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Conserved domains on  [gi|2217401332|ref|XP_047298732|]
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ATP-dependent RNA helicase DDX3Y isoform X2 [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 ...
 155-405 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: 589.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 155 FEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPIL 234
Cdd:cd18051     1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 235 SQIYTDGPGEALkaVKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 314
Cdd:cd18051    81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 315 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 394
Cdd:cd18051   159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238

                         250
                  ....*....|.
gi 2217401332 395 YIFLAVGRVGS 405
Cdd:cd18051   239 YIFLAVGRVGS 249
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 410-532 2.41e-56

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: 186.56  E-value: 2.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 410 ITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 489
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217401332 490 LVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGN 532
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGR 123
 
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 ...
 155-405 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: 589.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 155 FEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPIL 234
Cdd:cd18051     1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 235 SQIYTDGPGEALkaVKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 314
Cdd:cd18051    81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 315 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 394
Cdd:cd18051   159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238

                         250
                  ....*....|.
gi 2217401332 395 YIFLAVGRVGS 405
Cdd:cd18051   239 YIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
176-532 8.91e-164

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 475.02  E-value: 8.91e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 176 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEalkavkengry 255
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA----------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 256 grrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 335
Cdd:COG0513    72 ------PQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 336 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 415
Cdd:COG0513   146 VETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYY 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 416 WVEDLDKRSFLLDILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 495
Cdd:COG0513   222 LVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2217401332 496 AARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGN 532
Cdd:COG0513   301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGA 337
PTZ00110 PTZ00110
helicase; Provisional
 167-568 4.30e-120

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 367.56  E-value: 4.30e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 167 GSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeal 246
Cdd:PTZ00110  122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI--------- 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 247 kAVKENGRYGrrkQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMM 326
Cdd:PTZ00110  193 -NAQPLLRYG---DGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFL 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 327 ERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL-DEYIFLAVGRVG- 404
Cdd:PTZ00110  269 ESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDl 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 405 STSENITQKVVWVEDLDKRSFLLDILGATGSD-SLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFR 483
Cdd:PTZ00110  345 TACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFK 424

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 484 SGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGN-----------------------LEAKQEVP 540
Cdd:PTZ00110  425 TGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAkgasytfltpdkyrlardlvkvlREAKQPVP 504

                         410       420
                  ....*....|....*....|....*...
gi 2217401332 541 SWLENMAYEHHYKGGSRGRSKSNRFSGG 568
Cdd:PTZ00110  505 PELEKLSNERSNGTERRRWGGYGRFSNN 532
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 199-387 1.14e-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: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 199 TPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengrygrrkqyPISLVLAPTRELAVQIY 278
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG------------------PQALVLAPTRELAEQIY 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 279 EEARKFSYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDFCKYLVLDEADRMLDMGFEPQIRR 358
Cdd:pfam00270  63 EELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEE 140

                         170       180
                  ....*....|....*....|....*....
gi 2217401332 359 IVEQdtMPPKgvRHTMMFSATFPKEIQML 387
Cdd:pfam00270 141 ILRR--LPKK--RQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
190-413 9.06e-58

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 193.09  E-value: 9.06e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332  190 IELTRYTRPTPVQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkavkengRYGRRKQYPISLVLA 268
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-------------------EALKRGKGGRVLVLV 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332  269 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 347
Cdd:smart00487  62 PTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRL 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217401332  348 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRvgSTSENITQK 413
Cdd:smart00487 142 LDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 410-532 2.41e-56

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: 186.56  E-value: 2.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 410 ITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 489
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217401332 490 LVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGN 532
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGR 123
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 421-531 5.08e-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: 5.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 421 DKRSFLLDILgATGSDSLTLVFVETKKGADsLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGL 500
Cdd:pfam00271   1 EKLEALLELL-KKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217401332 501 DISNVRHVINFDLPSDIEEYVHRIGRTGRVG 531
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
450-531 1.66e-30

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 114.23  E-value: 1.66e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332  450 DSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGR 529
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 2217401332  530 VG 531
Cdd:smart00490  81 AG 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
299-529 5.23e-20

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 93.67  E-value: 5.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 299 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdfckyLVLDEA--------DrmldmgFEP---QIRRIVE 361
Cdd:COG0514    94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 362 QDTMPPkgvrhTMMFSATFPKE-----IQMLARDflDEYIFLA-VGRvgstsENITQKVVWVEDLDKRSFLLDILGATGS 435
Cdd:COG0514   163 RLPNVP-----VLALTATATPRvradiAEQLGLE--DPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPG 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 436 DSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATaVA-ARGLDISNVRHVINFDLP 514
Cdd:COG0514   231 GS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLP 308

                         250
                  ....*....|....*
gi 2217401332 515 SDIEEYVHRIGRTGR 529
Cdd:COG0514   309 KSIEAYYQEIGRAGR 323
PRK13766 PRK13766
Hef nuclease; Provisional
 436-529 1.82e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 57.58  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 436 DSLTLVFVETKKGADSLEDFLYHEGYAC------TSIHGDR--SQRDREEALHQFRSGKSPILVATAVAARGLDISNVRH 507
Cdd:PRK13766  365 DSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444

                          90       100
                  ....*....|....*....|...
gi 2217401332 508 VINFD-LPSDIeEYVHRIGRTGR 529
Cdd:PRK13766  445 VIFYEpVPSEI-RSIQRKGRTGR 466
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
 339-552 7.36e-05

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: 45.52  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 339 LVLDEADRMLDmgfEPQIRRIVEQDTMPPKGVRHTMMfSATFPKEIQMLARDFldEYIFLAVGRVGSTSENITQKVVWVE 418
Cdd:TIGR01587 128 LIFDEVHFYDE---YTLALILAVLEVLKDNDVPILLM-SATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILI 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 419 DLDKR---SFLLDILGATGSDSLTLVFVET-----------KKGADSLEDFLYHEGYActsiHGDRSQRDREEALHQFRS 484
Cdd:TIGR01587 202 ESDKVgeiSSLERLLEFIKKGGSIAIIVNTvdraqefyqqlKEKAPEEEIILYHSRFT----EKDRAKKEAELLREMKKS 277

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217401332 485 GKSPILVATAVAARGLDISnvrhvinFDL----PSDIEEYVHRIGRTGRVGNLEAKQ-EVPSWLENMAYEHHY 552
Cdd:TIGR01587 278 NEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYGRKIGENfEVYIITIAPEGKLFP 343
 
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 ...
 155-405 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: 589.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 155 FEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPIL 234
Cdd:cd18051     1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 235 SQIYTDGPGEALkaVKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 314
Cdd:cd18051    81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 315 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 394
Cdd:cd18051   159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238

                         250
                  ....*....|.
gi 2217401332 395 YIFLAVGRVGS 405
Cdd:cd18051   239 YIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
176-532 8.91e-164

