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Conserved domains on  [gi|169881239|ref|NP_001116137|]
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ATP-dependent RNA helicase DDX3Y isoform 1 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030640)

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

CATH:  3.40.50.300|1.20.1320.20
EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0005524|GO:0004386|GO:0003676
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 ...
 158-408 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: 590.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 158 FEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPIL 237
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 238 SQIYTDGPGEALkaVKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 317
Cdd:cd18051   81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 318 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 397
Cdd:cd18051  159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238

                        250
                 ....*....|.
gi 169881239 398 YIFLAVGRVGS 408
Cdd:cd18051  239 YIFLAVGRVGS 249
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 413-543 5.54e-60

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


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 196.96  E-value: 5.54e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 413 ITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 492
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169881239 493 LVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 543
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 158-408 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: 590.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 158 FEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPIL 237
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 238 SQIYTDGPGEALkaVKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 317
Cdd:cd18051   81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 318 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 397
Cdd:cd18051  159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238

                        250
                 ....*....|.
gi 169881239 398 YIFLAVGRVGS 408
Cdd:cd18051  239 YIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
179-566 1.24e-167

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 485.81  E-value: 1.24e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 179 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEalkavkengry 258
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA----------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 259 grrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 338
Cdd:COG0513   72 ------PQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 339 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 418
Cdd:COG0513  146 VETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYY 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 419 WVEDLDKRSFLLDILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 498
Cdd:COG0513  222 LVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169881239 499 AARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLveaKQEVP 566
Cdd:COG0513  301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLI---GQKIE 365
PTZ00110 PTZ00110
helicase; Provisional
 170-594 2.25e-129

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 392.60  E-value: 2.25e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 170 GSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeal 249
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI--------- 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 250 kAVKENGRYGrrkQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMM 329
Cdd:PTZ00110 193 -NAQPLLRYG---DGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFL 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 330 ERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL-DEYIFLAVGRVG- 407
Cdd:PTZ00110 269 ESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDl 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 408 STSENITQKVVWVEDLDKRSFLLDILGATGSD-SLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFR 486
Cdd:PTZ00110 345 TACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFK 424

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 487 SGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLVEAKQEVP 566
Cdd:PTZ00110 425 TGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVP 504

                        410       420
                 ....*....|....*....|....*...
gi 169881239 567 SWLENMAYEHHYKGGSRGRSKSNRFSGG 594
Cdd:PTZ00110 505 PELEKLSNERSNGTERRRWGGYGRFSNN 532
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 202-390 1.76e-60

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 199.39  E-value: 1.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  202 TPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengrygrrkqyPISLVLAPTRELAVQIY 281
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG------------------PQALVLAPTRELAEQIY 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  282 EEARKFSYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDFCKYLVLDEADRMLDMGFEPQIRR 361
Cdd:pfam00270  63 EELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEE 140

                         170       180
                  ....*....|....*....|....*....
gi 169881239  362 IVEQdtMPPKgvRHTMMFSATFPKEIQML 390
Cdd:pfam00270 141 ILRR--LPKK--RQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 413-543 5.54e-60

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 196.96  E-value: 5.54e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 413 ITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 492
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169881239 493 LVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 543
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
193-416 1.37e-57

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 193.09  E-value: 1.37e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239   193 IELTRYTRPTPVQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkavkengRYGRRKQYPISLVLA 271
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-------------------EALKRGKGGRVLVLV 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239   272 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 350
Cdd:smart00487  62 PTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRL 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169881239   351 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRvgSTSENITQK 416
Cdd:smart00487 142 LDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 424-534 6.38e-37

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 133.49  E-value: 6.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  424 DKRSFLLDILgATGSDSLTLVFVETKKGADsLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGL 503
Cdd:pfam00271   1 EKLEALLELL-KKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 169881239  504 DISNVRHVINFDLPSDIEEYVHRIGRTGRVG 534
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
453-534 1.66e-30

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 114.62  E-value: 1.66e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239   453 DSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGR 532
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 169881239   533 VG 534
Cdd:smart00490  81 AG 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
302-556 5.85e-21

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 96.75  E-value: 5.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 302 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdfckyLVLDEA--------DrmldmgFEP---QIRRIVE 364
Cdd:COG0514   94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 365 QDTMPPkgvrhTMMFSATFPKE-----IQMLARDflDEYIFLA-VGRvgstsENITQKVVWVEDLDKRSFLLDILGATGS 438
Cdd:COG0514  163 RLPNVP-----VLALTATATPRvradiAEQLGLE--DPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPG 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 439 DSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATaVA-ARGLDISNVRHVINFDLP 517
Cdd:COG0514  231 GS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLP 308

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 169881239 518 SDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLD 556
Cdd:COG0514  309 KSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
PRK13766 PRK13766
Hef nuclease; Provisional
 439-532 1.90e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 57.58  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 439 DSLTLVFVETKKGADSLEDFLYHEGYAC------TSIHGDR--SQRDREEALHQFRSGKSPILVATAVAARGLDISNVRH 510
Cdd:PRK13766 365 DSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444

                         90       100
                 ....*....|....*....|...
gi 169881239 511 VINFD-LPSDIeEYVHRIGRTGR 532
Cdd:PRK13766 445 VIFYEpVPSEI-RSIQRKGRTGR 466
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
 342-534 1.54e-04

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


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 44.37  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  342 LVLDEADRMLDmgfEPQIRRIVEQDTMPPKGVRHTMMfSATFPKEIQMLARDFldEYIFLAVGRVGSTSENITQKVVWVE 421
Cdd:TIGR01587 128 LIFDEVHFYDE---YTLALILAVLEVLKDNDVPILLM-SATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILI 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  422 DLDKR---SFLLDILGATGSDSLTLVFVET-----------KKGADSLEDFLYHEGYActsiHGDRSQRDREEALHQFRS 487
Cdd:TIGR01587 202 ESDKVgeiSSLERLLEFIKKGGSIAIIVNTvdraqefyqqlKEKAPEEEIILYHSRFT----EKDRAKKEAELLREMKKS 277

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 169881239  488 GKSPILVATAVAARGLDISnvrhvinFDL----PSDIEEYVHRIGRTGRVG 534
Cdd:TIGR01587 278 NEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYG 321
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 158-408 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: 590.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 158 FEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPIL 237
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 238 SQIYTDGPGEALkaVKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 317
Cdd:cd18051   81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 318 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 397
Cdd:cd18051  159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238

                        250
                 ....*....|.
gi 169881239 398 YIFLAVGRVGS 408
Cdd:cd18051  239 YIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
179-566 1.24e-167

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 485.81  E-value: 1.24e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 179 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEalkavkengry 258
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA----------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 259 grrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 338
Cdd:COG0513   72 ------PQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 339 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 418
Cdd:COG0513  146 VETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYY 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 419 WVEDLDKRSFLLDILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 498
Cdd:COG0513  222 LVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169881239 499 AARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLveaKQEVP 566
Cdd:COG0513  301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLI---GQKIE 365
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 180-407 7.59e-162

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: 463.11  E-value: 7.59e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 180 FSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkavkENGRYG 259
Cdd:cd17967    2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGP--------PSVGRG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 260 RRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFC 339
Cdd:cd17967   74 RRKAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSI 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169881239 340 KYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVG 407
Cdd:cd17967  154 KFLVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 137-407 6.72e-151

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: 437.09  E-value: 6.72e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 137 PLPPSERlEQELFSGGNTGINFEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKR 216
Cdd:cd18052    3 PPPPPED-EDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 217 DLMACAQTGSGKTAAFLLPILSQIYTDGpgeaLKAVKENGrygrrKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPC 296
Cdd:cd18052   82 DLMACAQTGSGKTAAFLLPVLTGMMKEG----LTASSFSE-----VQEPQALIVAPTRELANQIFLEARKFSYGTCIRPV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 297 VVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHT 376
Cdd:cd18052  153 VVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQT 232

