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Conserved domains on  [gi|1958750291|ref|XP_038958111|]
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probable ATP-dependent RNA helicase DDX4 isoform X3 [Rattus norvegicus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030645)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 262-514 0e+00

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: 543.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 262 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 341
Cdd:cd18052    12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 342 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC 421
Cdd:cd18052    92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 422 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFL 501
Cdd:cd18052   172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                         250
                  ....*....|...
gi 1958750291 502 KSNYLFVAVGQVG 514
Cdd:cd18052   252 KEDYLFLTVGRVG 264
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 520-649 1.72e-57

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


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 191.18  E-value: 1.72e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 520 VQQSILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 598
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958750291 599 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 649
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 262-514 0e+00

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: 543.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 262 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 341
Cdd:cd18052    12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 342 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC 421
Cdd:cd18052    92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 422 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFL 501
Cdd:cd18052   172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                         250
                  ....*....|...
gi 1958750291 502 KSNYLFVAVGQVG 514
Cdd:cd18052   252 KEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
294-659 8.89e-156

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 458.07  E-value: 8.89e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 294 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqePEC 373
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------PQA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 374 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 453
Cdd:COG0513    75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 454 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVGGACRDVQQSILQVGQYSK 532
Cdd:COG0513   155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 533 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 612
Cdd:COG0513   229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1958750291 613 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNHLAQ 659
Cdd:COG0513   309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRA 355
PTZ00110 PTZ00110
helicase; Provisional
 283-688 2.36e-117

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 363.71  E-value: 2.36e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 283 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITA 362
Cdd:PTZ00110  120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INA 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 363 S-RFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIG 441
Cdd:PTZ00110  195 QpLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTN 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 442 LKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKSNYLFVAVGQVG-GACRDV 520
Cdd:PTZ00110  275 LRRVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNI 350

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 521 QQSILQVGQYSKREKLVEILRNIGDE--RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 598
Cdd:PTZ00110  351 KQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPI 430

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 599 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFdTESDNHLAQPLVKVLSDAQQDVPAWLEE 678
Cdd:PTZ00110  431 MIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFL-TPDKYRLARDLVKVLREAKQPVPPELEK 509

                         410
                  ....*....|
gi 1958750291 679 IAFSSYAPPS 688
Cdd:PTZ00110  510 LSNERSNGTE 519
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 317-496 1.56e-60

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 200.93  E-value: 1.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 317 TPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELINQIYLEARKFSFG 396
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD---------KLDNGPQALVLAPTRELAEQIYEELKKLGKG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 397 TCVRAVVIYGGTQFGHSIRQIvQGCNILCATPGRLMDIIGKEKiGLKQVKYLVLDEADRMLDMGFGPEMKKLISCpgMPs 476
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146

                         170       180
                  ....*....|....*....|
gi 1958750291 477 kEQRQTLLFSATFPEEIQRL 496
Cdd:pfam00270 147 -KKRQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 520-649 1.72e-57

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 191.18  E-value: 1.72e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 520 VQQSILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 598
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958750291 599 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 649
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
308-511 1.68e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 177.68  E-value: 1.68e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291  308 IAKAGYTKLTPVQKYSIPIVLAG-RDLMACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqEPECIIVAPTRELINQI 386
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK----------GGRVLVLVPTRELAEQW 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291  387 YLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEM 465
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958750291  466 KKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVG 511
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLN-DPVFIDVG 191
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 531-640 3.37e-38

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: 137.34  E-value: 3.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 531 SKREKLVEILRNIGDERTMVFVETKKKADfIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLD 610
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958750291 611 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 640
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
559-640 2.72e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.45  E-value: 2.72e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291  559 DFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 638
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 1958750291  639 CG 640
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
528-646 7.33e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 94.41  E-value: 7.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 528 GQYSKREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKISTTSIHG--DRE------QREREQALGDFRCGK 595
Cdd:COG1111   332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958750291 596 CPVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNTGRAI 646
Cdd:COG1111   412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
PRK13766 PRK13766
Hef nuclease; Provisional
 532-646 6.66e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.76  E-value: 6.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 532 KREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKIST------TSIHGDREQREREQ--ALGDFRCGKCPVL 599
Cdd:PRK13766  348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGMSQKEQieILDKFRAGEFNVL 427

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958750291 600 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 646
Cdd:PRK13766  428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
 
Name Accession Description Interval E-value
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 262-514 0e+00

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: 543.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 262 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 341
Cdd:cd18052    12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 342 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC 421
Cdd:cd18052    92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 422 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFL 501
Cdd:cd18052   172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                         250
                  ....*....|...
gi 1958750291 502 KSNYLFVAVGQVG 514
Cdd:cd18052   252 KEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
294-659 8.89e-156

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 458.07  E-value: 8.89e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 294 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqePEC 373
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------PQA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 374 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 453
Cdd:COG0513    75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 454 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVGGACRDVQQSILQVGQYSK 532
Cdd:COG0513   155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 533 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 612
Cdd:COG0513   229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1958750291 613 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNHLAQ 659
Cdd:COG0513   309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRA 355
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 294-514 9.97e-146

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: 424.59  E-value: 9.97e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 294 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAS-RFKELQEPE 372
Cdd:cd17967     1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgRGRRKAYPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 373 CIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 452
Cdd:cd17967    81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750291 453 ADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVG 514
Cdd:cd17967   161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
PTZ00110 PTZ00110
helicase; Provisional
 283-688 2.36e-117

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 363.71  E-value: 2.36e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 283 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITA 362
Cdd:PTZ00110  120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INA 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 363 S-RFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIG 441
Cdd:PTZ00110  195 QpLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTN 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 442 LKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKSNYLFVAVGQVG-GACRDV 520
Cdd:PTZ00110  275 LRRVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNI 350

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 521 QQSILQVGQYSKREKLVEILRNIGDE--RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 598
Cdd:PTZ00110  351 KQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPI 430

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 599 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFdTESDNHLAQPLVKVLSDAQQDVPAWLEE 678
Cdd:PTZ00110  431 MIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFL-TPDKYRLARDLVKVLREAKQPVPPELEK 509

                         410
                  ....*....|
gi 1958750291 679 IAFSSYAPPS 688
Cdd:PTZ00110  510 LSNERSNGTE 519
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 273-514 7.34e-113

