 233
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
198-433 5.13e-71

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: 230.34  E-value: 5.13e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 198 ATGHNGPQPIDRFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIytdgpge 277
Cdd:cd17953    2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 278 alQAAKNSAQENGkygrrkqyPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPG 357
Cdd:cd17953   75 --KDQRPVKPGEG--------PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPG 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528483637 358 RLVDM--MERGKI-GLDYCNYLVLDEADRMLDMGFEPQIRRIVeqDTMPPKglRQTMMFSATFPKEIQILARDFLEDYI 433
Cdd:cd17953  145 RMIDIltANNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIV--NNIRPD--RQTVLFSATFPRKVEALARKVLHKPI 219
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
200-438 2.53e-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: 2.53e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 200 GHNGPQPIDRFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIytdgpgeal 279
Cdd:cd18050   54 GVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI--------- 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 280 qaaknsaqENGKYGRRKQYPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRL 359
Cdd:cd18050  125 --------NHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRL 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528483637 360 VDMMERGKIGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFLAVG 438
Cdd:cd18050  197 IDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
219-433 4.24e-69

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: 224.60  E-value: 4.24e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 219 IMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIytdgpgealqaaknSAQengKYGRRKQY 298
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI--------------MDQ---RELEKGEG 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 299 PISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVL 378
Cdd:cd17952   64 PIAVIVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVL 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528483637 379 DEADRMLDMGFEPQIRRIVEQdTMPPkglRQTMMFSATFPKEIQILARDFLEDYI 433
Cdd:cd17952  144 DEADRMFDMGFEYQVRSIVGH-VRPD---RQTLLFSATFKKKIEQLARDILSDPI 194
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
210-597 3.14e-67

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 232.82  E-value: 3.14e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 210 FHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDgpgeaLQAaknsaqen 289
Cdd:PRK11634   8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE-----LKA-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 290 gkygrrkqyPISLVLAPTRELALQIYDEARKFSYRSH-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 368
Cdd:PRK11634  75 ---------PQILVLAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 369 GLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFLAVGRVGSTSENIT 448
Cdd:PRK11634 146 DLSKLSGLVLDEADEMLRMGFIEDVETIMAQ--IPEG--HQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDIS 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 449 QKVVWVEENDKRSFLLDLLNAtvipsevqestgESVEKpgkdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRD 528
Cdd:PRK11634 222 QSYWTVWGMRKNEALVRFLEA------------EDFDA------AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQAL 283
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528483637 529 REEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNDK 597
Cdd:PRK11634 284 REQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENR 352
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
227-429 1.42e-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: 213.34  E-value: 1.42e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 227 RYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTdgpgeaLQAAKNSAQENGKYGrrkqypisLVLAP 306
Cdd:cd17945    9 GYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISR------LPPLDEETKDDGPYA--------LILAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 307 TRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLD 386
Cdd:cd17945   75 TRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMID 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528483637 387 MGFEPQIRRIVeqDTMPPKGL------------------RQTMMFSATFPKEIQILARDFL 429
Cdd:cd17945  155 MGFEPQVTKIL--DAMPVSNKkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYL 213
PTZ00424 PTZ00424
helicase 45; Provisional
207-605 9.11e-62

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 211.99  E-value: 9.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 207 IDRFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDgpgealqaaKNSA 286
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD---------LNAC 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 287 QengkygrrkqypiSLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERG 366
Cdd:PTZ00424  98 Q-------------ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 367 KIGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFLAVGRVGSTSEN 446
Cdd:PTZ00424 165 HLRVDDLKLFILDEADEMLSRGFKGQIYDVFKK--LPPD--VQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 447 ITQKVVWVEEND-KRSFLLDLLNATVIpseVQestgesvekpgkdslTLVFVETKKGADALEDFLYREGYACTSIHGDRS 525
Cdd:PTZ00424 241 IRQFYVAVEKEEwKFDTLCDLYETLTI---TQ---------------AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMD 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 526 QRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNDKNGNITKDL 605
Cdd:PTZ00424 303 QKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
232-424 2.75e-59

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: 197.08  E-value: 2.75e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637  232 TPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDGPGealqaaknsaqengkygrrkqyPISLVLAPTRELA 311
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG----------------------PQALVLAPTRELA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637  312 LQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDYCNYLVLDEADRMLDMGFEP 391
Cdd:pfam00270  59 EQIYEELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGP 136
                         170       180       190
                  ....*....|....*....|....*....|...
gi 528483637  392 QIRRIVEQdtMPPKglRQTMMFSATFPKEIQIL 424
Cdd:pfam00270 137 DLEEILRR--LPKK--RQILLLSATLPRNLEDL 165
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
219-431 6.75e-58

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: 194.61  E-value: 6.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 219 IMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLsqIYTDgpgeaLQAAKNSaQENGkygrrkqy 298
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF--IHLD-----LQPIPRE-QRNG-------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 299 PISLVLAPTRELALQIYDEARKFSYRSHVRPCVvYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVL 378
Cdd:cd17958   65 PGVLVLTPTRELALQIEAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVL 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528483637 379 DEADRMLDMGFEPQIRRIVeQDTMPPkglRQTMMFSATFPKEIQILARDFLED 431
Cdd:cd17958  144 DEADRMLDMGFEPQIRKIL-LDIRPD---RQTIMTSATWPDGVRRLAQSYLKD 192
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
227-435 8.72e-58