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 475.02  E-value: 8.91e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 176 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEalkavkengry 255
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA----------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 256 grrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 335
Cdd:COG0513    72 ------PQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 336 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 415
Cdd:COG0513   146 VETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYY 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 416 WVEDLDKRSFLLDILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 495
Cdd:COG0513   222 LVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2217401332 496 AARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGN 532
Cdd:COG0513   301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGA 337
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 177-404 3.26e-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: 3.26e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 177 FSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkavkENGRYG 256
Cdd:cd17967     2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGP--------PSVGRG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 257 RRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFC 336
Cdd:cd17967    74 RRKAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217401332 337 KYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVG 404
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 ...
 134-404 2.94e-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: 2.94e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 134 PLPPSERlEQELFSGGNTGINFEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKR 213
Cdd:cd18052     3 PPPPPED-EDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 214 DLMACAQTGSGKTAAFLLPILSQIYTDGpgeaLKAVKENGrygrrKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPC 293
Cdd:cd18052    82 DLMACAQTGSGKTAAFLLPVLTGMMKEG----LTASSFSE-----VQEPQALIVAPTRELANQIFLEARKFSYGTCIRPV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 294 VVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHT 373
Cdd:cd18052   153 VVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQT 232

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2217401332 374 MMFSATFPKEIQMLARDFLDE-YIFLAVGRVG 404
Cdd:cd18052   233 LMFSATFPEEIQRLAAEFLKEdYLFLTVGRVG 264
PTZ00110 PTZ00110
helicase; Provisional
 167-568 4.30e-120

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 367.56  E-value: 4.30e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 167 GSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeal 246
Cdd:PTZ00110  122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI--------- 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 247 kAVKENGRYGrrkQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMM 326
Cdd:PTZ00110  193 -NAQPLLRYG---DGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFL 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 327 ERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL-DEYIFLAVGRVG- 404
Cdd:PTZ00110  269 ESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDl 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 405 STSENITQKVVWVEDLDKRSFLLDILGATGSD-SLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFR 483
Cdd:PTZ00110  345 TACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFK 424

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 484 SGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGN-----------------------LEAKQEVP 540
Cdd:PTZ00110  425 TGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAkgasytfltpdkyrlardlvkvlREAKQPVP 504

                         410       420
                  ....*....|....*....|....*...
gi 2217401332 541 SWLENMAYEHHYKGGSRGRSKSNRFSGG 568
Cdd:PTZ00110  505 PELEKLSNERSNGTERRRWGGYGRFSNN 532
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 186-398 3.09e-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: 3.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 186 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkavkengrygRRKQYPISL 265
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK--------------KKGRGPQAL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 266 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 345
Cdd:cd00268    67 VLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEAD 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217401332 346 RMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFL 398
Cdd:cd00268   147 RMLDMGFEEDVEKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 195-532 9.34e-94

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 296.33  E-value: 9.34e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 195 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgealkavkeNGRYgRRKQypiSLVLAPTRELA 274
Cdd:PRK11776   24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--------------DVKR-FRVQ---ALVLCPTRELA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 275 VQIYEEARKFSyrsRVRP-------CvvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 347
Cdd:PRK11776   86 DQVAKEIRRLA---RFIPnikvltlC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 348 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYifLAVgRVGSTSEN--ITQKVVWVEDLDKRSF 425
Cdd:PRK11776  160 LDMGFQDAIDAIIRQ--APAR--RQTLLFSATYPEGIAAISQRFQRDP--VEV-KVESTHDLpaIEQRFYEVSPDERLPA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 426 LLDILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNV 505
Cdd:PRK11776  233 LQRLLLHHQPES-CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311

                         330       340
                  ....*....|....*....|....*..
gi 2217401332 506 RHVINFDLPSDIEEYVHRIGRTGRVGN 532
Cdd:PRK11776  312 EAVINYELARDPEVHVHRIGRTGRAGS 338
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 176-529 2.06e-92

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 292.87  E-value: 2.06e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 176 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkAVKengry 255
Cdd:PRK10590    2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQP-----HAK----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 256 GRRkqyPI-SLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 334
Cdd:PRK10590   72 GRR---PVrALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 335 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKV 414
Cdd:PRK10590  149 QVEILVLDEADRMLDMGFIHDIRRVLAK--LPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 415 VWVEDLDKRSFLLDILGaTGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATA 494
Cdd:PRK10590  225 HFVDKKRKRELLSQMIG-KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATD 303

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2217401332 495 VAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGR 529
Cdd:PRK10590  304 IAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 177-531 2.41e-86

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 277.95  E-value: 2.41e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 177 FSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEAlkavkengryg 256
Cdd:PRK01297   89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKE----------- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 257 RRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLE-RGCHLLVATPGRLVDMMERGKIGLDF 335
Cdd:PRK01297  158 RYMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDM 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 336 CKYLVLDEADRMLDMGFEPQIRRIVEQDtmPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 415
Cdd:PRK01297  238 VEVMVLDEADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVY 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 416 WVEDLDKRSFLLDILGATGSDSLtLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 495
Cdd:PRK01297  316 AVAGSDKYKLLYNLVTQNPWERV-MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDV 394

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2217401332 496 AARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVG 531
Cdd:PRK01297  395 AGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 161-532 5.00e-84

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 272.82  E-value: 5.00e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 161 IPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILS---QI 237
Cdd:PLN00206  107 LEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTI 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 238 YTDGPGEalkavkengrygRRKqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVA 317
Cdd:PLN00206  187 RSGHPSE------------QRN--PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVG 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 318 TPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPpkgvrHTMMFSATFPKEIQMLARDFLDEYIF 397
Cdd:PLN00206  253 TPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKDIIL 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 398 LAVGRVGSTSENITQKVVWVEDLDKRSFLLDILgaTGSDSLT---LVFVETKKGADSLEDFL-YHEGYACTSIHGDRSQR 473
Cdd:PLN00206  328 ISIGNPNRPNKAVKQLAIWVETKQKKQKLFDIL--KSKQHFKppaVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMK 405

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217401332 474 DREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGN 532
Cdd:PLN00206  406 ERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGE 464
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 186-398 2.53e-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: 2.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 186 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIyTDGPgealkavkengrYGRRKQYPISL 265
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI-NAQP------------PLERGDGPIVL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 266 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 345
Cdd:cd17966    68 VLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEAD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217401332 346 RMLDMGFEPQIRRIVEQdTMPPkgvRHTMMFSATFPKEIQMLARDFLDEYIFL 398
Cdd:cd17966   148 RMLDMGFEPQIRKIVDQ-IRPD---RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 176-532 9.27e-80

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 259.10  E-value: 9.27e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 176 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsQIYTDGPgealkavkengry 255
Cdd:PRK11192    2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAL-QHLLDFP------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 256 gRRKQYPIS-LVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 334
Cdd:PRK11192   68 -RRKSGPPRiLILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 335 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtmpPKGVRHTMMFSATFPKE-IQMLARDFLDEYIFLAVGrvGSTSE--NIT 411
Cdd:PRK11192  147 AVETLILDEADRMLDMGFAQDIETIAAE----TRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAE--PSRRErkKIH 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 412 QKVVWVEDLD-KRSFLLDILgATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPIL 490
Cdd:PRK11192  221 QWYYRADDLEhKTALLCHLL-KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVL 299

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2217401332 491 VATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGN 532
Cdd:PRK11192  300 VATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGR 341
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 176-531 2.10e-78