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: 341.25  E-value: 7.34e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 273 FDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL 352
Cdd:cd18051     1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 353 AHMMRDG-----ITASRF--KELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILC 425
Cdd:cd18051    81 SQIYEQGpgeslPSESGYygRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 426 ATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFLkSNY 505
Cdd:cd18051   161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFL-DNY 239


                  ....*....
gi 1958750291 506 LFVAVGQVG 514
Cdd:cd18051   240 IFLAVGRVG 248
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 295-687 3.71e-103

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 323.68  E-value: 3.71e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 295 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITASRFKelqePECI 374
Cdd:PRK11776    6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK-----LDVKRFR----VQAL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 375 IVAPTRELINQIYLEARKFSFGT-CVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 453
Cdd:PRK11776   77 VLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 454 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVGGAcRDVQQSILQVGQYSK 532
Cdd:PRK11776  157 DRMLDMGFQDAIDAIIRqAP-----ARRQTLLFSATYPEGIAAISQRFQR-DPVEVKVESTHDL-PAIEQRFYEVSPDER 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 533 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 612
Cdd:PRK11776  230 LPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958750291 613 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFdTESDNHLAQplvkVLSDAQQDVPAW--LEEIAFSSYAPP 687
Cdd:PRK11776  310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLV-APEEMQRAN----AIEDYLGRKLNWepLPSLSPLSGVPL 381
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 294-648 4.01e-90

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 288.76  E-value: 4.01e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 294 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMmrdgITASRFKELQePEC 373
Cdd:PRK11192    2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL----LDFPRRKSGP-PRI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 374 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 453
Cdd:PRK11192   77 LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 454 DRMLDMGFGPEMKKLiscpgmpSKEQR---QTLLFSATFP-EEIQRLAGEFLKsNYLFVAVgqvgGACRDVQQSILQvgQ 529
Cdd:PRK11192  157 DRMLDMGFAQDIETI-------AAETRwrkQTLLFSATLEgDAVQDFAERLLN-DPVEVEA----EPSRRERKKIHQ--W 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 530 Y-------SKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVAT 602
Cdd:PRK11192  223 YyraddleHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVAT 302

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1958750291 603 SVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 648
Cdd:PRK11192  303 DVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 308-688 1.33e-88

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 285.55  E-value: 1.33e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfKELQEPECIIVAPTRELINQIY 387
Cdd:PRK10590   16 VAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHA---KGRRPVRALILTPTRELAAQIG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 388 LEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 467
Cdd:PRK10590   93 ENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRR 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 468 LIScpGMPSKeqRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVGGACRDVQQSILQVGQYSKREKLVEILRNIGDER 547
Cdd:PRK10590  173 VLA--KLPAK--RQNLLFSATFSDDIKALAEKLLH-NPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGKGNWQQ 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 548 TMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTID 627
Cdd:PRK10590  248 VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPE 327

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750291 628 EYVHRIGRTGRCGNTGRAISFFDTesDNHlaqplvKVLSDAQQDVPAWLEEIAFSSYAP-PS 688
Cdd:PRK10590  328 DYVHRIGRTGRAAATGEALSLVCV--DEH------KLLRDIEKLLKKEIPRIAIPGYEPdPS 381
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 278-673 4.14e-87

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 283.60  E-value: 4.14e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 278 TILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAH--- 354
Cdd:PLN00206  106 KLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcct 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 355 MMRDGITASRfkelqEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDI 434
Cdd:PLN00206  186 IRSGHPSEQR-----NPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDL 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 435 IGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPskeqrQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVG 514
Cdd:PLN00206  261 LSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAK-DIILISIGNPN 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 515 GACRDVQQSILQVGQYSKREKLVEILRNIGDER--TMVFVETKKKADFIAtflcqEKISTT------SIHGDREQREREQ 586
Cdd:PLN00206  335 RPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLA-----NAITVVtglkalSIHGEKSMKERRE 409

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 587 ALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNhLAQPLVKVLS 666
Cdd:PLN00206  410 VMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRN-LFPELVALLK 488


                  ....*..
gi 1958750291 667 DAQQDVP 673
Cdd:PLN00206  489 SSGAAIP 495
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 295-648 4.73e-87

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 282.19  E-value: 4.73e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 295 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFkeLQEPECI 374
Cdd:PRK01297   89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERY--MGEPRAL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 375 IVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQI-VQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 453
Cdd:PRK01297  167 IIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 454 DRMLDMGFGPEMKKLIScpGMPSKEQRQTLLFSATFPEEIQRLAGEFLkSNYLFVAVGQVGGACRDVQQSILQVGQYSKR 533
Cdd:PRK01297  247 DRMLDMGFIPQVRQIIR--QTPRKEERQTLLFSATFTDDVMNLAKQWT-TDPAIVEIEPENVASDTVEQHVYAVAGSDKY 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 534 EKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIEN 613
Cdd:PRK01297  324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1958750291 614 VQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 648
Cdd:PRK01297  404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 304-508 2.10e-84

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: 265.07  E-value: 2.10e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 304 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkelqEPECIIVAPTRELI 383
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGR-----GPQALVLAPTRELA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 384 NQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGP 463
Cdd:cd00268    76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958750291 464 EMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGEFLKsNYLFV 508
Cdd:cd00268   156 DVEKILSaLP-----KDRQTLLFSATLPEEVKELAKKFLK-NPVRI 195
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 287-648 2.21e-78

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 262.19  E-value: 2.21e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 287 DAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFK 366
Cdd:PRK04537    3 DKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 367 ElqEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKI-GLKQV 445
Cdd:PRK04537   83 E--DPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHAC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 446 KYLVLDEADRMLDMGFGPEMKKLIScpGMPSKEQRQTLLFSATFPEEIQRLAGEFLKSNYLFVAVGQVGGACRdVQQSIL 525
Cdd:PRK04537  161 EICVLDEADRMFDLGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR-VRQRIY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 526 QVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVA 605
Cdd:PRK04537  238 FPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVA 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1958750291 606 ARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 648
Cdd:PRK04537  318 ARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 308-648 9.70e-73

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 242.57  E-value: 9.70e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkELQEPECIIVAPTRELINQIY 387
Cdd:PRK04837   23 LEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDR--KVNQPRALIMAPTRELAVQIH 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 388 LEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 467
Cdd:PRK04837  101 ADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRW 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 468 LIScpGMPSKEQRQTLLFSATFPEEIQRLAGEFLKS-NYLFVAVGQVGGacRDVQQSILqvgqY-SKREKLVEILRNIGD 545
Cdd:PRK04837  181 LFR--RMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVEPEQKTG--HRIKEELF----YpSNEEKMRLLQTLIEE 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 546 E---RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDL 622
Cdd:PRK04837  253 EwpdRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDL 332

