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Conserved domains on  [gi|17985987|ref|NP_536783|]
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belle, isoform A [Drosophila melanogaster]

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 ...
 275-522 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: 538.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 275 FDKYEDIPVEATGQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPIL 354
Cdd:cd18051   1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 355 NQMYELGH-VPPPQSTRQYSRRKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIV 433
Cdd:cd18051  81 SQIYEQGPgESLPSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 434 ATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNMPPTGQRQTLMFSATFPKQIQELASDFLSNYI 513
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYI 240


                ....*....
gi 17985987 514 FLAVGRVGS 522
Cdd:cd18051 241 FLAVGRVGS 249
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 527-663 9.30e-59

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: 195.80  E-value: 9.30e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 527 ITQTILWVYEPDKRSYLLDLLSSIRdgpeytKDSLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFR 606
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKL------KPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFR 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17985987 607 SGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFF 663
Cdd:cd18787  75 SGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 275-522 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: 538.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 275 FDKYEDIPVEATGQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPIL 354
Cdd:cd18051   1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 355 NQMYELGH-VPPPQSTRQYSRRKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIV 433
Cdd:cd18051  81 SQIYEQGPgESLPSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 434 ATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNMPPTGQRQTLMFSATFPKQIQELASDFLSNYI 513
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYI 240


                ....*....
gi 17985987 514 FLAVGRVGS 522
Cdd:cd18051 241 FLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
294-686 8.06e-165

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 483.50  E-value: 8.06e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 294 ITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMyelghvpppqstrQYS 373
Cdd:COG0513   1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-------------DPS 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 374 RRKQyPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENI 453
Cdd:COG0513  68 RPRA-PQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGV 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 454 RFLVLDEADRMLDMGFEPQIRRIVEQLnmPPtgQRQTLMFSATFPKQIQELASDFLSNYIFLAVGRVGSTSENITQTILW 533
Cdd:COG0513 147 ETLVLDEADRMLDMGFIEDIERILKLL--PK--ERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYL 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 534 VYEPDKRSYLLDLLSSIRDGpeytkdsLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPIL 613
Cdd:COG0513 223 VDKRDKLELLRRLLRDEDPE-------RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVL 295

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17985987 614 VATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFFNEKNRNICSDLLELlieTKQEIP 686
Cdd:COG0513 296 VATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKL---IGQKIE 365
PTZ00110 PTZ00110
helicase; Provisional
 287-697 1.36e-115

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 361.01  E-value: 1.36e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  287 GQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPilnqmyELGHVppp 366
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLP------AIVHI--- 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  367 qSTRQYSRRKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRG 446
Cdd:PTZ00110 193 -NAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESN 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  447 KVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNmpPtgQRQTLMFSATFPKQIQELASDFLSNY-IFLAVGRVG-STS 524
Cdd:PTZ00110 272 VTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIR--P--DRQTLMWSATWPKEVQSLARDLCKEEpVHVNVGSLDlTAC 347

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  525 ENITQTILWVYEPDKRSYLLDLLSSI-RDGPEytkdslTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALR 603
Cdd:PTZ00110 348 HNIKQEVFVVEEHEKRGKLKMLLQRImRDGDK------ILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLN 421

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  604 CFRSGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFFNEKNRNICSDLLELLIETKQ 683
Cdd:PTZ00110 422 EFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQ 501

                        410
                 ....*....|....
gi 17985987  684 EIPSFMEDMSSDRG 697
Cdd:PTZ00110 502 PVPPELEKLSNERS 515
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 319-504 1.36e-61

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 204.78  E-value: 1.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987   319 TPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMyelghvpppqstrqySRRKQYPLGLVLAPTRELATQIFEEA 398
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL---------------DKLDNGPQALVLAPTRELAEQIYEEL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987   399 KKFAYRSRMRPAVLYGGNNTSEQMRELdRGCHLIVATPGRLEDMITRgKVGLENIRFLVLDEADRMLDMGFEPQIRRIVE 478
Cdd:pfam00270  66 KKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILR 143

                         170       180
                  ....*....|....*....|....*.
gi 17985987   479 QLNmpptGQRQTLMFSATFPKQIQEL 504
Cdd:pfam00270 144 RLP----KKRQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 527-663 9.30e-59

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: 195.80  E-value: 9.30e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 527 ITQTILWVYEPDKRSYLLDLLSSIRdgpeytKDSLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFR 606
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKL------KPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFR 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17985987 607 SGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFF 663
Cdd:cd18787  75 SGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
315-529 2.28e-55

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 189.24  E-value: 2.28e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987    315 YDKPTPVQKHAIPIIING-RDLMACAQTGSGKTAAFLVPILnqmyelghvpppqstrQYSRRKQYPLGLVLAPTRELATQ 393
Cdd:smart00487   6 FEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPAL----------------EALKRGKGGRVLVLVPTRELAEQ 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987    394 IFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGC-HLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQ 472
Cdd:smart00487  70 WAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQ 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 17985987    473 IRRIVEQLNmpptGQRQTLMFSATFPKQIQELASDFLSNYIFLAVGRvgSTSENITQ 529
Cdd:smart00487 150 LEKLLKLLP----KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQ 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 538-654 1.04e-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: 136.19  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987   538 DKRSYLLDLLSSIRDGPeytkdslTLIFVETKKGADsLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILVATA 617
Cdd:pfam00271   1 EKLEALLELLKKERGGK-------VLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATD 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17985987   618 VAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMG 654
Cdd:pfam00271  73 VAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
573-654 7.85e-31

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 115.77  E-value: 7.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987    573 DSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGR 652
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 17985987    653 MG 654
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
535-652 6.17e-16

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 82.09  E-value: 6.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 535 YEPDKRSYLLDLLSSIRDGpeyTKDSLTLIFVETKKGADSLEEFLYQCNHPVT------SIHGDR--TQKEREEALRCFR 606
Cdd:COG1111 332 IEHPKLSKLREILKEQLGT---NPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFR 408

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17985987 607 SGDCPILVATAVAARGLDIPHVKHVINFDL-PSDVeEYVHRIGRTGR 652
Cdd:COG1111 409 AGEFNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR 454
PRK13766 PRK13766
Hef nuclease; Provisional
 558-652 6.78e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 62.58  E-value: 6.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  558 KDSLTLIFVETKKGADSLEEFLYQCNHPV------TSIHGDR--TQKEREEALRCFRSGDCPILVATAVAARGLDIPHVK 629
Cdd:PRK13766 364 PDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVD 443

                         90       100
                 ....*....|....*....|....
gi 17985987  630 HVINFD-LPSDVeEYVHRIGRTGR 652
Cdd:PRK13766 444 LVIFYEpVPSEI-RSIQRKGRTGR 466
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 275-522 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: 538.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 275 FDKYEDIPVEATGQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPIL 354
Cdd:cd18051   1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 355 NQMYELGH-VPPPQSTRQYSRRKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIV 433
Cdd:cd18051  81 SQIYEQGPgESLPSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 434 ATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNMPPTGQRQTLMFSATFPKQIQELASDFLSNYI 513
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYI 240


                ....*....
gi 17985987 514 FLAVGRVGS 522
Cdd:cd18051 241 FLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
294-686 8.06e-165

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 483.50  E-value: 8.06e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 294 ITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMyelghvpppqstrQYS 373
Cdd:COG0513   1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-------------DPS 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 374 RRKQyPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENI 453
Cdd:COG0513  68 RPRA-PQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGV 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 454 RFLVLDEADRMLDMGFEPQIRRIVEQLnmPPtgQRQTLMFSATFPKQIQELASDFLSNYIFLAVGRVGSTSENITQTILW 533
Cdd:COG0513 147 ETLVLDEADRMLDMGFIEDIERILKLL--PK--ERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYL 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 534 VYEPDKRSYLLDLLSSIRDGpeytkdsLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPIL 613
Cdd:COG0513 223 VDKRDKLELLRRLLRDEDPE-------RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVL 295

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17985987 614 VATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFFNEKNRNICSDLLELlieTKQEIP 686
Cdd:COG0513 296 VATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKL---IGQKIE 365
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 296-521 3.97e-151

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: 440.39  E-value: 3.97e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 296 SFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYELGHVPPPqstrqYSRR 375
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVG-----RGRR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 376 KQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRF 455
Cdd:cd17967  76 KAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKF 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17985987 456 LVLDEADRMLDMGFEPQIRRIVEQLNMPPTGQRQTLMFSATFPKQIQELASDFLSNYIFLAVGRVG 521
Cdd:cd17967 156 LVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 262-521 2.71e-149

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: 437.48  E-value: 2.71e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 262 EVELFGVGNTGINFDKYEDIPVEATGQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQT 341
Cdd:cd18052  10 EDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQT 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 342 GSGKTAAFLVPILNQMYELGhVPPPQSTRQysrrkQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQ 421
Cdd:cd18052  90 GSGKTAAFLLPVLTGMMKEG-LTASSFSEV-----QEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQ 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 422 MRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNMPPTGQRQTLMFSATFPKQI 501
Cdd:cd18052 164 IRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEI 243