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 259.88  E-value: 2.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 176 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgPGEAlkavkengry 255
Cdd:PRK04537   10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSR-PALA---------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 256 GRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI-GLD 334
Cdd:PRK04537   79 DRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 335 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKV 414
Cdd:PRK04537  159 ACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 415 VWVEDLDKRSFLLDILGATgSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATA 494
Cdd:PRK04537  237 YFPADEEKQTLLLGLLSRS-EGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATD 315

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2217401332 495 VAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVG 531
Cdd:PRK04537  316 VAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLG 352
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 177-532 1.78e-74

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 244.88  E-value: 1.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 177 FSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEalkavkengryG 256
Cdd:PRK04837   10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPE-----------D 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 257 RRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFC 336
Cdd:PRK04837   79 RKVNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 337 KYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVW 416
Cdd:PRK04837  159 QVVVLDEADRMFDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFY 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 417 VEDLDKRSFLLDILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVA 496
Cdd:PRK04837  237 PSNEEKMRLLQTLIEEEWPDR-AIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVA 315

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2217401332 497 ARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGN 532
Cdd:PRK04837  316 ARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGA 351
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 165-392 7.51e-71

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 228.42  E-value: 7.51e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 165 ATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGE 244
Cdd:cd17953     2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 245 AlkavkENGrygrrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVD 324
Cdd:cd17953    82 P-----GEG--------PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMID 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217401332 325 M--MERGKI-GLDFCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPKgvRHTMMFSATFPKEIQMLARDFL 392
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, ...
 163-401 4.95e-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: 4.95e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 163 VEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgp 242
Cdd:cd18049    12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI----- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 243 gealkavkENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRL 322
Cdd:cd18049    87 --------NHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217401332 323 VDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVG 401
Cdd:cd18049   159 IDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 177-531 1.70e-69

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 237.44  E-value: 1.70e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 177 FSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaLKAvkengryg 256
Cdd:PRK11634    8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE-----LKA-------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 257 rrkqyPISLVLAPTRELAVQIYEEARKFSYRSR-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 335
Cdd:PRK11634   75 -----PQILVLAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 336 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 415
Cdd:PRK11634  150 LSGLVLDEADEMLRMGFIEDVETIMAQ--IPEG--HQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYW 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 416 WVEDLDKRSFLLDILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 495
Cdd:PRK11634  226 TVWGMRKNEALVRFLEAEDFDA-AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDV 304

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2217401332 496 AARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVG 531
Cdd:PRK11634  305 AARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAG 340
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 167-401 3.12e-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: 223.35  E-value: 3.12e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 167 GSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeal 246
Cdd:cd18050    54 GVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI--------- 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 247 kavkENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMM 326
Cdd:cd18050   125 ----NHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217401332 327 ERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVG 401
Cdd:cd18050   201 EAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 186-396 4.91e-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: 4.91e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 186 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYtdgpgealkavkeNGRYGRRKQYPISL 265
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-------------DQRELEKGEGPIAV 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 266 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 345
Cdd:cd17952    68 IVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEAD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217401332 346 RMLDMGFEPQIRRIVEQdTMPPkgvRHTMMFSATFPKEIQMLARDFLDEYI 396
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 ...
 190-392 8.06e-64

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


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 209.87  E-value: 8.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 190 IELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALKavKENGrygrrkqyPISLVLAP 269
Cdd:cd17945     5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEET--KDDG--------PYALILAP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 270 TRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLD 349
Cdd:cd17945    75 TRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMID 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217401332 350 MGFEPQIRRIVeqDTMPP------------------KGVRHTMMFSATFPKEIQMLARDFL 392
Cdd:cd17945   155 MGFEPQVTKIL--DAMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYL 213
PTZ00424 PTZ00424
helicase 45; Provisional
 168-531 5.19e-61

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 208.53  E-value: 5.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 168 SNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaL 246
Cdd:PTZ00424   21 SNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIkPILDG-YDTIGQAQSGTGKTATFVIAALQLIDYD-----L 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 247 KAVKengrygrrkqypiSLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMM 326
Cdd:PTZ00424   95 NACQ-------------ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 327 ERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGST 406
Cdd:PTZ00424  162 DKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKK--LPPD--VQVALFSATMPNEILELTTKFMRDPKRILVKKDELT 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 407 SENITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGK 486
Cdd:PTZ00424  238 LEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGS 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2217401332 487 SPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVG 531
Cdd:PTZ00424  318 TRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFG 362
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 199-387 1.14e-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: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 199 TPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengrygrrkqyPISLVLAPTRELAVQIY 278
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG------------------PQALVLAPTRELAEQIY 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 279 EEARKFSYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDFCKYLVLDEADRMLDMGFEPQIRR 358
Cdd:pfam00270  63 EELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEE 140

                         170       180
                  ....*....|....*....|....*....
gi 2217401332 359 IVEQdtMPPKgvRHTMMFSATFPKEIQML 387
Cdd:pfam00270 141 ILRR--LPKK--RQILLLSATLPRNLEDL 165
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 194-389 8.77e-58

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


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 193.57  E-value: 8.77e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 194 RYTRPTPVQKHAI-PIIKGKRDLMACAQTGSGKTAAFLLPilsqiytdgpgeALKAVKENGRYGRRKQYPIsLVLAPTRE 272
Cdd:cd17964    13 GFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLP------------AIQSLLNTKPAGRRSGVSA-LIISPTRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 273 LAVQIYEEARKFSYRSR-VRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMME--RGKIGLDFCKYLVLDEADRML 348
Cdd:cd17964    80 LALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217401332 349 DMGFEPQIRRIVeqDTMPPKGVRH--TMMFSATFPKEIQMLAR 389
Cdd:cd17964   160 DMGFRPDLEQIL--RHLPEKNADPrqTLLFSATVPDEVQQIAR 200
DEXDc smart00487
DEAD-like helicases superfamily;
190-413 9.06e-58

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 193.09  E-value: 9.06e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332  190 IELTRYTRPTPVQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkavkengRYGRRKQYPISLVLA 268
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-------------------EALKRGKGGRVLVLV 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332  269 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 347
Cdd:smart00487  62 PTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRL 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217401332  348 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRvgSTSENITQK 413
Cdd:smart00487 142 LDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 410-532 2.41e-56