                         330       340
                  ....*....|....*....|....*.
gi 1958750291 623 PSTIDEYVHRIGRTGRCGNTGRAISF 648
Cdd:PRK04837  333 PDDCEDYVHRIGRTGRAGASGHSISL 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 294-650 1.30e-69

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 240.14  E-value: 1.30e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 294 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPEC 373
Cdd:PRK11634    7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD---------PELKAPQI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 374 IIVAPTRELINQIYLEARKFS-FGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 452
Cdd:PRK11634   78 LVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 453 ADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPEEIQRLAGEFLKSNYLfVAVgQVGGACR-DVQQSILQVGQYS 531
Cdd:PRK11634  158 ADEMLRMGFIEDVETIMA--QIP--EGHQTALFSATMPEAIRRITRRFMKEPQE-VRI-QSSVTTRpDISQSYWTVWGMR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 532 KREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDI 611
Cdd:PRK11634  232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1958750291 612 ENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 650
Cdd:PRK11634  312 ERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVE 350
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 308-508 5.21e-67

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: 219.55  E-value: 5.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITASRFKELQE-PECIIVAPTRELINQI 386
Cdd:cd17966     5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVH-----INAQPPLERGDgPIVLVLAPTRELAQQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 387 YLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMK 466
Cdd:cd17966    80 QQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958750291 467 KLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFV 508
Cdd:cd17966   160 KIVD----QIRPDRQTLMWSATWPKEVRRLAEDFLK-DYIQV 196
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 308-508 9.20e-61

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


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 203.20  E-value: 9.20e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLA-GRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKelqePECIIVAPTRELINQI 386
Cdd:cd17964     9 LTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSG----VSALIISPTRELALQI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 387 YLEARKF-SFGTCVRAVVIYGGTQFGHSIRQIV-QGCNILCATPGRLMDIIGKEKIG--LKQVKYLVLDEADRMLDMGFG 462
Cdd:cd17964    85 AAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLDMGFR 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958750291 463 PEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFLKSNYLFV 508
Cdd:cd17964   165 PDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 304-501 1.02e-60

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: 202.65  E-value: 1.02e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 304 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitASRFKELQE-PECIIVAPTREL 382
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-----DQRELEKGEgPIAVIVAPTREL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 383 INQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 462
Cdd:cd17952    76 AQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFE 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958750291 463 PEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFL 501
Cdd:cd17952   156 YQVRSIVG----HVRPDRQTLLFSATFKKKIEQLARDIL 190
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 317-496 1.56e-60

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 200.93  E-value: 1.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 317 TPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELINQIYLEARKFSFG 396
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD---------KLDNGPQALVLAPTRELAEQIYEELKKLGKG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 397 TCVRAVVIYGGTQFGHSIRQIvQGCNILCATPGRLMDIIGKEKiGLKQVKYLVLDEADRMLDMGFGPEMKKLISCpgMPs 476
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146

                         170       180
                  ....*....|....*....|
gi 1958750291 477 kEQRQTLLFSATFPEEIQRL 496
Cdd:pfam00270 147 -KKRQILLLSATLPRNLEDL 165
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 283-503 1.97e-60

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: 202.61  E-value: 1.97e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 283 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITA 362
Cdd:cd17953     2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRH-----IKD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 363 SRF-KELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDII---GKE 438
Cdd:cd17953    77 QRPvKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGR 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958750291 439 KIGLKQVKYLVLDEADRMLDMGFGPEMKKLIscpgMPSKEQRQTLLFSATFPEEIQRLAGEFLKS 503
Cdd:cd17953   157 VTNLRRVTYVVLDEADRMFDMGFEPQIMKIV----NNIRPDRQTVLFSATFPRKVEALARKVLHK 217
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 308-503 9.71e-59

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: 198.31  E-value: 9.71e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfKELQEPECIIVAPTRELINQIY 387
Cdd:cd17945     5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEE-TKDDGPYALILAPTRELAQQIE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 388 LEARKFSFGTCVRAVVIYGGtqfgHSIRQIV----QGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGP 463
Cdd:cd17945    84 EETQKFAKPLGIRVVSIVGG----HSIEEQAfslrNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750291 464 EMKKLIScpGMPS------------------KEQRQTLLFSATFPEEIQRLAGEFLKS 503
Cdd:cd17945   160 QVTKILD--AMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRR 215
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 520-649 1.72e-57

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 191.18  E-value: 1.72e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 520 VQQSILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 598
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958750291 599 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 649
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 281-511 6.42e-57

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: 193.69  E-value: 6.42e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 281 VEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgI 360
Cdd:cd18049    12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH-----I 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 361 TASRFKELQE-PECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEK 439
Cdd:cd18049    87 NHQPFLERGDgPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750291 440 IGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVG 511
Cdd:cd18049   167 TNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLK-DYIHINIG 233
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 304-511 9.65e-57

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: 192.03  E-value: 9.65e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 304 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqEPECIIVAPTRELI 383
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-------GLRALILAPTRELA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 384 NQIYLEARKFSFGTCVRAVVIYGGT--QFGHSIRQIvQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGF 461
Cdd:cd17957    74 SQIYRELLKLSKGTGLRIVLLSKSLeaKAKDGPKSI-TKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGF 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958750291 462 GPEMKKLI-SCpgmpSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVG 511
Cdd:cd17957   153 REQTDEILaAC----TNPNLQRSLFSATIPSEVEELARSVMK-DPIRIIVG 198
PTZ00424 PTZ00424
helicase 45; Provisional
 294-657 7.09e-54

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 190.81  E-value: 7.09e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 294 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitasrfkeLQEPEC 373
Cdd:PTZ00424   29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD---------LNACQA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 374 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 453
Cdd:PTZ00424  100 LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 454 DRMLDMGFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLAGEFLKSNYLfVAVGQVGGACRDVQQSILQVGQYS-K 532
Cdd:PTZ00424  180 DEMLSRGFKGQIYDVFK--KLPP--DVQVALFSATMPNEILELTTKFMRDPKR-ILVKKDELTLEGIRQFYVAVEKEEwK 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 533 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 612
Cdd:PTZ00424  255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1958750291 613 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNHL 657
Cdd:PTZ00424  335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQL 379
DEXDc smart00487
DEAD-like helicases superfamily;
308-511 1.68e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 177.68  E-value: 1.68e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291  308 IAKAGYTKLTPVQKYSIPIVLAG-RDLMACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqEPECIIVAPTRELINQI 386
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK----------GGRVLVLVPTRELAEQW 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291  387 YLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEM 465
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958750291  466 KKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVG 511
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLN-DPVFIDVG 191
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 281-511 5.57e-51