                        250       260       270
                 ....*....|....*....|....*....|..
gi 169881239 377 MMFSATFPKEIQMLARDFLDE-YIFLAVGRVG 407
Cdd:cd18052  233 LMFSATFPEEIQRLAAEFLKEdYLFLTVGRVG 264
PTZ00110 PTZ00110
helicase; Provisional
 170-594 2.25e-129

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 392.60  E-value: 2.25e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 170 GSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeal 249
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI--------- 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 250 kAVKENGRYGrrkQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMM 329
Cdd:PTZ00110 193 -NAQPLLRYG---DGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFL 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 330 ERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL-DEYIFLAVGRVG- 407
Cdd:PTZ00110 269 ESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDl 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 408 STSENITQKVVWVEDLDKRSFLLDILGATGSD-SLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFR 486
Cdd:PTZ00110 345 TACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFK 424

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 487 SGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLVEAKQEVP 566
Cdd:PTZ00110 425 TGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVP 504

                        410       420
                 ....*....|....*....|....*...
gi 169881239 567 SWLENMAYEHHYKGGSRGRSKSNRFSGG 594
Cdd:PTZ00110 505 PELEKLSNERSNGTERRRWGGYGRFSNN 532
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 198-548 1.74e-98

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 309.42  E-value: 1.74e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 198 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgealkavkeNGRYgRRKQypiSLVLAPTRELA 277
Cdd:PRK11776  24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--------------DVKR-FRVQ---ALVLCPTRELA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 278 VQIYEEARKFSyrsRVRP-------CvvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 350
Cdd:PRK11776  86 DQVAKEIRRLA---RFIPnikvltlC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 351 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYifLAVgRVGSTSEN--ITQKVVWVEDLDKRSF 428
Cdd:PRK11776 160 LDMGFQDAIDAIIRQ--APAR--RQTLLFSATYPEGIAAISQRFQRDP--VEV-KVESTHDLpaIEQRFYEVSPDERLPA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 429 LLDILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNV 508
Cdd:PRK11776 233 LQRLLLHHQPES-CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 169881239 509 RHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNM 548
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEM 351
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 189-401 5.98e-95

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: 290.88  E-value: 5.98e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 189 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkavkengrygRRKQYPISL 268
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK--------------KKGRGPQAL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 269 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 348
Cdd:cd00268   67 VLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEAD 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169881239 349 RMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFL 401
Cdd:cd00268  147 RMLDMGFEEDVEKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 179-566 1.69e-94

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 299.03  E-value: 1.69e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 179 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkAVKengry 258
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQP-----HAK----- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 259 GRRkqyPI-SLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 337
Cdd:PRK10590  72 GRR---PVrALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLD 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 338 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKV 417
Cdd:PRK10590 149 QVEILVLDEADRMLDMGFIHDIRRVLAK--LPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 418 VWVEDLDKRSFLLDILGaTGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATA 497
Cdd:PRK10590 225 HFVDKKRKRELLSQMIG-KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATD 303

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169881239 498 VAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLveaKQEVP 566
Cdd:PRK10590 304 IAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL---KKEIP 369
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 164-591 1.61e-92

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 295.93  E-value: 1.61e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 164 IPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILS---QI 240
Cdd:PLN00206 107 LEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTI 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 241 YTDGPGEalkavkengrygRRKqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVA 320
Cdd:PLN00206 187 RSGHPSE------------QRN--PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVG 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 321 TPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPpkgvrHTMMFSATFPKEIQMLARDFLDEYIF 400
Cdd:PLN00206 253 TPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKDIIL 327

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 401 LAVGRVGSTSENITQKVVWVEDLDKRSFLLDILgaTGSDSLT---LVFVETKKGADSLEDFL-YHEGYACTSIHGDRSQR 476
Cdd:PLN00206 328 ISIGNPNRPNKAVKQLAIWVETKQKKQKLFDIL--KSKQHFKppaVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMK 405

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 477 DREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLD 556
Cdd:PLN00206 406 ERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 169881239 557 LLVEAKQEVPSWLENmayeHHYKGGSRGRSKSNRF 591
Cdd:PLN00206 486 LLKSSGAAIPRELAN----SRYLGSGRKRKKKRRY 516
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 180-545 3.92e-89

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 285.65  E-value: 3.92e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 180 FSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEAlkavkengryg 259
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKE----------- 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 260 RRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLE-RGCHLLVATPGRLVDMMERGKIGLDF 338
Cdd:PRK01297 158 RYMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDM 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 339 CKYLVLDEADRMLDMGFEPQIRRIVEQDtmPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 418
Cdd:PRK01297 238 VEVMVLDEADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVY 315

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 419 WVEDLDKRSFLLDILGATGSDSLtLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 498
Cdd:PRK01297 316 AVAGSDKYKLLYNLVTQNPWERV-MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDV 394

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 169881239 499 AARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNE 545
Cdd:PRK01297 395 AGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGE 441
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 189-401 4.62e-83

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: 259.99  E-value: 4.62e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 189 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIyTDGPgealkavkengrYGRRKQYPISL 268
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI-NAQP------------PLERGDGPIVL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 269 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 348
Cdd:cd17966   68 VLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEAD 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169881239 349 RMLDMGFEPQIRRIVEQdTMPPkgvRHTMMFSATFPKEIQMLARDFLDEYIFL 401
Cdd:cd17966  148 RMLDMGFEPQIRKIVDQ-IRPD---RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 179-542 8.29e-82

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 265.27  E-value: 8.29e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 179 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsQIYTDGPgealkavkengry 258
Cdd:PRK11192   2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAL-QHLLDFP------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 259 gRRKQYPIS-LVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 337
Cdd:PRK11192  68 -RRKSGPPRiLILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCR 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 338 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtmpPKGVRHTMMFSATFPKE-IQMLARDFLDEYIFLAVGrvGSTSE--NIT 414
Cdd:PRK11192 147 AVETLILDEADRMLDMGFAQDIETIAAE----TRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAE--PSRRErkKIH 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 415 QKVVWVEDLD-KRSFLLDILgATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPIL 493
Cdd:PRK11192 221 QWYYRADDLEhKTALLCHLL-KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVL 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 169881239 494 VATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSF 542
Cdd:PRK11192 300 VATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 179-567 1.96e-81

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 268.36  E-value: 1.96e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 179 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgPGEAlkavkengry 258
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSR-PALA---------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 259 GRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI-GLD 337
Cdd:PRK04537  79 DRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 338 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKV 417
Cdd:PRK04537 159 ACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 418 VWVEDLDKRSFLLDILGATgSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATA 497
Cdd:PRK04537 237 YFPADEEKQTLLLGLLSRS-EGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATD 315

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 498 VAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKnmnITKDLLDLLVEAKQEVPS 567
Cdd:PRK04537 316 VAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACER---YAMSLPDIEAYIEQKIPV 382
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 180-542 1.30e-76

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 251.04  E-value: 1.30e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 180 FSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEalkavkengryG 259
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPE-----------D 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 260 RRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFC 339
Cdd:PRK04837  79 RKVNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 340 KYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVW 419
Cdd:PRK04837 159 QVVVLDEADRMFDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFY 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 420 VEDLDKRSFLLDILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVA 499
Cdd:PRK04837 237 PSNEEKMRLLQTLIEEEWPDR-AIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVA 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 169881239 500 ARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSF 542
Cdd:PRK04837 316 ARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 180-542 7.00e-71