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: 186.56  E-value: 2.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 410 ITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 489
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217401332 490 LVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGN 532
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGR 123
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 195-393 2.52e-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: 2.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 195 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQ-IYTDgpgealkavkengrygRRKQYPISLVLAPTREL 273
Cdd:cd17947    10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERlLYRP----------------KKKAATRVLVLVPTREL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 274 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDFCKYLVLDEADRMLDMGF 352
Cdd:cd17947    74 AMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGF 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217401332 353 EPQIRRIVEqdtMPPKGvRHTMMFSATFPKEIQMLARDFLD 393
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 ...
 186-401 3.06e-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: 3.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 186 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALKAvkengrygrrkqypisL 265
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRA----------------L 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 266 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGG-ADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 344
Cdd:cd17957    65 ILAPTRELASQIYRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEA 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217401332 345 DRMLDMGFEPQIRRIVEQDTMPPKgvrHTMMFSATFPKEIQMLARDFLDEYIFLAVG 401
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 ...
 186-394 4.09e-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: 4.09e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 186 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqIYTDGpgEALKAVKENGrygrrkqyPISL 265
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF--IHLDL--QPIPREQRNG--------PGVL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 266 VLAPTRELAVQIYEEARKFSYRSRVRPCVvYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 345
Cdd:cd17958    69 VLTPTRELALQIEAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEAD 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217401332 346 RMLDMGFEPQIRRIVeQDTMPPkgvRHTMMFSATFPKEIQMLARDFLDE 394
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 ...
 195-397 2.27e-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: 2.27e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 195 YTRPTPVQKHAIP-IIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDGpgealkavkengrYGrrkqyPISLVLAPTREL 273
Cdd:cd17955    19 IKEPTPIQKLCIPeILAG-RDVIGGAKTGSGKTAAFALPILQRLSEDP-------------YG-----IFALVLTPTREL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 274 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMME---RGKIGLDFCKYLVLDEADRMLDM 350
Cdd:cd17955    80 AYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217401332 351 GFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIF 397
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 ...
 197-392 4.91e-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: 4.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 197 RPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgeaLKAVKENGRYG-RRKQYPISLVLAPTRELAV 275
Cdd:cd17951    12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI-----------MFALEQEKKLPfIKGEGPYGLIVCPSRELAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 276 QIYEEARKFSYR------SRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLD 349
Cdd:cd17951    81 QTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217401332 350 MGFEPQIRRIVEQDtmppKGVRHTMMFSATFPKEIQMLARDFL 392
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 ...
 177-389 9.73e-52

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: 9.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 177 FSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgealkavkengryg 256
Cdd:cd17954     2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 257 rrKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDF 335
Cdd:cd17954    66 --PQRFFALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKS 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217401332 336 CKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPKgvRHTMMFSATFPKEIQMLAR 389
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 ...
 177-396 2.32e-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: 2.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 177 FSDIDMG-EIIMGNIELTrYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengry 255
Cdd:cd17940     1 FEDYGLKrELLMGIFEKG-FEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV------------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 256 grrkqypI-SLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 334
Cdd:cd17940    68 -------IqALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLS 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217401332 335 FCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPKgvRHTMMFSATFPKEIQmlarDFLDEYI 396
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) ...
 194-398 2.00e-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: 2.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 194 RYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkavkengRYgRRKQYPISLVLAPTREL 273
Cdd:cd17949    10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEP-----------RV-DRSDGTLALVLVPTREL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 274 AVQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDFCKYLVLDEADRMLDMG 351
Cdd:cd17949    78 ALQIYEVLEKLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217401332 352 FEPQIRRIVE--------QDTMPPKGV-RHTMMFSATFPKEIQMLARDFLDEYIFL 398
Cdd:cd17949   158 FEKDITKILEllddkrskAGGEKSKPSrRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 176-398 5.95e-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: 5.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 176 NFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgEALKAvkENGRY 255
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMI---------EKLKA--HSPTV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 256 GRRkqypiSLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 335
Cdd:cd17959    71 GAR-----ALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSS 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217401332 336 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFL 398
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, ...
 195-392 1.14e-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: 1.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 195 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYtdgpgealkavkeNGRYGRRKQYPISLVLAPTRELA 274
Cdd:cd17960    10 FTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILL-------------KRKANLKKGQVGALIISPTRELA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 275 VQIYEEARKF--SYRSRVRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMMERGKIGLDF--CKYLVLDEADRMLD 349
Cdd:cd17960    77 TQIYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKVksLEVLVLDEADRLLD 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217401332 350 MGFEPQIRRIVEQdtmPPKGvRHTMMFSATFPKEIQMLARDFL 392
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 ...
 182-379 8.21e-46

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: 8.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 182 MGEIIMGnIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkavkengrygrrkQY 261
Cdd:cd17938     7 MPELIKA-VEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------------------------QI 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 262 PISLVLAPTRELAVQIYEEARKFSY---RSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKY 338
Cdd:cd17938    61 VVALILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRF 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217401332 339 LVLDEADRMLDMGFEPQIRRIVEQdtMPPKGVR----HTMMFSAT 379
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 ...
 195-400 2.13e-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: 2.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 195 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIY------TDGPGealkavkengrygrrkqypiSLVLA 268
Cdd:cd17941    10 FIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwtpEDGLG--------------------ALIIS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 269 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQirdLER--GCHLLVATPGRLVDMMERgKIGLDF--CKYLVLDEA 344
Cdd:cd17941    70 PTRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE---KERinRMNILVCTPGRLLQHMDE-TPGFDTsnLQMLVLDEA 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217401332 345 DRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAV 400
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 ...
 189-396 2.76e-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: 2.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 189 NIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTdgpgealkavkengrygrRKQYPISLVLA 268
Cdd:cd17962     4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT------------------EHRNPSALILT 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 269 PTRELAVQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 347
Cdd:cd17962    66 PTRELAVQIEDQAKELmKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTM 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217401332 348 LDMGFEPQIRRIVEQDTMPPKgvrhTMMFSATFPKEIQMLARDFLDEYI 396
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 ...
 194-389 1.51e-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: 1.51e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 194 RYTRPTPVQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeaLKAVKENGRYGRRKqYPISLVLAPTRE 272
Cdd:cd17946     9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERL--------LSQKSSNGVGGKQK-PLRALILTPTRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 273 LAVQI---YEEARKFsyrSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL---DFCKYLVLDEADR 346
Cdd:cd17946    80 LAVQVkdhLKAIAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLanlKSLRFLVLDEADR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2217401332 347 MLDMG-FEP--QIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLAR 389
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 ...
 186-389 1.45e-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: 1.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 186 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTdgpgeaLKAVKENGRYGrrkqypisL 265
Cdd:cd17942     1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK------LKFKPRNGTGV--------I 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 266 VLAPTRELAVQIYEEARKF-SYRSRVRPCVVyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKiglDF----CKYLV 340
Cdd:cd17942    67 IISPTRELALQIYGVAKELlKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTK---GFlyknLQCLI 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217401332 341 LDEADRMLDMGFEPQIRRIVEqdtMPPKGvRHTMMFSATFPKEIQMLAR 389
Cdd:cd17942   143 IDEADRILEIGFEEEMRQIIK---LLPKR-RQTMLFSATQTRKVEDLAR 187
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 195-392 3.67e-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: 3.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 195 YTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDGPgeALKAvkengrygrrkqypisLVLAPTREL 273
Cdd:cd17939    17 FEKPSAIQQRAIvPIIKG-RDVIAQAQSGTGKTATFSIGALQRIDTTVR--ETQA----------------LVLAPTREL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 274 AVQIYE--EARKFSYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMG 351
Cdd:cd17939    78 AQQIQKvvKALGDYMGVKVHACI--GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217401332 352 FEPQIRRIVeqdTMPPKGVRhTMMFSATFPKEIQMLARDFL 392
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 ...
 195-392 1.16e-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: 1.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 195 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeaLKAVKENGRYgrrkQYPISLVLAPTRELA 274
Cdd:cd17961    14 WEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKI--------LKAKAESGEE----QGTRALILVPTRELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 275 VQIYEEARKFSY--RSRVRpCV-VYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL-DFCKYLVLDEADRMLDM 350
Cdd:cd17961    82 QQVSKVLEQLTAycRKDVR-VVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217401332 351 GFEPQIRRIVEqdtMPPKGVRHTMMfSATFPKEIQMLARDFL 392
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 ...
 195-391 4.42e-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: 4.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 195 YTRPTPVQKHAIPIIKGK--RDLMACAQTGSGKTAAFLLPILSQIYTdgpgealkavkengrygrRKQYPISLVLAPTRE 272
Cdd:cd17963    14 FNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDP------------------TLKSPQALCLAPTRE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 273 LAVQIYEEARKF-SY-----RSRVRPCVVYGGADIGQQIrdlergchlLVATPGRLVDMMERGKIGLDFCKYLVLDEADR 346
Cdd:cd17963    76 LARQIGEVVEKMgKFtgvkvALAVPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQLDLKKIKILVLDEADV 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2217401332 347 MLDM-GFEPQIRRIVEqdtMPPKGVRhTMMFSATFPKEIQMLARDF 391
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 ...
 177-392 4.61e-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: 4.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 177 FSDIDMGEIIMGNIELTRYTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaLKAVKengry 255
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAImPCIKG-YDVIAQAQSGTGKTATFSISILQQIDTS-----LKATQ----- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 256 grrkqypiSLVLAPTRELAVQIYE--EARKFSYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL 333
Cdd:cd18046    70 --------ALVLAPTRELAQQIQKvvMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRT 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217401332 334 DFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL 392
Cdd:cd18046   140 DYIKMFVLDEADEMLSRGFKDQIYDIFQK--LPPD--TQVVLLSATMPNDVLEVTTKFM 194
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 421-531 5.08e-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: 5.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 421 DKRSFLLDILgATGSDSLTLVFVETKKGADsLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGL 500
Cdd:pfam00271   1 EKLEALLELL-KKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217401332 501 DISNVRHVINFDLPSDIEEYVHRIGRTGRVG 531
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 ...
 198-392 2.27e-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: 2.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 198 PTPVQKHAIP-IIKGKrDLMACAQTGSGKTAAFLLPILSQIYTDgPGEalkavkengrygrrkqypIS-LVLAPTRELAV 275
Cdd:cd17950    25 PSEVQHECIPqAILGM-DVLCQAKSGMGKTAVFVLSTLQQLEPV-DGQ------------------VSvLVICHTRELAF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 276 QIYEEARKFS-YRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM---LDM 350
Cdd:cd17950    85 QISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleqLDM 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217401332 351 gfepqiRRIVeQD--TMPPKGvRHTMMFSATFPKEIQMLARDFL 392
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, ...
 195-397 1.92e-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: 1.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 195 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPilsqiytdgpgeALKAVKengrygRRKQYPISLVLAPTRELA 274
Cdd:cd17943    10 FQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVI------------ALESLD------LERRHPQVLILAPTREIA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 275 VQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 353
Cdd:cd17943    72 VQIHDVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQ 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217401332 354 PQIRRIveqDTMPPKGvRHTMMFSATFPKE-IQMLARdFLDEYIF 397
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 ...
 195-394 2.42e-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: 2.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 195 YTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTdgpgealkAVKEngrygrrkqyPISLVLAPTREL 273
Cdd:cd18045    19 FEKPSAIQQRAIkPIIKG-RDVIAQSQSGTGKTATFSISVLQCLDI--------QVRE----------TQALILSPTREL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 274 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 353
Cdd:cd18045    80 AVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217401332 354 PQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDE 394
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 ...
 192-382 9.15e-31

