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Conserved domains on  [gi|42572719|ref|NP_974455|]
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DEA(D/H)-box RNA helicase family protein [Arabidopsis thaliana]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423521)

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

CATH:  1.20.1320.20|3.40.50.300
EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0005524
PubMed:  20206133
SCOP:  4000282|3002019

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
152-536 1.37e-163

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 473.87  E-value: 1.37e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 152 TFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDqHVERPRgsravypf 231
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS-RPRAPQ-------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 232 AVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDE 311
Cdd:COG0513  74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDE 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 312 ADRMLDMGFEPQIRKIVEQMdmPPRgvRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVGSSTDLITQRVEFVQESDKR 391
Cdd:COG0513 154 ADRMLDMGFIEDIERILKLL--PKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKL 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 392 SHLMDLLHAQRETQdkqslTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVAARG 471
Cdd:COG0513 230 ELLRRLLRDEDPER-----AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARG 304

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42572719 472 LDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNaqlARSLAELMQEANQEVPE 536
Cdd:COG0513 305 IDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDE---RRLLRAIEKLIGQKIEE 366
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
152-536 1.37e-163

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 473.87  E-value: 1.37e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 152 TFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDqHVERPRgsravypf 231
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS-RPRAPQ-------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 232 AVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDE 311
Cdd:COG0513  74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDE 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 312 ADRMLDMGFEPQIRKIVEQMdmPPRgvRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVGSSTDLITQRVEFVQESDKR 391
Cdd:COG0513 154 ADRMLDMGFIEDIERILKLL--PKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKL 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 392 SHLMDLLHAQRETQdkqslTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVAARG 471
Cdd:COG0513 230 ELLRRLLRDEDPER-----AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARG 304

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42572719 472 LDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNaqlARSLAELMQEANQEVPE 536
Cdd:COG0513 305 IDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDE---RRLLRAIEKLIGQKIEE 366
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 152-372 2.63e-159

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: 455.02  E-value: 2.63e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 152 TFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERPRGSRAVYPF 231
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRRKAYPS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 232 AVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDE 311
Cdd:cd17967  81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42572719 312 ADRMLDMGFEPQIRKIVEQMDMPPRGVRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVG 372
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
PTZ00110 PTZ00110
helicase; Provisional
 143-546 7.09e-129

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 389.52  E-value: 7.09e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  143 GGDVPPPVNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKdQHVERP 222
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINA-QPLLRY 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  223 RGSravyPFAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQ 302
Cdd:PTZ00110 201 GDG----PIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLR 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  303 MIRFLALDEADRMLDMGFEPQIRKIVEQMdmppRGVRQTMLFSATFPSQIQRLAADFMSNY-IFLAVGrvgsSTDL---- 377
Cdd:PTZ00110 277 RVTYLVLDEADRMLDMGFEPQIRKIVSQI----RPDRQTLMWSATWPKEVQSLARDLCKEEpVHVNVG----SLDLtach 348

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  378 -ITQRVEFVQESDKRSHLMDLLHAQRETQDKqslTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKT 456
Cdd:PTZ00110 349 nIKQEVFVVEEHEKRGKLKMLLQRIMRDGDK---ILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKT 425

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  457 GRTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNAQLARSLAELMQEANQEVPE 536
Cdd:PTZ00110 426 GKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPP 505

                        410
                 ....*....|
gi 42572719  537 WLTRYASRAS 546
Cdd:PTZ00110 506 ELEKLSNERS 515
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 175-355 9.12e-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: 199.39  E-value: 9.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719   175 TPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVerprgsravyPFAVILSPTRELACQIHDEAKKFSY 254
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG----------PQALVLAPTRELAEQIYEELKKLGK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719   255 QTGVKVVVAYGGTPIHQQLRELeRGCDILVATPGRLNDLLERaRVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMdmp 334
Cdd:pfam00270  71 GLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL--- 145

                         170       180
                  ....*....|....*....|.
gi 42572719   335 pRGVRQTMLFSATFPSQIQRL 355
Cdd:pfam00270 146 -PKKRQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
166-381 1.64e-53

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 181.54  E-value: 1.64e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719    166 IRRCKYVRPTPVQRHAIPILLA-ERDLMACAQTGSGKTAAFCFPIISgimkdqhverpRGSRAVYPFAVILSPTRELACQ 244
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALE-----------ALKRGKGGRVLVLVPTRELAEQ 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719    245 IHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGC-DILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQ 323
Cdd:smart00487  70 WAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQ 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 42572719    324 IRKIVEQMdmppRGVRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRvgSSTDLITQR 381
Cdd:smart00487 150 LEKLLKLL----PKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
 342-504 6.46e-03

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


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 39.36  E-value: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719   342 MLFSATFPSQIQRLAADfMSNYIFLAvGRVGSSTDLITQRVEFVQESDKR---SHLMDLLhaqrETQDKQSLTLVFVETK 418
Cdd:TIGR01587 159 LLMSATLPKFLKEYAEK-IGYVEFNE-PLDLKEERRFENHRFILIESDKVgeiSSLERLL----EFIKKGGSIAIIVNTV 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719   419 RGADTLENWL--CMNEFPATSIHG-----DRTQQEREVALRSFKTGRTPILVATDVAARGLDIphvahvvNFDL----PN 487
Cdd:TIGR01587 233 DRAQEFYQQLkeKAPEEEIILYHSrftekDRAKKEAELLREMKKSNEKFVIVATQVIEASLDI-------SADVmiteLA 305

                         170
                  ....*....|....*..
gi 42572719   488 DIDDYVHRIGRTGRAGK 504
Cdd:TIGR01587 306 PIDSLIQRLGRLHRYGR 322
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
152-536 1.37e-163

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 473.87  E-value: 1.37e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 152 TFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDqHVERPRgsravypf 231
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS-RPRAPQ-------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 232 AVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDE 311
Cdd:COG0513  74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDE 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 312 ADRMLDMGFEPQIRKIVEQMdmPPRgvRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVGSSTDLITQRVEFVQESDKR 391
Cdd:COG0513 154 ADRMLDMGFIEDIERILKLL--PKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKL 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 392 SHLMDLLHAQRETQdkqslTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVAARG 471
Cdd:COG0513 230 ELLRRLLRDEDPER-----AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARG 304

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42572719 472 LDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNaqlARSLAELMQEANQEVPE 536
Cdd:COG0513 305 IDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDE---RRLLRAIEKLIGQKIEE 366
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 152-372 2.63e-159

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: 455.02  E-value: 2.63e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 152 TFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERPRGSRAVYPF 231
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRRKAYPS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 232 AVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDE 311
Cdd:cd17967  81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42572719 312 ADRMLDMGFEPQIRKIVEQMDMPPRGVRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVG 372
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 131-373 5.50e-142

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: 412.13  E-value: 5.50e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 131 FDAYEDIPVETSGGDVPPPVNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPII 210
Cdd:cd18051   1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 211 SGIMKDQHVERP------RGSRAVYPFAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILV 284
Cdd:cd18051  81 SQIYEQGPGESLpsesgyYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 285 ATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMDMPPRGVRQTMLFSATFPSQIQRLAADFMSNYI 364
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYI 240


                ....*....
gi 42572719 365 FLAVGRVGS 373
Cdd:cd18051 241 FLAVGRVGS 249
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 126-372 7.70e-137

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: 399.34  E-value: 7.70e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 126 NTGINFDAYEDIPVETSGGDVPPPVNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAF 205
Cdd:cd18052  18 QTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAF 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 206 CFPIISGIMKDQhVERPRGSRAVYPFAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVA 285
Cdd:cd18052  98 LLPVLTGMMKEG-LTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVA 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 286 TPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMDMPPRGVRQTMLFSATFPSQIQRLAADFM-SNYI 364
Cdd:cd18052 177 TPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFLkEDYL 256


                ....*...
gi 42572719 365 FLAVGRVG 372
Cdd:cd18052 257 FLTVGRVG 264
PTZ00110 PTZ00110
helicase; Provisional
 143-546 7.09e-129

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 389.52  E-value: 7.09e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  143 GGDVPPPVNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKdQHVERP 222
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINA-QPLLRY 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  223 RGSravyPFAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQ 302
Cdd:PTZ00110 201 GDG----PIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLR 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  303 MIRFLALDEADRMLDMGFEPQIRKIVEQMdmppRGVRQTMLFSATFPSQIQRLAADFMSNY-IFLAVGrvgsSTDL---- 377
Cdd:PTZ00110 277 RVTYLVLDEADRMLDMGFEPQIRKIVSQI----RPDRQTLMWSATWPKEVQSLARDLCKEEpVHVNVG----SLDLtach 348