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 241.68  E-value: 7.00e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 180 FSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaLKAvkengryg 259
Cdd:PRK11634   8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE-----LKA-------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 260 rrkqyPISLVLAPTRELAVQIYEEARKFSYRSR-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 338
Cdd:PRK11634  75 -----PQILVLAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 339 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 418
Cdd:PRK11634 150 LSGLVLDEADEMLRMGFIEDVETIMAQ--IPEG--HQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYW 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 419 WVEDLDKRSFLLDILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 498
Cdd:PRK11634 226 TVWGMRKNEALVRFLEAEDFDA-AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDV 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 169881239 499 AARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSF 542
Cdd:PRK11634 305 AARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 168-395 1.27e-70

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: 228.42  E-value: 1.27e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 168 ATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGE 247
Cdd:cd17953    2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 248 AlkavkENGrygrrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVD 327
Cdd:cd17953   82 P-----GEG--------PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMID 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169881239 328 M--MERGKI-GLDFCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPKgvRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17953  149 IltANNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIV--NNIRPD--RQTVLFSATFPRKVEALARKVL 215
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 166-404 8.31e-70

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


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 226.81  E-value: 8.31e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 166 VEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgp 245
Cdd:cd18049   12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI----- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 246 gealkavkENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRL 325
Cdd:cd18049   87 --------NHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRL 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169881239 326 VDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVG 404
Cdd:cd18049  159 IDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 170-404 1.98e-68

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: 224.50  E-value: 1.98e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 170 GSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeal 249
Cdd:cd18050   54 GVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI--------- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 250 kavkENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMM 329
Cdd:cd18050  125 ----NHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL 200

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169881239 330 ERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVG 404
Cdd:cd18050  201 EAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 189-399 8.04e-67

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: 217.67  E-value: 8.04e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 189 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYtdgpgealkavkeNGRYGRRKQYPISL 268
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-------------DQRELEKGEGPIAV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 269 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 348
Cdd:cd17952   68 IVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEAD 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169881239 349 RMLDMGFEPQIRRIVEQdTMPPkgvRHTMMFSATFPKEIQMLARDFLDEYI 399
Cdd:cd17952  148 RMFDMGFEYQVRSIVGH-VRPD---RQTLLFSATFKKKIEQLARDILSDPI 194
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 193-395 1.29e-63

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: 209.87  E-value: 1.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 193 IELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALKavKENGrygrrkqyPISLVLAP 272
Cdd:cd17945    5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEET--KDDG--------PYALILAP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 273 TRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLD 352
Cdd:cd17945   75 TRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMID 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169881239 353 MGFEPQIRRIVeqDTMPP------------------KGVRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17945  155 MGFEPQVTKIL--DAMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYL 213
PTZ00424 PTZ00424
helicase 45; Provisional
 171-554 2.80e-63

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 215.08  E-value: 2.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 171 SNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaL 249
Cdd:PTZ00424  21 SNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIkPILDG-YDTIGQAQSGTGKTATFVIAALQLIDYD-----L 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 250 KAVKengrygrrkqypiSLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMM 329
Cdd:PTZ00424  95 NACQ-------------ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 330 ERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGST 409
Cdd:PTZ00424 162 DKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKK--LPPD--VQVALFSATMPNEILELTTKFMRDPKRILVKKDELT 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 410 SENITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGK 489
Cdd:PTZ00424 238 LEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGS 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169881239 490 SPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDL 554
Cdd:PTZ00424 318 TRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 202-390 1.76e-60

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 199.39  E-value: 1.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  202 TPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengrygrrkqyPISLVLAPTRELAVQIY 281
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG------------------PQALVLAPTRELAEQIY 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  282 EEARKFSYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDFCKYLVLDEADRMLDMGFEPQIRR 361
Cdd:pfam00270  63 EELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEE 140

                         170       180
                  ....*....|....*....|....*....
gi 169881239  362 IVEQdtMPPKgvRHTMMFSATFPKEIQML 390
Cdd:pfam00270 141 ILRR--LPKK--RQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 413-543 5.54e-60

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 196.96  E-value: 5.54e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 413 ITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 492
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169881239 493 LVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 543
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 197-392 1.33e-57

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: 193.57  E-value: 1.33e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 197 RYTRPTPVQKHAI-PIIKGKRDLMACAQTGSGKTAAFLLPilsqiytdgpgeALKAVKENGRYGRRKQYPIsLVLAPTRE 275
Cdd:cd17964   13 GFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLP------------AIQSLLNTKPAGRRSGVSA-LIISPTRE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 276 LAVQIYEEARKFSYRSR-VRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMME--RGKIGLDFCKYLVLDEADRML 351
Cdd:cd17964   80 LALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 169881239 352 DMGFEPQIRRIVeqDTMPPKGVRH--TMMFSATFPKEIQMLAR 392
Cdd:cd17964  160 DMGFRPDLEQIL--RHLPEKNADPrqTLLFSATVPDEVQQIAR 200
DEXDc smart00487
DEAD-like helicases superfamily;
193-416 1.37e-57

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 193.09  E-value: 1.37e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239   193 IELTRYTRPTPVQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkavkengRYGRRKQYPISLVLA 271
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-------------------EALKRGKGGRVLVLV 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239   272 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 350
Cdd:smart00487  62 PTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRL 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169881239   351 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRvgSTSENITQK 416
Cdd:smart00487 142 LDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 198-396 3.76e-56

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: 189.00  E-value: 3.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 198 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQ-IYTDgpgealkavkengrygRRKQYPISLVLAPTREL 276
Cdd:cd17947   10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERlLYRP----------------KKKAATRVLVLVPTREL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 277 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDFCKYLVLDEADRMLDMGF 355
Cdd:cd17947   74 AMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGF 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 169881239 356 EPQIRRIVEqdtMPPKGvRHTMMFSATFPKEIQMLARDFLD 396
Cdd:cd17947  154 ADELKEILR---LCPRT-RQTMLFSATMTDEVKDLAKLSLN 190
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 189-404 4.56e-56

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: 188.95  E-value: 4.56e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 189 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALKAvkengrygrrkqypisL 268
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRA----------------L 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 269 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGG-ADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 347
Cdd:cd17957   65 ILAPTRELASQIYRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEA 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169881239 348 DRMLDMGFEPQIRRIVEQDTMPPKgvrHTMMFSATFPKEIQMLARDFLDEYIFLAVG 404
Cdd:cd17957  145 DKLFEPGFREQTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 189-397 5.27e-55

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: 186.13  E-value: 5.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 189 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqIYTDGpgEALKAVKENGrygrrkqyPISL 268
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF--IHLDL--QPIPREQRNG--------PGVL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 269 VLAPTRELAVQIYEEARKFSYRSRVRPCVvYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 348
Cdd:cd17958   69 VLTPTRELALQIEAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEAD 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 169881239 349 RMLDMGFEPQIRRIVeQDTMPPkgvRHTMMFSATFPKEIQMLARDFLDE 397
Cdd:cd17958  148 RMLDMGFEPQIRKIL-LDIRPD---RQTIMTSATWPDGVRRLAQSYLKD 192
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 198-400 3.32e-54

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: 184.35  E-value: 3.32e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 198 YTRPTPVQKHAIP-IIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDGpgealkavkengrYGrrkqyPISLVLAPTREL 276
Cdd:cd17955   19 IKEPTPIQKLCIPeILAG-RDVIGGAKTGSGKTAAFALPILQRLSEDP-------------YG-----IFALVLTPTREL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 277 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMME---RGKIGLDFCKYLVLDEADRMLDM 353
Cdd:cd17955   80 AYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 169881239 354 GFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIF 400
Cdd:cd17955  160 SFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 200-395 7.16e-54