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: 179.05  E-value: 5.57e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 281 VEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgI 360
Cdd:cd18050    50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVH-----I 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 361 TASRFKELQE-PECIIVAPTRELINQIYLEArkFSFGTCVR--AVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGK 437
Cdd:cd18050   125 NHQPYLERGDgPICLVLAPTRELAQQVQQVA--DDYGKSSRlkSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEA 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958750291 438 EKIGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVG 511
Cdd:cd18050   203 GKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLR-DYVQINIG 271
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 308-502 1.25e-50

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: 175.14  E-value: 1.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRdgitasRFKELQEPECIIVAPTRELINQIY 387
Cdd:cd17947     5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY------RPKKKAATRVLVLVPTRELAMQCF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 388 LEARKFS-FGTCVRAVVIyGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVLDEADRMLDMGFGPEM 465
Cdd:cd17947    79 SVLQQLAqFTDITFALAV-GGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADEL 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958750291 466 KKLI-SCPgmpskEQRQTLLFSATFPEEIQRLAGEFLK 502
Cdd:cd17947   158 KEILrLCP-----RTRQTMLFSATMTDEVKDLAKLSLN 190
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 295-508 2.00e-50

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: 175.11  E-value: 2.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 295 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD--GITAsrfkelqepe 372
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDpyGIFA---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 373 cIIVAPTRELINQIyleARKF-SFGTC--VRAVVIYGGTQFghsIRQ---IVQGCNILCATPGRLMDII---GKEKIGLK 443
Cdd:cd17955    71 -LVLTPTRELAYQI---AEQFrALGAPlgLRCCVIVGGMDM---VKQaleLSKRPHIVVATPGRLADHLrssDDTTKVLS 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958750291 444 QVKYLVLDEADRMLDMGFGPEMKKLISCpgMPSKeqRQTLLFSATFPEEIQRLAGEFLKSNYLFV 508
Cdd:cd17955   144 RVKFLVLDEADRLLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 307-502 3.60e-50

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: 174.19  E-value: 3.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 307 NIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMmrDGITASRFKElQEPECIIVAPTRELINQI 386
Cdd:cd17958     4 EIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL--DLQPIPREQR-NGPGVLVLTPTRELALQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 387 YLEARKFSFGTcVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMK 466
Cdd:cd17958    81 EAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958750291 467 KLIscpgMPSKEQRQTLLFSATFPEEIQRLAGEFLK 502
Cdd:cd17958   160 KIL----LDIRPDRQTIMTSATWPDGVRRLAQSYLK 191
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 294-496 3.92e-50

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: 174.04  E-value: 3.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 294 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitASRFkelqepEC 373
Cdd:cd17954     1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---PQRF------FA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 374 IIVAPTRELINQI--YLEARKFSFGtcVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVL 450
Cdd:cd17954    72 LVLAPTRELAQQIseQFEALGSSIG--LKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVM 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958750291 451 DEADRMLDMGFGPEMKKLISCpgMPSkeQRQTLLFSATFPEEIQRL 496
Cdd:cd17954   150 DEADRLLNMDFEPEIDKILKV--IPR--ERTTYLFSATMTTKVAKL 191
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 308-497 7.24e-50

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: 173.15  E-value: 7.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhMMRDGITASRFKELQepeCIIVAPTRELINQIY 387
Cdd:cd17960     5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLE-ILLKRKANLKKGQVG---ALIISPTRELATQIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 388 LEARKF--SFGTCVRAVVIYGGTQFGHSIRQIV-QGCNILCATPGRLMDIIG--KEKIGLKQVKYLVLDEADRMLDMGFG 462
Cdd:cd17960    81 EVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLGFE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958750291 463 PEMKKLISCpgMPskEQRQTLLFSATFPEEIQRLA 497
Cdd:cd17960   161 ADLNRILSK--LP--KQRRTGLFSATQTDAVEELI 191
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 294-491 3.08e-49

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: 171.72  E-value: 3.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 294 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL----AHMMRDGITAsrfkelq 369
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIeklkAHSPTVGARA------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 370 epecIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLV 449
Cdd:cd17959    75 ----LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVV 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958750291 450 LDEADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPE 491
Cdd:cd17959   151 FDEADRLFEMGFAEQLHEILS--RLP--ENRQTLLFSATLPK 188
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 300-502 5.82e-49

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: 171.23  E-value: 5.82e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 300 LCQTLNNNIakaGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitASRFKELQEPECIIVAPT 379
Cdd:cd17949     1 LVSHLKSKM---GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSL---EPRVDRSDGTLALVLVPT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 380 RELINQIYLEARKF--SFGTCVRAVVIyGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVLDEADRM 456
Cdd:cd17949    75 RELALQIYEVLEKLlkPFHWIVPGYLI-GGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958750291 457 LDMGFGPEMKKLIS---------CPGMPSKEQRQTLLFSATFPEEIQRLAGEFLK 502
Cdd:cd17949   154 LDMGFEKDITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLK 208
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 295-505 5.90e-47

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: 165.16  E-value: 5.90e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 295 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL--AHMMRDGITAsrfkelqepe 372
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILekIDPKKDVIQA---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 373 cIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 452
Cdd:cd17940    71 -LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958750291 453 ADRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGEFLKSNY 505
Cdd:cd17940   150 ADKLLSQDFQPIIEKILNfLP-----KERQILLFSATFPLTVKNFMDRHMHNPY 198
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 308-510 1.96e-46

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: 163.61  E-value: 1.96e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitasRFKELQEPECIIVAPTRELINQIY 387
Cdd:cd17941     5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE-----RWTPEDGLGALIISPTRELAMQIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 388 LEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQgCNILCATPGRL---MDiigkEKIGL--KQVKYLVLDEADRMLDMGFG 462
Cdd:cd17941    80 EVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLlqhMD----ETPGFdtSNLQMLVLDEADRILDMGFK 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958750291 463 PEMKKLIScpGMPSKeqRQTLLFSATFPEEIQRLAGEFLKsNYLFVAV 510
Cdd:cd17941   155 ETLDAIVE--NLPKS--RQTLLFSATQTKSVKDLARLSLK-NPEYISV 197
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 308-508 9.54e-46