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: 194.72  E-value: 8.72e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 227 RYTRPTPVQKHAI-PIIKSKRDLMACAQTGSGKTAAFLLPvlsqiytdgpgeALQAAKNSaqengkYGRRKQYPIS-LVL 304
Cdd:cd17964   13 GFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLP------------AIQSLLNT------KPAGRRSGVSaLII 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 305 APTRELALQIYDEARKFSYRSH-VRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMME--RGKIGLDYCNYLVLDE 380
Cdd:cd17964   75 SPTRELALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528483637 381 ADRMLDMGFEPQIRRIVEQDTMPPKGLRQTMMFSATFPKEIQILARDFL-EDYIFL 435
Cdd:cd17964  155 ADRLLDMGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLkKDYKFI 210
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
447-594 1.83e-57

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 190.80  E-value: 1.83e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 447 ITQKVVWVEENDKRSFLLDLLNatvipsevqestgeSVEKPGKdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQ 526
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLL--------------EKLKPGK---AIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQ 63
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528483637 527 RDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 594
Cdd:cd18787   64 EERERALKKFRSGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
228-426 3.51e-57

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: 192.47  E-value: 3.51e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 228 YTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQ-IYTDgpgealqaaknsaqengkygRRKQYPISLVLAP 306
Cdd:cd17947   10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERlLYRP--------------------KKKAATRVLVLVP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 307 TRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDYCNYLVLDEADRML 385
Cdd:cd17947   70 TRELAMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRML 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528483637 386 DMGFEPQIRRIVEqdtMPPKGlRQTMMFSATFPKEIQILAR 426
Cdd:cd17947  150 EEGFADELKEILR---LCPRT-RQTMLFSATMTDEVKDLAK 186
DEXDc smart00487
DEAD-like helicases superfamily;
223-450 2.85e-55

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 187.70  E-value: 2.85e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637   223 INLSRYTRPTPVQKHAIP-IIKSKRDLMACAQTGSGKTAAFLLPVLsqiytdgpgealqaaknsaqengKYGRRKQYPIS 301
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-----------------------EALKRGKGGRV 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637   302 LVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDYCNYLVLDE 380
Cdd:smart00487  58 LVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDE 137
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637   381 ADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFLAVGRvgSTSENITQK 450
Cdd:smart00487 138 AHRLLDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
230-435 3.24e-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: 187.55  E-value: 3.24e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 230 RPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQiytdgpgeALQAAKNSAQENGkygrrkQYPISLVLAPTRE 309
Cdd:cd17951   12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMF--------ALEQEKKLPFIKG------EGPYGLIVCPSRE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 310 LALQIYDEARKFSYR------SHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADR 383
Cdd:cd17951   78 LARQTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADR 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528483637 384 MLDMGFEPQIRRIVEQDtmppKGLRQTMMFSATFPKEIQILARDFLEDYIFL 435
Cdd:cd17951  158 MIDMGFEEDIRTIFSYF----KGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
219-438 3.24e-54

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: 184.71  E-value: 3.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 219 IMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDGPGEALQAaknsaqengkygrrkqy 298
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRA----------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 299 pisLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGG-ADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLV 377
Cdd:cd17957   64 ---LILAPTRELASQIYRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLV 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528483637 378 LDEADRMLDMGFEPQIRRIVEQDTMPPKglrQTMMFSATFPKEIQILARDFLEDYIFLAVG 438
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 ...
228-434 2.51e-53

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: 182.42  E-value: 2.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 228 YTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDGpgealqaaknsaqengkYGrrkqyPISLVLAPT 307
Cdd:cd17955   19 IKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDP-----------------YG-----IFALVLTPT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 308 RELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMME---RGKIGLDYCNYLVLDEADRM 384
Cdd:cd17955   77 RELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRL 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528483637 385 LDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIF 434
Cdd:cd17955  157 LTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
210-430 1.82e-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: 174.79  E-value: 1.82e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 210 FHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDgpgealqaaKNSAQen 289
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPK---------KDVIQ-- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 290 gkygrrkqypiSLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIG 369
Cdd:cd17940   70 -----------ALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVAD 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528483637 370 LDYCNYLVLDEADRMLDMGFEPQIRRIVeqDTMPPKglRQTMMFSATFPKEIQILARDFLE 430
Cdd:cd17940  139 LSHCKTLVLDEADKLLSQDFQPIIEKIL--NFLPKE--RQILLFSATFPLTVKNFMDRHMH 195
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
227-435 6.49e-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: 173.54  E-value: 6.49e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 227 RYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQiytdgpgeaLQAAKNSAQengkygrRKQYPISLVLAP 306
Cdd:cd17949   10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQR---------LLSLEPRVD-------RSDGTLALVLVP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 307 TRELALQIYDEARKFSYRSH-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDYCNYLVLDEADRM 384
Cdd:cd17949   74 TRELALQIYEVLEKLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528483637 385 LDMGFEPQIRRIVE-----------QDTMPPKglRQTMMFSATFPKEIQILARDFLEDYIFL 435
Cdd:cd17949  154 LDMGFEKDITKILEllddkrskaggEKSKPSR--RQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
228-431 2.80e-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: 171.35  E-value: 2.80e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 228 YTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDgpgealqaaknsaqengkygrrKQYPISLVLAPT 307
Cdd:cd17954   20 WKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN----------------------PQRFFALVLAPT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 308 RELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDYCNYLVLDEADRMLD 386
Cdd:cd17954   78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLN 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 528483637 387 MGFEPQIRRIVEqdTMPPKglRQTMMFSATFPKEIQILARDFLED 431
Cdd:cd17954  158 MDFEPEIDKILK--VIPRE--RTTYLFSATMTTKVAKLQRASLKN 198
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
228-435 7.28e-47