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: 9.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 192 LTRY--TRPTPVQKHAIP-IIKGKRDLMAcAQTGSGKTAAFLLPILSQIYTDgpgEALKAVKENGrygrrkqyPISLVLA 268
Cdd:cd17948     5 LQRQgiTKPTTVQKQGIPsILRGRNTLCA-AETGSGKTLTYLLPIIQRLLRY---KLLAEGPFNA--------PRGLVIT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 269 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIgQQIRDLERG-CHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 347
Cdd:cd17948    73 PSRELAEQIGSVAQSLTEGLGLKVKVITGGRTK-RQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTL 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2217401332 348 LDMGFEPQIRRIVEQ-----------DTMPPKGvrHTMMFSATFPK 382
Cdd:cd17948   152 LDDSFNEKLSHFLRRfplasrrsentDGLDPGT--QLVLVSATMPS 195
HELICc smart00490
helicase superfamily c-terminal domain;
450-531 1.66e-30

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 114.23  E-value: 1.66e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332  450 DSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGR 529
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 2217401332  530 VG 531
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 ...
 200-392 2.51e-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: 2.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 200 PVQ-KHAIPIIKGKrDLMACAQTGSGKTAAFLLPILsqiytdgpgEALKAVKENGRYGRRkqyPISLVLAPTRELAVQIY 278
Cdd:cd17944    15 PIQvKTFHPVYSGK-DLIAQARTGTGKTFSFAIPLI---------EKLQEDQQPRKRGRA---PKVLVLAPTRELANQVT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 279 EEARKFSYRSRVrpCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRR 358
Cdd:cd17944    82 KDFKDITRKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2217401332 359 IV-EQDTMPPKGVRHTMMFSATFPKEIQMLARDFL 392
Cdd:cd17944   160 ILsVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 194-387 3.88e-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: 3.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 194 RYTRPTPVQKHAIP-IIKG--------KRDLMACAQTGSGKTAAFLLPILsQIYTDGPGEALKAvkengrygrrkqypis 264
Cdd:cd17956     9 GITSAFPVQAAVIPwLLPSskstppyrPGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVPRLRA---------------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 265 LVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL--------LVATPGRLVDMMERGK-IGLDF 335
Cdd:cd17956    72 LIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGrylsrvdiLVATPGRLVDHLNSTPgFTLKH 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217401332 336 CKYLVLDEADRMLDMGFE---PQIRRIVEQDTMP------------PKGVR-HTMMFSATF---PKEIQML 387
Cdd:cd17956   152 LRFLVIDEADRLLNQSFQdwlETVMKALGRPTAPdlgsfgdanlleRSVRPlQKLLFSATLtrdPEKLSSL 222
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 182-391 1.90e-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: 1.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 182 MGEIIMGNIELTRYTRPTPVQKHAIPIIKGKR----------------DLMACAQTGSGKTAAFLLPILSQIY---TDGP 242
Cdd:cd17965    15 IKEILKGSNKTDEEIKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKrqeQEPF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 243 GEALKAVKENGRYGRrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVV-YGGADIGQQIRDLERG-CHLLVATPG 320
Cdd:cd17965    95 EEAEEEYESAKDTGR----PRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLAFKGrIDILVTTPG 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217401332 321 RLVDMME-RGKIgLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgVRHTMMFSATFPKEIQMLARDF 391
Cdd:cd17965   171 KLASLAKsRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APK--LKHLILCSATIPKEFDKTLRKL 237
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
210-526 7.90e-22

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 99.71  E-value: 7.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 210 KGKRDLMACAQTGSGKTAAfllpilsqiytdgpgeALKAVKENGRYGRrkqypiSLVLAPTRELAVQIYEEARKFsyrsr 289
Cdd:COG1061    98 RGGGRGLVVAPTGTGKTVL----------------ALALAAELLRGKR------VLVLVPRRELLEQWAEELRRF----- 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 290 vrpcvvYGGADIGQQIRDleRGCHLLVATPGRLVDMMERGKIGlDFCKYLVLDEADRmldmGFEPQIRRIVEQdtMPPKg 369
Cdd:COG1061   151 ------LGDPLAGGGKKD--SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEA--FPAA- 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 370 vrHTMMFSAT------FPKEI-------------QMLARDFLDEYIFLAV--------GRVGSTSENITQKVVwVEDLDK 422
Cdd:COG1061   215 --YRLGLTATpfrsdgREILLflfdgivyeyslkEAIEDGYLAPPEYYGIrvdltderAEYDALSERLREALA-ADAERK 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 423 RSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI 502
Cdd:COG1061   292 DKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371