                       250       260
                ....*....|....*....|.
gi 17985987 502 QELASDFL-SNYIFLAVGRVG 521
Cdd:cd18052 244 QRLAAEFLkEDYLFLTVGRVG 264
PTZ00110 PTZ00110
helicase; Provisional
 287-697 1.36e-115

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 361.01  E-value: 1.36e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  287 GQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPilnqmyELGHVppp 366
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLP------AIVHI--- 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  367 qSTRQYSRRKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRG 446
Cdd:PTZ00110 193 -NAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESN 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  447 KVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNmpPtgQRQTLMFSATFPKQIQELASDFLSNY-IFLAVGRVG-STS 524
Cdd:PTZ00110 272 VTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIR--P--DRQTLMWSATWPKEVQSLARDLCKEEpVHVNVGSLDlTAC 347

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  525 ENITQTILWVYEPDKRSYLLDLLSSI-RDGPEytkdslTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALR 603
Cdd:PTZ00110 348 HNIKQEVFVVEEHEKRGKLKMLLQRImRDGDK------ILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLN 421

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  604 CFRSGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFFNEKNRNICSDLLELLIETKQ 683
Cdd:PTZ00110 422 EFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQ 501

                        410
                 ....*....|....
gi 17985987  684 EIPSFMEDMSSDRG 697
Cdd:PTZ00110 502 PVPPELEKLSNERS 515
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 253-686 1.84e-98

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 315.19  E-value: 1.84e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  253 KLGARDERLEVELFGVGNTGINFDK---YEDIPVEATGQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPII 329
Cdd:PLN00206  76 RLPATDECFYVRDPGSTSGLSSSQAellRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAA 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  330 INGRDLMACAQTGSGKTAAFLVPILNQ--MYELGHVPppqstrqySRRKqyPLGLVLAPTRELATQIFEEAKKFAYRSRM 407
Cdd:PLN00206 156 LSGRSLLVSADTGSGKTASFLVPIISRccTIRSGHPS--------EQRN--PLAMVLTPTRELCVQVEDQAKVLGKGLPF 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  408 RPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNMPptgq 487
Cdd:PLN00206 226 KTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP---- 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  488 rQTLMFSATFPKQIQELASDFLSNYIFLAVGRVGSTSENITQTILWVYEPDKRSYLLDLL-SSIRDGPEytkdslTLIFV 566
Cdd:PLN00206 302 -QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILkSKQHFKPP------AVVFV 374

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  567 ETKKGADSLEEFLYQCNH-PVTSIHGDRTQKEREEALRCFRSGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVH 645
Cdd:PLN00206 375 SSRLGADLLANAITVVTGlKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIH 454

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 17985987  646 RIGRTGRMGNLGVATSFFNEKNRNICSDLLELLIETKQEIP 686
Cdd:PLN00206 455 QIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIP 495
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 295-666 1.69e-93

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 300.18  E-value: 1.69e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  295 TSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMyelghvpppqSTRQYsr 374
Cdd:PRK11776   4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL----------DVKRF-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  375 RKQyplGLVLAPTRELATQIFEEAKKFAyrsRMRPAV----LYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGL 450
Cdd:PRK11776  72 RVQ---ALVLCPTRELADQVAKEIRRLA---RFIPNIkvltLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  451 ENIRFLVLDEADRMLDMGFEPQIRRIVEQlnMPPtgQRQTLMFSATFPKQIQELASDFLSNYifLAVgRVGSTSEN--IT 528
Cdd:PRK11776 146 DALNTLVLDEADRMLDMGFQDAIDAIIRQ--APA--RRQTLLFSATYPEGIAAISQRFQRDP--VEV-KVESTHDLpaIE 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  529 QtilWVYE--PDKRSYLLDLLSSirdgpEYTKDSlTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFR 606
Cdd:PRK11776 219 Q---RFYEvsPDERLPALQRLLL-----HHQPES-CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFA 289

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  607 SGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFFNEK 666
Cdd:PRK11776 290 NRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 296-686 5.37e-91

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 293.64  E-value: 5.37e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  296 SFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYElgHVPPPQSTRqysrr 375
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLIT--RQPHAKGRR----- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  376 kqyPL-GLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIR 454
Cdd:PRK10590  75 ---PVrALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  455 FLVLDEADRMLDMGFEPQIRRIVEQLnmPPtgQRQTLMFSATFPKQIQELASDFLSNYIFLAVGRVGSTSENITQTILWV 534
Cdd:PRK10590 152 ILVLDEADRMLDMGFIHDIRRVLAKL--PA--KRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFV 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  535 YEPDKRsyllDLLSSIRDGPEYTKdslTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILV 614
Cdd:PRK10590 228 DKKRKR----ELLSQMIGKGNWQQ---VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLV 300

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17985987  615 ATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFfneknrnICSDLLELL--IET--KQEIP 686
Cdd:PRK10590 301 ATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSL-------VCVDEHKLLrdIEKllKKEIP 369
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 306-515 1.62e-90

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: 282.79  E-value: 1.62e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 306 IRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYELGHVPPPQstrqysrrkqyPLGLVLA 385
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRG-----------PQALVLA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 386 PTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRML 465
Cdd:cd00268  70 PTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRML 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17985987 466 DMGFEPQIRRIVEQLNMpptgQRQTLMFSATFPKQIQELASDFLSNYIFL 515
Cdd:cd00268 150 DMGFEEDVEKILSALPK----DRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 295-662 3.73e-85

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 277.21  E-value: 3.73e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  295 TSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILnqmyelghvpppQSTRQYSR 374
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAL------------QHLLDFPR 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  375 RKQ-YPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENI 453
Cdd:PRK11192  69 RKSgPPRILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  454 RFLVLDEADRMLDMGFEPQIRRIVEQLNmpptGQRQTLMFSATFP-KQIQELASDFLSNYIFLAVGrvGSTSE--NITQt 530
Cdd:PRK11192 149 ETLILDEADRMLDMGFAQDIETIAAETR----WRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAE--PSRRErkKIHQ- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  531 ilWVYEPDKRSYLLDLLSSIRDGPEYTKdslTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDC 610
Cdd:PRK11192 222 --WYYRADDLEHKTALLCHLLKQPEVTR---SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRV 296

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17985987  611 PILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSF 662
Cdd:PRK11192 297 NVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 295-662 2.76e-84

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 274.54  E-value: 2.76e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  295 TSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNqmYELGHvPPPQStrqysR 374
Cdd:PRK04837   8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFH--YLLSH-PAPED-----R 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  375 RKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIR 454
Cdd:PRK04837  80 KVNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  455 FLVLDEADRMLDMGFEPQIRRIVEQlnMPPTGQRQTLMFSATFPKQIQELASDFLSNYIFLAVGRVGSTSENITQTILWV 534
Cdd:PRK04837 160 VVVLDEADRMFDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  535 YEPDKRSYLLDLLSsiRDGPEYTkdsltLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILV 614
Cdd:PRK04837 238 SNEEKMRLLQTLIE--EEWPDRA-----IIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILV 310

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 17985987  615 ATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSF 662
Cdd:PRK04837 311 ATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 277-665 3.05e-83

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 273.71  E-value: 3.05e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  277 KYEDIPVEATgqnvpPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQ 356
Cdd:PRK01297  74 KLEDFVVEPQ-----EGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQ 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  357 myeLGHVPPPQStrqysRRKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELD-RGCHLIVAT 435
Cdd:PRK01297 149 ---LLQTPPPKE-----RYMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVAT 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  436 PGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQlnMPPTGQRQTLMFSATFPKQIQELASDFLSNYIFL 515
Cdd:PRK01297 221 PGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQ--TPRKEERQTLLFSATFTDDVMNLAKQWTTDPAIV 298

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  516 AVGRVGSTSENITQTILWVYEPDKRSYLLDLLssiRDGPeYTKdslTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQ 595
Cdd:PRK01297 299 EIEPENVASDTVEQHVYAVAGSDKYKLLYNLV---TQNP-WER---VMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQ 371

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  596 KEREEALRCFRSGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFFNE 665
Cdd:PRK01297 372 HKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGE 441
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 293-687 5.98e-76

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 257.19  E-value: 5.98e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  293 NITSFDdvqLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYelghvpppqsTRQ- 371
Cdd:PRK04537  10 TFSSFD---LHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLL----------SRPa 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  372 -YSRRKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKV-G 449
Cdd:PRK04537  77 lADRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  450 LENIRFLVLDEADRMLDMGFEPQIRRIVEQlnMPPTGQRQTLMFSATFPKQIQELASDFLSNYIFLAVGRVGSTSENITQ 529
Cdd:PRK04537 157 LHACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  530 TILWVYEPDKRSYLLDLLSSirdgpeyTKDSLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGD 609
Cdd:PRK04537 235 RIYFPADEEKQTLLLGLLSR-------SEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQ 307