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: 164.79  E-value: 7.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 228 YTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIytdgpgealqaaKNSAQENGKYGrrkqypisLVLAPT 307
Cdd:cd17959   21 YKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL------------KAHSPTVGARA--------LILSPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 308 RELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLDM 387
Cdd:cd17959   81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 528483637 388 GFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFL 435
Cdd:cd17959  161 GFAEQLHEILSR--LPEN--RQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
228-429 1.78e-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: 163.52  E-value: 1.78e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 228 YTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYtdgpgealqaaknsaqeNGKYGRRKQYPISLVLAPT 307
Cdd:cd17960   10 FTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILL-----------------KRKANLKKGQVGALIISPT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 308 RELALQIYDEARKF--SYRSHVRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMMERGKIGLDY--CNYLVLDEAD 382
Cdd:cd17960   73 RELATQIYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKVksLEVLVLDEAD 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528483637 383 RMLDMGFEPQIRRIVEQdtmPPKGlRQTMMFSATFPKEIQILARDFL 429
Cdd:cd17960  153 RLLDLGFEADLNRILSK---LPKQ-RRTGLFSATQTDAVEELIKAGL 195
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
226-437 2.55e-45

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: 160.53  E-value: 2.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 226 SRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIY------TDGPGealqaaknsaqengkygrrkqyp 299
Cdd:cd17941    8 AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwtpEDGLG----------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 300 iSLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQirdLER--GCHLLVATPGRLVDMMERgKIGLDYCNY-- 375
Cdd:cd17941   65 -ALIISPTRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE---KERinRMNILVCTPGRLLQHMDE-TPGFDTSNLqm 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528483637 376 LVLDEADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYIFLAV 437
Cdd:cd17941  140 LVLDEADRILDMGFKETLDAIVEN--LPKS--RQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
222-433 3.50e-43

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 154.24  E-value: 3.50e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 222 NINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTdgpgealqaaknsaqengkygrRKQYPIS 301
Cdd:cd17962    4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT----------------------EHRNPSA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 302 LVLAPTRELALQIYDEARKF-SYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDE 380
Cdd:cd17962   62 LILTPTRELAVQIEDQAKELmKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDE 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528483637 381 ADRMLDMGFEPQIRRIVEQDTMPPkglrQTMMFSATFPKEIQILARDFLEDYI 433
Cdd:cd17962  142 ADTMLKMGFQQQVLDILENISHDH----QTILVSATIPRGIEQLAGQLLQNPV 190
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
214-416 2.90e-42

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: 152.09  E-value: 2.90e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 214 EMG---EIIMGnINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLsqiytdgpgealqaaknsaqeng 290
Cdd:cd17938    3 ELGvmpELIKA-VEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 291 kygrrkQYPISLVLAPTRELALQIYDEARKFSY---RSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK 367
Cdd:cd17938   59 ------QIVVALILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGK 132
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528483637 368 IGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMP---PKGLR-QTMMFSAT 416
Cdd:cd17938  133 LDLSSVRFFVLDEADRLLSQGNLETINRIYNR--IPkitSDGKRlQVIVCSAT 183
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
228-426 9.06e-42

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: 150.59  E-value: 9.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 228 YTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTdgpgealqaaKNSAQENGKYGrrkqypisLVLAPT 307
Cdd:cd17942   10 FTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK----------LKFKPRNGTGV--------IIISPT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 308 RELALQIYDEARKF-SYRSHVRPCVVyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKiGLDYCN--YLVLDEADRM 384
Cdd:cd17942   72 RELALQIYGVAKELlKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTK-GFLYKNlqCLIIDEADRI 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 528483637 385 LDMGFEPQIRRIVEqdtMPPKGlRQTMMFSATFPKEIQILAR 426
Cdd:cd17942  150 LEIGFEEEMRQIIK---LLPKR-RQTMLFSATQTRKVEDLAR 187
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
227-422 1.47e-40

DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 148.54  E-value: 1.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 227 RYTRPTPVQKHAIP-IIKSKRDLMACAQTGSGKTAAFLLPVLSQIytdgpgeaLQAAKnsaqENGKYGRRKqYPISLVLA 305
Cdd:cd17946    9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERL--------LSQKS----SNGVGGKQK-PLRALILT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 306 PTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL---DYCNYLVLDEAD 382
Cdd:cd17946   76 PTRELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLanlKSLRFLVLDEAD 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 528483637 383 RMLDMG-FEP--QIRRIVEQDTMPPKGLRQTMMFSATFPKEIQ 422
Cdd:cd17946  156 RMLEKGhFAEleKILELLNKDRAGKKRKRQTFVFSATLTLDHQ 198
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
212-431 1.28e-38

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: 141.69  E-value: 1.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 212 DLEMGEIIMGNINLSRYTRPTPVQKHAI-PIIKsKRDLMACAQTGSGKTAAFLLPVLSQIYTDGPgeALQAaknsaqeng 290
Cdd:cd17939    1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIvPIIK-GRDVIAQAQSGTGKTATFSIGALQRIDTTVR--ETQA--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 291 kygrrkqypisLVLAPTRELALQIYD--EARKFSYRSHVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 368
Cdd:cd17939   69 -----------LVLAPTRELAQQIQKvvKALGDYMGVKVHACI--GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSL 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528483637 369 GLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGlrQTMMFSATFPKEIQILARDFLED 431
Cdd:cd17939  136 RTDKIKMFVLDEADEMLSRGFKDQIYDIFQF--LPPET--QVVLFSATMPHEVLEVTKKFMRD 194
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
228-435 1.94e-38