                         330       340
                  ....*....|....*....|....
gi 2217401332 503 SNVRHVINFDLPSDIEEYVHRIGR 526
Cdd:COG1061   372 PRLDVAILLRPTGSPREFIQRLGR 395
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
299-529 5.23e-20

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 93.67  E-value: 5.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 299 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdfckyLVLDEA--------DrmldmgFEP---QIRRIVE 361
Cdd:COG0514    94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 362 QDTMPPkgvrhTMMFSATFPKE-----IQMLARDflDEYIFLA-VGRvgstsENITQKVVWVEDLDKRSFLLDILGATGS 435
Cdd:COG0514   163 RLPNVP-----VLALTATATPRvradiAEQLGLE--DPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPG 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 436 DSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATaVA-ARGLDISNVRHVINFDLP 514
Cdd:COG0514   231 GS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLP 308

                         250
                  ....*....|....*
gi 2217401332 515 SDIEEYVHRIGRTGR 529
Cdd:COG0514   309 KSIEAYYQEIGRAGR 323
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 174-388 4.60e-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: 4.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 174 IENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGK--RDLMACAQTGSGKTAAFLLPILSqiytdgpgealkavke 251
Cdd:cd18048    17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLS---------------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 252 ngRYGRRKQYPISLVLAPTRELAVQ---IYEEARKFSYRSRV----RPCVVYGGADIGQQIrdlergchlLVATPGRLVD 324
Cdd:cd18048    81 --RVDALKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQViyaiRGNRPGKGTDIEAQI---------VIGTPGTVLD 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217401332 325 MMERGK-IGLDFCKYLVLDEADRMLDM-GFEPQIRRIveQDTMPPKGvrHTMMFSATFPKEIQMLA 388
Cdd:cd18048   150 WCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRV--KRSMPKEC--QMLLFSATFEDSVWAFA 211
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
422-529 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 2217401332 422 KRSFLLDILG---ATGSDSLTLVFVETKKGADSLEDFLYHEGYACT------SIHGDR--SQRDREEALHQFRSGKSPIL 490
Cdd:COG1111   336 KLSKLREILKeqlGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGEFNVL 415

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217401332 491 VATAVAARGLDISNVRHVINFDL-PSDIeEYVHRIGRTGR 529
Cdd:COG1111   416 VATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR 454
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 439-526 5.14e-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: 5.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 439 TLVFVETKKGADSLEDFLYHEGYACTSI-------HGDRSQ--------RDREEALHQFRSGKSPILVATAVAARGLDIS 503
Cdd:cd18802    28 GIIFVERRATAVVLSRLLKEHPSTLAFIrcgfligRGNSSQrkrslmtqRKQKETLDKFRDGELNLLIATSVLEEGIDVP 107

                          90       100
                  ....*....|....*....|...
gi 2217401332 504 NVRHVINFDLPSDIEEYVHRIGR 526
Cdd:cd18802   108 ACNLVIRFDLPKTLRSYIQSRGR 130
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 217-379 1.36e-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: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 217 ACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengrygrrkqypiSLVLAPTRELAVQIYEEARK-FSYRSRVRpcVV 295
Cdd:cd00046     6 ITAPTGSGKTLAALLAALLLLLKKGKK--------------------VLVLVPTKALALQTAERLRElFGPGIRVA--VL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 296 YGGADIGQQIRDLERGCHLLVATPGRLVDMMER-GKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMpPKGVRhTM 374
Cdd:cd00046    64 VGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAG-LKNAQ-VI 141


                  ....*
gi 2217401332 375 MFSAT 379
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 ...
 175-388 2.41e-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: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 175 ENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGK--RDLMACAQTGSGKTAAFLLPILSQIytdgpGEALKavken 252
Cdd:cd18047     1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-----EPANK----- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 253 grygrrkqYPISLVLAPTRELAVQ---IYEEARKFSyrsrvrPCVVYGGADIGQQirdLERGC----HLLVATPGRLVDM 325
Cdd:cd18047    71 --------YPQCLCLSPTYELALQtgkVIEQMGKFY------PELKLAYAVRGNK---LERGQkiseQIVIGTPGTVLDW 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217401332 326 MERGK-IGLDFCKYLVLDEADRML-DMGFEPQIRRIveqDTMPPKGVRhTMMFSATFPKEIQMLA 388
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 ...
 407-531 1.47e-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: 64.92  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 407 SENITQKVVWVEDLDKRSFLLD-ILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSG 485
Cdd:cd18794     1 RPNLFYSVRPKDKKDEKLDLLKrIKVEHLGGS-GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2217401332 486 KSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVG 531
Cdd:cd18794    80 KIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 440-525 5.74e-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: 5.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 440 LVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP--ILVATAVAARGLDISNVRHVINFDL---P 514
Cdd:cd18793    31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPwwnP 110

                          90
                  ....*....|....
gi 2217401332 515 SDIE---EYVHRIG 525
Cdd:cd18793   111 AVEEqaiDRAHRIG 124
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 440-530 5.84e-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: 5.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 440 LVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP--ILVATAVAARGLDISNVRHVINFDLP--S 515
Cdd:COG0553   553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWwnP 632

                          90
                  ....*....|....*....
gi 2217401332 516 DIEEY----VHRIGRTGRV 530
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 ...
 471-529 1.63e-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: 1.63e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 471 SQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFD-LPSDIeEYVHRIGRTGR 529
Cdd:cd18801    75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 489-536 2.23e-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: 54.25  E-value: 2.23e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217401332 489 ILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLEAK 536
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGE 72
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 196-532 4.55e-09

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 59.46  E-value: 4.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 196 TRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEAlkavkengrygrrkqypisLVLAPTRELAV 275
Cdd:COG1205    55 ERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGATA-------------------LYLYPTKALAR 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 276 QIYEEARKF--SYRSRVRPCVVYGgaDIGQQIRD--LERGcHLLVATPgrlvDMMERgkiGL--------DF---CKYLV 340
Cdd:COG1205   116 DQLRRLRELaeALGLGVRVATYDG--DTPPEERRwiREHP-DIVLTNP----DMLHY---GLlphhtrwaRFfrnLRYVV 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 341 LDEA---------------DRMldmgfepqiRRIVEQdtmppKGVRHTMMF-SATF--PKEiqmLARDFLDEYiFLAVGR 402
Cdd:COG1205   186 IDEAhtyrgvfgshvanvlRRL---------RRICRH-----YGSDPQFILaSATIgnPAE---HAERLTGRP-VTVVDE 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 403 VGSTSENITQkVVW----VEDLDKRSFLL---DILG-ATGSDSLTLVFVETKKGA----DSLEDFLYHEGYAcTSIHGDR 470
Cdd:COG1205   248 DGSPRGERTF-VLWnpplVDDGIRRSALAeaaRLLAdLVREGLRTLVFTRSRRGAellaRYARRALREPDLA-DRVAAYR 325