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: 183.31  E-value: 7.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 200 RPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgeaLKAVKENGRYG-RRKQYPISLVLAPTRELAV 278
Cdd:cd17951   12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI-----------MFALEQEKKLPfIKGEGPYGLIVCPSRELAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 279 QIYEEARKFSYR------SRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLD 352
Cdd:cd17951   81 QTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 169881239 353 MGFEPQIRRIVEQDtmppKGVRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17951  161 MGFEEDIRTIFSYF----KGQRQTLLFSATMPKKIQNFAKSAL 199
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 180-392 1.38e-51

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: 177.12  E-value: 1.38e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 180 FSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgealkavkengryg 259
Cdd:cd17954    2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 260 rrKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDF 338
Cdd:cd17954   66 --PQRFFALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKS 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 169881239 339 CKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPKgvRHTMMFSATFPKEIQMLAR 392
Cdd:cd17954  144 LKFLVMDEADRLLNMDFEPEIDKILK--VIPRE--RTTYLFSATMTTKVAKLQR 193
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 180-399 3.21e-49

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: 170.56  E-value: 3.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 180 FSDIDMG-EIIMGNIELTrYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengry 258
Cdd:cd17940    1 FEDYGLKrELLMGIFEKG-FEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV------------ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 259 grrkqypI-SLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 337
Cdd:cd17940   68 -------IqALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLS 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169881239 338 FCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPKgvRHTMMFSATFPKEIQmlarDFLDEYI 399
Cdd:cd17940  141 HCKTLVLDEADKLLSQDFQPIIEKIL--NFLPKE--RQILLFSATFPLTVK----NFMDRHM 194
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 197-401 2.75e-48

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: 168.53  E-value: 2.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 197 RYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkavkengRYgRRKQYPISLVLAPTREL 276
Cdd:cd17949   10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEP-----------RV-DRSDGTLALVLVPTREL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 277 AVQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDFCKYLVLDEADRMLDMG 354
Cdd:cd17949   78 ALQIYEVLEKLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMG 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169881239 355 FEPQIRRIVE--------QDTMPPKGV-RHTMMFSATFPKEIQMLARDFLDEYIFL 401
Cdd:cd17949  158 FEKDITKILEllddkrskAGGEKSKPSrRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 179-401 8.12e-48

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 167.10  E-value: 8.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 179 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgEALKAvkENGRY 258
Cdd:cd17959    2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMI---------EKLKA--HSPTV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 259 GRRkqypiSLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 338
Cdd:cd17959   71 GAR-----ALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSS 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169881239 339 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFL 401
Cdd:cd17959  146 VEYVVFDEADRLFEMGFAEQLHEILSR--LPEN--RQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 198-395 1.56e-47

DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 166.21  E-value: 1.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 198 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYtdgpgealkavkeNGRYGRRKQYPISLVLAPTRELA 277
Cdd:cd17960   10 FTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILL-------------KRKANLKKGQVGALIISPTRELA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 278 VQIYEEARKF--SYRSRVRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMMERGKIGLDF--CKYLVLDEADRMLD 352
Cdd:cd17960   77 TQIYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKVksLEVLVLDEADRLLD 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 169881239 353 MGFEPQIRRIVEQdtmPPKGvRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17960  157 LGFEADLNRILSK---LPKQ-RRTGLFSATQTDAVEELIKAGL 195
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 185-382 1.09e-45

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: 160.95  E-value: 1.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 185 MGEIIMGnIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkavkengrygrrkQY 264
Cdd:cd17938    7 MPELIKA-VEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------------------------QI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 265 PISLVLAPTRELAVQIYEEARKFSY---RSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKY 341
Cdd:cd17938   61 VVALILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRF 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 169881239 342 LVLDEADRMLDMGFEPQIRRIVEQdtMPPKGVR----HTMMFSAT 382
Cdd:cd17938  141 FVLDEADRLLSQGNLETINRIYNR--IPKITSDgkrlQVIVCSAT 183
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 198-403 2.78e-44

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: 157.07  E-value: 2.78e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 198 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIY------TDGPGealkavkengrygrrkqypiSLVLA 271
Cdd:cd17941   10 FIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwtpEDGLG--------------------ALIIS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 272 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQirdLER--GCHLLVATPGRLVDMMERgKIGLDF--CKYLVLDEA 347
Cdd:cd17941   70 PTRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE---KERinRMNILVCTPGRLLQHMDE-TPGFDTsnLQMLVLDEA 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169881239 348 DRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAV 403
Cdd:cd17941  146 DRILDMGFKETLDAIVEN--LPKS--RQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 192-399 3.55e-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: 153.86  E-value: 3.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 192 NIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTdgpgealkavkengrygrRKQYPISLVLA 271
Cdd:cd17962    4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT------------------EHRNPSALILT 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 272 PTRELAVQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 350
Cdd:cd17962   66 PTRELAVQIEDQAKELmKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTM 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 169881239 351 LDMGFEPQIRRIVEQDTMPPKgvrhTMMFSATFPKEIQMLARDFLDEYI 399
Cdd:cd17962  146 LKMGFQQQVLDILENISHDHQ----TILVSATIPRGIEQLAGQLLQNPV 190
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 197-392 1.95e-42

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


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 153.16  E-value: 1.95e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 197 RYTRPTPVQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeaLKAVKENGRYGRRKqYPISLVLAPTRE 275
Cdd:cd17946    9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERL--------LSQKSSNGVGGKQK-PLRALILTPTRE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 276 LAVQI---YEEARKFsyrSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL---DFCKYLVLDEADR 349
Cdd:cd17946   80 LAVQVkdhLKAIAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLanlKSLRFLVLDEADR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 169881239 350 MLDMG-FEP--QIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLAR 392
Cdd:cd17946  157 MLEKGhFAEleKILELLNKDRAGKKRKRQTFVFSATLTLDHQLPLK 202
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 189-392 1.78e-39

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: 143.65  E-value: 1.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 189 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTdgpgeaLKAVKENGRYGrrkqypisL 268
Cdd:cd17942    1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK------LKFKPRNGTGV--------I 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 269 VLAPTRELAVQIYEEARKF-SYRSRVRPCVVyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKiglDF----CKYLV 343
Cdd:cd17942   67 IISPTRELALQIYGVAKELlKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTK---GFlyknLQCLI 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 169881239 344 LDEADRMLDMGFEPQIRRIVEqdtMPPKGvRHTMMFSATFPKEIQMLAR 392
Cdd:cd17942  143 IDEADRILEIGFEEEMRQIIK---LLPKR-RQTMLFSATQTRKVEDLAR 187
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 198-395 4.48e-39