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: 141.17  E-value: 1.94e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 228 YTRPTPVQKHAIPIIKSK--RDLMACAQTGSGKTAAFLLPVLSQIYTdgpgealqaaknsaqengkygrRKQYPISLVLA 305
Cdd:cd17963   14 FNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDP----------------------TLKSPQALCLA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 306 PTRELALQIYDEARKF-SY-----RSHVRPCVVYGGADIGQQIrdlergchlLVATPGRLVDMMERGKIGLDYCNYLVLD 379
Cdd:cd17963   72 PTRELARQIGEVVEKMgKFtgvkvALAVPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQLDLKKIKILVLD 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528483637 380 EADRMLDM-GFEPQIRRIVEqdtMPPKGLrQTMMFSATFPKEIQILARDFLEDYIFL 435
Cdd:cd17963  143 EADVMLDTqGHGDQSIRIKR---MLPRNC-QILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
228-429 3.63e-38

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 140.80  E-value: 3.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 228 YTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIytdgpgeaLQAAKNSAQENGKYgrrkqypiSLVLAPT 307
Cdd:cd17961   14 WEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKI--------LKAKAESGEEQGTR--------ALILVPT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 308 RELALQIYDEARKFSY--RSHVRpCV-VYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL-DYCNYLVLDEADR 383
Cdd:cd17961   78 RELAQQVSKVLEQLTAycRKDVR-VVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADL 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528483637 384 MLDMGFEPQIRRIVEqdtMPPKGLrQTMMFSATFPKEIQILARDFL 429
Cdd:cd17961  157 VLSYGYEEDLKSLLS---YLPKNY-QTFLMSATLSEDVEALKKLVL 198
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
210-431 5.53e-37

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: 137.48  E-value: 5.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 210 FHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDgPGEalqaaknsaqen 289
Cdd:cd17950    4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPV-DGQ------------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 290 gkygrrkqypIS-LVLAPTRELALQIYDEARKFS-YRSHVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERG 366
Cdd:cd17950   71 ----------VSvLVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREK 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 367 KIGLDYCNYLVLDEADRM---LDMgfepqiRRIVeQD--TMPPKGlRQTMMFSATFPKEIQILARDFLED 431
Cdd:cd17950  141 KLKLSHVKHFVLDECDKMleqLDM------RRDV-QEifRATPHD-KQVMMFSATLSKEIRPVCKKFMQD 202
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
210-433 9.19e-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: 9.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 210 FHDLEMGEIIMGNINLSRYTRPTPVQKHAI-PIIKSkRDLMACAQTGSGKTAAFLLPVLSQIYTDGPgeALQAaknsaqe 288
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAImPCIKG-YDVIAQAQSGTGKTATFSISILQQIDTSLK--ATQA------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 289 ngkygrrkqypisLVLAPTRELALQIYD--EARKFSYRSHVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERG 366
Cdd:cd18046   71 -------------LVLAPTRELAQQIQKvvMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRR 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528483637 367 KIGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLEDYI 433
Cdd:cd18046  136 YLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQK--LPPD--TQVVLLSATMPNDVLEVTTKFMRDPI 198
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
486-585 6.19e-36

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: 130.79  E-value: 6.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637  486 KPGKDSLTLVFVETKKGADAlEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINF 565
Cdd:pfam00271  11 KKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINY 89
                          90       100
                  ....*....|....*....|
gi 528483637  566 DLPSDIEEYVHRIGRTGRVG 585
Cdd:pfam00271  90 DLPWNPASYIQRIGRAGRAG 109
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
228-434 6.26e-34

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: 128.15  E-value: 6.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 228 YTRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLsqiytdgpgealqaaknsaqENGKYGRRKqyPISLVLAPT 307
Cdd:cd17943   10 FQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL--------------------ESLDLERRH--PQVLILAPT 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 308 RELALQIYDEARKF-SYRSHVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLD 386
Cdd:cd17943   68 REIAVQIHDVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLME 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528483637 387 MGFEPQIRRIveqDTMPPKGlRQTMMFSATFPKE-IQILARdFLEDYIF 434
Cdd:cd17943  147 GSFQKDVNWI---FSSLPKN-KQVIAFSATYPKNlDNLLAR-YMRKPVL 190
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
210-431 8.43e-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: 8.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 210 FHDLEMGEIIMGNINLSRYTRPTPVQKHAI-PIIKSkRDLMACAQTGSGKTAAFLLPVLsqiytdgpgealQAAKNSAQE 288
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIkPIIKG-RDVIAQSQSGTGKTATFSISVL------------QCLDIQVRE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 289 ngkygrrkqyPISLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 368
Cdd:cd18045   68 ----------TQALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSL 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528483637 369 GLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKglRQTMMFSATFPKEIQILARDFLED 431
Cdd:cd18045  138 RTRHIKMLVLDEADEMLNKGFKEQIYDVYRY--LPPA--TQVVLVSATLPQDILEMTNKFMTD 196
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
233-429 1.73e-30