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217401332 471 SQ---RDREEALHQFRSGKSPILVAT-AVAArGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGN 532
Cdd:COG1205   326 AGylpEERREIERGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQ 390
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
199-531 6.81e-09

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 58.75  E-value: 6.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 199 TPVQKHAIP--IIKGKRdLMACAQTGSGKTAafllpiLSQIYtdgpgeALKAVKENGRygrrkqypiSLVLAPTRELAVQ 276
Cdd:COG1204    24 YPPQAEALEagLLEGKN-LVVSAPTASGKTL------IAELA------ILKALLNGGK---------ALYIVPLRALASE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 277 IYEEARKFSYRSRVRPCVVYGGADIGqqIRDLERgCHLLVATPGRLvDMMERGKIGL--DFcKYLVLDEA---------- 344
Cdd:COG1204    82 KYREFKRDFEELGIKVGVSTGDYDSD--DEWLGR-YDILVATPEKL-DSLLRNGPSWlrDV-DLVVVDEAhliddesrgp 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 345 ------DRMLDMGFEPQIrriveqdtmppkgvrhtmMF-SATF--PKEI-QMLARDF---------LDEYIFLAvGRVGS 405
Cdd:COG1204   157 tlevllARLRRLNPEAQI------------------VAlSATIgnAEEIaEWLDAELvksdwrpvpLNEGVLYD-GVLRF 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 406 TSENITQKVVWVedldkrSFLLDILGATGSdslTLVFVETKKGADSL------------------------EDFL----- 456
Cdd:COG1204   218 DDGSRRSKDPTL------ALALDLLEEGGQ---VLVFVSSRRDAESLakkladelkrrltpeereeleelaEELLevsee 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 457 YHEGYACTSI--------HGDRSQRDREEALHQFRSGKSPILVATAVAARGLdisN--VRHVI------NFDLPSDIEEY 520
Cdd:COG1204   289 THTNEKLADClekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEF 365

                         410
                  ....*....|.
gi 2217401332 521 VHRIGRTGRVG 531
Cdd:COG1204   366 KQMAGRAGRPG 376
PRK13766 PRK13766
Hef nuclease; Provisional
 436-529 1.82e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 57.58  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 436 DSLTLVFVETKKGADSLEDFLYHEGYAC------TSIHGDR--SQRDREEALHQFRSGKSPILVATAVAARGLDISNVRH 507
Cdd:PRK13766  365 DSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444

                          90       100
                  ....*....|....*....|...
gi 2217401332 508 VINFD-LPSDIeEYVHRIGRTGR 529
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 ...
 197-379 3.09e-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: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 197 RPTPVQKHAIPIIKG------KRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkAVKENGRYgrrkqypiSLVLAPT 270
Cdd:cd17918    15 SLTKDQAQAIKDIEKdlhspePMDRLLSGDVGSGKTLVALGAAL-------------LAYKNGKQ--------VAILVPT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 271 RELAVQIYEEARKfsYRSRVRPCVVYGG--ADIGQQIrDLERGCHLLVAtpgrlvdmMERGKIGLDFckyLVLDEADRMl 348
Cdd:cd17918    74 EILAHQHYEEARK--FLPFINVELVTGGtkAQILSGI-SLLVGTHALLH--------LDVKFKNLDL---VIVDEQHRF- 138

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217401332 349 dmgfepqirRIVEQDTMPPKGVRHTMMFSAT 379
Cdd:cd17918   139 ---------GVAQREALYNLGATHFLEATAT 160
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
194-247 3.91e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 53.18  E-value: 3.91e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217401332 194 RYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKT-AAFlLPILSQIYTDGPGEALK 247
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 ...
 202-344 4.04e-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: 4.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 202 QKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgealkavkengrYGRRkqypiSLVLAPTRELAVQIYEEA 281
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD--------------PGSR-----ALYLYPTKALAQDQLRSL 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217401332 282 RKF--SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPgrlvDMME-----RGKIGLDFC---KYLVLDEA 344
Cdd:cd17923    66 RELleQLGLGIRVATYDGDTPREERRAIIRNPPRILLTNP----DMLHyallpHHDRWARFLrnlRYVVLDEA 134
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 203-380 2.94e-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: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 203 KHAIPIIKGKRDLMACAQTGSGKTA-AFLLPILsqiytdgpgealkavkengrygrRKQYPIsLVLAPTRELAVQIYEEA 281
Cdd:cd17926     9 LEAWLAHKNNRRGILVLPTGSGKTLtALALIAY-----------------------LKELRT-LIVVPTDALLDQWKERF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 282 RKFSYRSRVrpCVVYGGADIGQqirdleRGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRmldmGFEPQIRRIVE 361
Cdd:cd17926    65 EDFLGDSSI--GLIGGGKKKDF------DDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEILK 132

                         170
                  ....*....|....*....
gi 2217401332 362 QDTMPPKgvrhtMMFSATF 380
Cdd:cd17926   133 ELNAKYR-----LGLTATP 146
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 212-344 5.65e-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: 5.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 212 KRDLMACAQTGSGKT--AAFLLPILSQIytdgpgeaLKAVKENGRygrrkqypISLVLAPTRELAVQIYEEARKFSYrSR 289
Cdd:cd18034    16 KRNTIVVLPTGSGKTliAVMLIKEMGEL--------NRKEKNPKK--------RAVFLVPTVPLVAQQAEAIRSHTD-LK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217401332 290 VRPCvvYGGADIGQQIRDLERGC----HLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 344
Cdd:cd18034    79 VGEY--SGEMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK13767 PRK13767
ATP-dependent helicase; Provisional
 194-319 7.93e-06

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 49.11  E-value: 7.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 194 RYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALkavkENGRYgrrkqypiSLVLAPTREL 273
Cdd:PRK13767   29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGEL----EDKVY--------CLYVSPLRAL 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217401332 274 A-----------VQIYEEARKFSYR-SRVRPCVVYGGADIGQQIRDLERGCHLLVATP 319
Cdd:PRK13767   97 NndihrnleeplTEIREIAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTP 154
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 199-344 1.17e-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: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 199 TPVQKHAI-PIIKGKRDLMACAQTGSGKTAAFLLPIlsqiytdgpgeaLKAVKENGRygrrkqypISLVLAPTRELAVQI 277
Cdd:cd17921     3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAI------------LRALATSGG--------KAVYIAPTRALVNQK 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217401332 278 YEEARKFSYRSRVRPCVVYGGADIGqqiRDLERGCHLLVATPGRLVDMMERGKIGLDF-CKYLVLDEA 344
Cdd:cd17921    63 EADLRERFGPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGERLIQdVRLVVVDEA 127
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 457-531 2.60e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.40  E-value: 2.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217401332 457 YHEGYactsihgDRSQRDR-EEAlhqFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVG 531
Cdd:PRK11057  266 YHAGL-------DNDVRADvQEA---FQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
 339-552 7.36e-05