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  378 -ITQRVEFVQESDKRSHLMDLLHAQRETQDKqslTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKT 456
Cdd:PTZ00110 349 nIKQEVFVVEEHEKRGKLKMLLQRIMRDGDK---ILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKT 425

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  457 GRTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNAQLARSLAELMQEANQEVPE 536
Cdd:PTZ00110 426 GKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPP 505

                        410
                 ....*....|
gi 42572719  537 WLTRYASRAS 546
Cdd:PTZ00110 506 ELEKLSNERS 515
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 151-528 2.81e-97

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 305.19  E-value: 2.81e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  151 NTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGImkdqHVERPRgsravyP 230
Cdd:PRK11776   4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL----DVKRFR------V 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  231 FAVILSPTRELACQIHDEAKKFSYQT-GVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLAL 309
Cdd:PRK11776  74 QALVLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  310 DEADRMLDMGFEPQIRKIVEQMdmPPRgvRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVGSSTDlITQRVEFVQESD 389
Cdd:PRK11776 154 DEADRMLDMGFQDAIDAIIRQA--PAR--RQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IEQRFYEVSPDE 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  390 KRSHLMDLL-HAQRETqdkqslTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVA 468
Cdd:PRK11776 229 RLPALQRLLlHHQPES------CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVA 302

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  469 ARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNAQLARSLAELMQ 528
Cdd:PRK11776 303 ARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLG 362
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 171-535 1.33e-96

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 303.27  E-value: 1.33e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  171 YVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHveRPRGSRAVYpfAVILSPTRELACQIHDEAK 250
Cdd:PRK10590  21 YREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQP--HAKGRRPVR--ALILTPTRELAAQIGENVR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  251 KFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQ 330
Cdd:PRK10590  97 DYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLAK 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  331 MdmPPRgvRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVGSSTDLITQRVEFVQESDKRSHLMDLLHAQRETQdkqsl 410
Cdd:PRK10590 177 L--PAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGKGNWQQ----- 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  411 TLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVAARGLDIPHVAHVVNFDLPNDID 490
Cdd:PRK10590 248 VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPE 327

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 42572719  491 DYVHRIGRTGRAGKSGIATAFFNENNAQLARSLAELMQeanQEVP 535
Cdd:PRK10590 328 DYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK---KEIP 369
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 165-366 4.52e-93

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 284.72  E-value: 4.52e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 165 NIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERPRgsravyPFAVILSPTRELACQ 244
Cdd:cd00268   4 ALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRG------PQALVLAPTRELAMQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 245 IHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQI 324
Cdd:cd00268  78 IAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDV 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 42572719 325 RKIVEQmdMPPRgvRQTMLFSATFPSQIQRLAADFMSNYIFL 366
Cdd:cd00268 158 EKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLKNPVRI 195
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 135-538 3.38e-90

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 288.61  E-value: 3.38e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  135 EDIPVETSGGDVPPPVNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIIS--G 212
Cdd:PLN00206 105 RKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcC 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  213 IMKDQHVERPRGsravyPFAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLND 292
Cdd:PLN00206 185 TIRSGHPSEQRN-----PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLID 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  293 LLERARVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMDMPprgvrQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVG 372
Cdd:PLN00206 260 LLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKDIILISIGNPN 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  373 SSTDLITQRVEFVQESDKRSHLMDLLHAQretQDKQSLTLVFVETKRGADTLENWLCM-NEFPATSIHGDRTQQEREVAL 451
Cdd:PLN00206 335 RPNKAVKQLAIWVETKQKKQKLFDILKSK---QHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVM 411

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  452 RSFKTGRTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNAQLARSLAELMQEAN 531
Cdd:PLN00206 412 KSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSG 491


                 ....*..
gi 42572719  532 QEVPEWL 538
Cdd:PLN00206 492 AAIPREL 498
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 152-511 1.67e-89

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 284.14  E-value: 1.67e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  152 TFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIIsgimkdQH-VERPR---GSRA 227
Cdd:PRK11192   2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAL------QHlLDFPRrksGPPR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  228 VypfaVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFL 307
Cdd:PRK11192  76 I----LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  308 ALDEADRMLDMGFEPQIRKIVEQMdmppRGVRQTMLFSATFPSQ-IQRLAADFMSNYIFLAVGRVGSSTDLITQrveFVQ 386
Cdd:PRK11192 152 ILDEADRMLDMGFAQDIETIAAET----RWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQ---WYY 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  387 ESDKRSHLMDLLhAQRETQDKQSLTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATD 466
Cdd:PRK11192 225 RADDLEHKTALL-CHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATD 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 42572719  467 VAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAF 511
Cdd:PRK11192 304 VAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 135-517 3.27e-88

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 282.19  E-value: 3.27e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  135 EDIPVETSGGDvpppvNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIM 214
Cdd:PRK01297  76 EDFVVEPQEGK-----TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  215 KDQ-HVERPRGSravyPFAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELE-RGCDILVATPGRLND 292
Cdd:PRK01297 151 QTPpPKERYMGE----PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLD 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  293 LLERARVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMdmPPRGVRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVG 372
Cdd:PRK01297 227 FNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPEN 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  373 SSTDLITQRVEFVQESDKRSHLMDLLhaqreTQDKQSLTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALR 452
Cdd:PRK01297 305 VASDTVEQHVYAVAGSDKYKLLYNLV-----TQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLE 379

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42572719  453 SFKTGRTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNA 517
Cdd:PRK01297 380 GFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDA 444
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 175-511 1.89e-83

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 267.99  E-value: 1.89e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  175 TPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMkdQHvERPRGSRAVYPFAVILSPTRELACQIHDEAKKFSY 254
Cdd:PRK04837  32 TPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLL--SH-PAPEDRKVNQPRALIMAPTRELAVQIHADAEPLAQ 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  255 QTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMdmP 334
Cdd:PRK04837 109 ATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRWLFRRM--P 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  335 PRGVRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVGSSTDLITQRVEFVQESDKRSHLMDLLhaQRETQDKqslTLVF 414
Cdd:PRK04837 187 PANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLI--EEEWPDR---AIIF 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  415 VETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVH 494
Cdd:PRK04837 262 ANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVH 341

                        330
                 ....*....|....*..
gi 42572719  495 RIGRTGRAGKSGIATAF 511
Cdd:PRK04837 342 RIGRTGRAGASGHSISL 358
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 152-535 4.09e-79

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 261.04  E-value: 4.09e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  152 TFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMK-----DQHVERPRgsr 226
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSrpalaDRKPEDPR--- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  227 avypfAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARV-SMQMIR 305
Cdd:PRK04537  87 -----ALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  306 FLALDEADRMLDMGFEPQIRKIVEQMdmPPRGVRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVGSSTDLITQRVEFV 385
Cdd:PRK04537 162 ICVLDEADRMFDLGFIKDIRFLLRRM--PERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  386 QESDKRSHLMDLLhaqreTQDKQSLTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVAT 465
Cdd:PRK04537 240 ADEEKQTLLLGLL-----SRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVAT 314

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  466 DVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNEnnaQLARSLAELMQEANQEVP 535
Cdd:PRK04537 315 DVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACE---RYAMSLPDIEAYIEQKIP 381
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 166-366 9.28e-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: 237.27  E-value: 9.28e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 166 IRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERPRGsravyPFAVILSPTRELACQI 245
Cdd:cd17966   5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDG-----PIVLVLAPTRELAQQI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 246 HDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIR 325
Cdd:cd17966  80 QQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 42572719 326 KIVEQMdmppRGVRQTMLFSATFPSQIQRLAADFMSNYIFL 366
Cdd:cd17966 160 KIVDQI----RPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 152-534 1.72e-72

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 244.76  E-value: 1.72e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  152 TFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGImkDQHVERPRgsravypf 231
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPELKAPQ-------- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  232 AVILSPTRELACQIHDEAKKFS-YQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALD 310
Cdd:PRK11634  77 ILVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  311 EADRMLDMGFEPQIRKIVEQMdmpPRGvRQTMLFSATFPSQIQRLAADFMSNYIFLavgRVGSSTDL---ITQRVEFVQE 387
Cdd:PRK11634 157 EADEMLRMGFIEDVETIMAQI---PEG-HQTALFSATMPEAIRRITRRFMKEPQEV---RIQSSVTTrpdISQSYWTVWG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  388 SDKRSHLMDLLhaqrETQDKQSlTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDV 467
Cdd:PRK11634 230 MRKNEALVRFL----EAEDFDA-AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDV 304