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: 118.80  E-value: 1.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 233 PVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIytdgpgealqaaknsaQENGKYGRRKQYPISLVLAPTRELAL 312
Cdd:cd17944   15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKL----------------QEDQQPRKRGRAPKVLVLAPTRELAN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 313 QIYDEARKFSYRSHVrpCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRMLDMGFEPQ 392
Cdd:cd17944   79 QVTKDFKDITRKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQ 156
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 528483637 393 IRRIV-EQDTMPPKGLRQTMMFSATFPKEIQILARDFL 429
Cdd:cd17944  157 VEEILsVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
HELICc smart00490
helicase superfamily c-terminal domain;
504-585 1.11e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 112.31  E-value: 1.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637   504 DALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 583
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 528483637   584 VG 585
Cdd:smart00490  81 AG 82
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
224-433 1.49e-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: 117.08  E-value: 1.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 224 NLSRY--TRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDgpgealqaaKNSAqengkyGRRKQYPIS 301
Cdd:cd17948    4 ILQRQgiTKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRY---------KLLA------EGPFNAPRG 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 302 LVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIgQQIRDLERG-CHLLVATPGRLVDMMERGKIGLDYCNYLVLDE 380
Cdd:cd17948   69 LVITPSRELAEQIGSVAQSLTEGLGLKVKVITGGRTK-RQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDE 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528483637 381 ADRMLDMGFEPQIRRIVEQ---------DTMPPKGLRQTMMFSATFPKEiqilARDFLEDYI 433
Cdd:cd17948  148 ADTLLDDSFNEKLSHFLRRfplasrrseNTDGLDPGTQLVLVSATMPSG----VGEVLSKVI 205
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
227-426 2.00e-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: 110.80  E-value: 2.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 227 RYTRPTPVQKHAIP-IIKS--------KRDLMACAQTGSGKTAAFLLPVLsQIYTDGPGEALQAaknsaqengkygrrkq 297
Cdd:cd17956    9 GITSAFPVQAAVIPwLLPSskstppyrPGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVPRLRA---------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 298 ypisLVLAPTRELALQIYDEARKFSYRSHVRPCVVYGGADIGQQIRDLERGCHL--------LVATPGRLVDMMERGK-I 368
Cdd:cd17956   72 ----LIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGrylsrvdiLVATPGRLVDHLNSTPgF 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528483637 369 GLDYCNYLVLDEADRMLDMGFE---PQIRRIVEQDTMPPKGLR-------------QTMMFSATFPKEIQILAR 426
Cdd:cd17956  148 TLKHLRFLVIDEADRLLNQSFQdwlETVMKALGRPTAPDLGSFgdanllersvrplQKLLFSATLTRDPEKLSS 221
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
215-436 5.76e-24

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: 101.68  E-value: 5.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 215 MGEIIMGNINLSRYTRPTPVQKHAIPII------KSKRD-----------LMAcAQTGSGKTAAFLLPVLSQIytdgpGE 277
Cdd:cd17965   15 IKEILKGSNKTDEEIKPSPIQTLAIKKLlktlmrKVTKQtsneepklevfLLA-AETGSGKTLAYLAPLLDYL-----KR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 278 ALQAAKNSAQENGKYGRRKQYPISLVLAPTRELALQIYDEARKFSYRSHVRPCVV-YGGADIGQQIRDLERG-CHLLVAT 355
Cdd:cd17965   89 QEQEPFEEAEEEYESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLAFKGrIDILVTT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 356 PGRLVDMME-RGKIgLDYCNYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgLRQTMMFSATFPKEIQILARDFLEDYIF 434
Cdd:cd17965  169 PGKLASLAKsRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APK--LKHLILCSATIPKEFDKTLRKLFPDVVR 243

                 ..
gi 528483637 435 LA 436
Cdd:cd17965  244 IA 245
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
336-595 1.65e-19

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 92.13  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 336 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdycnyLVLDEA--------DrmldmgFEP---QIRRIVE 398
Cdd:COG0514   94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 399 QDTMPPkglrqTMMFSATFPKEIQ--ILARDFLED-YIFLA-VGRvgstsENITQKVVWVEENDKRSFLLDLLnatvips 474
Cdd:COG0514  163 RLPNVP-----VLALTATATPRVRadIAEQLGLEDpRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFL------- 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 475 evQESTGESvekpgkdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVATaVA-ARG 553
Cdd:COG0514  226 --KEHPGGS---------GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMG 293
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 528483637 554 LDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFN 595
Cdd:COG0514  294 IDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYG 335
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
171-580 5.58e-19

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 91.24  E-value: 5.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 171 NERLEHELFSGSNTGINFEKYDDIPVEATGHNGPQPIDRFHDLEMGEIIMGNINLSRYTRPTPVQKHAI-----PIIKSK 245
Cdd:COG1061   21 LDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALeallaALERGG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 246 RDLMACAQTGSGKTAAFLLpVLSQIYTDGPgealqaaknsaqengkygrrkqypiSLVLAPTRELALQIYDEARKFsyrs 325
Cdd:COG1061  101 GRGLVVAPTGTGKTVLALA-LAAELLRGKR-------------------------VLVLVPRRELLEQWAEELRRF---- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 326 hvrpcvvYGGADIGQQIRDleRGCHLLVATPGRLVDMMERGKIGlDYCNYLVLDEADRmldmGFEPQIRRIVEQdtMPPK 405
Cdd:COG1061  151 -------LGDPLAGGGKKD--SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEA--FPAA 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 406 ---GLrqtmmfSAT------FPKEI-------------QILARDFLEDYIFLAVgrvgstsenitqKVVWVEENDKRSFL 463
Cdd:COG1061  215 yrlGL------TATpfrsdgREILLflfdgivyeyslkEAIEDGYLAPPEYYGI------------RVDLTDERAEYDAL 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 464 LDLLNATVIPSE--VQESTGESVEKPGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRC 541
Cdd:COG1061  277 SERLREALAADAerKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGEL 356
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 528483637 542 PILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGR 580
Cdd:COG1061  357 RILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
207-431 1.87e-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: 85.07  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 207 IDRFHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSK--RDLMACAQTGSGKTAAFLLPVLSQIytdgpgealqaakn 284
Cdd:cd18048   17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV-------------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 285 saqengkyGRRKQYPISLVLAPTRELALQ---IYDEARKFSYRSHV----RPCVVYGGADIGQQIrdlergchlLVATPG 357
Cdd:cd18048   83 --------DALKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQViyaiRGNRPGKGTDIEAQI---------VIGTPG 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528483637 358 RLVDMMERGK-IGLDYCNYLVLDEADRMLDM-GFEPQIRRIveQDTMPPKGlrQTMMFSATFPKEIQILARDFLED 431
Cdd:cd18048  146 TVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRV--KRSMPKEC--QMLLFSATFEDSVWAFAERIVPD 217
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
489-583 1.02e-14