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: 161.76  E-value: 9.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmmrDGITASRFKELQEPECIIVAPTRELINQIY 387
Cdd:cd17942     5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-----ELLYKLKFKPRNGTGVIIISPTRELALQIY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 388 LEARKF------SFGTCVravviyGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGL-KQVKYLVLDEADRMLDMG 460
Cdd:cd17942    80 GVAKELlkyhsqTFGIVI------GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILEIG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958750291 461 FGPEMKKLISCpgMPSkeQRQTLLFSATFPEEIQRLAGEFLKSNYLFV 508
Cdd:cd17942   154 FEEEMRQIIKL--LPK--RRQTMLFSATQTRKVEDLARISLKKKPLYV 197
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 308-503 3.16e-44

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: 157.89  E-value: 3.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASrFKELQEPECIIVAPTRELINQIY 387
Cdd:cd17951     5 LKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLP-FIKGEGPYGLIVCPSRELARQTH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 388 ---------LEARKFSfgtCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLD 458
Cdd:cd17951    84 evieyyckaLQEGGYP---QLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958750291 459 MGFGPEMKKLISCpgmpSKEQRQTLLFSATFPEEIQrlagEFLKS 503
Cdd:cd17951   161 MGFEEDIRTIFSY----FKGQRQTLLFSATMPKKIQ----NFAKS 197
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 304-502 1.35e-43

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


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 155.78  E-value: 1.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 304 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELI 383
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL---------TEHRNPSALILTPTRELA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 384 NQIYLEARKFSFGTC-VRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 462
Cdd:cd17962    72 VQIEDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQ 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958750291 463 PEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLK 502
Cdd:cd17962   152 QQVLDILE----NISHDHQTILVSATIPRGIEQLAGQLLQ 187
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 295-497 1.39e-40

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: 147.85  E-value: 1.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 295 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmmrdgitasrfkelQEPECI 374
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------QIVVAL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 375 IVAPTRELINQIYLEARKFSF---GTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLD 451
Cdd:cd17938    65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958750291 452 EADRMLDMGFGPEMKKLIS-CPGMPSKEQR-QTLLFSATF-PEEIQRLA 497
Cdd:cd17938   145 EADRLLSQGNLETINRIYNrIPKITSDGKRlQVIVCSATLhSFEVKKLA 193
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 308-489 4.52e-40

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


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 147.39  E-value: 4.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIP-IVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQI 386
Cdd:cd17946     5 LADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTRELAVQV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 387 --YLEA-RKFsfgTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGK--EKIG-LKQVKYLVLDEADRMLDMG 460
Cdd:cd17946    85 kdHLKAiAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEgnEHLAnLKSLRFLVLDEADRMLEKG 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958750291 461 FGPEMKKLISC---PGMPSKEQRQTLLFSATF 489
Cdd:cd17946   162 HFAELEKILELlnkDRAGKKRKRQTFVFSATL 193
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 531-640 3.37e-38

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: 137.34  E-value: 3.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 531 SKREKLVEILRNIGDERTMVFVETKKKADfIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLD 610
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958750291 611 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 640
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 312-505 3.81e-37

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: 138.06  E-value: 3.81e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 312 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKElqePECIIVAPTRELINQIYLE-- 389
Cdd:cd17944     9 GVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRA---PKVLVLAPTRELANQVTKDfk 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 390 --ARKFSFgTCvravvIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 467
Cdd:cd17944    86 diTRKLSV-AC-----FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958750291 468 LISCPGMPSKEQR-QTLLFSATFPEEIQRLAGEFLKSNY 505
Cdd:cd17944   160 ILSVSYKKDSEDNpQTLLFSATCPDWVYNVAKKYMKSQY 198
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 308-503 5.28e-36

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: 134.63  E-value: 5.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgiTASRFKElQEPECIIVAPTRELINQIY 387
Cdd:cd17961     9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKA--KAESGEE-QGTRALILVPTRELAQQVS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 388 LEARKFSFGTC--VRAVVIyggTQFGHSIRQIVQ---GCNILCATPGRLMDII-GKEKIGLKQVKYLVLDEADRMLDMGF 461
Cdd:cd17961    86 KVLEQLTAYCRkdVRVVNL---SASSSDSVQRALlaeKPDIVVSTPARLLSHLeSGSLLLLSTLKYLVIDEADLVLSYGY 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958750291 462 GPEMKKLIS-CPGMPskeqrQTLLFSATFPEEIQRLAGEFLKS 503
Cdd:cd17961   163 EEDLKSLLSyLPKNY-----QTFLMSATLSEDVEALKKLVLHN 200
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 300-496 2.01e-35

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: 133.91  E-value: 2.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 300 LCQTLNNNiakaGYTKLTPVQKYSIPIVLAG---------RDLMACAQTGSGKTAAFLLPILAhmmrdgITASRFK-ELQ 369
Cdd:cd17956     1 LLKNLQNN----GITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQ------ALSKRVVpRLR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 370 epeCIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC--------NILCATPGRLMD-IIGKEKI 440
Cdd:cd17956    71 ---ALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDhLNSTPGF 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958750291 441 GLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQR----------------QTLLFSATF---PEEIQRL 496
Cdd:cd17956   148 TLKHLRFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLgsfgdanllersvrplQKLLFSATLtrdPEKLSSL 222
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 304-502 4.86e-34

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: 128.85  E-value: 4.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 304 LNNNIAKA----GYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILahmmrdgitaSRFKE-LQEPECIIV 376
Cdd:cd17963     1 LKPELLKGlyamGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAML----------SRVDPtLKSPQALCL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 377 APTRELINQIYLEARKFSFGT------CVRAVVIYGGTQFGHsirQIVQGcnilcaTPGRLMDIIGKEKIGLKQVKYLVL 450
Cdd:cd17963    71 APTRELARQIGEVVEKMGKFTgvkvalAVPGNDVPRGKKITA---QIVIG------TPGTVLDWLKKRQLDLKKIKILVL 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750291 451 DEADRMLDM-GFGPE---MKKLI--SCpgmpskeqrQTLLFSATFPEEIQRLAGEFLK 502
Cdd:cd17963   142 DEADVMLDTqGHGDQsirIKRMLprNC---------QILLFSATFPDSVRKFAEKIAP 190
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 307-491 1.70e-30