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17985987  610 CPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFFNEKNRNICSDlLELLIEtkQEIPS 687
Cdd:PRK04537 308 LEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPD-IEAYIE--QKIPV 382
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 302-515 3.36e-75

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: 242.27  E-value: 3.36e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 302 LTEIIRNNvalarYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPilnqmyELGHVpppqSTRQYSRRKQYPLG 381
Cdd:cd17966   2 MDELKRQG-----FTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLP------AIVHI----NAQPPLERGDGPIV 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 382 LVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEA 461
Cdd:cd17966  67 LVLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEA 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17985987 462 DRMLDMGFEPQIRRIVEQLNmPptgQRQTLMFSATFPKQIQELASDFLSNYIFL 515
Cdd:cd17966 147 DRMLDMGFEPQIRKIVDQIR-P---DRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 295-670 3.70e-70

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 242.83  E-value: 3.70e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  295 TSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYElgHVPPPQStrqysr 374
Cdd:PRK11634   6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDP--ELKAPQI------ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  375 rkqyplgLVLAPTRELATQIFEEAKKFAYRSRMRPAV-LYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENI 453
Cdd:PRK11634  78 -------LVLAPTRELAVQVAEAMTDFSKHMRGVNVVaLYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  454 RFLVLDEADRMLDMGFEPQIRRIVEQLnmpPTGQrQTLMFSATFPKQIQELASDFLSNYIFLAVGRVGSTSENITQTILW 533
Cdd:PRK11634 151 SGLVLDEADEMLRMGFIEDVETIMAQI---PEGH-QTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWT 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  534 VYEPDKRSYLLDLLssirdgpEYTKDSLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPIL 613
Cdd:PRK11634 227 VWGMRKNEALVRFL-------EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDIL 299

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17985987  614 VATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFFNEKNRNI 670
Cdd:PRK11634 300 IATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRL 356
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 285-513 1.46e-69

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


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 228.42  E-value: 1.46e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 285 ATGQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYelgHVP 364
Cdd:cd17953   2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIK---DQR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 365 PPQStrqysrrKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMIT 444
Cdd:cd17953  79 PVKP-------GEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILT 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17985987 445 --RGKV-GLENIRFLVLDEADRMLDMGFEPQIRRIVEqlNMPPtgQRQTLMFSATFPKQIQELASDFLSNYI 513
Cdd:cd17953 152 anNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIVN--NIRP--DRQTVLFSATFPRKVEALARKVLHKPI 219
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 306-513 6.19e-69

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


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 225.76  E-value: 6.19e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 306 IRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNqmyelgHVpppqSTRQYSRRKQYPLGLVLA 385
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLV------HI----MDQRELEKGEGPIAVIVA 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 386 PTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRML 465
Cdd:cd17952  71 PTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMF 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17985987 466 DMGFEPQIRRIVEQLNmPptgQRQTLMFSATFPKQIQELASDFLSNYI 513
Cdd:cd17952 151 DMGFEYQVRSIVGHVR-P---DRQTLLFSATFKKKIEQLARDILSDPI 194
PTZ00424 PTZ00424
helicase 45; Provisional
 294-662 2.08e-67

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 228.94  E-value: 2.08e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  294 ITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMyelghvpppqstrQYS 373
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI-------------DYD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  374 RRKQYplGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENI 453
Cdd:PTZ00424  94 LNACQ--ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  454 RFLVLDEADRMLDMGFEPQIRRIVEQLnmPPtgQRQTLMFSATFPKQIQELASDFLSNYIFLAVGRVGSTSENITQTILW 533
Cdd:PTZ00424 172 KLFILDEADEMLSRGFKGQIYDVFKKL--PP--DVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVA 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  534 VyepDKRSYLLDLLSSIRDGPEYTKdslTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPIL 613
Cdd:PTZ00424 248 V---EKEEWKFDTLCDLYETLTITQ---AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVL 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 17985987  614 VATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSF 662
Cdd:PTZ00424 322 ITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINF 370
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 302-515 5.59e-67

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: 221.42  E-value: 5.59e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 302 LTEIIRNnvalARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYELghvpPPqstRQYSRRKQYPLG 381
Cdd:cd17945   1 LLRVIRK----LGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRL----PP---LDEETKDDGPYA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 382 LVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEA 461
Cdd:cd17945  70 LILAPTRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEA 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17985987 462 DRMLDMGFEPQIRRIVEQlnMPPTG------------------QRQTLMFSATFPKQIQELASDFLSNYIFL 515
Cdd:cd17945 150 DRMIDMGFEPQVTKILDA--MPVSNkkpdteeaeklaasgkhrYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 283-518 3.98e-62

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: 208.71  E-value: 3.98e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 283 VEATGQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPilnQMYELGH 362
Cdd:cd18049  12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLP---AIVHINH 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 363 VPppqstrqYSRRKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDM 442
Cdd:cd18049  89 QP-------FLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17985987 443 ITRGKVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNmpptGQRQTLMFSATFPKQIQELASDFLSNYIFLAVG 518
Cdd:cd18049 162 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 319-504 1.36e-61

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 204.78  E-value: 1.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987   319 TPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMyelghvpppqstrqySRRKQYPLGLVLAPTRELATQIFEEA 398
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL---------------DKLDNGPQALVLAPTRELAEQIYEEL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987   399 KKFAYRSRMRPAVLYGGNNTSEQMRELdRGCHLIVATPGRLEDMITRgKVGLENIRFLVLDEADRMLDMGFEPQIRRIVE 478
Cdd:pfam00270  66 KKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILR 143

                         170       180
                  ....*....|....*....|....*.
gi 17985987   479 QLNmpptGQRQTLMFSATFPKQIQEL 504
Cdd:pfam00270 144 RLP----KKRQILLLSATLPRNLEDL 165
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 287-518 2.59e-61

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: 207.94  E-value: 2.59e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 287 GQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPilnQMYELGHVPpp 366
Cdd:cd18050  54 GVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLP---AIVHINHQP-- 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 367 qstrqYSRRKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRG 446
Cdd:cd18050 129 -----YLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAG 203

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17985987 447 KVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNmpptGQRQTLMFSATFPKQIQELASDFLSNYIFLAVG 518
Cdd:cd18050 204 KTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 313-515 2.83e-61

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: 205.51  E-value: 2.83e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 313 ARYDKPTPVQKHAIPIII-NGRDLMACAQTGSGKTAAFLVPILNQMYElghVPPPQSTRQYSrrkqyplGLVLAPTRELA 391
Cdd:cd17964  12 MGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLN---TKPAGRRSGVS-------ALIISPTRELA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 392 TQIFEEAKKFAYRSR-MRPAVLYGGNNTSEQMRELDR-GCHLIVATPGRLEDMI--TRGKVGLENIRFLVLDEADRMLDM 467
Cdd:cd17964  82 LQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLenPGVAKAFTDLDYLVLDEADRLLDM 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17985987 468 GFEPQIRRIVEQLNMPPTGQRQTLMFSATFPKQIQELASDFL-SNYIFL 515
Cdd:cd17964 162 GFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLkKDYKFI 210
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 306-518 2.54e-60

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: 202.43  E-value: 2.54e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 306 IRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYElghvpppqstrqySRRKQYPLGLVLA 385
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK-------------PRKKKGLRALILA 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 386 PTRELATQIFEEAKKFAYRSRMRPAVLYGGN-NTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRM 464
Cdd:cd17957  68 PTRELASQIYRELLKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKL 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17985987 465 LDMGFEPQIRRIVEQLNMPptgQRQTLMFSATFPKQIQELASDFLSNYIFLAVG 518
Cdd:cd17957 148 FEPGFREQTDEILAACTNP---NLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 527-663 9.30e-59

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: 195.80  E-value: 9.30e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 527 ITQTILWVYEPDKRSYLLDLLSSIRdgpeytKDSLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFR 606
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKL------KPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFR 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17985987 607 SGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFF 663
Cdd:cd18787  75 SGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 315-506 1.74e-58

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 197.48  E-value: 1.74e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 315 YDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQmyeLGHVPPpqsTRQYSRrkqyplGLVLAPTRELATQI 394
Cdd:cd17947  10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILER---LLYRPK---KKAATR------VLVLVPTRELAMQC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 395 FEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGK-VGLENIRFLVLDEADRMLDMGFEPQI 473
Cdd:cd17947  78 FSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADEL 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 17985987 474 RRIVEQLnmppTGQRQTLMFSATFPKQIQELAS 506
Cdd:cd17947 158 KEILRLC----PRTRQTMLFSATMTDEVKDLAK 186
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 317-505 1.66e-57