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 77.85  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 489 KDSLTLVFVETKKGADALEDFLYREGYACT------SIHGDR--SQRDREEALHQFRSGRCPILVATAVAARGLDISNVK 560
Cdd:COG1111  352 PDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVD 431
                         90       100
                 ....*....|....*....|....
gi 528483637 561 HVINFDL-PSDIeEYVHRIGRTGR 583
Cdd:COG1111  432 LVIFYEPvPSEI-RSIQRKGRTGR 454
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
489-580 3.25e-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: 70.31  E-value: 3.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 489 KDSLTLVFVETKKGADALEDFL-----YREGYACTSIHG----------DRSQRDREEALHQFRSGRCPILVATAVAARG 553
Cdd:cd18802   24 PDFRGIIFVERRATAVVLSRLLkehpsTLAFIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGELNLLIATSVLEEG 103
                         90       100
                 ....*....|....*....|....*..
gi 528483637 554 LDISNVKHVINFDLPSDIEEYVHRIGR 580
Cdd:cd18802  104 IDVPACNLVIRFDLPKTLRSYIQSRGR 130
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
210-431 1.97e-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: 69.75  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 210 FHDLEMGEIIMGNINLSRYTRPTPVQKHAIPIIKSK--RDLMACAQTGSGKTAAFLLPVLSQIytdGPgealqAAKNSAq 287
Cdd:cd18047    3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EP-----ANKYPQ- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 288 engkygrrkqypiSLVLAPTRELALQ---IYDEARKFSyrshvrPCVVYGGADIGQQirdLERGC----HLLVATPGRLV 360
Cdd:cd18047   74 -------------CLCLSPTYELALQtgkVIEQMGKFY------PELKLAYAVRGNK---LERGQkiseQIVIGTPGTVL 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528483637 361 DMMERGK-IGLDYCNYLVLDEADRML-DMGFEPQIRRIveqDTMPPKGLrQTMMFSATFPKEIQILARDFLED 431
Cdd:cd18047  132 DWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRI---QRMLPRNC-QMLLFSATFEDSVWKFAQKVVPD 200
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
250-416 5.20e-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: 67.04  E-value: 5.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 250 ACAQTGSGKTAAFLLPVLSQIYTDGPGealqaaknsaqengkygrrkqypiSLVLAPTRELALQIYDEARKFsYRSHVRP 329
Cdd:cd00046    6 ITAPTGSGKTLAALLAALLLLLKKGKK------------------------VLVLVPTKALALQTAERLREL-FGPGIRV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 330 CVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMER-GKIGLDYCNYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGlr 408
Cdd:cd00046   61 AVLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNA-- 138

                 ....*...
gi 528483637 409 QTMMFSAT 416
Cdd:cd00046  139 QVILLSAT 146
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
493-585 5.77e-12

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: 63.38  E-value: 5.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 493 TLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIE 572
Cdd:cd18794   33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
                         90
                 ....*....|...
gi 528483637 573 EYVHRIGRTGRVG 585
Cdd:cd18794  113 SYYQESGRAGRDG 125
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
494-579 1.49e-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: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 494 LVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSG-RCPI-LVATAVAARGLDISNVKHVINFDL---P 568
Cdd:cd18793   31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGGVGLNLTAANRVILYDPwwnP 110
                         90
                 ....*....|....
gi 528483637 569 SDIE---EYVHRIG 579
Cdd:cd18793  111 AVEEqaiDRAHRIG 124
PRK13766 PRK13766
Hef nuclease; Provisional
489-583 2.60e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 63.74  E-value: 2.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 489 KDSLTLVFVETKKGADALEDFLYREGYAC------TSIHGDR--SQRDREEALHQFRSGRCPILVATAVAARGLDISNVK 560
Cdd:PRK13766 364 PDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVD 443
                         90       100
                 ....*....|....*....|....
gi 528483637 561 HVINFD-LPSDIeEYVHRIGRTGR 583
Cdd:PRK13766 444 LVIFYEpVPSEI-RSIQRKGRTGR 466
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
484-583 4.59e-10

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: 58.52  E-value: 4.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 484 VEKPGKDSLTLVFVETKKGADALEDFLYRE----------GYACTSIHGDRSQRDREEALHQFRSGRCPILVATAVAARG 553
Cdd:cd18801   24 KKQEGSDTRVIIFSEFRDSAEEIVNFLSKIrpgiratrfiGQASGKSSKGMSQKEQKEVIEQFRKGGYNVLVATSIGEEG 103
                         90       100       110
                 ....*....|....*....|....*....|.
gi 528483637 554 LDISNVKHVINFD-LPSDIeEYVHRIGRTGR 583
Cdd:cd18801  104 LDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
494-584 2.76e-09