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 142.85  E-value: 4.48e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 198 YTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDGPgeALKAvkengrygrrkqypisLVLAPTREL 276
Cdd:cd17939   17 FEKPSAIQQRAIvPIIKG-RDVIAQAQSGTGKTATFSIGALQRIDTTVR--ETQA----------------LVLAPTREL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 277 AVQIYE--EARKFSYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMG 354
Cdd:cd17939   78 AQQIQKvvKALGDYMGVKVHACI--GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 169881239 355 FEPQIRRIVeqdTMPPKGVRhTMMFSATFPKEIQMLARDFL 395
Cdd:cd17939  156 FKDQIYDIF---QFLPPETQ-VVLFSATMPHEVLEVTKKFM 192
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 198-395 1.41e-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: 141.57  E-value: 1.41e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 198 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeaLKAVKENGRYgrrkQYPISLVLAPTRELA 277
Cdd:cd17961   14 WEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKI--------LKAKAESGEE----QGTRALILVPTRELA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 278 VQIYEEARKFSY--RSRVRpCV-VYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL-DFCKYLVLDEADRMLDM 353
Cdd:cd17961   82 QQVSKVLEQLTAycRKDVR-VVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 169881239 354 GFEPQIRRIVEqdtMPPKGVRHTMMfSATFPKEIQMLARDFL 395
Cdd:cd17961  161 GYEEDLKSLLS---YLPKNYQTFLM-SATLSEDVEALKKLVL 198
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 198-394 5.33e-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: 139.63  E-value: 5.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 198 YTRPTPVQKHAIPIIKGK--RDLMACAQTGSGKTAAFLLPILSQIYTdgpgealkavkengrygrRKQYPISLVLAPTRE 275
Cdd:cd17963   14 FNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDP------------------TLKSPQALCLAPTRE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 276 LAVQIYEEARKF-SY-----RSRVRPCVVYGGADIGQQIrdlergchlLVATPGRLVDMMERGKIGLDFCKYLVLDEADR 349
Cdd:cd17963   76 LARQIGEVVEKMgKFtgvkvALAVPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQLDLKKIKILVLDEADV 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 169881239 350 MLDM-GFEPQIRRIVEqdtMPPKGVRhTMMFSATFPKEIQMLARDF 394
Cdd:cd17963  147 MLDTqGHGDQSIRIKR---MLPRNCQ-ILLFSATFPDSVRKFAEKI 188
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 180-395 5.48e-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: 137.19  E-value: 5.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 180 FSDIDMGEIIMGNIELTRYTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaLKAVKengry 258
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAImPCIKG-YDVIAQAQSGTGKTATFSISILQQIDTS-----LKATQ----- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 259 grrkqypiSLVLAPTRELAVQIYE--EARKFSYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL 336
Cdd:cd18046   70 --------ALVLAPTRELAQQIQKvvMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRT 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169881239 337 DFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd18046  140 DYIKMFVLDEADEMLSRGFKDQIYDIFQK--LPPD--TQVVLLSATMPNDVLEVTTKFM 194
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 424-534 6.38e-37

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 133.49  E-value: 6.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  424 DKRSFLLDILgATGSDSLTLVFVETKKGADsLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGL 503
Cdd:pfam00271   1 EKLEALLELL-KKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 169881239  504 DISNVRHVINFDLPSDIEEYVHRIGRTGRVG 534
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 201-395 2.65e-35

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


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 132.47  E-value: 2.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 201 PTPVQKHAIP-IIKGKrDLMACAQTGSGKTAAFLLPILSQIYTDgPGEalkavkengrygrrkqypIS-LVLAPTRELAV 278
Cdd:cd17950   25 PSEVQHECIPqAILGM-DVLCQAKSGMGKTAVFVLSTLQQLEPV-DGQ------------------VSvLVICHTRELAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 279 QIYEEARKFS-YRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM---LDM 353
Cdd:cd17950   85 QISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleqLDM 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 169881239 354 gfepqiRRIVeQD--TMPPKGvRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17950  165 ------RRDV-QEifRATPHD-KQVMMFSATLSKEIRPVCKKFM 200
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 198-400 2.21e-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: 129.31  E-value: 2.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 198 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPilsqiytdgpgeALKAVKengrygRRKQYPISLVLAPTRELA 277
Cdd:cd17943   10 FQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVI------------ALESLD------LERRHPQVLILAPTREIA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 278 VQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 356
Cdd:cd17943   72 VQIHDVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQ 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 169881239 357 PQIRRIveqDTMPPKGvRHTMMFSATFPKE-IQMLARdFLDEYIF 400
Cdd:cd17943  151 KDVNWI---FSSLPKN-KQVIAFSATYPKNlDNLLAR-YMRKPVL 190
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 198-397 2.72e-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: 123.73  E-value: 2.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 198 YTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTdgpgealkAVKEngrygrrkqyPISLVLAPTREL 276
Cdd:cd18045   19 FEKPSAIQQRAIkPIIKG-RDVIAQSQSGTGKTATFSISVLQCLDI--------QVRE----------TQALILSPTREL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 277 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 356
Cdd:cd18045   80 AVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 169881239 357 PQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDE 397
Cdd:cd18045  160 EQIYDVYRY--LPPA--TQVVLVSATLPQDILEMTNKFMTD 196
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 195-385 1.02e-30

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 120.16  E-value: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 195 LTRY--TRPTPVQKHAIP-IIKGKRDLMAcAQTGSGKTAAFLLPILSQIYTDgpgEALKAVKENGrygrrkqyPISLVLA 271
Cdd:cd17948    5 LQRQgiTKPTTVQKQGIPsILRGRNTLCA-AETGSGKTLTYLLPIIQRLLRY---KLLAEGPFNA--------PRGLVIT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 272 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIgQQIRDLERG-CHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 350
Cdd:cd17948   73 PSRELAEQIGSVAQSLTEGLGLKVKVITGGRTK-RQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTL 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 169881239 351 LDMGFEPQIRRIVEQ-----------DTMPPKGvrHTMMFSATFPK 385
Cdd:cd17948  152 LDDSFNEKLSHFLRRfplasrrsentDGLDPGT--QLVLVSATMPS 195
HELICc smart00490
helicase superfamily c-terminal domain;
453-534 1.66e-30

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 114.62  E-value: 1.66e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239   453 DSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGR 532
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 169881239   533 VG 534
Cdd:smart00490  81 AG 82
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 203-395 3.18e-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: 118.03  E-value: 3.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 203 PVQ-KHAIPIIKGKrDLMACAQTGSGKTAAFLLPILsqiytdgpgEALKAVKENGRYGRRkqyPISLVLAPTRELAVQIY 281
Cdd:cd17944   15 PIQvKTFHPVYSGK-DLIAQARTGTGKTFSFAIPLI---------EKLQEDQQPRKRGRA---PKVLVLAPTRELANQVT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 282 EEARKFSYRSRVrpCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRR 361
Cdd:cd17944   82 KDFKDITRKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 169881239 362 IV-EQDTMPPKGVRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17944  160 ILsVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 197-390 4.17e-26

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: 106.95  E-value: 4.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 197 RYTRPTPVQKHAIP-IIKG--------KRDLMACAQTGSGKTAAFLLPILsQIYTDGPGEALKAvkengrygrrkqypis 267
Cdd:cd17956    9 GITSAFPVQAAVIPwLLPSskstppyrPGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVPRLRA---------------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 268 LVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL--------LVATPGRLVDMMERGK-IGLDF 338
Cdd:cd17956   72 LIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGrylsrvdiLVATPGRLVDHLNSTPgFTLKH 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169881239 339 CKYLVLDEADRMLDMGFE---PQIRRIVEQDTMP------------PKGVR-HTMMFSATF---PKEIQML 390
Cdd:cd17956  152 LRFLVIDEADRLLNQSFQdwlETVMKALGRPTAPdlgsfgdanlleRSVRPlQKLLFSATLtrdPEKLSSL 222
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 185-394 2.03e-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: 102.84  E-value: 2.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 185 MGEIIMGNIELTRYTRPTPVQKHAIPIIKGKR----------------DLMACAQTGSGKTAAFLLPILSQIY---TDGP 245
Cdd:cd17965   15 IKEILKGSNKTDEEIKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKrqeQEPF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 246 GEALKAVKENGRYGRrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVV-YGGADIGQQIRDLERG-CHLLVATPG 323
Cdd:cd17965   95 EEAEEEYESAKDTGR----PRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLAFKGrIDILVTTPG 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169881239 324 RLVDMME-RGKIgLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgVRHTMMFSATFPKEIQMLARDF 394
Cdd:cd17965  171 KLASLAKsRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APK--LKHLILCSATIPKEFDKTLRKL 237
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
213-529 5.79e-22