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42572719  468 AARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNAQLARSLAELMQEANQEV 534
Cdd:PRK11634 305 AARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEV 371
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 142-356 7.04e-70

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


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 225.33  E-value: 7.04e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 142 SGGDVPPPVNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVER 221
Cdd:cd17953   3 RGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 222 PRGsravyPFAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLL--ERARV 299
Cdd:cd17953  83 GEG-----PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRV 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42572719 300 -SMQMIRFLALDEADRMLDMGFEPQIRKIVEQMdmppRGVRQTMLFSATFPSQIQRLA 356
Cdd:cd17953 158 tNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNI----RPDRQTVLFSATFPRKVEALA 211
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 166-364 3.65e-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: 222.68  E-value: 3.65e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 166 IRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERPRGsravyPFAVILSPTRELACQI 245
Cdd:cd17952   5 IRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEG-----PIAVIVAPTRELAQQI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 246 HDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIR 325
Cdd:cd17952  80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42572719 326 KIVEQMdmppRGVRQTMLFSATFPSQIQRLAADFMSNYI 364
Cdd:cd17952 160 SIVGHV----RPDRQTLLFSATFKKKIEQLARDILSDPI 194
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 166-366 1.84e-66

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: 216.42  E-value: 1.84e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 166 IRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHveRPRGSRAVYPFAVILSPTRELACQI 245
Cdd:cd17945   5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPP--LDEETKDDGPYALILAPTRELAQQI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 246 HDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIR 325
Cdd:cd17945  83 EEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVT 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42572719 326 KIVEQM----------DMPPRGV------RQTMLFSATFPSQIQRLAADFMSNYIFL 366
Cdd:cd17945 163 KILDAMpvsnkkpdteEAEKLAAsgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 166-366 4.12e-62

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: 204.35  E-value: 4.12e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 166 IRRCKYVRPTPVQRHAIPILLA-ERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERPRGSRAVypfavILSPTRELACQ 244
Cdd:cd17964   9 LTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSAL-----IISPTRELALQ 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 245 IHDEAKKF-SYQTGVKVVVAYGGTPIHQQLRELER-GCDILVATPGRLNDLLE--RARVSMQMIRFLALDEADRMLDMGF 320
Cdd:cd17964  84 IAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLDMGF 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 42572719 321 EPQIRKIVEQMDMPPRGVRQTMLFSATFPSQIQRLAADFM-SNYIFL 366
Cdd:cd17964 164 RPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLkKDYKFI 210
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 165-369 3.19e-61

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: 201.66  E-value: 3.19e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 165 NIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERPRgsravypfAVILSPTRELACQ 244
Cdd:cd17957   4 NLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLR--------ALILAPTRELASQ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 245 IHDEAKKFSYQTGVKVVVAYGGT-PIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQ 323
Cdd:cd17957  76 IYRELLKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQ 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42572719 324 IRKIVEQMDMPprgVRQTMLFSATFPSQIQRLAADFMSNYIFLAVG 369
Cdd:cd17957 156 TDEILAACTNP---NLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 175-355 9.12e-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: 199.39  E-value: 9.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719   175 TPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVerprgsravyPFAVILSPTRELACQIHDEAKKFSY 254
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG----------PQALVLAPTRELAEQIYEELKKLGK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719   255 QTGVKVVVAYGGTPIHQQLRELeRGCDILVATPGRLNDLLERaRVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMdmp 334
Cdd:pfam00270  71 GLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL--- 145

                         170       180
                  ....*....|....*....|.
gi 42572719   335 pRGVRQTMLFSATFPSQIQRL 355
Cdd:pfam00270 146 -PKKRQILLLSATLPRNLEDL 165
PTZ00424 PTZ00424
helicase 45; Provisional
 150-541 5.95e-60

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 205.06  E-value: 5.95e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  150 VNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERprgsravy 229
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQ-------- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  230 pfAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLAL 309
Cdd:PTZ00424  99 --ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFIL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  310 DEADRMLDMGFEPQIRKIVEQMdmpPRGVrQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVGSSTDLITQRVEFVQESD 389
Cdd:PTZ00424 177 DEADEMLSRGFKGQIYDVFKKL---PPDV-QVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEE 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  390 -KRSHLMDLLHAQRETQdkqslTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVA 468
Cdd:PTZ00424 253 wKFDTLCDLYETLTITQ-----AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLL 327

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42572719  469 ARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNAQLARSLAELMQEANQEVPEWLTRY 541
Cdd:PTZ00424 328 ARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADY 400
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 139-369 1.04e-59

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: 199.08  E-value: 1.04e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 139 VETSGGDVPPPVNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQH 218
Cdd:cd18049  12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPF 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 219 VERPRGsravyPFAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERAR 298
Cdd:cd18049  92 LERGDG-----PICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK 166

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42572719 299 VSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMdmppRGVRQTMLFSATFPSQIQRLAADFMSNYIFLAVG 369
Cdd:cd18049 167 TNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI----RPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 378-512 2.96e-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: 193.88  E-value: 2.96e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 378 ITQRVEFVQESDKRSHLMDLLhaqrETQDKQSLTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTG 457
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLL----LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSG 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42572719 458 RTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFF 512
Cdd:cd18787  77 KVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 165-362 8.79e-59

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: 195.38  E-value: 8.79e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 165 NIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPiisGIMKDQHVERPRGSRaVYPFAVILSPTRELACQ 244
Cdd:cd17958   4 EIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLP---GFIHLDLQPIPREQR-NGPGVLVLTPTRELALQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 245 IHDEAKKFSYQtGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQI 324
Cdd:cd17958  80 IEAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 42572719 325 RKIVeqMDMPPRgvRQTMLFSATFPSQIQRLAADFMSN 362
Cdd:cd17958 159 RKIL--LDIRPD--RQTIMTSATWPDGVRRLAQSYLKD 192
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 171-357 2.99e-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: 193.63  E-value: 2.99e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 171 YVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIIsgimkdqhvER--PRGSRAVYPFAVILSPTRELACQIHDE 248
Cdd:cd17947  10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPIL---------ERllYRPKKKAATRVLVLVPTRELAMQCFSV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 249 AKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERAR-VSMQMIRFLALDEADRMLDMGFEPQIRKI 327
Cdd:cd17947  81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADELKEI 160

                       170       180       190
                ....*....|....*....|....*....|
gi 42572719 328 VEqmdMPPRGvRQTMLFSATFPSQIQRLAA 357
Cdd:cd17947 161 LR---LCPRT-RQTMLFSATMTDEVKDLAK 186
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 153-365 2.16e-57

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: 191.67  E-value: 2.16e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 153 FADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDqhverPRGsravyPFA 232
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSED-----PYG-----IFA 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 233 VILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLE---RARVSMQMIRFLAL 309
Cdd:cd17955  71 LVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVL 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42572719 310 DEADRMLDMGFEPQIRKIVEQmdMPPRgvRQTMLFSATFPSQIQRLAADFMSNYIF 365
Cdd:cd17955 151 DEADRLLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 139-369 1.66e-56

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: 191.76  E-value: 1.66e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 139 VETSGGDVPPPVNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQH 218
Cdd:cd18050  50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPY 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 219 VERPRGsravyPFAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERAR 298
Cdd:cd18050 130 LERGDG-----PICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK 204

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42572719 299 VSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMdmppRGVRQTMLFSATFPSQIQRLAADFMSNYIFLAVG 369
Cdd:cd18050 205 TNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI----RPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEXDc smart00487
DEAD-like helicases superfamily;
166-381 1.64e-53

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 181.54  E-value: 1.64e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719    166 IRRCKYVRPTPVQRHAIPILLA-ERDLMACAQTGSGKTAAFCFPIISgimkdqhverpRGSRAVYPFAVILSPTRELACQ 244
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALE-----------ALKRGKGGRVLVLVPTRELAEQ 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719    245 IHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGC-DILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQ 323
Cdd:smart00487  70 WAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQ 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 42572719    324 IRKIVEQMdmppRGVRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRvgSSTDLITQR 381
Cdd:smart00487 150 LEKLLKLL----PKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 170-356 5.76e-53

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: 180.23  E-value: 5.76e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 170 KYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQH---VERPRGsravyPFAVILSPTRELACQIH 246
Cdd:cd17951   9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKklpFIKGEG-----PYGLIVCPSRELARQTH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 247 DEAKKFSYQ------TGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGF 320
Cdd:cd17951  84 EVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGF 163