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: 195.25  E-value: 1.66e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 317 KPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYElghvpppQSTRQYSRRKQYPLGLVLAPTRELATQIFE 396
Cdd:cd17951  12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALE-------QEKKLPFIKGEGPYGLIVCPSRELARQTHE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 397 EAKKFAYR------SRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFE 470
Cdd:cd17951  85 VIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFE 164

                       170       180       190
                ....*....|....*....|....*....|....*
gi 17985987 471 PQIRRIVEQLnmppTGQRQTLMFSATFPKQIQELA 505
Cdd:cd17951 165 EDIRTIFSYF----KGQRQTLLFSATMPKKIQNFA 195
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 302-511 1.72e-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: 189.21  E-value: 1.72e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 302 LTEIIRNNvalarYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPilnQMYELGHVPPPQSTRQYsrrkqyPLG 381
Cdd:cd17958   2 MKEIKKQG-----FEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLP---GFIHLDLQPIPREQRNG------PGV 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 382 LVLAPTRELATQIFEEAKKFAYRSrMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEA 461
Cdd:cd17958  68 LVLTPTRELALQIEAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEA 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17985987 462 DRMLDMGFEPQIRRIVeqLNMPPtgQRQTLMFSATFPKQIQELASDFLSN 511
Cdd:cd17958 147 DRMLDMGFEPQIRKIL--LDIRP--DRQTIMTSATWPDGVRRLAQSYLKD 192
DEXDc smart00487
DEAD-like helicases superfamily;
315-529 2.28e-55

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 189.24  E-value: 2.28e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987    315 YDKPTPVQKHAIPIIING-RDLMACAQTGSGKTAAFLVPILnqmyelghvpppqstrQYSRRKQYPLGLVLAPTRELATQ 393
Cdd:smart00487   6 FEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPAL----------------EALKRGKGGRVLVLVPTRELAEQ 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987    394 IFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGC-HLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQ 472
Cdd:smart00487  70 WAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQ 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 17985987    473 IRRIVEQLNmpptGQRQTLMFSATFPKQIQELASDFLSNYIFLAVGRvgSTSENITQ 529
Cdd:smart00487 150 LEKLLKLLP----KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQ 200
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 297-514 3.08e-55

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: 188.97  E-value: 3.08e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 297 FDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMyelghvpppqSTRQYSrrk 376
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL----------SEDPYG--- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 377 qyPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMIT---RGKVGLENI 453
Cdd:cd17955  68 --IFALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRV 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17985987 454 RFLVLDEADRMLDMGFEPQIRRIVEQLnmPPtgQRQTLMFSATFPKQIQELASDFLSNYIF 514
Cdd:cd17955 146 KFLVLDEADRLLTGSFEDDLATILSAL--PP--KRQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 314-515 1.72e-54

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: 187.02  E-value: 1.72e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 314 RYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMyelghvpppQSTRQYSRRKQYPLGLVLAPTRELATQ 393
Cdd:cd17949  10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL---------LSLEPRVDRSDGTLALVLVPTRELALQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 394 IFEEAKKFAYRSR-MRPAVLYGGNN-TSEQMReLDRGCHLIVATPGRLEDMITRGKV-GLENIRFLVLDEADRMLDMGFE 470
Cdd:cd17949  81 IYEVLEKLLKPFHwIVPGYLIGGEKrKSEKAR-LRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMGFE 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17985987 471 PQIRRIVEQLN---------MPPTGQRQTLMFSATFPKQIQELASDFLSNYIFL 515
Cdd:cd17949 160 KDITKILELLDdkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 306-511 1.95e-53

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: 183.93  E-value: 1.95e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 306 IRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYElghvpppqstRQYSRRKQYPLGLVLA 385
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLK----------RKANLKKGQVGALIIS 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 386 PTRELATQIFEEAKKFA--YRSRMRPAVLYGGNNTSEQMRELDR-GCHLIVATPGRLEDMITR--GKVGLENIRFLVLDE 460
Cdd:cd17960  71 PTRELATQIYEVLQSFLehHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDE 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17985987 461 ADRMLDMGFEPQIRRIVEQLnmpPTgQRQTLMFSATFPKQIQELASDFLSN 511
Cdd:cd17960 151 ADRLLDLGFEADLNRILSKL---PK-QRRTGLFSATQTDAVEELIKAGLRN 197
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 315-515 3.17e-52

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: 180.58  E-value: 3.17e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 315 YDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYElghvpppQSTRQYSRrkqyplGLVLAPTRELATQI 394
Cdd:cd17959  21 YKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKA-------HSPTVGAR------ALILSPTRELALQT 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 395 FEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIR 474
Cdd:cd17959  88 LKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLH 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17985987 475 RIVEQLnmPPTgqRQTLMFSATFPKQIQELASDFLSNYIFL 515
Cdd:cd17959 168 EILSRL--PEN--RQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 296-511 7.74e-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: 179.43  E-value: 7.74e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 296 SFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYElghvpppqstrqysrR 375
Cdd:cd17954   1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLE---------------N 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 376 KQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGK-VGLENIR 454
Cdd:cd17954  66 PQRFFALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLK 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17985987 455 FLVLDEADRMLDMGFEPQIRRIVEQLnmpPTgQRQTLMFSATFPKQIQELASDFLSN 511
Cdd:cd17954 146 FLVMDEADRLLNMDFEPEIDKILKVI---PR-ERTTYLFSATMTTKVAKLQRASLKN 198
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 313-517 8.33e-50

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: 173.63  E-value: 8.33e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 313 ARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYELghvpppqstrQYSRRKQypLG-LVLAPTRELA 391
Cdd:cd17941   8 AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE----------RWTPEDG--LGaLIISPTRELA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 392 TQIFEEAKKFAYRSRMRPAVLYGGNNTSEqmrELDR--GCHLIVATPGR-LEDMITRGKVGLENIRFLVLDEADRMLDMG 468
Cdd:cd17941  76 MQIFEVLRKVGKYHSFSAGLIIGGKDVKE---EKERinRMNILVCTPGRlLQHMDETPGFDTSNLQMLVLDEADRILDMG 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17985987 469 FEPQIRRIVEQLnmPPtgQRQTLMFSATFPKQIQELASDFLSNYIFLAV 517
Cdd:cd17941 153 FKETLDAIVENL--PK--SRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 309-513 1.19e-49

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: 173.12  E-value: 1.19e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 309 NVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYElghvpppqstrqysrRKQYPLGLVLAPTR 388
Cdd:cd17962   4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT---------------EHRNPSALILTPTR 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 389 ELATQIFEEAKKFAY-RSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDM 467
Cdd:cd17962  69 ELAVQIEDQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKM 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17985987 468 GFEPQIRRIVEQLnmppTGQRQTLMFSATFPKQIQELASDFLSNYI 513
Cdd:cd17962 149 GFQQQVLDILENI----SHDHQTILVSATIPRGIEQLAGQLLQNPV 190
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 306-497 9.90e-47

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: 166.26  E-value: 9.90e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 306 IRNNVALARYDKPTPVQKHAIP-IIINGRDLMACAQTGSGKTAAFLVPILNQMYELghvpppQSTRQYSRRKQYPLGLVL 384
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQ------KSSNGVGGKQKPLRALIL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 385 APTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGK---VGLENIRFLVLDEA 461
Cdd:cd17946  75 TPTRELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEA 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17985987 462 DRMLDMG-FEpQIRRIVEQLNMPPTG---QRQTLMFSATF 497
Cdd:cd17946 155 DRMLEKGhFA-ELEKILELLNKDRAGkkrKRQTFVFSATL 193
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 297-511 1.99e-46

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: 164.39  E-value: 1.99e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 297 FDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMY-ELGHVpppQStrqysrr 375
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDpKKDVI---QA------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 376 kqyplgLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRF 455
Cdd:cd17940  71 ------LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKT 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17985987 456 LVLDEADRMLDMGFEPQIRRIVEQLnmPPtgQRQTLMFSATFPKQIQELASDFLSN 511
Cdd:cd17940 145 LVLDEADKLLSQDFQPIIEKILNFL--PK--ERQILLFSATFPLTVKNFMDRHMHN 196
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 302-496 4.93e-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: 163.26  E-value: 4.93e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 302 LTEIIRNnVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILnqmyelghvpppqstrqysrrkQYPLG 381
Cdd:cd17938   7 MPELIKA-VEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------------QIVVA 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 382 LVLAPTRELATQIFEEAKKFAY---RSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVL 458
Cdd:cd17938  64 LILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVL 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17985987 459 DEADRMLDMGFEPQIRRIVEQlnMP---PTGQR-QTLMFSAT 496
Cdd:cd17938 144 DEADRLLSQGNLETINRIYNR--IPkitSDGKRlQVIVCSAT 183
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 315-511 5.20e-46