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: 45.52  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 339 LVLDEADRMLDmgfEPQIRRIVEQDTMPPKGVRHTMMfSATFPKEIQMLARDFldEYIFLAVGRVGSTSENITQKVVWVE 418
Cdd:TIGR01587 128 LIFDEVHFYDE---YTLALILAVLEVLKDNDVPILLM-SATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILI 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 419 DLDKR---SFLLDILGATGSDSLTLVFVET-----------KKGADSLEDFLYHEGYActsiHGDRSQRDREEALHQFRS 484
Cdd:TIGR01587 202 ESDKVgeiSSLERLLEFIKKGGSIAIIVNTvdraqefyqqlKEKAPEEEIILYHSRFT----EKDRAKKEAELLREMKKS 277

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217401332 485 GKSPILVATAVAARGLDISnvrhvinFDL----PSDIEEYVHRIGRTGRVGNLEAKQ-EVPSWLENMAYEHHY 552
Cdd:TIGR01587 278 NEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYGRKIGENfEVYIITIAPEGKLFP 343
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
 466-531 1.49e-04

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


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 42.33  E-value: 1.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217401332 466 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVI-----NFDLpSDIEEYVHRIGRTGRVG 531
Cdd:cd18810    57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGL-AQLYQLRGRVGRSKERA 126
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 439-526 2.65e-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: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 439 TLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDRE-EALHQFRSGKS--PILVATAVAARGLDISNVRHVInFDLP- 514
Cdd:cd18799     9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV-FLRPt 87

                          90
                  ....*....|...
gi 2217401332 515 -SDIeEYVHRIGR 526
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 ...
 439-529 3.73e-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: 41.10  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 439 TLVFVETKKGADSLED---FLYHEGYACTSI---HG--DRSQRDR-EEALhqfRSGKSPILVATAVAARGLDISNVRHVI 509
Cdd:cd18796    41 TLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAAL---KRGDLKVVVATSSLELGIDIGDVDLVI 117

                          90       100
                  ....*....|....*....|
gi 2217401332 510 NFDLPSDIEEYVHRIGRTGR 529
Cdd:cd18796   118 QIGSPKSVARLLQRLGRSGH 137
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 466-535 8.86e-04

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 40.33  E-value: 8.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217401332 466 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVI-----NFDLpSDIeeyvHRI-GRTGRvGNLEA 535
Cdd:cd18792    66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIiedadRFGL-SQL----HQLrGRVGR-GKHQS 135
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 201-328 1.16e-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: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 201 VQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgEALKAVKENGRYGRRKQYpislvLAPTRELAVQIYE 279
Cdd:cd18023     5 IQSEVFPdLLYSDKNFVVSAPTGSGKTVLFELAIL---------RLLKERNPLPWGNRKVVY-----IAPIKALCSEKYD 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217401332 280 EAR-KFsyrSRVRPCVVYGGADigQQIRDLE--RGCHLLVATPGRLvDMMER 328
Cdd:cd18023    71 DWKeKF---GPLGLSCAELTGD--TEMDDTFeiQDADIILTTPEKW-DSMTR 116
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 212-346 1.23e-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: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 212 KRDLMACAQTGSGKTAAFLLPILSQIytdgpgealkaVKENGRYgrrkqypisLVLAPTRELAVQIYEEARKFsyRSRVR 291
Cdd:cd18035    16 NGNTLIVLPTGLGKTIIAILVAADRL-----------TKKGGKV---------LILAPSRPLVEQHAENLKRV--LNIPD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217401332 292 PCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADR 346
Cdd:cd18035    74 KITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 466-535 1.73e-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: 39.63  E-value: 1.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217401332 466 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISN-----VRHVINFDLPSdieeyVHRI-GRTGRvGNLEA 535
Cdd:cd18811    67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGR-GDHQS 136
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 213-343 2.06e-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: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 213 RDLMACAQTGSGKTAAFLLPILSQIYtDGPGEALKAvkengrygrrkqypisLVLAPTRELAVQIYE------EARKFSY 286
Cdd:cd17922     2 RNVLIAAPTGSGKTEAAFLPALSSLA-DEPEKGVQV----------------LYISPLKALINDQERrleeplDEIDLEI 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217401332 287 RSRVRpcvvYGgaDIGQQIRD--LERGCHLLVATPGRLVDMMERGKIGLDF--CKYLVLDE 343
Cdd:cd17922    65 PVAVR----HG--DTSQSEKAkqLKNPPGILITTPESLELLLVNKKLRELFagLRYVVVDE 119
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 466-529 2.07e-03

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 39.15  E-value: 2.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217401332 466 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI--SNVRHVINFDLPSDiEEYVHRIGRTGR 529
Cdd:cd18789    74 ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLpeANVAIQISGHGGSR-RQEAQRLGRILR 138
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 200-384 2.49e-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: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 200 PVQKHAIP--IIKGKRdLMACAQTGSGKTaafLLPILSqiytdgpgeALKAVKENGRygrrkqypiSLVLAPTRELAVQI 277
Cdd:cd18028     4 PPQAEAVRagLLKGEN-LLISIPTASGKT---LIAEMA---------MVNTLLEGGK---------ALYLVPLRALASEK 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 278 YEEarkFSYRSRVrpcvvygGADIGQQIRDLERG------CHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMG 351
Cdd:cd18028    62 YEE---FKKLEEI-------GLKVGISTGDYDEDdewlgdYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEE 131

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2217401332 352 FEPQIRRIVEQDTMPPKGVRhTMMFSATF--PKEI 384
Cdd:cd18028   132 RGPTLESIVARLRRLNPNTQ-IIGLSATIgnPDEL 165
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 439-536 6.05e-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: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 439 TLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDlpSDIE 518
Cdd:cd18790    30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKE 107

                          90       100
                  ....*....|....*....|....*
gi 2217401332 519 EY-------VHRIGRTGRvgNLEAK 536
Cdd:cd18790   108 GFlrsetslIQTIGRAAR--NVNGK 130
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 436-530 6.64e-03

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 39.78  E-value: 6.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332  436 DSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFR---SGKSPILVATAVAARGLDISNVRHVINFD 512
Cdd:PLN03142   487 DSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkpgSEKFVFLLSTRAGGLGINLATADIVILYD 566

                           90       100
                   ....*....|....*....|....*.
gi 2217401332  513 lpSD--------IEEYVHRIGRTGRV 530
Cdd:PLN03142   567 --SDwnpqvdlqAQDRAHRIGQKKEV 590
ResIII pfam04851
Type III restriction enzyme, res subunit;
198-381 7.97e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 37.65  E-value: 7.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 198 PTPVQKHAI-----PIIKGKRDLMACAQTGSGKTaafllpilsqiYTdgpgeALKAVKEngrygRRKQYPIS--LVLAPT 270
Cdd:pfam04851   4 LRPYQIEAIenlleSIKNGQKRGLIVMATGSGKT-----------LT-----AAKLIAR-----LFKKGPIKkvLFLVPR 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217401332 271 RELAVQIYEEARKFSyrsrvrPCVVYGGADIGQQIRDLERG-CHLLVATPGRLV--DMMERGKIGLDFCKYLVLDEADRm 347
Cdd:pfam04851  63 KDLLEQALEEFKKFL------PNYVEIGEIISGDKKDESVDdNKIVVTTIQSLYkaLELASLELLPDFFDVIIIDEAHR- 135

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217401332 348 ldmGFEPQIRRIVEQDTmPPKGVRhtmmFSATFP 381
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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