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 119.78  E-value: 1.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 307 NIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkELQEPECIIVAPTRELINQI 386
Cdd:cd17948     4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEG--PFNAPRGLVITPSRELAEQI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 387 YLEARKFSFGTCVRAVVIYGgtqfGHSIRQIV----QGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 462
Cdd:cd17948    82 GSVAQSLTEGLGLKVKVITG----GRTKRQIRnphfEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958750291 463 PEMKKLIS-CP-GMPSKEQR-------QTLLFSATFPE 491
Cdd:cd17948   158 EKLSHFLRrFPlASRRSENTdgldpgtQLVLVSATMPS 195
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 308-503 1.26e-29

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: 116.68  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILaHMMRdgitasrfKELQEPECIIVAPTRELINQIY 387
Cdd:cd17950    17 IVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL-QQLE--------PVDGQVSVLVICHTRELAFQIS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 388 LEARKFS-FGTCVRAVVIYGGTQFGHSIRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDmgfGPEM 465
Cdd:cd17950    88 NEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE---QLDM 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958750291 466 KKLI-----SCPgmpskEQRQTLLFSATFPEEIQRLAGEFLKS 503
Cdd:cd17950   165 RRDVqeifrATP-----HDKQVMMFSATLSKEIRPVCKKFMQD 202
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 297-501 2.16e-29

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: 115.88  E-value: 2.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 297 EANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhmmrdgITASRFKELQepeCIIV 376
Cdd:cd17939     1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQ------RIDTTVRETQ---ALVL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 377 APTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRM 456
Cdd:cd17939    72 APTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEM 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958750291 457 LDMGFGPEMKKLISCpgMPSKEqrQTLLFSATFPEEIQRLAGEFL 501
Cdd:cd17939   152 LSRGFKDQIYDIFQF--LPPET--QVVLFSATMPHEVLEVTKKFM 192
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 295-502 7.21e-29

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: 114.47  E-value: 7.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 295 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECI 374
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQID---------TSLKATQAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 375 IVAPTRELINQI--YLEARKFSFGTCVRAVViyGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 452
Cdd:cd18046    72 VLAPTRELAQQIqkVVMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDE 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958750291 453 ADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPEEIQRLAGEFLK 502
Cdd:cd18046   150 ADEMLSRGFKDQIYDIFQ--KLP--PDTQVVLLSATMPNDVLEVTTKFMR 195
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 295-501 1.83e-28

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: 112.95  E-value: 1.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 295 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhmMRDgitasrfKELQEPECI 374
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ--CLD-------IQVRETQAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 375 IVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEAD 454
Cdd:cd18045    72 ILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEAD 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958750291 455 RMLDMGFgpemKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFL 501
Cdd:cd18045   152 EMLNKGF----KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFM 194
HELICc smart00490
helicase superfamily c-terminal domain;
559-640 2.72e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.45  E-value: 2.72e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291  559 DFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 638
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 1958750291  639 CG 640
Cdd:smart00490  81 AG 82
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 308-508 6.81e-27

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: 108.12  E-value: 6.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLlpILAHMMRDgitasrfKELQEPECIIVAPTRELINQIY 387
Cdd:cd17943     5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFV--VIALESLD-------LERRHPQVLILAPTREIAVQIH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 388 LEARKF-SFGTCVRAVVIYGGTQFGHSIRQIvQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMK 466
Cdd:cd17943    76 DVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958750291 467 KLIScpGMPskEQRQTLLFSATFPEEIQRLAGEFLkSNYLFV 508
Cdd:cd17943   155 WIFS--SLP--KNKQVIAFSATYPKNLDNLLARYM-RKPVLV 191
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 281-497 3.62e-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: 92.78  E-value: 3.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 281 VEVSGHD-APP--AILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILahm 355
Cdd:cd18048     3 VEVLQRDpTSPlfSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 356 mrdgitaSRFKELQE-PECIIVAPTRELINQ---IYLEARKFsfgtCVRAVVIYG--GTQFGHSIRQIVQgcnILCATPG 429
Cdd:cd18048    80 -------SRVDALKLyPQCLCLSPTFELALQtgkVVEEMGKF----CVGIQVIYAirGNRPGKGTDIEAQ---IVIGTPG 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 430 RLMDIIGKEK-IGLKQVKYLVLDEADRMLDM-GFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLA 497
Cdd:cd18048   146 TVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKR--SMPK--ECQMLLFSATFEDSVWAFA 211
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 307-500 4.06e-20

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: 90.51  E-value: 4.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 307 NIAKAGYTKL------TPVQKYSIPIVLAGR----------------DLMACAQTGSGKTAAFLLPILAHMMRDGITASR 364
Cdd:cd17965    16 KEILKGSNKTdeeikpSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPFE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 365 FKELQE--------PECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGtqFGHSIRQIVQ----GCNILCATPGRLM 432
Cdd:cd17965    96 EAEEEYesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSG--FGPSYQRLQLafkgRIDILVTTPGKLA 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750291 433 DIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLAGEF 500
Cdd:cd17965   174 SLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIK--RAPK--LKHLILCSATIPKEFDKTLRKL 237
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
312-652 6.48e-20

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 93.67  E-value: 6.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 312 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPtreLI----NQI- 386
Cdd:COG0514    14 GYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPAL---LLPGLT------------LVVSP---LIalmkDQVd 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 387 YLEARKfsfgtcVRAVVIYGG---TQFGHSIRQIVQG-CNILCATPGRLM-----DIIGKEKIGLkqvkyLVLDEA---- 453
Cdd:COG0514    76 ALRAAG------IRAAFLNSSlsaEERREVLRALRAGeLKLLYVAPERLLnprflELLRRLKISL-----FAIDEAhcis 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 454 ----DrmldmgFGPE---MKKLI-SCPGMPskeqrqTLLFSATFPEE-----IQRLAgefLKSNYLFVavgqvGGACRD- 519
Cdd:COG0514   145 qwghD------FRPDyrrLGELReRLPNVP------VLALTATATPRvradiAEQLG---LEDPRVFV-----GSFDRPn 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 520 VQQSILQVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVL 599
Cdd:COG0514   205 LRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVI 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958750291 600 VATSvaARGL--DIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTE 652
Cdd:COG0514   285 VATI--AFGMgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
528-646 7.33e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 94.41  E-value: 7.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 528 GQYSKREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKISTTSIHG--DRE------QREREQALGDFRCGK 595
Cdd:COG1111   332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958750291 596 CPVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNTGRAI 646
Cdd:COG1111   412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
329-650 2.73e-19