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: 163.26  E-value: 5.20e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 315 YDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILnqmyelghvpppqstRQYSRRKQYPLGLVLAPTRELATQI 394
Cdd:cd17939  17 FEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGAL---------------QRIDTTVRETQALVLAPTRELAQQI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 395 FEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIR 474
Cdd:cd17939  82 QKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIY 161

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17985987 475 RIVEQLNmpptGQRQTLMFSATFPKQIQELASDFLSN 511
Cdd:cd17939 162 DIFQFLP----PETQVVLFSATMPHEVLEVTKKFMRD 194
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 297-513 1.92e-41

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: 150.29  E-value: 1.92e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 297 FDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQM-YELGHvppPQStrqysrr 375
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIdTSLKA---TQA------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 376 kqyplgLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRF 455
Cdd:cd18046  71 ------LVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKM 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17985987 456 LVLDEADRMLDMGFEPQIRRIVEQLnmPPTgqRQTLMFSATFPKQIQELASDFLSNYI 513
Cdd:cd18046 145 FVLDEADEMLSRGFKDQIYDIFQKL--PPD--TQVVLLSATMPNDVLEVTTKFMRDPI 198
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 315-505 3.29e-41

DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 149.43  E-value: 3.29e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 315 YDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYELGHVPppqstrqysrrKQYPLGLVLAPTRELATQI 394
Cdd:cd17942  10 FTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKP-----------RNGTGVIIISPTRELALQI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 395 FEEAKKF-AYRSRMRpAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGL-ENIRFLVLDEADRMLDMGFEPQ 472
Cdd:cd17942  79 YGVAKELlKYHSQTF-GIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILEIGFEEE 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 17985987 473 IRRIVEQLnmpPTgQRQTLMFSATFPKQIQELA 505
Cdd:cd17942 158 MRQIIKLL---PK-RRQTMLFSATQTRKVEDLA 186
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 311-517 6.46e-40

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: 146.19  E-value: 6.46e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 311 ALAR--YDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYELghvpppqstRQYSRRKQYPLGLVLAPTR 388
Cdd:cd17961   8 AIAKlgWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKA---------KAESGEEQGTRALILVPTR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 389 ELATQIFEEAKKFAY--RSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRG-KVGLENIRFLVLDEADRML 465
Cdd:cd17961  79 ELAQQVSKVLEQLTAycRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGsLLLLSTLKYLVIDEADLVL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17985987 466 DMGFEPQIRRIVEQLnmpPTGqRQTLMFSATFPKQIQELASDFLSNYIFLAV 517
Cdd:cd17961 159 SYGYEEDLKSLLSYL---PKN-YQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 313-514 1.05e-39

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: 145.10  E-value: 1.05e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 313 ARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMyelghvpppqstrqySRRKQYPLGLVLAPTRELAT 392
Cdd:cd17943   8 AGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL---------------DLERRHPQVLILAPTREIAV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 393 QIFEEAKKFA-YRSRMRPAVLYGGNNTSEQMRELdRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEP 471
Cdd:cd17943  73 QIHDVFKKIGkKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQK 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17985987 472 QIRRIVEQLnmpPTgQRQTLMFSATFPKQIQELASDFLSNYIF 514
Cdd:cd17943 152 DVNWIFSSL---PK-NKQVIAFSATYPKNLDNLLARYMRKPVL 190
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 317-507 2.52e-38

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: 142.51  E-value: 2.52e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 317 KPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYELGHVPppqstrqySRRKQYPLGLVLAPTRELATQIFE 396
Cdd:cd17948  12 KPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLA--------EGPFNAPRGLVITPSRELAEQIGS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 397 EAKKFAYRSRMRPAVLYGGnNTSEQMR-----ELDrgchLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEP 471
Cdd:cd17948  84 VAQSLTEGLGLKVKVITGG-RTKRQIRnphfeEVD----ILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNE 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17985987 472 QIRRIVEQL-----NMPPTGQR----QTLMFSATFPKQIQELASD 507
Cdd:cd17948 159 KLSHFLRRFplasrRSENTDGLdpgtQLVLVSATMPSGVGEVLSK 203
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 295-511 3.08e-38

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: 141.33  E-value: 3.08e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 295 TSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQmyeLGHVPPPQSTrqysr 374
Cdd:cd17950   2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQ---LEPVDGQVSV----- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 375 rkqyplgLVLAPTRELATQIFEEAKKFA-YRSRMRPAVLYGGNNTSEQMREL-DRGCHLIVATPGRLEDMITRGKVGLEN 452
Cdd:cd17950  74 -------LVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSH 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17985987 453 IRFLVLDEADRM---LDMgfepqiRRIVEQLNMPPTGQRQTLMFSATFPKQIQELASDFLSN 511
Cdd:cd17950 147 VKHFVLDECDKMleqLDM------RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQD 202
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 538-654 1.04e-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: 136.19  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987   538 DKRSYLLDLLSSIRDGPeytkdslTLIFVETKKGADsLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILVATA 617
Cdd:pfam00271   1 EKLEALLELLKKERGGK-------VLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATD 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17985987   618 VAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMG 654
Cdd:pfam00271  73 VAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 297-511 5.74e-37

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: 137.60  E-value: 5.74e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 297 FDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILnQMYELghvpppqSTRQysrrk 376
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDI-------QVRE----- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 377 qyPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFL 456
Cdd:cd18045  68 --TQALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKML 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17985987 457 VLDEADRMLDMGFEPQIRRIVEQLnmPPTgqRQTLMFSATFPKQIQELASDFLSN 511
Cdd:cd18045 146 VLDEADEMLNKGFKEQIYDVYRYL--PPA--TQVVLVSATLPQDILEMTNKFMTD 196
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 315-515 1.95e-36

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: 135.78  E-value: 1.95e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 315 YDKPTPVQKHAIPIIING--RDLMACAQTGSGKTAAFLVPILNQmyelghVPPpqstrqysrRKQYPLGLVLAPTRELAT 392
Cdd:cd17963  14 FNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSR------VDP---------TLKSPQALCLAPTRELAR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 393 QIFEEAKKFAYRSRMRPAVLYGGN--NTSEQMREldrgcHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDM-GF 469
Cdd:cd17963  79 QIGEVVEKMGKFTGVKVALAVPGNdvPRGKKITA-----QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGH 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17985987 470 EPQIRRIVEQLNMPptgqRQTLMFSATFPKQIQELASDFLSNYIFL 515
Cdd:cd17963 154 GDQSIRIKRMLPRN----CQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 320-509 1.47e-33

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


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 128.04  E-value: 1.47e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 320 PVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMyelghvpppQSTRQYSRRKQYPLGLVLAPTRELATQIFEEAK 399
Cdd:cd17944  15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKL---------QEDQQPRKRGRAPKVLVLAPTRELANQVTKDFK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 400 KFAyrSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIRRIV-E 478
Cdd:cd17944  86 DIT--RKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsV 163

                       170       180       190
                ....*....|....*....|....*....|.
gi 17985987 479 QLNMPPTGQRQTLMFSATFPKQIQELASDFL 509
Cdd:cd17944 164 SYKKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
HELICc smart00490
helicase superfamily c-terminal domain;
573-654 7.85e-31

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 115.77  E-value: 7.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987    573 DSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGR 652
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 17985987    653 MG 654
Cdd:smart00490  81 AG 82
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 320-506 1.45e-27

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 111.57  E-value: 1.45e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 320 PVQKHAIPIIING---------RDLMACAQTGSGKTAAFLVPILNQMyelghvpppqSTRQYSRRKqyplGLVLAPTREL 390
Cdd:cd17956  15 PVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQAL----------SKRVVPRLR----ALIVVPTKEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 391 ATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHL--------IVATPGRLEDMITRGK-VGLENIRFLVLDEA 461
Cdd:cd17956  81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGrylsrvdiLVATPGRLVDHLNSTPgFTLKHLRFLVIDEA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17985987 462 DRMLDMGF--------------EPQIRRIVEQLNM--PPTGQRQTLMFSATFPKQIQELAS 506
Cdd:cd17956 161 DRLLNQSFqdwletvmkalgrpTAPDLGSFGDANLleRSVRPLQKLLFSATLTRDPEKLSS 221
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 297-499 1.04e-22

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


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 98.22  E-value: 1.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 297 FDDVQLTEIIRN---NVALARYD------KPTPVQKHAIPIII---------------NGRDL-MACAQTGSGKTAAFLV 351
Cdd:cd17965   1 FDQLKLLPSVREaiiKEILKGSNktdeeiKPSPIQTLAIKKLLktlmrkvtkqtsneePKLEVfLLAAETGSGKTLAYLA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 352 PILNQMYELGHVPPPQSTRQYSRRKQY--PLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMREL--DR 427
Cdd:cd17965  81 PLLDYLKRQEQEPFEEAEEEYESAKDTgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLafKG 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17985987 428 GCHLIVATPGRLEDMI-TRGKVgLENIRFLVLDEADRMLDMGFEPQIRRIVEQlnMPPTGQrqtLMF-SATFPK 499
Cdd:cd17965 161 RIDILVTTPGKLASLAkSRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APKLKH---LILcSATIPK 228
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
331-649 2.58e-21