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42572719 321 EPQIRKIVEQMdmppRGVRQTMLFSATFPSQIQRLA 356
Cdd:cd17951 164 EEDIRTIFSYF----KGQRQTLLFSATMPKKIQNFA 195
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 152-355 6.63e-53

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: 179.82  E-value: 6.63e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 152 TFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIIsgimkdQHV-ERPRgsravYP 230
Cdd:cd17954   1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPIL------QALlENPQ-----RF 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 231 FAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERAR-VSMQMIRFLAL 309
Cdd:cd17954  70 FALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVM 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42572719 310 DEADRMLDMGFEPQIRKIVEQMdmpPRGvRQTMLFSATFPSQIQRL 355
Cdd:cd17954 150 DEADRLLNMDFEPEIDKILKVI---PRE-RTTYLFSATMTTKVAKL 191
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 152-366 1.87e-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: 178.65  E-value: 1.87e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 152 TFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISgimKDQHVERPRGSRAVypf 231
Cdd:cd17959   2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIE---KLKAHSPTVGARAL--- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 232 avILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDE 311
Cdd:cd17959  76 --ILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDE 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42572719 312 ADRMLDMGFEPQIRKIVEQmdMPPRgvRQTMLFSATFPSQIQRLAADFMSNYIFL 366
Cdd:cd17959 154 ADRLFEMGFAEQLHEILSR--LPEN--RQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 170-366 1.63e-50

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


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 173.93  E-value: 1.63e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 170 KYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQhverPRGSRAVYPFAVILSPTRELACQIHDEA 249
Cdd:cd17949  10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLE----PRVDRSDGTLALVLVPTRELALQIYEVL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 250 ----KKFSYqtgvkVVVAY--GGTPIHQQLRELERGCDILVATPGRLNDLLERARV-SMQMIRFLALDEADRMLDMGFEP 322
Cdd:cd17949  86 ekllKPFHW-----IVPGYliGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMGFEK 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42572719 323 QIRKIVEQMD-----------MPPRgvRQTMLFSATFPSQIQRLAADFMSNYIFL 366
Cdd:cd17949 161 DITKILELLDdkrskaggeksKPSR--RQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 166-348 2.01e-48

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: 168.96  E-value: 2.01e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 166 IRRCKYVRPTPVQRHAIP-ILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHvERPRGSRAVYPFAVILSPTRELACQ 244
Cdd:cd17946   5 LADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKS-SNGVGGKQKPLRALILTPTRELAVQ 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 245 IHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERAR---VSMQMIRFLALDEADRMLDMG-F 320
Cdd:cd17946  84 VKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADRMLEKGhF 163

                       170       180       190
                ....*....|....*....|....*....|.
gi 42572719 321 EpQIRKIVEQMDMPPRGV---RQTMLFSATF 348
Cdd:cd17946 164 A-ELEKILELLNKDRAGKkrkRQTFVFSATL 193
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 153-362 3.85e-48

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: 167.09  E-value: 3.85e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 153 FADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGI-MKDQHVErprgsravypf 231
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdPKKDVIQ----------- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 232 AVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDE 311
Cdd:cd17940  70 ALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42572719 312 ADRMLDMGFEPQIRKIVeqmDMPPRGvRQTMLFSATFPSQIQRLAADFMSN 362
Cdd:cd17940 150 ADKLLSQDFQPIIEKIL---NFLPKE-RQILLFSATFPLTVKNFMDRHMHN 196
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 174-362 5.59e-48

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


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 166.60  E-value: 5.59e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 174 PTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERPRGsravyPFAVILSPTRELACQIHDEAKKF- 252
Cdd:cd17960  13 MTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQ-----VGALIISPTRELATQIYEVLQSFl 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 253 -SYQTGVKVVVAYGGTPIHQQLRELER-GCDILVATPGRLNDLLERARVSMQMIRF--LALDEADRMLDMGFEPQIRKIV 328
Cdd:cd17960  88 eHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKVKSLevLVLDEADRLLDLGFEADLNRIL 167

                       170       180       190
                ....*....|....*....|....*....|....
gi 42572719 329 EQMdmpPRGvRQTMLFSATFPSQIQRLAADFMSN 362
Cdd:cd17960 168 SKL---PKQ-RRTGLFSATQTDAVEELIKAGLRN 197
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 162-364 1.75e-46

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: 162.33  E-value: 1.75e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 162 LNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVerprgsravyPFAVILSPTREL 241
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRN----------PSALILTPTREL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 242 ACQIHDEAKKF-SYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGF 320
Cdd:cd17962  71 AVQIEDQAKELmKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGF 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42572719 321 EPQIRKIVEQMDMPPrgvrQTMLFSATFPSQIQRLAADFMSNYI 364
Cdd:cd17962 151 QQQVLDILENISHDH----QTILVSATIPRGIEQLAGQLLQNPV 190
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 153-362 1.37e-45

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


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 160.18  E-value: 1.37e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 153 FADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMkdqhverprgsravypfA 232
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV-----------------A 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 233 VILSPTRELACQIHDEAKKFS-YQTGVKVVVAY--GGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLAL 309
Cdd:cd17938  64 LILEPSRELAEQTYNCIENFKkYLDNPKLRVALliGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVL 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42572719 310 DEADRMLDMGFEPQIRKIVEQmdMPPRGVR----QTMLFSATFPS-QIQRLAADFMSN 362
Cdd:cd17938 144 DEADRLLSQGNLETINRIYNR--IPKITSDgkrlQVIVCSATLHSfEVKKLADKIMHF 199
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 166-368 5.93e-44

DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 155.53  E-value: 5.93e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 166 IRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIIsgimkdQHVERPRGSRAVYPFAVILSPTRELACQI 245
Cdd:cd17941   5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLL------EKLYRERWTPEDGLGALIISPTRELAMQI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 246 HDEAKKFSYQTGVKVVVAYGGTPIHQqlrELER--GCDILVATPGRL------NDLLERARVSMqmirfLALDEADRMLD 317
Cdd:cd17941  79 FEVLRKVGKYHSFSAGLIIGGKDVKE---EKERinRMNILVCTPGRLlqhmdeTPGFDTSNLQM-----LVLDEADRILD 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42572719 318 MGFEPQIRKIVEQmdMPPrgVRQTMLFSATFPSQIQRLAADFMSNYIFLAV 368
Cdd:cd17941 151 MGFKETLDAIVEN--LPK--SRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 166-356 1.43e-42

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


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 151.74  E-value: 1.43e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 166 IRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHveRPRGSRAVypfaVILSPTRELACQI 245
Cdd:cd17942   5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKF--KPRNGTGV----IIISPTRELALQI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 246 HDEAK---KFSYQTGVKVVvayGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSM-QMIRFLALDEADRMLDMGFE 321
Cdd:cd17942  79 YGVAKellKYHSQTFGIVI---GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILEIGFE 155

                       170       180       190
                ....*....|....*....|....*....|....*
gi 42572719 322 PQIRKIVEQmdMPPRgvRQTMLFSATFPSQIQRLA 356
Cdd:cd17942 156 EEMRQIIKL--LPKR--RQTMLFSATQTRKVEDLA 186
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 166-365 4.02e-42

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: 150.49  E-value: 4.02e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 166 IRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFcfpiisGIMKDQHVERPRGSravyPFAVILSPTRELACQI 245
Cdd:cd17943   5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVF------VVIALESLDLERRH----PQVLILAPTREIAVQI 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 246 HDEAKKF-SYQTGVKVVVAYGGTPIHQQLRELeRGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQI 324
Cdd:cd17943  75 HDVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDV 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 42572719 325 RKIVEQMdmpPRGvRQTMLFSATFPSQIQRLAADFMSNYIF 365
Cdd:cd17943 154 NWIFSSL---PKN-KQVIAFSATYPKNLDNLLARYMRKPVL 190
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 166-355 4.88e-42

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: 150.43  E-value: 4.88e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 166 IRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERPRGsravYPFAVILSPTRELACQI 245
Cdd:cd17961   9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQ----GTRALILVPTRELAQQV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 246 HDEAKKFSYQTGVKV-VVAYGG----TPIHQQLRELErgcDILVATPGRLNDLLERARVSMQ-MIRFLALDEADRMLDMG 319
Cdd:cd17961  85 SKVLEQLTAYCRKDVrVVNLSAsssdSVQRALLAEKP---DIVVSTPARLLSHLESGSLLLLsTLKYLVIDEADLVLSYG 161