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 100.10  E-value: 5.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 213 KGKRDLMACAQTGSGKTAAfllpilsqiytdgpgeALKAVKENGRYGRrkqypiSLVLAPTRELAVQIYEEARKFsyrsr 292
Cdd:COG1061   98 RGGGRGLVVAPTGTGKTVL----------------ALALAAELLRGKR------VLVLVPRRELLEQWAEELRRF----- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 293 vrpcvvYGGADIGQQIRDleRGCHLLVATPGRLVDMMERGKIGlDFCKYLVLDEADRmldmGFEPQIRRIVEQdtMPPKg 372
Cdd:COG1061  151 ------LGDPLAGGGKKD--SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEA--FPAA- 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 373 vrHTMMFSAT------FPKEI-------------QMLARDFLDEYIFLAV--------GRVGSTSENITQKVVwVEDLDK 425
Cdd:COG1061  215 --YRLGLTATpfrsdgREILLflfdgivyeyslkEAIEDGYLAPPEYYGIrvdltderAEYDALSERLREALA-ADAERK 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 426 RSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI 505
Cdd:COG1061  292 DKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371

                        330       340
                 ....*....|....*....|....
gi 169881239 506 SNVRHVINFDLPSDIEEYVHRIGR 529
Cdd:COG1061  372 PRLDVAILLRPTGSPREFIQRLGR 395
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
302-556 5.85e-21

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 96.75  E-value: 5.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 302 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdfckyLVLDEA--------DrmldmgFEP---QIRRIVE 364
Cdd:COG0514   94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 365 QDTMPPkgvrhTMMFSATFPKE-----IQMLARDflDEYIFLA-VGRvgstsENITQKVVWVEDLDKRSFLLDILGATGS 438
Cdd:COG0514  163 RLPNVP-----VLALTATATPRvradiAEQLGLE--DPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPG 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 439 DSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATaVA-ARGLDISNVRHVINFDLP 517
Cdd:COG0514  231 GS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLP 308

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 169881239 518 SDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLD 556
Cdd:COG0514  309 KSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 177-391 4.85e-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: 83.53  E-value: 4.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 177 IENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGK--RDLMACAQTGSGKTAAFLLPILSqiytdgpgealkavke 254
Cdd:cd18048   17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLS---------------- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 255 ngRYGRRKQYPISLVLAPTRELAVQ---IYEEARKFSYRSRV----RPCVVYGGADIGQQIrdlergchlLVATPGRLVD 327
Cdd:cd18048   81 --RVDALKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQViyaiRGNRPGKGTDIEAQI---------VIGTPGTVLD 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169881239 328 MMERGK-IGLDFCKYLVLDEADRMLDM-GFEPQIRRIveQDTMPPKGvrHTMMFSATFPKEIQMLA 391
Cdd:cd18048  150 WCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRV--KRSMPKEC--QMLLFSATFEDSVWAFA 211
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
425-532 1.63e-14

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 77.08  E-value: 1.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 425 KRSFLLDILG---ATGSDSLTLVFVETKKGADSLEDFLYHEGYACT------SIHGDR--SQRDREEALHQFRSGKSPIL 493
Cdd:COG1111  336 KLSKLREILKeqlGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGEFNVL 415

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 169881239 494 VATAVAARGLDISNVRHVINFDL-PSDIeEYVHRIGRTGR 532
Cdd:COG1111  416 VATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR 454
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 442-529 5.39e-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: 69.54  E-value: 5.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 442 TLVFVETKKGADSLEDFLYHEGYACTSI-------HGDRSQ--------RDREEALHQFRSGKSPILVATAVAARGLDIS 506
Cdd:cd18802   28 GIIFVERRATAVVLSRLLKEHPSTLAFIrcgfligRGNSSQrkrslmtqRKQKETLDKFRDGELNLLIATSVLEEGIDVP 107

                         90       100
                 ....*....|....*....|...
gi 169881239 507 NVRHVINFDLPSDIEEYVHRIGR 529
Cdd:cd18802  108 ACNLVIRFDLPKTLRSYIQSRGR 130
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 220-382 1.43e-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: 68.58  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 220 ACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengrygrrkqypiSLVLAPTRELAVQIYEEARK-FSYRSRVRpcVV 298
Cdd:cd00046    6 ITAPTGSGKTLAALLAALLLLLKKGKK--------------------VLVLVPTKALALQTAERLRElFGPGIRVA--VL 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 299 YGGADIGQQIRDLERGCHLLVATPGRLVDMMER-GKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMpPKGVRhTM 377
Cdd:cd00046   64 VGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAG-LKNAQ-VI 141


                 ....*
gi 169881239 378 MFSAT 382
Cdd:cd00046  142 LLSAT 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 178-391 2.53e-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: 69.36  E-value: 2.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 178 ENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGK--RDLMACAQTGSGKTAAFLLPILSQIytdgpGEALKavken 255
Cdd:cd18047    1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-----EPANK----- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 256 grygrrkqYPISLVLAPTRELAVQ---IYEEARKFSyrsrvrPCVVYGGADIGQQirdLERGC----HLLVATPGRLVDM 328
Cdd:cd18047   71 --------YPQCLCLSPTYELALQtgkVIEQMGKFY------PELKLAYAVRGNK---LERGQkiseQIVIGTPGTVLDW 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169881239 329 MERGK-IGLDFCKYLVLDEADRML-DMGFEPQIRRIveqDTMPPKGVRhTMMFSATFPKEIQMLA 391
Cdd:cd18047  134 CSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRI---QRMLPRNCQ-MLLFSATFEDSVWKFA 194
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 410-534 1.25e-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: 65.31  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 410 SENITQKVVWVEDLDKRSFLLD-ILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSG 488
Cdd:cd18794    1 RPNLFYSVRPKDKKDEKLDLLKrIKVEHLGGS-GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 169881239 489 KSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVG 534
Cdd:cd18794   80 KIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 443-528 6.01e-12

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 63.26  E-value: 6.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 443 LVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP--ILVATAVAARGLDISNVRHVINFDL---P 517
Cdd:cd18793   31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPwwnP 110

                         90
                 ....*....|....
gi 169881239 518 SDIE---EYVHRIG 528
Cdd:cd18793  111 AVEEqaiDRAHRIG 124
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 199-539 3.98e-10

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 62.93  E-value: 3.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 199 TRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEAlkavkengrygrrkqypisLVLAPTRELAV 278
Cdd:COG1205   55 ERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGATA-------------------LYLYPTKALAR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 279 QIYEEARKF--SYRSRVRPCVVYGgaDIGQQIRD--LERGcHLLVATPgrlvDMMERgkiGL--------DF---CKYLV 343
Cdd:COG1205  116 DQLRRLRELaeALGLGVRVATYDG--DTPPEERRwiREHP-DIVLTNP----DMLHY---GLlphhtrwaRFfrnLRYVV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 344 LDEA---------------DRMldmgfepqiRRIVEQdtmppKGVRHTMMF-SATF--PKEiqmLARDFLDEYiFLAVGR 405
Cdd:COG1205  186 IDEAhtyrgvfgshvanvlRRL---------RRICRH-----YGSDPQFILaSATIgnPAE---HAERLTGRP-VTVVDE 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 406 VGSTSENITQkVVW----VEDLDKRSFLL---DILG-ATGSDSLTLVFVETKKGA----DSLEDFLYHEGYAcTSIHGDR 473
Cdd:COG1205  248 DGSPRGERTF-VLWnpplVDDGIRRSALAeaaRLLAdLVREGLRTLVFTRSRRGAellaRYARRALREPDLA-DRVAAYR 325

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 474 SQ---RDREEALHQFRSGKSPILVAT-AVAArGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLA 539
Cdd:COG1205  326 AGylpEERREIERGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 443-533 6.23e-10

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 62.16  E-value: 6.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 443 LVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP--ILVATAVAARGLDISNVRHVINFDLP--S 518
Cdd:COG0553  553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWwnP 632

                         90
                 ....*....|....*....
gi 169881239 519 DIEEY----VHRIGRTGRV 533
Cdd:COG0553  633 AVEEQaidrAHRIGQTRDV 651
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 474-532 1.58e-09