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 92.01  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 329 AGRDLMACAQTGSGKTAAFLLpILAHMMRDGITasrfkelqepecIIVAPTRELINQIYLEARKFsfgtcvravviYGGT 408
Cdd:COG1061    99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGKRV------------LVLVPRRELLEQWAEELRRF-----------LGDP 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 409 QFGHSIRQIvqGCNILCATPGRLMDIIGKEKIGlKQVKYLVLDEADRmldmGFGPEMKKLIScpgmpSKEQRQTLLFSAT 488
Cdd:COG1061   155 LAGGGKKDS--DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILE-----AFPAAYRLGLTAT 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 489 ------FPEEIQRLAG--------EFLKSNYL----FVAV-------GQVGGACRDVQQSILQVGQYSKREKLVEILRNI 543
Cdd:COG1061   223 pfrsdgREILLFLFDGivyeyslkEAIEDGYLappeYYGIrvdltdeRAEYDALSERLREALAADAERKDKILRELLREH 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 544 GD-ERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDL 622
Cdd:COG1061   303 PDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP 382

                         330       340
                  ....*....|....*....|....*...
gi 1958750291 623 PSTIDEYVHRIGRTGRCGNTGRAISFFD 650
Cdd:COG1061   383 TGSPREFIQRLGRGLRPAPGKEDALVYD 410
PRK13766 PRK13766
Hef nuclease; Provisional
 532-646 6.66e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.76  E-value: 6.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 532 KREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKIST------TSIHGDREQREREQ--ALGDFRCGKCPVL 599
Cdd:PRK13766  348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGMSQKEQieILDKFRAGEFNVL 427

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958750291 600 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 646
Cdd:PRK13766  428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 294-497 2.17e-14

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: 72.45  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 294 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILAHMMrdgiTASRFKelqep 371
Cdd:cd18047     2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE----PANKYP----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 372 ECIIVAPTRELINQ---IYLEARKF----SFGTCVRavviyggtqfGHSIRQIVQ-GCNILCATPGRLMDIIGKEK-IGL 442
Cdd:cd18047    73 QCLCLSPTYELALQtgkVIEQMGKFypelKLAYAVR----------GNKLERGQKiSEQIVIGTPGTVLDWCSKLKfIDP 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958750291 443 KQVKYLVLDEADRMLDMGfGPEMKKLISCPGMPskEQRQTLLFSATFPEEIQRLA 497
Cdd:cd18047   143 KKIKVFVLDEADVMIATQ-GHQDQSIRIQRMLP--RNCQMLLFSATFEDSVWKFA 194
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 530-635 2.35e-14

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 70.70  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 530 YSKREKLVEILRN----IGDERTMVFVET---------------KKKADFIATFLCQEKISTTSIHGDREQREREQALGD 590
Cdd:cd18802     6 IPKLQKLIEILREyfpkTPDFRGIIFVERratavvlsrllkehpSTLAFIRCGFLIGRGNSSQRKRSLMTQRKQKETLDK 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958750291 591 FRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGR 635
Cdd:cd18802    86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 532-646 6.42e-14

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: 69.31  E-value: 6.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 532 KREKLVEILRNI-------GDERTMVFVETKKKADFIATFLCQEK--------ISTTSIHGDREQREREQ--ALGDFRCG 594
Cdd:cd18801    10 KLEKLEEIVKEHfkkkqegSDTRVIIFSEFRDSAEEIVNFLSKIRpgiratrfIGQASGKSSKGMSQKEQkeVIEQFRKG 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958750291 595 KCPVLVATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 646
Cdd:cd18801    90 GYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR-KRQGRVV 140
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 536-649 1.21e-13

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: 68.39  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 536 LVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQ 615
Cdd:cd18794    21 LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVR 100

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958750291 616 HVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 649
Cdd:cd18794   101 FVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
308-638 2.95e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 73.01  E-value: 2.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 308 IAKAGYTKLTPVQKYSIP-IVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGItasrfkelqepeCIIVAPTRELINQI 386
Cdd:COG1204    15 LKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK------------ALYIVPLRALASEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 387 YLEARKF--SFGtcVRAVVIYGGTQfghSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEAdRML-DMGFGP 463
Cdd:COG1204    83 YREFKRDfeELG--IKVGVSTGDYD---SDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLIdDESRGP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 464 --EM---KKLISCPGMpskeqrQTLLFSATF--PEEIQR-LAGEFLKSNY----LFVAVgqvggacrdVQQSILQVGQYS 531
Cdd:COG1204   157 tlEVllaRLRRLNPEA------QIVALSATIgnAEEIAEwLDAELVKSDWrpvpLNEGV---------LYDGVLRFDDGS 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 532 KREKLVEI---LRNIGDE-RTMVFVETKKKA-----------------------DFIATFL--CQEKISTTSI------- 575
Cdd:COG1204   222 RRSKDPTLalaLDLLEEGgQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELleVSEETHTNEKladclek 301

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750291 576 -----HGD--REQRER-EQAlgdFRCGKCPVLVATSVAARGLdieN--VQHVI------NFDLPSTIDEYVHRIGRTGR 638
Cdd:COG1204   302 gvafhHAGlpSELRRLvEDA---FREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGR 374
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 330-488 9.42e-13

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 66.27  E-value: 9.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 330 GRDLMACAQTGSGKTAAFLLPILAHMmrdgitasrfkELQEPECIIVAPTRELINQIYLEARKFsFGTCVRAVVIYGGTQ 409
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLL-----------LKKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 410 FGHSIRQIVQGCNILCATPGRL-MDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRqtLLFSAT 488
Cdd:cd00046    69 AEEREKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV--ILLSAT 146
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 297-646 1.88e-12