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42572719 320 FEPQIRKIVEQMdmpPRGVrQTMLFSATFPSQIQRL 355
Cdd:cd17961 162 YEEDLKSLLSYL---PKNY-QTFLMSATLSEDVEAL 193
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 161-366 4.47e-38

DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 139.25  E-value: 4.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 161 ALNLNIRRCKYVRPTPVQRHAIPILLAE--RDLMACAQTGSGKTAAFCFPIISGIMKDQHverprgsravYPFAVILSPT 238
Cdd:cd17963   4 ELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLK----------SPQALCLAPT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 239 RELACQIHDEAKKFSYQTGVKVVVA------YGGTPIHQQlrelergcdILVATPGRLNDLLERARVSMQMIRFLALDEA 312
Cdd:cd17963  74 RELARQIGEVVEKMGKFTGVKVALAvpgndvPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEA 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42572719 313 DRMLDM-GFEPQIRKIveqMDMPPRGVrQTMLFSATFPSQIQRLAADFMSNYIFL 366
Cdd:cd17963 145 DVMLDTqGHGDQSIRI---KRMLPRNC-QILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 171-362 4.93e-37

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: 136.69  E-value: 4.93e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 171 YVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVerprgsravyPFAVILSPTRELACQIHDEAK 250
Cdd:cd17939  17 FEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRE----------TQALVLAPTRELAQQIQKVVK 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 251 KFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIRKIVEq 330
Cdd:cd17939  87 ALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQ- 165

                       170       180       190
                ....*....|....*....|....*....|..
gi 42572719 331 mdMPPRGVrQTMLFSATFPSQIQRLAADFMSN 362
Cdd:cd17939 166 --FLPPET-QVVLFSATMPHEVLEVTKKFMRD 194
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 176-360 6.88e-36

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: 133.43  E-value: 6.88e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 176 PVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHvERPRGsRAvyPFAVILSPTRELACQIHDEAKKFSYQ 255
Cdd:cd17944  15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQ-PRKRG-RA--PKVLVLAPTRELANQVTKDFKDITRK 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 256 tgVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIRKIV-EQMDMP 334
Cdd:cd17944  91 --LSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsVSYKKD 168

                       170       180
                ....*....|....*....|....*.
gi 42572719 335 PRGVRQTMLFSATFPSQIQRLAADFM 360
Cdd:cd17944 169 SEDNPQTLLFSATCPDWVYNVAKKYM 194
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 389-503 7.84e-36

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 130.02  E-value: 7.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719   389 DKRSHLMDLLHAQRETQdkqslTLVFVETKRGADtLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVA 468
Cdd:pfam00271   1 EKLEALLELLKKERGGK-----VLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVA 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 42572719   469 ARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAG 503
Cdd:pfam00271  75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 153-362 8.02e-36

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: 133.62  E-value: 8.02e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 153 FADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIIsgimkdQHVERPRGSRAVypfa 232
Cdd:cd17950   4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL------QQLEPVDGQVSV---- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 233 VILSPTRELACQIHDEAKKFS-YQTGVKVVVAYGGTPIHQQLRELERGC-DILVATPGRLNDLLERARVSMQMIRFLALD 310
Cdd:cd17950  74 LVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLD 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42572719 311 EADRM---LDMGfepqiRKIVEQMDMPPRGvRQTMLFSATFPSQIQRLAADFMSN 362
Cdd:cd17950 154 ECDKMleqLDMR-----RDVQEIFRATPHD-KQVMMFSATLSKEIRPVCKKFMQD 202
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 165-350 1.69e-34

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: 130.56  E-value: 1.69e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 165 NIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHV-ERPRGSravyPFAVILSPTRELAC 243
Cdd:cd17948   4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLaEGPFNA----PRGLVITPSRELAE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 244 QIHDEAKKFSYQTGVKVVVAYGGTPIhQQLRELERG-CDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEP 322
Cdd:cd17948  80 QIGSVAQSLTEGLGLKVKVITGGRTK-RQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNE 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 42572719 323 QIRKIVEQ----------MDMPPRGVrQTMLFSATFPS 350
Cdd:cd17948 159 KLSHFLRRfplasrrsenTDGLDPGT-QLVLVSATMPS 195
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 171-362 8.03e-34

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: 127.97  E-value: 8.03e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 171 YVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGImkDQHVERPRgsravypfAVILSPTRELACQIHDEAK 250
Cdd:cd18045  19 FEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL--DIQVRETQ--------ALILSPTRELAVQIQKVLL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 251 KFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQ 330
Cdd:cd18045  89 ALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRY 168

                       170       180       190
                ....*....|....*....|....*....|..
gi 42572719 331 mdMPPRgvRQTMLFSATFPSQIQRLAADFMSN 362
Cdd:cd18045 169 --LPPA--TQVVLVSATLPQDILEMTNKFMTD 196
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 153-364 1.93e-33

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: 126.79  E-value: 1.93e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 153 FADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGImkDQHVERPRgsravypfA 232
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI--DTSLKATQ--------A 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 233 VILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEA 312
Cdd:cd18046  71 LVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEA 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42572719 313 DRMLDMGFEPQIRKIVEQMdmpPRGVrQTMLFSATFPSQIQRLAADFMSNYI 364
Cdd:cd18046 151 DEMLSRGFKDQIYDIFQKL---PPDT-QVVLLSATMPNDVLEVTTKFMRDPI 198
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 165-357 5.16e-31

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: 120.81  E-value: 5.16e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 165 NIRRCKYVRPTPVQRHAIPILLAE---------RDLMACAQTGSGKTAAFCFPIISgIMKDQHVERPRgsravypfAVIL 235
Cdd:cd17956   4 NLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQ-ALSKRVVPRLR--------ALIV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 236 SPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIH---QQLRELERG-----CDILVATPGRLND-LLERARVSMQMIRF 306
Cdd:cd17956  75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKkeqKLLLVDTSGrylsrVDILVATPGRLVDhLNSTPGFTLKHLRF 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42572719 307 LALDEADRMLDMGF--------------EPQIRKIVEQMDMPPRGVR--QTMLFSATFPSQIQRLAA 357
Cdd:cd17956 155 LVIDEADRLLNQSFqdwletvmkalgrpTAPDLGSFGDANLLERSVRplQKLLFSATLTRDPEKLSS 221
HELICc smart00490
helicase superfamily c-terminal domain;
422-503 9.17e-30

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 112.31  E-value: 9.17e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719    422 DTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGR 501
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 42572719    502 AG 503
Cdd:smart00490  81 AG 82
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 171-367 7.57e-29

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: 115.17  E-value: 7.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 171 YVRPTPVQRHAIPILLAER----------------DLMACAQTGSGKTAAFCFPIISGImKDQHVERPRGSRAVY----- 229
Cdd:cd17965  28 EIKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYL-KRQEQEPFEEAEEEYesakd 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 230 ---PFAVILSPTRELACQIHDEAKKFSYQTGVKV-VVAYGGTPIHQQLRELERG-CDILVATPGRLNDLlerARVSMQM- 303
Cdd:cd17965 107 tgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIkTFSSGFGPSYQRLQLAFKGrIDILVTTPGKLASL---AKSRPKIl 183

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42572719 304 --IRFLALDEADRMLDMGFEPQIRKIVEQMdmppRGVRQTMLFSATFPSQIQRLAADFMSNYIFLA 367
Cdd:cd17965 184 srVTHLVVDEADTLFDRSFLQDTTSIIKRA----PKLKHLILCSATIPKEFDKTLRKLFPDVVRIA 245
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 139-356 1.64e-21

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: 93.55  E-value: 1.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 139 VETSGGDVPPP---VNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAE--RDLMACAQTGSGKTAAFCFPIISGI 213
Cdd:cd18048   3 VEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 214 mkdqhverprGSRAVYPFAVILSPTRELACQ---IHDEAKKFSyqTGVKVVVAYGGTPIHQQLReLERgcDILVATPGRL 290
Cdd:cd18048  83 ----------DALKLYPQCLCLSPTFELALQtgkVVEEMGKFC--VGIQVIYAIRGNRPGKGTD-IEA--QIVIGTPGTV 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42572719 291 NDLLERAR-VSMQMIRFLALDEADRMLDM-GFEPQIRKIveQMDMPPRGvrQTMLFSATFPSQIQRLA 356
Cdd:cd18048 148 LDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRV--KRSMPKEC--QMLLFSATFEDSVWAFA 211
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
176-534 2.51e-19