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 60.24  E-value: 2.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 494 LVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGR-CP-ILVATAVAARGLDISNVKHVINFDLP--S 569
Cdd:COG0553  553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPvFLISLKAGGEGLNLTAADHVIHYDLWwnP 632
                         90
                 ....*....|....*....
gi 528483637 570 DIEEY----VHRIGRTGRV 584
Cdd:COG0553  633 AVEEQaidrAHRIGQTRDV 651
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
229-590 6.49e-09

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: 59.08  E-value: 6.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 229 TRPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDGPGEAlqaaknsaqengkygrrkqypisLVLAPTR 308
Cdd:COG1205   55 ERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGATA-----------------------LYLYPTK 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 309 ELAlqiYDEARKFS-----YRSHVRPCVVYGgaDIGQQIRD--LERGcHLLVATPgrlvDMMERGkI------------G 369
Cdd:COG1205  112 ALA---RDQLRRLRelaeaLGLGVRVATYDG--DTPPEERRwiREHP-DIVLTNP----DMLHYG-LlphhtrwarffrN 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 370 LDycnYLVLDEA---------------DRMldmgfepqiRRIVEQdtmppKGLRQTMMF-SATF--PKEiqilardfled 431
Cdd:COG1205  181 LR---YVVIDEAhtyrgvfgshvanvlRRL---------RRICRH-----YGSDPQFILaSATIgnPAE----------- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 432 yiflavgrvgsTSENIT-QKVVWVEEND----KRSFLL---DLLNATVIPSEVQES---TGESVEKPGKdslTLVFVETK 500
Cdd:COG1205  233 -----------HAERLTgRPVTVVDEDGsprgERTFVLwnpPLVDDGIRRSALAEAarlLADLVREGLR---TLVFTRSR 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 501 KGA--------DALEDFL-------YREGYactsihgdrSQRDREEALHQFRSGRCPILVAT-AVAArGLDISNVKHVIN 564
Cdd:COG1205  299 RGAellaryarRALREPDladrvaaYRAGY---------LPEERREIERGLRSGELLGVVSTnALEL-GIDIGGLDAVVL 368
                        410       420
                 ....*....|....*....|....*.
gi 528483637 565 FDLPSDIEEYVHRIGRTGRVGNLGLA 590
Cdd:COG1205  369 AGYPGTRASFWQQAGRAGRRGQDSLV 394
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
543-583 1.91e-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: 51.55  E-value: 1.91e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 528483637 543 ILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 583
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
226-280 2.34e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 54.34  E-value: 2.34e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528483637 226 SRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKT-AAFlLPVLSQIYTDGPGEALQ 280
Cdd:COG1201   20 ARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELP 74
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
232-381 2.87e-07

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 53.75  E-value: 2.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 232 TPVQKHAIP-IIKSKRDLMACAQTGSGKTA-AFLlpvlsqiytdgpgealqAAKNSAQENGKygrrkqypiSLVLAPTRE 309
Cdd:COG1204   24 YPPQAEALEaGLLEGKNLVVSAPTASGKTLiAEL-----------------AILKALLNGGK---------ALYIVPLRA 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528483637 310 LALQIYDEARKFSYRSHVRPCVVYGGADIGqqIRDLERgCHLLVATPGRLvDMMERGKIG-LDYCNYLVLDEA 381
Cdd:COG1204   78 LASEKYREFKRDFEELGIKVGVSTGDYDSD--DEWLGR-YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA 146
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
230-354 4.04e-07

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 50.88  E-value: 4.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 230 RPTPVQKHAIPII------KSKRDLMACAQTGSGKTAAFLLPvlsqiytdgpgeALQAAKNSAQengkygrrkqypiSLV 303
Cdd:cd17918   15 SLTKDQAQAIKDIekdlhsPEPMDRLLSGDVGSGKTLVALGA------------ALLAYKNGKQ-------------VAI 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528483637 304 LAPTRELALQIYDEARKFSYRSHVRpcVVYGG--ADIGQQIrDLERGCHLLVA 354
Cdd:cd17918   70 LVPTEILAHQHYEEARKFLPFINVE--LVTGGtkAQILSGI-SLLVGTHALLH 119
PRK13767 PRK13767
ATP-dependent helicase; Provisional
225-263 8.31e-06

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 49.11  E-value: 8.31e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 528483637 225 LSRYTRPTPVQKHAIPIIKSKRDLMACAQTGSGKT-AAFL 263
Cdd:PRK13767  27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL 66
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
236-417 1.38e-05