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 98.94  E-value: 2.58e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 331 NGRDLMACAQTGSGKT--AAFLVpilNQMYELGHVpppqstrqysrrkqyplgLVLAPTRELATQIFEEAKKFayrsrmR 408
Cdd:COG1061  99 GGGRGLVVAPTGTGKTvlALALA---AELLRGKRV------------------LVLVPRRELLEQWAEELRRF------L 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 409 PAVLYGGNntseqmrELDRGCHLIVATPGRLEDMITRGKVGlENIRFLVLDEADRmldmGFEPQIRRIVEQLNmpptgQR 488
Cdd:COG1061 152 GDPLAGGG-------KKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFP-----AA 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 489 QTLMFSAT------------------FPKQIQELASD-FLSNYIFLAVgRVGSTSEN-----ITQTILWVYEPDKRsYLL 544
Cdd:COG1061 215 YRLGLTATpfrsdgreillflfdgivYEYSLKEAIEDgYLAPPEYYGI-RVDLTDERaeydaLSERLREALAADAE-RKD 292

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 545 DLLSSIRDgpEYTKDSLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILVATAVAARGLD 624
Cdd:COG1061 293 KILRELLR--EHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVD 370

                       330       340
                ....*....|....*....|....*
gi 17985987 625 IPHVKHVINFDLPSDVEEYVHRIGR 649
Cdd:COG1061 371 VPRLDVAILLRPTGSPREFIQRLGR 395
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 293-505 1.29e-20

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: 91.62  E-value: 1.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 293 NITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIING--RDLMACAQTGSGKTAAFLVPILNQMyelghvpppqstr 370
Cdd:cd18048  16 SVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV------------- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 371 qySRRKQYPLGLVLAPTRELATQ---IFEEAKKFAYRSRMRPAVLygGNNTSeqmRELDRGCHLIVATPGRLEDMITRGK 447
Cdd:cd18048  83 --DALKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQVIYAIR--GNRPG---KGTDIEAQIVIGTPGTVLDWCFKLR 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 448 -VGLENIRFLVLDEADRMLDM-GFEPQIRRIveQLNMPPTGqrQTLMFSATFPKQIQELA 505
Cdd:cd18048 156 lIDVTNISVFVLDEADVMINVqGHSDHSVRV--KRSMPKEC--QMLLFSATFEDSVWAFA 211
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
410-690 6.96e-18

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 87.50  E-value: 6.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 410 AVLYGGNNTSEQ---MRELDRG-CHLIVATPGRLE-----DMITRGKVGLenirfLVLDEA--------DrmldmgFEP- 471
Cdd:COG0514  85 AFLNSSLSAEERrevLRALRAGeLKLLYVAPERLLnprflELLRRLKISL-----FAIDEAhcisqwghD------FRPd 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 472 --QIRRIVEQLNMPPTgqrqtLMFSATFPKQIQE-----LAsdfLSN-YIFLA-VGRvgstsENITQTILWVYEPDKRSY 542
Cdd:COG0514 154 yrRLGELRERLPNVPV-----LALTATATPRVRAdiaeqLG---LEDpRVFVGsFDR-----PNLRLEVVPKPPDDKLAQ 220

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 543 LLDLLSSIRDGPeytkdslTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILVATaVA-AR 621
Cdd:COG0514 221 LLDFLKEHPGGS-------GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGM 292

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17985987 622 GLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFFNEKNRNIcsdlLELLIETKQEIPSFME 690
Cdd:COG0514 293 GIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAI----QRFFIEQSPPDEERKR 357
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 543-655 2.24e-17

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: 79.56  E-value: 2.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 543 LLDLLSSIRDgpeYTKDSLTLIFVETKKGADSLEEFLYqcNHPVTSIH-----------------GDRTQKEREEALRCF 605
Cdd:cd18802  12 LIEILREYFP---KTPDFRGIIFVERRATAVVLSRLLK--EHPSTLAFircgfligrgnssqrkrSLMTQRKQKETLDKF 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17985987 606 RSGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRtGRMGN 655
Cdd:cd18802  87 RDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPN 135
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
535-652 6.17e-16

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 82.09  E-value: 6.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 535 YEPDKRSYLLDLLSSIRDGpeyTKDSLTLIFVETKKGADSLEEFLYQCNHPVT------SIHGDR--TQKEREEALRCFR 606
Cdd:COG1111 332 IEHPKLSKLREILKEQLGT---NPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFR 408

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17985987 607 SGDCPILVATAVAARGLDIPHVKHVINFDL-PSDVeEYVHRIGRTGR 652
Cdd:COG1111 409 AGEFNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR 454
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 296-505 3.65e-15

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: 75.14  E-value: 3.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 296 SFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIING--RDLMACAQTGSGKTAAFLVPILNqmyelgHVPPPQSTRQYs 373
Cdd:cd18047   2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLS------QVEPANKYPQC- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 374 rrkqyplgLVLAPTRELATQ---IFEEAKKFAYRSRMRPAVLygGNNTSEQMRELDRgchLIVATPGRLEDMITRGK-VG 449
Cdd:cd18047  75 --------LCLSPTYELALQtgkVIEQMGKFYPELKLAYAVR--GNKLERGQKISEQ---IVIGTPGTVLDWCSKLKfID 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17985987 450 LENIRFLVLDEADRML-DMGFEPQIRRIVEQLnmpPTGQrQTLMFSATFPKQIQELA 505
Cdd:cd18047 142 PKKIKVFVLDEADVMIaTQGHQDQSIRIQRML---PRNC-QMLLFSATFEDSVWKFA 194
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 332-496 4.37e-14

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: 70.12  E-value: 4.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 332 GRDLMACAQTGSGKTAAFLVPILNQMYElghvpppqstrqysRRKQYplgLVLAPTRELATQIFEEAKKFAYRSrMRPAV 411
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLK--------------KGKKV---LVLVPTKALALQTAERLRELFGPG-IRVAV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 412 LYGGNNTSEQMRELDRGCHLIVATPGRLEDMITR-GKVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNMPPTGQRqt 490
Cdd:cd00046  63 LVGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV-- 140


                ....*.
gi 17985987 491 LMFSAT 496
Cdd:cd00046 141 ILLSAT 146
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
319-654 2.15e-12

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 70.31  E-value: 2.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 319 TPVQKHAIP-IIINGRDLMACAQTGSGKTA-AFLvPILNQMYELGHVpppqstrqysrrkqyplgLVLAPTRELATQIFE 396
Cdd:COG1204  24 YPPQAEALEaGLLEGKNLVVSAPTASGKTLiAEL-AILKALLNGGKA------------------LYIVPLRALASEKYR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 397 EAKKFAYRSRMRPAVLYGGNNTSEqmRELDRgCHLIVATPGRLeDMITRGKVG-LENIRFLVLDEAdRMLDMGfepqiRR 475
Cdd:COG1204  85 EFKRDFEELGIKVGVSTGDYDSDD--EWLGR-YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA-HLIDDE-----SR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 476 ------IVEQLNM--PPTgqrQTLMFSATFPKqIQELAS-----DFLSNY---------IFLAVGRVGSTSENITQTILW 533
Cdd:COG1204 155 gptlevLLARLRRlnPEA---QIVALSATIGN-AEEIAEwldaeLVKSDWrpvplnegvLYDGVLRFDDGSRRSKDPTLA 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 534 -------------VYEPDKRS------YLLDLLSSIRDGPEYTKDSLTLIFVETKKGADSLEEFLYQC-NHPVTSIHGDR 593
Cdd:COG1204 231 laldlleeggqvlVFVSSRRDaeslakKLADELKRRLTPEEREELEELAEELLEVSEETHTNEKLADClEKGVAFHHAGL 310

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17985987 594 TQKEREEALRCFRSGDCPILVATAVAARGLDIPhVKHVI------NFDLPSDVEEYVHRIGRTGRMG 654
Cdd:COG1204 311 PSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirdtkrGGMVPIPVLEFKQMAGRAGRPG 376
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 322-461 2.74e-11

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: 62.99  E-value: 2.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 322 QKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYelghvpppqstRQYSRRkqyplGLVLAPTRELATQIFEEAKKF 401
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL-----------RDPGSR-----ALYLYPTKALAQDQLRSLREL 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17985987 402 A--YRSRMRPAVLYGgnNTSEQMRE--LDRGCHLIVATPGRLEDMITRGKVG----LENIRFLVLDEA 461
Cdd:cd17923  69 LeqLGLGIRVATYDG--DTPREERRaiIRNPPRILLTNPDMLHYALLPHHDRwarfLRNLRYVVLDEA 134
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 291-659 3.49e-11