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 91.36  E-value: 2.51e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 176 PVQRHAIPILLAERDLMACAQTGSGKTAafCF---------------PIISgIMKDQhVE--RPRGSRAVYpfavilspt 238
Cdd:COG0514  20 PGQEEIIEAVLAGRDALVVMPTGGGKSL--CYqlpalllpgltlvvsPLIA-LMKDQ-VDalRAAGIRAAF--------- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 239 relacqIH-----DEAKkfsyqtgvkvvvayggtpihQQLRELERG-CDILVATPGRLN-----DLLERARVSMqmirfL 307
Cdd:COG0514  87 ------LNsslsaEERR--------------------EVLRALRAGeLKLLYVAPERLLnprflELLRRLKISL-----F 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 308 ALDEA--------DrmldmgFEP---QIRKIVEQMDMPPRgvrqtMLFSATFPSQ-----IQRLAadfMSN-YIFLavgr 370
Cdd:COG0514 136 AIDEAhcisqwghD------FRPdyrRLGELRERLPNVPV-----LALTATATPRvradiAEQLG---LEDpRVFV---- 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 371 vgSSTDL--ITQRVEFVQESDKRSHLMDLLHAQREtqdkQSlTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQERE 448
Cdd:COG0514 198 --GSFDRpnLRLEVVPKPPDDKLAQLLDFLKEHPG----GS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEERE 270

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 449 VALRSFKTGRTPILVATdVA-ARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNAQLARSLAE-- 525
Cdd:COG0514 271 ANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEqs 349


                ....*....
gi 42572719 526 LMQEANQEV 534
Cdd:COG0514 350 PPDEERKRV 358
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 152-356 5.96e-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: 73.99  E-value: 5.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 152 TFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAE--RDLMACAQTGSGKTAAFCFPIISgimkdqHVErprgSRAVY 229
Cdd:cd18047   2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLS------QVE----PANKY 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 230 PFAVILSPTRELACQ---IHDEAKKFSYQtgvkVVVAYgGTPIHQQLRELERGCDILVATPGRLNDLLERAR-VSMQMIR 305
Cdd:cd18047  72 PQCLCLSPTYELALQtgkVIEQMGKFYPE----LKLAY-AVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKfIDPKKIK 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42572719 306 FLALDEADRML-DMGFEPQIRKIveqMDMPPRGVrQTMLFSATFPSQIQRLA 356
Cdd:cd18047 147 VFVLDEADVMIaTQGHQDQSIRI---QRMLPRNC-QMLLFSATFEDSVWKFA 194
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 394-505 9.55e-15

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 71.47  E-value: 9.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 394 LMDLLHAQREtQDKQSLTLVFVETKRGADTLENWL-----CMNEFPATSI--HGDRTQQEREV--------ALRSFKTGR 458
Cdd:cd18802  12 LIEILREYFP-KTPDFRGIIFVERRATAVVLSRLLkehpsTLAFIRCGFLigRGNSSQRKRSLmtqrkqkeTLDKFRDGE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 42572719 459 TPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRtGRAGKS 505
Cdd:cd18802  91 LNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNS 136
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 193-347 1.41e-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: 71.28  E-value: 1.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 193 ACAQTGSGKTAAFcFPIIsgimkDQHVERPRgsravyPFAVILSPTRELACQIHDEAKKFsYQTGVKVVVAYGGTPIHQQ 272
Cdd:cd00046   6 ITAPTGSGKTLAA-LLAA-----LLLLLKKG------KKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAEER 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42572719 273 LRELERGCDILVATPGRLNDLLERA-RVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMDMPPRGvrQTMLFSAT 347
Cdd:cd00046  73 EKNKLGDADIIIATPDMLLNLLLREdRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNA--QVILLSAT 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
187-481 4.60e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 75.06  E-value: 4.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 187 AERDLMACAQTGSGKTAAFCFpIISGIMKDQHVerprgsravypfaVILSPTRELACQIHDEAKKFsyqtgvkvvvaYGG 266
Cdd:COG1061  99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGKRV-------------LVLVPRRELLEQWAEELRRF-----------LGD 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 267 TPIHQqlRELERGCDILVATPGRLNDLLERARVSmQMIRFLALDEADRmldmGFEPQIRKIVEQMDMPPRgvrqtMLFSA 346
Cdd:COG1061 154 PLAGG--GKKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAYR-----LGLTA 221

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 347 T------FPSQIQR-------------LAADFMSNYIFLAVgrvgsSTDLITQRVEFVQESDKRSHLMDLLHAQ------ 401
Cdd:COG1061 222 TpfrsdgREILLFLfdgivyeyslkeaIEDGYLAPPEYYGI-----RVDLTDERAEYDALSERLREALAADAERkdkilr 296

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 402 --RETQDKQSLTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVAARGLDIPHVAH 479
Cdd:COG1061 297 elLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDV 376


                ..
gi 42572719 480 VV 481
Cdd:COG1061 377 AI 378
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
387-504 2.41e-13

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 73.23  E-value: 2.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 387 ESDKRSHLMDLLHAQRETQDKqSLTLVFVETKRGADTLENWLCMNEFPAT------SIHGDR--TQQEREVALRSFKTGR 458
Cdd:COG1111 333 EHPKLSKLREILKEQLGTNPD-SRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGE 411

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 42572719 459 TPILVATDVAARGLDIPHVAHVVNFDL-PNDIdDYVHRIGRTGRAGK 504
Cdd:COG1111 412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGRKRE 457
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 175-312 6.74e-12

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: 64.59  E-value: 6.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 175 TPVQRHAIPILLAERD-LMACAQTGSGKTAAFCFPIISGIMKDqhverprGSRAVYpfaviLSPTRELACQIHDEAKKFS 253
Cdd:cd17921   3 NPIQREALRALYLSGDsVLVSAPTSSGKTLIAELAILRALATS-------GGKAVY-----IAPTRALVNQKEADLRERF 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 254 YQTGVKVVVAYGGTPIhqqLRELERGCDILVATPGRLNDLLERARV-SMQMIRFLALDEA 312
Cdd:cd17921  71 GPLGKNVGLLTGDPSV---NKLLLAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
175-312 1.48e-11

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 67.23  E-value: 1.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 175 TPVQRHAIP-ILLAERDLMACAQTGSGKTAAFCFPIISGIMKdqhverprGSRAVYpfaviLSPTRELACQIHDEAKKFS 253
Cdd:COG1204  24 YPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLN--------GGKALY-----IVPLRALASEKYREFKRDF 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 254 YQTGVKVVVAYGgtPIHQQLRELERgCDILVATPGRLnDLLERARVS-MQMIRFLALDEA 312
Cdd:COG1204  91 EELGIKVGVSTG--DYDSDDEWLGR-YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA 146
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 394-497 6.56e-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: 60.18  E-value: 6.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 394 LMDLLHAQRETQDKqslTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTP--ILVATDVAARG 471
Cdd:cd18793  16 LLELLEELREPGEK---VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVG 92

                        90       100       110
                ....*....|....*....|....*....|..
gi 42572719 472 LDIPHVAHVVNFDL---PNDID---DYVHRIG 497
Cdd:cd18793  93 LNLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 178-312 5.00e-10

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: 59.14  E-value: 5.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 178 QRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDqhverpRGSRAVYpfaviLSPTRELAcqiHDEAKKFS---- 253
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD------PGSRALY-----LYPTKALA---QDQLRSLRelle 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42572719 254 -YQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLL----ERARVSMQMIRFLALDEA 312
Cdd:cd17923  71 qLGLGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 442-506 1.82e-09

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 54.25  E-value: 1.82e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42572719 442 RTQQEREVALRSFKtgrtpILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSG 506
Cdd:cd18785  11 NSIEHAEEIASSLE-----ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 384-512 1.83e-09

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: 56.06  E-value: 1.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 384 FVQESDKRSHLMDLLHAQRETQDKQSlTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILV 463
Cdd:cd18794   7 SVRPKDKKDEKLDLLKRIKVEHLGGS-GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIV 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 42572719 464 ATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFF 512
Cdd:cd18794  86 ATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 173-508 6.34e-09