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: 45.37  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 236 KHAIPIIKSKRDLMACAQTGSGKTA-AFLLPVLsqiytdgpgealqaaknsaqengkygrRKQYPIsLVLAPTRELALQI 314
Cdd:cd17926    9 LEAWLAHKNNRRGILVLPTGSGKTLtALALIAY---------------------------LKELRT-LIVVPTDALLDQW 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 315 YDEARKFSYRSHVrpCVVYGGADIGQqirdleRGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEADRmldmGFEPQIR 394
Cdd:cd17926   61 KERFEDFLGDSSI--GLIGGGKKKDF------DDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFS 128
                        170       180
                 ....*....|....*....|...
gi 528483637 395 RIVEQDTMPPKglrqtMMFSATF 417
Cdd:cd17926  129 EILKELNAKYR-----LGLTATP 146
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
235-381 1.50e-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: 46.04  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 235 QKHAIPIIKSKRDLMACAQTGSGKTAAFLLPVLSQIYTDgpgealqaaknsaqengkYGRRkqypiSLVLAPTRELAlqi 314
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD------------------PGSR-----ALYLYPTKALA--- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 315 YDEARKFS-----YRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPgrlvDMME-----RGKIGLDYCN---YLVLDEA 381
Cdd:cd17923   59 QDQLRSLRelleqLGLGIRVATYDGDTPREERRAIIRNPPRILLTNP----DMLHyallpHHDRWARFLRnlrYVVLDEA 134
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
232-381 2.00e-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: 45.72  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 232 TPVQKHAI-PIIKSKRDLMACAQTGSGKTAAFLlpvlsqiytdgpgeaLQAAKNSAQENGKygrrkqypiSLVLAPTREL 310
Cdd:cd17921    3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAE---------------LAILRALATSGGK---------AVYIAPTRAL 58
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528483637 311 ALQIYDEARKFSYRSHVRPCVVYGGADIGqqiRDLERGCHLLVATPGRLvDMMER--GKIGLDYCNYLVLDEA 381
Cdd:cd17921   59 VNQKEADLRERFGPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKL-DLLLRngGERLIQDVRLVVVDEA 127
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
493-583 2.39e-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: 44.95  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 493 TLVFVETKKGA--------DALEDFLYREGYACTsiHG--DRSQRDR-EEALhqfRSGRCPILVATAVAARGLDISNVKH 561
Cdd:cd18796   41 TLVFTNTRSQAerlaqrlrELCPDRVPPDFIALH--HGslSRELREEvEAAL---KRGDLKVVVATSSLELGIDIGDVDL 115
                         90       100
                 ....*....|....*....|..
gi 528483637 562 VINFDLPSDIEEYVHRIGRTGR 583
Cdd:cd18796  116 VIQIGSPKSVARLLQRLGRSGH 137
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
520-611 1.10e-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: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 520 IHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISN-----VKHVINFDLPSdieeyVHRIgrTGRVGNLGLATSFF 594
Cdd:cd18811   67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQL--RGRVGRGDHQSYCL 139
                         90       100
                 ....*....|....*....|
gi 528483637 595 ---NDKNGNITKDLLDILVE 611
Cdd:cd18811  140 lvyKDPLTETAKQRLRVMTE 159
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
245-381 1.51e-04

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 43.41  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 245 KRDLMACAQTGSGKT--AAFLLPVLSQIytdgpgealqaaKNSAQENGKygrrkqypISLVLAPTRELALQIYdEArkfs 322
Cdd:cd18034   16 KRNTIVVLPTGSGKTliAVMLIKEMGEL------------NRKEKNPKK--------RAVFLVPTVPLVAQQA-EA---- 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528483637 323 YRSHVRPCV--VYGGADIGQQIRDLERGC----HLLVATPGRLVDMMERGKIGLDYCNYLVLDEA 381
Cdd:cd18034   71 IRSHTDLKVgeYSGEMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
543-585 1.87e-04

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 44.70  E-value: 1.87e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 528483637 543 ILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVG 585
Cdd:PRK11057 289 IVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
493-580 1.97e-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: 41.39  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 493 TLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDRE-EALHQFRSG--RCPILVATAVAARGLDISNVKHVInFDLP- 568
Cdd:cd18799    9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV-FLRPt 87
                         90
                 ....*....|...
gi 528483637 569 -SDIeEYVHRIGR 580
Cdd:cd18799   88 eSRT-LFLQMLGR 99
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
520-594 2.57e-04

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: 41.85  E-value: 2.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528483637 520 IHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDI--SNVKHVINFDLPSDiEEYVHRIGRTGRVGNLGLATSFF 594
Cdd:cd18789   74 ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLpeANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
520-585 5.96e-04

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 41.10  E-value: 5.96e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528483637 520 IHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVI-----NFDLpSDIEEYVHRIGRTGRVG 585
Cdd:cd18792   66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIiedadRFGL-SQLHQLRGRVGRGKHQS 135
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
520-585 7.49e-04

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: 40.40  E-value: 7.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528483637 520 IHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVI-----NFDLpSDIEEYVHRIGRTGRVG 585
Cdd:cd18810   57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGL-AQLYQLRGRVGRSKERA 126
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
519-627 2.67e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.06  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637  519 SIHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTG-RVGnlGLATSFFNDK 597
Cdd:PRK09751  306 SHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGLFFPR 383
                          90       100       110
                  ....*....|....*....|....*....|
gi 528483637  598 NgniTKDLLDILVEAKQEVPSWLESLAYEH 627
Cdd:PRK09751  384 T---RRDLVDSAVIVECMFAGRLENLTPPH 410
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
246-281 3.94e-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: 38.72  E-value: 3.94e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 528483637 246 RDLMACAQTGSGKTAAFLLPVLSQIYtDGPGEALQA 281
Cdd:cd17922    2 RNVLIAAPTGSGKTEAAFLPALSSLA-DEPEKGVQV 36
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
302-383 4.45e-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: 38.65  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 302 LVLAPTRELALQIYDEARKFsyRSHVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCNYLVLDEA 381
Cdd:cd18035   49 LILAPSRPLVEQHAENLKRV--LNIPDKITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126

                 ..
gi 528483637 382 DR 383
Cdd:cd18035  127 HH 128
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
493-583 9.48e-03

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 37.61  E-value: 9.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528483637 493 TLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPILVATAVAARGLDISNVKHVINFDlpSDIE 572
Cdd:cd18790   30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKE 107
                         90
                 ....*....|....*...
gi 528483637 573 EY-------VHRIGRTGR 583
Cdd:cd18790  108 GFlrsetslIQTIGRAAR 125
 
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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