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: 66.78  E-value: 3.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 291 PPNITSFDDVQLTEIIRnnvALARY--DKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYElghvpPPQS 368
Cdd:COG1205  31 EARYAPWPDWLPPELRA---ALKKRgiERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE-----DPGA 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 369 TrqysrrkqyplGLVLAPTRELATQIFEEAKKFA--YRSRMRPAVLYGGnnTSEQMRE--LDRGcHLIVATPgrleDMIT 444
Cdd:COG1205 103 T-----------ALYLYPTKALARDQLRRLRELAeaLGLGVRVATYDGD--TPPEERRwiREHP-DIVLTNP----DMLH 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 445 RG------KVG--LENIRFLVLDEA---------------DRMldmgfepqiRRIVEQLNMPPtgqrQTLMFSATfpkqI 501
Cdd:COG1205 165 YGllphhtRWArfFRNLRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRHYGSDP----QFILASAT----I 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 502 ---QELASDfLSNYIFLAVGRVGSTSENITQtILW----VYEPDKRSYLL---DLLSS-IRDGpeyTKdslTLIFVETKK 570
Cdd:COG1205 228 gnpAEHAER-LTGRPVTVVDEDGSPRGERTF-VLWnpplVDDGIRRSALAeaaRLLADlVREG---LR---TLVFTRSRR 299

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 571 GA--------DSLEEFLYqcNHPVTSIHGDRTQKEREEALRCFRSGDCPILVAT-AVAArGLDIPHVKHVINFDLPSDVE 641
Cdd:COG1205 300 GAellaryarRALREPDL--ADRVAAYRAGYLPEERREIERGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRA 376

                       410
                ....*....|....*...
gi 17985987 642 EYVHRIGRTGRMGNLGVA 659
Cdd:COG1205 377 SFWQQAGRAGRRGQDSLV 394
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 537-648 5.88e-11

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 60.95  E-value: 5.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 537 PDKRSY--------LLDLLSSIRDGPEytKdslTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSG 608
Cdd:cd18793   2 PPKIEEvvsgkleaLLELLEELREPGE--K---VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 17985987 609 -DCPI-LVATAVAARGLDIPHVKHVINFDLP--SDVEEY----VHRIG 648
Cdd:cd18793  77 pDIRVfLLSTKAGGVGLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 534-654 1.20e-10

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: 59.91  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 534 VYEPDKRSYLLDLLSSIRDgpeYTKDSLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPIL 613
Cdd:cd18794   8 VRPKDKKDEKLDLLKRIKV---EHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17985987 614 VATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMG 654
Cdd:cd18794  85 VATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 539-652 2.44e-10

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 59.29  E-value: 2.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 539 KRSYLLDLLSSIRDGPEYTKDSLTLIFVETKKGADSLEEFLYQcNHPVTSIH---------GDR--TQKEREEALRCFRS 607
Cdd:cd18801  10 KLEKLEEIVKEHFKKKQEGSDTRVIIFSEFRDSAEEIVNFLSK-IRPGIRATrfigqasgkSSKgmSQKEQKEVIEQFRK 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17985987 608 GDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGR 652
Cdd:cd18801  89 GGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
PRK13766 PRK13766
Hef nuclease; Provisional
 558-652 6.78e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 62.58  E-value: 6.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  558 KDSLTLIFVETKKGADSLEEFLYQCNHPV------TSIHGDR--TQKEREEALRCFRSGDCPILVATAVAARGLDIPHVK 629
Cdd:PRK13766 364 PDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVD 443

                         90       100
                 ....*....|....*....|....
gi 17985987  630 HVINFD-LPSDVeEYVHRIGRTGR 652
Cdd:PRK13766 444 LVIFYEpVPSEI-RSIQRKGRTGR 466
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 593-652 1.74e-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: 54.63  E-value: 1.74e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 593 RTQKEREEALRCFRsgdcpILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGR 652
Cdd:cd18785  11 NSIEHAEEIASSLE-----ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 539-654 7.22e-09

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 59.47  E-value: 7.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 539 KRSYLLDLLSSIRDGPEytKdslTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSG-DCP-ILVAT 616
Cdd:COG0553 534 KLEALLELLEELLAEGE--K---VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpEAPvFLISL 608

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17985987 617 AVAARGLDIPHVKHVINFDLP--SDVEEyvHRIGRTGRMG 654
Cdd:COG0553 609 KAGGEGLNLTAADHVIHYDLWwnPAVEE--QAIDRAHRIG 646
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 319-461 1.06e-08

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: 55.35  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 319 TPVQKHAI-PIIINGRDLMACAQTGSGKTAAFLVPILnqmyelghvpppQSTRQYSRRKQYplglvLAPTRELATQIFEE 397
Cdd:cd17921   3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAIL------------RALATSGGKAVY-----IAPTRALVNQKEAD 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17985987 398 AKKFAYRSRMRPAVLYGgnNTSEQMRELDRgCHLIVATPGRLEDMITRGKV-GLENIRFLVLDEA 461
Cdd:cd17921  66 LRERFGPLGKNVGLLTG--DPSVNKLLLAE-ADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 562-652 1.86e-08

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: 54.19  E-value: 1.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 562 TLIFVETKKGADSLEE---FLYQCNHPVTSI---HGDRTQKEREEALRCFRSGDCPILVATAVAARGLDIPHVKHVINFD 635
Cdd:cd18796  41 TLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120

                        90
                ....*....|....*..
gi 17985987 636 LPSDVEEYVHRIGRTGR 652
Cdd:cd18796 121 SPKSVARLLQRLGRSGH 137
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 333-461 5.60e-08

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: 53.81  E-value: 5.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 333 RDLMACAQTGSGKTaafLVPIL--NQMYELGHVPPPQSTRQysrrkqyplgLVLAPTRELATQIFEEAKKF------AYR 404
Cdd:cd18034  17 RNTIVVLPTGSGKT---LIAVMliKEMGELNRKEKNPKKRA----------VFLVPTVPLVAQQAEAIRSHtdlkvgEYS 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17985987 405 SRMRPAVlyggnNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEA 461
Cdd:cd18034  84 GEMGVDK-----WTKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK13767 PRK13767
ATP-dependent helicase; Provisional
 314-460 5.63e-08

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 56.43  E-value: 5.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  314 RYDKPTPVQKHAIPIIINGRDLMACAQTGSGKT-AAFLVpILNQMYELGhvpppqstrqysRRKQYPLG---LVLAPTRE 389
Cdd:PRK13767  29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLA-IIDELFRLG------------REGELEDKvycLYVSPLRA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987  390 LA-----------TQIFEEAKKFAYR-SRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMIT----RGKvgLENI 453
Cdd:PRK13767  96 LNndihrnleeplTEIREIAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLNspkfREK--LRTV 173


                 ....*..
gi 17985987  454 RFLVLDE 460
Cdd:PRK13767 174 KWVIVDE 180
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
313-361 1.13e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 55.49  E-value: 1.13e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 17985987 313 ARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKT-AAFLvPILNQMYELG 361
Cdd:COG1201  20 ARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFL-PALDELARRP 68
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 317-464 3.62e-07

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 50.88  E-value: 3.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 317 KPTPVQKHAIPIIING------RDLMACAQTGSGKTAAFLVPILnqMYelghvpppqstrqYSRRKQYplgLVLAPTREL 390
Cdd:cd17918  15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAAL--LA-------------YKNGKQV---AILVPTEIL 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17985987 391 ATQIFEEAKKFAyrSRMRPAVLYGGnnTSEQMREldrGCHLIVATPGRLEDmitrgKVGLENIRFLVLDEADRM 464
Cdd:cd17918  77 AHQHYEEARKFL--PFINVELVTGG--TKAQILS---GISLLVGTHALLHL-----DVKFKNLDLVIVDEQHRF 138
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
 526-690 7.07e-07

C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 50.00  E-value: 7.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 526 NITQTilWVYEPDKRSYLLDLLSSIRDGpeytkdslTLIFVETKKG---ADSLEEFLYQCNHPVTSIHGDRtqkerEEAL 602
Cdd:cd18798   1 NIVDV--YIEDSDSLEKLLELVKKLGDG--------GLIFVSIDYGkeyAEELKEFLERHGIKAELALSST-----EKNL 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 603 RCFRSGDCPILVATA----VAARGLDIPH-VKHVINFDLPsdVEEYVHRIGRTGRM--GNLGVATSFFNEKNRNICSDLL 675
Cdd:cd18798  66 EKFEEGEIDVLIGVAsyygVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRLyaGGLTKGLSVVLVDDPELFEALK 143

                       170
                ....*....|....*..
gi 17985987 676 E--LLIETKQEIPSFME 690
Cdd:cd18798 144 KrlKLILDEFIFKELEE 160
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 545-652 1.57e-06

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: 48.78  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 545 DLLSSIRDGPEytKDSLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILVATAVAARGLD 624
Cdd:cd18790  15 DLLGEIRKRVA--RGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLD 92