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 59.08  E-value: 6.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 173 RPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDqhverpRGSRAVYpfaviLSPTRELAcqiHDEAKKF 252
Cdd:COG1205  56 RLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED------PGATALY-----LYPTKALA---RDQLRRL 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 253 S-----YQTGVKVVVAYGGTPIHQQlRELERGCDILVATP-----------GRLNDLLERarvsmqmIRFLALDEA---- 312
Cdd:COG1205 122 RelaeaLGLGVRVATYDGDTPPEER-RWIREHPDIVLTNPdmlhygllphhTRWARFFRN-------LRYVVIDEAhtyr 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 313 -----------DRMldmgfepqiRKIVEQMDMPPrgvrQTMLFSATfpsqIQRlAADFMSNYI---FLAVGRVGSStdli 378
Cdd:COG1205 194 gvfgshvanvlRRL---------RRICRHYGSDP----QFILASAT----IGN-PAEHAERLTgrpVTVVDEDGSP---- 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 379 TQRVEFV-------QESDKRSHL---MDLL--HAQRETQdkqslTLVFVETKRGADTLENWL---CMNEFPATSI---HG 440
Cdd:COG1205 252 RGERTFVlwnpplvDDGIRRSALaeaARLLadLVREGLR-----TLVFTRSRRGAELLARYArraLREPDLADRVaayRA 326

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42572719 441 DRTQQEREVALRSFKTGRTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIA 508
Cdd:COG1205 327 GYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 189-311 2.77e-08

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: 53.74  E-value: 2.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 189 RDLMACAQTGSGKTAAFCFPIISGIMKdqhvERPRGSRAVYpfaviLSPTRELACQIHDEAKKFS--YQTGVKVVVAYGG 266
Cdd:cd17922   2 RNVLIAAPTGSGKTEAAFLPALSSLAD----EPEKGVQVLY-----ISPLKALINDQERRLEEPLdeIDLEIPVAVRHGD 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 42572719 267 TPIHQQLRELERGCDILVATPGRLNDLL--ERARVSMQMIRFLALDE 311
Cdd:cd17922  73 TSQSEKAKQLKNPPGILITTPESLELLLvnKKLRELFAGLRYVVVDE 119
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 370-499 9.07e-08

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 55.23  E-value: 9.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 370 RVGSSTDLITQ-RVEFVQESDKRSHLMDLLHAQRETQDKqslTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQERE 448
Cdd:COG0553 513 QICSHPALLLEeGAELSGRSAKLEALLELLEELLAEGEK---VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERD 589

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42572719 449 VALRSFKTGRTP--ILVATDVAARGLDIPHVAHVVNFDL---PNDID---DYVHRIGRT 499
Cdd:COG0553 590 ELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLwwnPAVEEqaiDRAHRIGQT 648
PRK13766 PRK13766
Hef nuclease; Provisional
 390-504 1.28e-07

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 54.88  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  390 KRSHLMDLLHAQRETQDKqSLTLVFVETKRGADTLENWLCMNEFPA------TSIHGDR--TQQEREVALRSFKTGRTPI 461
Cdd:PRK13766 348 KLEKLREIVKEQLGKNPD-SRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNV 426

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 42572719  462 LVATDVAARGLDIPHVAHVVNFD-LPNDIdDYVHRIGRTGRAGK 504
Cdd:PRK13766 427 LVSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGRQEE 469
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
 194-312 3.12e-07

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 51.11  E-value: 3.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 194 CAQTGSGKTAAFCFPIIsgimkdQHVERPRGSRAVYpfaviLSPTRELACQIHDE-AKKFSYQTGVKVVVAYGGTPihQQ 272
Cdd:cd18021  25 GAPTGSGKTVCAELALL------RHWRQNPKGRAVY-----IAPMQELVDARYKDwRAKFGPLLGKKVVKLTGETS--TD 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 42572719 273 LRELERGcDILVATPGRLnDLLER---ARVSMQMIRFLALDEA 312
Cdd:cd18021  92 LKLLAKS-DVILATPEQW-DVLSRrwkQRKNVQSVELFIADEL 132
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 411-505 5.69e-07

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: 49.57  E-value: 5.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 411 TLVFVETKRGAdtlENW------LCMNEFPATSI---HGDRTQQEREVALRSFKTGRTPILVATDVAARGLDIPHVAHVV 481
Cdd:cd18796  41 TLVFTNTRSQA---ERLaqrlreLCPDRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVI 117

                        90       100
                ....*....|....*....|....
gi 42572719 482 NFDLPNDIDDYVHRIGRTGRAGKS 505
Cdd:cd18796 118 QIGSPKSVARLLQRLGRSGHRPGA 141
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 177-311 6.28e-07

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: 50.43  E-value: 6.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 177 VQRHAIPILL-AERDLMACAQTGSGKTAAFCFPIISGIMKdqHVERPRGSR-AVYpfaviLSPTRELACQIHDEAK-KFS 253
Cdd:cd18023   5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKE--RNPLPWGNRkVVY-----IAPIKALCSEKYDDWKeKFG 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42572719 254 yQTGVKVVVAYGGTPIhQQLRELeRGCDILVATPGRLNDLLERAR--VSM-QMIRFLALDE 311
Cdd:cd18023  78 -PLGLSCAELTGDTEM-DDTFEI-QDADIILTTPEKWDSMTRRWRdnGNLvQLVALVLIDE 135
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
170-311 7.95e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 52.41  E-value: 7.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 170 KYVRPTPVQRHAIPILLAERDLMACAQTGSGKT-AAFCFPIISGIMKDQHVERPRGSRAVYpfaviLSPTRELACQIHD- 247
Cdd:COG1201  21 RFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDELARRPRPGELPDGLRVLY-----ISPLKALANDIERn 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42572719 248 --------EAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLL--ERARVSMQMIRFLALDE 311
Cdd:COG1201  96 lrapleeiGEAAGLPLPEIRVGVRTGDTPASERQRQRRRPPHILITTPESLALLLtsPDARELLRGVRTVIVDE 169
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 188-312 8.04e-07

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: 49.96  E-value: 8.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 188 ERDLMACAQTGSGKTaafcfpIISgIM--KDQHvERPRGSRAVYPFAVILSPTRELACQihdEAKKFSYQTGVKVVVAYG 265
Cdd:cd18034  16 KRNTIVVLPTGSGKT------LIA-VMliKEMG-ELNRKEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSG 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 42572719 266 G----TPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEA 312
Cdd:cd18034  85 EmgvdKWTKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK13767 PRK13767
ATP-dependent helicase; Provisional
 170-311 2.35e-06

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 50.65  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  170 KYVRPTPVQRHAIPILLAERDLMACAQTGSGKT-AAFCfPIISGIMK-DQHVERPRGSRAVYpfaviLSPTRELACQIH- 246
Cdd:PRK13767  29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL-AIIDELFRlGREGELEDKVYCLY-----VSPLRALNNDIHr 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42572719  247 ----------DEAKKFSYQ-TGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLE--RARVSMQMIRFLALDE 311
Cdd:PRK13767 103 nleeplteirEIAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLNspKFREKLRTVKWVIVDE 180
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 443-501 4.62e-06

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: 46.58  E-value: 4.62e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 443 TQQEREVALRSFKTGRTPILVATDVAARGLDIPHVAHVVNFD-LPNDIdDYVHRIGRTGR 501
Cdd:cd18801  75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
 195-474 8.83e-06

CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 48.54  E-value: 8.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 195 AQTGSGKT-AAFCFpiisgIMKdqHVERPRGSRAVYPFavilsPTRELACQIHDEAKKFSyqtGVKVVVAYGGTPIH--Q 271
Cdd:COG1203 154 APTGGGKTeAALLF-----ALR--LAAKHGGRRIIYAL-----PFTSIINQTYDRLRDLF---GEDVLLHHSLADLDllE 218

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 272 QLRELERGC------------DILVATpgrlND-LLER--ARVSMQMIRFLAL-------DEADrMLDMGFEPQIRKIVE 329
Cdd:COG1203 219 EEEEYESEArwlkllkelwdaPVVVTT----IDqLFESlfSNRKGQERRLHNLansviilDEVQ-AYPPYMLALLLRLLE 293

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 330 QMDMPprGVRqTMLFSATFPsQIQRlaaDFMSNYIFLAVGRVGSSTD----LITQRVEFVQESDKRSHLMDLLHAQRETQ 405
Cdd:COG1203 294 WLKNL--GGS-VILMTATLP-PLLR---EELLEAYELIPDEPEELPEyfraFVRKRVELKEGPLSDEELAELILEALHKG 366

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42572719 406 DKqslTLVFVETKRGADTLENWL--CMNEFPATSIHG-----DRTQQEREVaLRSFKTGRTPILVATDVAARGLDI 474
Cdd:COG1203 367 KS---VLVIVNTVKDAQELYEALkeKLPDEEVYLLHSrfcpaDRSEIEKEI-KERLERGKPCILVSTQVVEAGVDI 438
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 411-481 1.89e-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: 1.89e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42572719 411 TLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREV-ALRSFKTGRT--PILVATDVAARGLDIPHVAHVV 481
Cdd:cd18799   9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV 82
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 438-512 1.98e-05