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 56.60  E-value: 1.58e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 474 SQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFD-LPSDIeEYVHRIGRTGR 532
Cdd:cd18801   75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 492-532 7.24e-09

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 52.71  E-value: 7.24e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 169881239 492 ILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGR 532
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
202-534 7.63e-09

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 58.75  E-value: 7.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 202 TPVQKHAIP--IIKGKRdLMACAQTGSGKTAafllpiLSQIYtdgpgeALKAVKENGRygrrkqypiSLVLAPTRELAVQ 279
Cdd:COG1204   24 YPPQAEALEagLLEGKN-LVVSAPTASGKTL------IAELA------ILKALLNGGK---------ALYIVPLRALASE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 280 IYEEARKFSYRSRVRPCVVYGGADIGqqIRDLERgCHLLVATPGRLvDMMERGKIGL--DFcKYLVLDEA---------- 347
Cdd:COG1204   82 KYREFKRDFEELGIKVGVSTGDYDSD--DEWLGR-YDILVATPEKL-DSLLRNGPSWlrDV-DLVVVDEAhliddesrgp 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 348 ------DRMLDMGFEPQIrriveqdtmppkgvrhtmMF-SATF--PKEI-QMLARDF---------LDEYIFLAvGRVGS 408
Cdd:COG1204  157 tlevllARLRRLNPEAQI------------------VAlSATIgnAEEIaEWLDAELvksdwrpvpLNEGVLYD-GVLRF 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 409 TSENITQKVVWVedldkrSFLLDILGATGSdslTLVFVETKKGADSL------------------------EDFL----- 459
Cdd:COG1204  218 DDGSRRSKDPTL------ALALDLLEEGGQ---VLVFVSSRRDAESLakkladelkrrltpeereeleelaEELLevsee 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 460 YHEGYACTSI--------HGDRSQRDREEALHQFRSGKSPILVATAVAARGLdisN--VRHVI------NFDLPSDIEEY 523
Cdd:COG1204  289 THTNEKLADClekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEF 365

                        410
                 ....*....|.
gi 169881239 524 VHRIGRTGRVG 534
Cdd:COG1204  366 KQMAGRAGRPG 376
PRK13766 PRK13766
Hef nuclease; Provisional
 439-532 1.90e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 57.58  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 439 DSLTLVFVETKKGADSLEDFLYHEGYAC------TSIHGDR--SQRDREEALHQFRSGKSPILVATAVAARGLDISNVRH 510
Cdd:PRK13766 365 DSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444

                         90       100
                 ....*....|....*....|...
gi 169881239 511 VINFD-LPSDIeEYVHRIGRTGR 532
Cdd:PRK13766 445 VIFYEpVPSEI-RSIQRKGRTGR 466
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 200-382 3.25e-08

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 53.96  E-value: 3.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 200 RPTPVQKHAIPIIKG------KRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkAVKENGRYgrrkqypiSLVLAPT 273
Cdd:cd17918   15 SLTKDQAQAIKDIEKdlhspePMDRLLSGDVGSGKTLVALGAAL-------------LAYKNGKQ--------VAILVPT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 274 RELAVQIYEEARKfsYRSRVRPCVVYGG--ADIGQQIrDLERGCHLLVAtpgrlvdmMERGKIGLDFckyLVLDEADRMl 351
Cdd:cd17918   74 EILAHQHYEEARK--FLPFINVELVTGGtkAQILSGI-SLLVGTHALLH--------LDVKFKNLDL---VIVDEQHRF- 138

                        170       180       190
                 ....*....|....*....|....*....|.
gi 169881239 352 dmgfepqirRIVEQDTMPPKGVRHTMMFSAT 382
Cdd:cd17918  139 ---------GVAQREALYNLGATHFLEATAT 160
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
197-250 3.62e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 53.57  E-value: 3.62e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169881239 197 RYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKT-AAFlLPILSQIYTDGPGEALK 250
Cdd:COG1201   21 RFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELP 74
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 205-347 4.24e-07

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: 50.66  E-value: 4.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 205 QKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgealkavkengrYGRRkqypiSLVLAPTRELAVQIYEEA 284
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD--------------PGSR-----ALYLYPTKALAQDQLRSL 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169881239 285 RKF--SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPgrlvDMME-----RGKIGLDFC---KYLVLDEA 347
Cdd:cd17923   66 RELleQLGLGIRVATYDGDTPREERRAIIRNPPRILLTNP----DMLHyallpHHDRWARFLrnlRYVVLDEA 134
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 206-383 3.08e-06

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: 47.30  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 206 KHAIPIIKGKRDLMACAQTGSGKTA-AFLLPILsqiytdgpgealkavkengrygrRKQYPIsLVLAPTRELAVQIYEEA 284
Cdd:cd17926    9 LEAWLAHKNNRRGILVLPTGSGKTLtALALIAY-----------------------LKELRT-LIVVPTDALLDQWKERF 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 285 RKFSYRSRVrpCVVYGGADIGQqirdleRGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRmldmGFEPQIRRIVE 364
Cdd:cd17926   65 EDFLGDSSI--GLIGGGKKKDF------DDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEILK 132

                        170
                 ....*....|....*....
gi 169881239 365 QDTMPPKgvrhtMMFSATF 383
Cdd:cd17926  133 ELNAKYR-----LGLTATP 146
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 215-347 5.93e-06

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: 47.65  E-value: 5.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 215 KRDLMACAQTGSGKT--AAFLLPILSQIytdgpgeaLKAVKENGRygrrkqypISLVLAPTRELAVQIYEEARKFSYrSR 292
Cdd:cd18034   16 KRNTIVVLPTGSGKTliAVMLIKEMGEL--------NRKEKNPKK--------RAVFLVPTVPLVAQQAEAIRSHTD-LK 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169881239 293 VRPCvvYGGADIGQQIRDLERGC----HLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 347
Cdd:cd18034   79 VGEY--SGEMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 460-556 6.71e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 49.33  E-value: 6.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 460 YHEGYactsihgDRSQRDR-EEAlhqFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGL 538
Cdd:PRK11057 266 YHAGL-------DNDVRADvQEA---FQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAE 335

                         90
                 ....*....|....*...
gi 169881239 539 ATSFFNEKNMNITKDLLD 556
Cdd:PRK11057 336 AMLFYDPADMAWLRRCLE 353
PRK13767 PRK13767
ATP-dependent helicase; Provisional
 197-322 7.91e-06

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 49.11  E-value: 7.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 197 RYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALkavkENGRYgrrkqypiSLVLAPTREL 276
Cdd:PRK13767  29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGEL----EDKVY--------CLYVSPLRAL 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 169881239 277 A-----------VQIYEEARKFSYR-SRVRPCVVYGGADIGQQIRDLERGCHLLVATP 322
Cdd:PRK13767  97 NndihrnleeplTEIREIAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTP 154
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 202-347 1.23e-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: 46.10  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 202 TPVQKHAI-PIIKGKRDLMACAQTGSGKTAAFLLPIlsqiytdgpgeaLKAVKENGRygrrkqypISLVLAPTRELAVQI 280
Cdd:cd17921    3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAI------------LRALATSGG--------KAVYIAPTRALVNQK 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169881239 281 YEEARKFSYRSRVRPCVVYGGADIGqqiRDLERGCHLLVATPGRLVDMMERGKIGLDF-CKYLVLDEA 347
Cdd:cd17921   63 EADLRERFGPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGERLIQdVRLVVVDEA 127
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
 469-534 1.53e-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: 42.33  E-value: 1.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169881239 469 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVI-----NFDLpSDIEEYVHRIGRTGRVG 534
Cdd:cd18810   57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGL-AQLYQLRGRVGRSKERA 126
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
 342-534 1.54e-04