                        90       100       110
                ....*....|....*....|....*....|....*
gi 17985987 625 IPHVKHVINFDlpSDVEEY-------VHRIGRTGR 652
Cdd:cd18790  93 LPEVSLVAILD--ADKEGFlrsetslIQTIGRAAR 125
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 320-508 2.06e-06

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: 48.87  E-value: 2.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 320 PVQKHAI-PIIINGRDLMACAQTGSGKTAAFLVPILNQMYELGHvpppqstrqysrrkqyplGLVLAPTRELATQIFEEA 398
Cdd:cd18028   4 PPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGK------------------ALYLVPLRALASEKYEEF 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 399 KKFaYRSRMRPAVLYGGNNtsEQMRELDRgCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIRRIVE 478
Cdd:cd18028  66 KKL-EEIGLKVGISTGDYD--EDDEWLGD-YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVA 141

                       170       180       190
                ....*....|....*....|....*....|
gi 17985987 479 QLNMpPTGQRQTLMFSATFPkQIQELASDF 508
Cdd:cd18028 142 RLRR-LNPNTQIIGLSATIG-NPDELAEWL 169
ResIII pfam04851
Type III restriction enzyme, res subunit;
317-498 5.29e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 47.28  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987   317 KPTPVQKHAIPIIINGRDL--------MAcaqTGSGKT--AAFLVPILNQMYELGHVpppqstrqysrrkqyplgLVLAP 386
Cdd:pfam04851   3 ELRPYQIEAIENLLESIKNgqkrglivMA---TGSGKTltAAKLIARLFKKGPIKKV------------------LFLVP 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987   387 TRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQmreldRGCHLIVATPGRL--EDMITRGKVGLENIRFLVLDEADRm 464
Cdd:pfam04851  62 RKDLLEQALEEFKKFLPNYVEIGEIISGDKKDESV-----DDNKIVVTTIQSLykALELASLELLPDFFDVIIIDEAHR- 135

                         170       180       190
                  ....*....|....*....|....*....|....
gi 17985987   465 ldmGFEPQIRRIVEQLNMPptgqrQTLMFSATFP 498
Cdd:pfam04851 136 ---SGASSYRNILEYFKPA-----FLLGLTATPE 161
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
 330-463 6.28e-06

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 47.81  E-value: 6.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 330 INGRDLMACAQTGSGKTaafLVPILNQMYELGHVPppqstrqySRRKQYPlgLVLAPTRELATQIFEEAKKFAYRSRMRP 409
Cdd:cd17927  15 LKGKNTIICLPTGSGKT---FVAVLICEHHLKKFP--------AGRKGKV--VFLANKVPLVEQQKEVFRKHFERPGYKV 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17985987 410 AVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRG-KVGLENIRFLVLDEADR 463
Cdd:cd17927  82 TGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGtIVSLSDFSLLVFDECHN 136
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 332-460 1.26e-05

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: 46.04  E-value: 1.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 332 GRDLMACAQTGSGKT-AAFLvPILNQMYElghvPPPQSTRQysrrkqyplgLVLAPTRELATQIFEEAKKFA--YRSRMR 408
Cdd:cd17922   1 GRNVLIAAPTGSGKTeAAFL-PALSSLAD----EPEKGVQV----------LYISPLKALINDQERRLEEPLdeIDLEIP 65

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17985987 409 PAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVG--LENIRFLVLDE 460
Cdd:cd17922  66 VAVRHGDTSQSEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 382-463 2.05e-05

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 45.97  E-value: 2.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 382 LVLAPTRELATQIFEEAKKFAyrSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEA 461
Cdd:cd18035  49 LILAPSRPLVEQHAENLKRVL--NIPDKITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126


                ..
gi 17985987 462 DR 463
Cdd:cd18035 127 HH 128
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 321-460 2.61e-05

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 45.81  E-value: 2.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 321 VQKHAIPIIING-RDLMACAQTGSGKTAAFLVPILNQMYElghVPPPQSTRqysRRKQYplglvLAPTRELATQIFEEAK 399
Cdd:cd18023   5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKE---RNPLPWGN---RKVVY-----IAPIKALCSEKYDDWK 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17985987 400 -KFAyrsrmRPAVLYG---GNNTSEQMRELdRGCHLIVATPGRLEDMITRGKVG---LENIRFLVLDE 460
Cdd:cd18023  74 eKFG-----PLGLSCAeltGDTEMDDTFEI-QDADIILTTPEKWDSMTRRWRDNgnlVQLVALVLIDE 135
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 562-649 2.70e-05

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: 44.09  E-value: 2.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 562 TLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKERE-EALRCFRSGD--CPILVATAVAARGLDIPHVKHVInFDLPS 638
Cdd:cd18799   9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGElkPPILVTVDLLTTGVDIPEVDNVV-FLRPT 87

                        90
                ....*....|..
gi 17985987 639 DVE-EYVHRIGR 649
Cdd:cd18799  88 ESRtLFLQMLGR 99
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 586-654 5.91e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 46.63  E-value: 5.91e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17985987  586 VTSIHGDRTQKEREEALRCFRSGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMG 654
Cdd:PRK11057 263 AAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 589-652 1.23e-04

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 43.10  E-value: 1.23e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 589 IHGDRTQKEREEALRCFRSGDCPILVATAVAARGLDIPH-----VKHVINFDLPSdveeyVHRI-GRTGR 652
Cdd:cd18811  67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGR 131
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 562-663 2.44e-04

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 42.24  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 562 TLIFVETKkgaDSLEEFLYQCNHPVtsIHGDRTQKEREEALRCFRSGDCPILVATAVAARGLDIP--HVKHVINFDLPSD 639
Cdd:cd18789  52 IIVFTDNV---EALYRYAKRLLKPF--ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPeaNVAIQISGHGGSR 126

                        90       100
                ....*....|....*....|....
gi 17985987 640 vEEYVHRIGRTGRMGNLGVATSFF 663
Cdd:cd18789 127 -RQEAQRLGRILRPKKGGGKNAFF 149
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
 334-509 4.56e-04

N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 42.03  E-value: 4.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 334 DLMACAQTGSGKTAAFLVPILNQMYElgHVPPpqstRQYSRRKQYPLgLVLAPTRELATQIFEE-AKKFAYRSrMRPAVL 412
Cdd:cd18020  19 NMLICAPTGAGKTNIAMLTILHEIRQ--HVNQ----GGVIKKDDFKI-VYIAPMKALAAEMVEKfSKRLAPLG-IKVKEL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 413 YGGNNTSEqmRELDRgCHLIVATPGRLeDMITRGKVG----LENIRFLVLDEAdRML--DMG--FEPQIRRIVEQLNMPP 484
Cdd:cd18020  91 TGDMQLTK--KEIAE-TQIIVTTPEKW-DVVTRKSSGdvalSQLVRLLIIDEV-HLLhdDRGpvIESLVARTLRQVESTQ 165

                       170       180
                ....*....|....*....|....*
gi 17985987 485 TGQRqTLMFSATFPKQIQelASDFL 509
Cdd:cd18020 166 SMIR-IVGLSATLPNYLD--VADFL 187
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 589-626 1.62e-03

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 39.94  E-value: 1.62e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 17985987 589 IHGDRTQKEREEALRCFRSGDCPILVATAVAARGLDIP 626
Cdd:cd18792  66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVP 103
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 559-654 2.20e-03

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 41.81  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987   559 DSLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILVATAVAARGLDIPHVKHVINFDLPS 638
Cdd:PLN03137  680 DECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPK 759

                          90
                  ....*....|....*.
gi 17985987   639 DVEEYVHRIGRTGRMG 654
Cdd:PLN03137  760 SIEGYHQECGRAGRDG 775
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
 338-463 2.71e-03

DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 39.61  E-value: 2.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 338 CAQTGSGKTAAFLVPILNqmyelghvpppqstrqYSRrkQYPLGLV--LAPTRELATQIFEEAKKFAYRSRMRPAVLYGG 415
Cdd:cd18033  22 ALPTGLGKTFIAAVVMLN----------------YYR--WFPKGKIvfMAPTKPLVSQQIEACYKITGIPSSQTAELTGS 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 17985987 416 NNTSEQmRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADR 463
Cdd:cd18033  84 VPPTKR-AELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHR 130
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
 332-412 4.44e-03

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 39.20  E-value: 4.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985987 332 GRDLMACAQTGSGKTAAFLVPILNQMYelghvpppqstRQYSRRkqyplgLVLA-PTRELATQIFEEAKKFAYRSRMRPA 410
Cdd:cd17930   1 PGLVILEAPTGSGKTEAALLWALKLAA-----------RGGKRR------IIYAlPTRATINQMYERIREILGRLDDEDK 63


                ..
gi 17985987 411 VL 412
Cdd:cd17930  64 VL 65
 
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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