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: 44.93  E-value: 1.98e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42572719 438 IHGDRTQQEREVALRSFKTGRTPILVATDVAARGLDIP--HVAHVVNFdLPNDIDDYVHRIGRTGRAGKSGIATAFF 512
Cdd:cd18789  74 ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPeaNVAIQISG-HGGSRRQEAQRLGRILRPKKGGGKNAFF 149
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 176-349 2.84e-05

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: 45.02  E-value: 2.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 176 PVQRHAI-PILLAERDLMACAQTGSGKTAAFCFPIISGIMkdqhverpRGSRAVYpfaviLSPTRELACQIHDEAKKFsY 254
Cdd:cd18028   4 PPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLL--------EGGKALY-----LVPLRALASEKYEEFKKL-E 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 255 QTGVKVVVAYGGTPIHQqlrELERGCDILVATPGRLNDLLeRARVS-MQMIRFLALDEADRMLDMGFEPQIRKIVEQMDM 333
Cdd:cd18028  70 EIGLKVGISTGDYDEDD---EWLGDYDIIVATYEKFDSLL-RHSPSwLRDVGVVVVDEIHLISDEERGPTLESIVARLRR 145

                       170
                ....*....|....*.
gi 42572719 334 PPRGVRQTMLfSATFP 349
Cdd:cd18028 146 LNPNTQIIGL-SATIG 160
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 414-534 6.11e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 45.86  E-value: 6.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719  414 FVETKRGA-------------DTLENwLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVAARGLDIPHVAHV 480
Cdd:PRK11057 230 YVQEQRGKsgiiycnsrakveDTAAR-LQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFV 308

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42572719  481 VNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENN-AQLARSLAELMQEANQEV 534
Cdd:PRK11057 309 VHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADmAWLRRCLEEKPAGQQQDI 363
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
 176-354 6.78e-05

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 44.06  E-value: 6.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 176 PVQRHAIPILLAERDLMACAQTGSGKT-----AAFCF--------PIISgIMKDQhVERprgsravypfavilsptrela 242
Cdd:cd17920  15 PGQLEAINAVLAGRDVLVVMPTGGGKSlcyqlPALLLdgvtlvvsPLIS-LMQDQ-VDR--------------------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 243 CQihdeakkfsyQTGVKVVVAYGGTPIHQQLRELER----GCDILVATPGRLN-----DLLERARvSMQMIRFLALDEAD 313
Cdd:cd17920  72 LQ----------QLGIRAAALNSTLSPEEKREVLLRikngQYKLLYVTPERLLspdflELLQRLP-ERKRLALIVVDEAH 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42572719 314 RMLDMG--FEP---QIRKIVEQMDMPPrgvrqTMLFSATFPSQIQR 354
Cdd:cd17920 141 CVSQWGhdFRPdylRLGRLRRALPGVP-----ILALTATATPEVRE 181
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 438-504 3.33e-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: 41.56  E-value: 3.33e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42572719 438 IHGDRTQQEREVALRSFKTGRTPILVATDVAARGLDIPH-----VAHVVNFDLPNdiddyVHRI-GRTGRAGK 504
Cdd:cd18811  67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGRGDH 134
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
 442-506 7.60e-04

C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain]  Cd Length: 238  Bit Score: 41.46  E-value: 7.60e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42572719 442 RTQQEREVALRSFKTGRTPILVATDVAARGLDIPHV--AHVVNFDLPNDIDDY---------VHRI-GRTGRAGKSG 506
Cdd:cd18804 128 RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVtlVGILNADSGLNSPDFraserafqlLTQVsGRAGRGDKPG 204
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 173-286 7.98e-04

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: 40.86  E-value: 7.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 173 RPTPVQRHAIPILLAE------RDLMACAQTGSGKTAAFCFPIISgimkdqHVERPRGsravypfAVILSPTRELACQIH 246
Cdd:cd17918  15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL------AYKNGKQ-------VAILVPTEILAHQHY 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 42572719 247 DEAKKFSYQTGVKVVVAYGGTPIHQqlrelerGCDILVAT 286
Cdd:cd17918  82 EEARKFLPFINVELVTGGTKAQILS-------GISLLVGT 114
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 396-484 9.99e-04

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: 40.31  E-value: 9.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 396 DLLHAQRETQDKQSLTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVAARGLDIP 475
Cdd:cd18790  15 DLLGEIRKRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLP 94


                ....*....
gi 42572719 476 HVAHVVNFD 484
Cdd:cd18790  95 EVSLVAILD 103
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
 186-314 1.03e-03

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: 40.88  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 186 LAERDLMACAQTGSGKTaafcfpIISGIMKDQHVERPRGSRAVYpfAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYG 265
Cdd:cd17927  15 LKGKNTIICLPTGSGKT------FVAVLICEHHLKKFPAGRKGK--VVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSG 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 42572719 266 GTPIHQQLRELERGCDILVATPGRL-NDLLERARVSMQMIRFLALDEADR 314
Cdd:cd17927  87 DTSENVSVEQIVESSDVIIVTPQILvNDLKSGTIVSLSDFSLLVFDECHN 136
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
 342-504 1.78e-03

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 40.88  E-value: 1.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 342 MLFSATFPSQIQRLAADfMSNYIFLavgrvgSSTDLITQRVEFVQESDKRShLMDLLHAQR--ETQDKQSLTLVFVETKR 419
Cdd:cd09639 158 LLMSATLPKFLKEYAEK-IGYVEEN------EPLDLKPNERAPFIKIESDK-VGEISSLERllEFIKKGGSVAIIVNTVD 229

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 420 GADTLENWL--CMNEFPATSIHG-----DRTQQEREVaLRSFKTGRTPILVATDVAARGLDIphvahvvNFDL----PND 488
Cdd:cd09639 230 RAQEFYQQLkeKGPEEEIMLIHSrftekDRAKKEAEL-LLEFKKSEKFVIVATQVIEASLDI-------SVDVmiteLAP 301

                       170
                ....*....|....*.
gi 42572719 489 IDDYVHRIGRTGRAGK 504
Cdd:cd09639 302 IDSLIQRLGRLHRYGE 317
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
 173-343 4.49e-03

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 38.46  E-value: 4.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 173 RPTPVQRHAIPILLAERDLMACAQTGSGKTAafcFPIISGIMKDQhverpRGSRAVYPFavilsPTRELACQIHDEAKKF 252
Cdd:cd17924  17 PPWGAQRTWAKRLLRGKSFAIIAPTGVGKTT---FGLATSLYLAS-----KGKRSYLIF-----PTKSLVKQAYERLSKY 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719 253 SYQTG--VKVVVAYGGTPIHQQLRELER----GCDILVATPGRLNDLLEraRVSMQMIRFLALDEAD----------RML 316
Cdd:cd17924  84 AEKAGveVKILVYHSRLKKKEKEELLEKiekgDFDILVTTNQFLSKNFD--LLSNKKFDFVFVDDVDavlkssknidRLL 161

                       170       180
                ....*....|....*....|....*...
gi 42572719 317 DM-GFEpqiRKIVEQMDMPPRGVRQTML 343
Cdd:cd17924 162 KLlGFG---QLVVSSATGRPRGIRPLLF 186
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
 342-504 6.46e-03

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


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 39.36  E-value: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719   342 MLFSATFPSQIQRLAADfMSNYIFLAvGRVGSSTDLITQRVEFVQESDKR---SHLMDLLhaqrETQDKQSLTLVFVETK 418
Cdd:TIGR01587 159 LLMSATLPKFLKEYAEK-IGYVEFNE-PLDLKEERRFENHRFILIESDKVgeiSSLERLL----EFIKKGGSIAIIVNTV 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572719   419 RGADTLENWL--CMNEFPATSIHG-----DRTQQEREVALRSFKTGRTPILVATDVAARGLDIphvahvvNFDL----PN 487
Cdd:TIGR01587 233 DRAQEFYQQLkeKAPEEEIILYHSrftekDRAKKEAELLREMKKSNEKFVIVATQVIEASLDI-------SADVmiteLA 305

                         170
                  ....*....|....*..
gi 42572719   488 DIDDYVHRIGRTGRAGK 504
Cdd:TIGR01587 306 PIDSLIQRLGRLHRYGR 322
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 438-475 6.96e-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: 37.63  E-value: 6.96e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 42572719 438 IHGDRTQQEREVALRSFKTGRTPILVATDVAARGLDIP 475
Cdd:cd18792  66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVP 103
 
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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