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


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 44.37  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  342 LVLDEADRMLDmgfEPQIRRIVEQDTMPPKGVRHTMMfSATFPKEIQMLARDFldEYIFLAVGRVGSTSENITQKVVWVE 421
Cdd:TIGR01587 128 LIFDEVHFYDE---YTLALILAVLEVLKDNDVPILLM-SATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILI 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  422 DLDKR---SFLLDILGATGSDSLTLVFVET-----------KKGADSLEDFLYHEGYActsiHGDRSQRDREEALHQFRS 487
Cdd:TIGR01587 202 ESDKVgeiSSLERLLEFIKKGGSIAIIVNTvdraqefyqqlKEKAPEEEIILYHSRFT----EKDRAKKEAELLREMKKS 277

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 169881239  488 GKSPILVATAVAARGLDISnvrhvinFDL----PSDIEEYVHRIGRTGRVG 534
Cdd:TIGR01587 278 NEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYG 321
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 442-529 2.77e-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: 41.01  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 442 TLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDRE-EALHQFRSGKS--PILVATAVAARGLDISNVRHVInFDLP- 517
Cdd:cd18799    9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV-FLRPt 87

                         90
                 ....*....|...
gi 169881239 518 -SDIeEYVHRIGR 529
Cdd:cd18799   88 eSRT-LFLQMLGR 99
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 442-532 3.41e-04

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: 41.48  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 442 TLVFVETKKGADSLED---FLYHEGYACTSI---HG--DRSQRDR-EEALhqfRSGKSPILVATAVAARGLDISNVRHVI 512
Cdd:cd18796   41 TLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAAL---KRGDLKVVVATSSLELGIDIGDVDLVI 117

                         90       100
                 ....*....|....*....|
gi 169881239 513 NFDLPSDIEEYVHRIGRTGR 532
Cdd:cd18796  118 QIGSPKSVARLLQRLGRSGH 137
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 469-543 3.51e-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: 41.47  E-value: 3.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169881239 469 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI--SNVRHVINFDLPSDiEEYVHRIGRTGRVGNLGLATSFF 543
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 ...
 469-534 1.06e-03

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 40.33  E-value: 1.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169881239 469 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVI-----NFDLpSDIEEYVHRIGRTGRVG 534
Cdd:cd18792   66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIiedadRFGL-SQLHQLRGRVGRGKHQS 135
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 204-331 1.22e-03

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 40.80  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 204 VQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgEALKAVKENGRYGRRKQYpislvLAPTRELAVQIYE 282
Cdd:cd18023    5 IQSEVFPdLLYSDKNFVVSAPTGSGKTVLFELAIL---------RLLKERNPLPWGNRKVVY-----IAPIKALCSEKYD 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169881239 283 EAR-KFsyrSRVRPCVVYGGADigQQIRDLE--RGCHLLVATPGRLvDMMER 331
Cdd:cd18023   71 DWKeKF---GPLGLSCAELTGD--TEMDDTFeiQDADIILTTPEKW-DSMTR 116
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 215-349 1.29e-03

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 40.19  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 215 KRDLMACAQTGSGKTAAFLLPILSQIytdgpgealkaVKENGRYgrrkqypisLVLAPTRELAVQIYEEARKFsyRSRVR 294
Cdd:cd18035   16 NGNTLIVLPTGLGKTIIAILVAADRL-----------TKKGGKV---------LILAPSRPLVEQHAENLKRV--LNIPD 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169881239 295 PCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADR 349
Cdd:cd18035   74 KITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 216-346 2.16e-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: 39.49  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 216 RDLMACAQTGSGKTAAFLLPILSQIYtDGPGEALKAvkengrygrrkqypisLVLAPTRELAVQIYE------EARKFSY 289
Cdd:cd17922    2 RNVLIAAPTGSGKTEAAFLPALSSLA-DEPEKGVQV----------------LYISPLKALINDQERrleeplDEIDLEI 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169881239 290 RSRVRpcvvYGgaDIGQQIRD--LERGCHLLVATPGRLVDMMERGKIGLDF--CKYLVLDE 346
Cdd:cd17922   65 PVAVR----HG--DTSQSEKAkqLKNPPGILITTPESLELLLVNKKLRELFagLRYVVVDE 119
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 203-387 2.61e-03

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 39.24  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 203 PVQKHAIP--IIKGKRdLMACAQTGSGKTaafLLPILSqiytdgpgeALKAVKENGRygrrkqypiSLVLAPTRELAVQI 280
Cdd:cd18028    4 PPQAEAVRagLLKGEN-LLISIPTASGKT---LIAEMA---------MVNTLLEGGK---------ALYLVPLRALASEK 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 281 YEEarkFSYRSRVrpcvvygGADIGQQIRDLERG------CHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMG 354
Cdd:cd18028   62 YEE---FKKLEEI-------GLKVGISTGDYDEDdewlgdYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEE 131

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 169881239 355 FEPQIRRIVEQDTMPPKGVRhTMMFSATF--PKEI 387
Cdd:cd18028  132 RGPTLESIVARLRRLNPNTQ-IIGLSATIgnPDEL 165
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
 468-577 2.65e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.06  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  468 SIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTG-RVGnlGLATSFFNEK 546
Cdd:PRK09751  306 SHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGLFFPR 383

                          90       100       110
                  ....*....|....*....|....*....|.
gi 169881239  547 NmniTKDLLDLLVEAKQEVPSWLENMAYEHH 577
Cdd:PRK09751  384 T---RRDLVDSAVIVECMFAGRLENLTPPHN 411
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 469-532 4.35e-03

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: 38.48  E-value: 4.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 469 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISN-----VRHVINFDLPSdieeyVHRI-GRTGR 532
Cdd:cd18811   67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGR 131
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 439-533 6.26e-03

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 39.78  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  439 DSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFR---SGKSPILVATAVAARGLDISNVRHVINFD 515
Cdd:PLN03142  487 DSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkpgSEKFVFLLSTRAGGLGINLATADIVILYD 566

                          90       100
                  ....*....|....*....|....*.
gi 169881239  516 lpSD--------IEEYVHRIGRTGRV 533
Cdd:PLN03142  567 --SDwnpqvdlqAQDRAHRIGQKKEV 590
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 442-532 7.57e-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: 38.00  E-value: 7.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239 442 TLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDlpSDIE 521
Cdd:cd18790   30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKE 107

                         90
                 ....*....|....*...
gi 169881239 522 EY-------VHRIGRTGR 532
Cdd:cd18790  108 GFlrsetslIQTIGRAAR 125
ResIII pfam04851
Type III restriction enzyme, res subunit;
201-384 8.35e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 37.65  E-value: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  201 PTPVQKHAI-----PIIKGKRDLMACAQTGSGKTaafllpilsqiYTdgpgeALKAVKEngrygRRKQYPIS--LVLAPT 273
Cdd:pfam04851   4 LRPYQIEAIenlleSIKNGQKRGLIVMATGSGKT-----------LT-----AAKLIAR-----LFKKGPIKkvLFLVPR 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169881239  274 RELAVQIYEEARKFSyrsrvrPCVVYGGADIGQQIRDLERG-CHLLVATPGRLV--DMMERGKIGLDFCKYLVLDEADRm 350
Cdd:pfam04851  63 KDLLEQALEEFKKFL------PNYVEIGEIISGDKKDESVDdNKIVVTTIQSLYkaLELASLELLPDFFDVIIIDEAHR- 135

                         170       180       190
                  ....*....|....*....|....*....|....
gi 169881239  351 ldmGFEPQIRRIVEQDTmPPKGVRhtmmFSATFP 384
Cdd:pfam04851 136 ---SGASSYRNILEYFK-PAFLLG----LTATPE 161
 
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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