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: 70.63  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 297 EANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD-GITAsrfkelqepecII 375
Cdd:COG1205    38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDpGATA-----------LY 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 376 VAPTRELINQIYLEARKF--SFGTCVRAVVIYGGTQFghSIRQ-IVQGCNILCATPgrlmDII------GKEKIG--LKQ 444
Cdd:COG1205   107 LYPTKALARDQLRRLRELaeALGLGVRVATYDGDTPP--EERRwIREHPDIVLTNP----DMLhygllpHHTRWArfFRN 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 445 VKYLVLDEA---------------DRMLDMgfgpeMKKLISCPgmpskeqrQTLLFSATF--PEEI-QRLAGEflksnyL 506
Cdd:COG1205   181 LRYVVIDEAhtyrgvfgshvanvlRRLRRI-----CRHYGSDP--------QFILASATIgnPAEHaERLTGR------P 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 507 FVAVGQVGGAC--RDV---QQSILQVGQY-SKREKLVEILRNIGDE--RTMVFVETKKKADFIATFL---CQEKISTTSI 575
Cdd:COG1205   242 VTVVDEDGSPRgeRTFvlwNPPLVDDGIRrSALAEAARLLADLVREglRTLVFTRSRRGAELLARYArraLREPDLADRV 321

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958750291 576 HGDR------EQREREQALgdfRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAI 646
Cdd:COG1205   322 AAYRagylpeERREIERGL---RSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 531-634 7.67e-12

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 63.26  E-value: 7.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 531 SKREKLVEILRNI--GDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDF-RCGKCPV-LVATSVAA 606
Cdd:cd18793    11 GKLEALLELLEELrePGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnEDPDIRVfLLSTKAGG 90

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958750291 607 RGLDIENVQHVINFDLP--STIDEY----VHRIG 634
Cdd:cd18793    91 VGLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 312-672 4.82e-11

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 65.89  E-value: 4.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 312 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPTRELI-NQI-YLE 389
Cdd:PRK11057   22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL---VLDGLT------------LVVSPLISLMkDQVdQLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 390 ARKFSfGTCVRAvviyggTQFGHSIRQIVQGCN-----ILCATPGRLM--DIIgkEKIGLKQVKYLVLDEADRMLDMG-- 460
Cdd:PRK11057   87 ANGVA-AACLNS------TQTREQQLEVMAGCRtgqikLLYIAPERLMmdNFL--EHLAHWNPALLAVDEAHCISQWGhd 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 461 FGPEMKKL----ISCPGMPskeqrqTLLFSATFPE----EIQRLAGeflksnylfvavgqvggacrdVQQSILQVGQYSK 532
Cdd:PRK11057  158 FRPEYAALgqlrQRFPTLP------FMALTATADDttrqDIVRLLG---------------------LNDPLIQISSFDR 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 533 ---REKLVE-------ILRNIGDERT---MVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVL 599
Cdd:PRK11057  211 pniRYTLVEkfkpldqLMRYVQEQRGksgIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIV 290

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958750291 600 VATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNHLAQPLVKVLSDAQQDV 672
Cdd:PRK11057  291 VATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDI 363
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 316-453 1.31e-09

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: 58.04  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 316 LTPVQKYSI-PIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITasrfkelqepeCIIVAPTRELINQIYLEARKFs 394
Cdd:cd17921     2 LNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK-----------AVYIAPTRALVNQKEADLRER- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 395 FGTCVRAVVIYGGtQFGHSIRQIvQGCNILCATPGRLMDIIGKEKI-GLKQVKYLVLDEA 453
Cdd:cd17921    70 FGPLGKNVGLLTG-DPSVNKLLL-AEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 531-636 6.02e-09

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 59.47  E-value: 6.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 531 SKREKLVEILRNI--GDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGK-CPV-LVATSVAA 606
Cdd:COG0553   533 AKLEALLELLEELlaEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLKAGG 612

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958750291 607 RGLdieNVQ---HVINFDLP-------STIDEyVHRIGRT 636
Cdd:COG0553   613 EGL---NLTaadHVIHYDLWwnpaveeQAIDR-AHRIGQT 648
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
 337-635 5.72e-08

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: 55.86  E-value: 5.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 337 AQTGSGKTAAFLLPILAHMMRDGitASRFkelqepecIIVAPTRELINQIYLEARKFSFGtcvrAVVIYGGTQFGHSIRQ 416
Cdd:COG1203   154 APTGGGKTEAALLFALRLAAKHG--GRRI--------IYALPFTSIINQTYDRLRDLFGE----DVLLHHSLADLDLLEE 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 417 IVQGCN---------------ILCATPGRLMDII-----GKEKIGLKQV-KYLVLDEADrMLDMGFGPEMKKLIscpgmp 475
Cdd:COG1203   220 EEEYESearwlkllkelwdapVVVTTIDQLFESLfsnrkGQERRLHNLAnSVIILDEVQ-AYPPYMLALLLRLL------ 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 476 sKEQRQ----TLLFSATFPEEIQrlagEFLKSNYLFV--AVGQVGGACRDVQQSILQV--GQYSkREKLVEILRNI--GD 545
Cdd:COG1203   293 -EWLKNlggsVILMTATLPPLLR----EELLEAYELIpdEPEELPEYFRAFVRKRVELkeGPLS-DEELAELILEAlhKG 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 546 ERTMVFVETKKKAdfIATF-LCQEKISTTSIH--------GDREQREREqALGDFRCGKCPVLVATSVAARGLDienvqh 616
Cdd:COG1203   367 KSVLVIVNTVKDA--QELYeALKEKLPDEEVYllhsrfcpADRSEIEKE-IKERLERGKPCILVSTQVVEAGVD------ 437

                         330       340
                  ....*....|....*....|...
gi 1958750291 617 vINFDL----PSTIDEYVHRIGR 635
Cdd:COG1203   438 -IDFDVvirdLAPLDSLIQRAGR 459
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 598-638 5.93e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 50.40  E-value: 5.93e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958750291 598 VLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 638
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
PRK13767 PRK13767
ATP-dependent helicase; Provisional
 313-387 2.83e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 54.12  E-value: 2.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958750291 313 YTKLTPVQKYSIPIVLAGRDLMACAQTGSGKT-AAFLLPIlahmmRDGITASRFKELQEP-ECIIVAPTRELINQIY 387
Cdd:PRK13767   30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAII-----DELFRLGREGELEDKvYCLYVSPLRALNNDIH 101
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 315-488 7.05e-07

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 50.11  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 315 KLTPVQKYSIPIVLAG------RDLMACAQTGSGKTAAFLLPILAhmmrdgiTASRFKELqepecIIVAPTRELINQIYL 388
Cdd:cd17918    15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL-------AYKNGKQV-----AILVPTEILAHQHYE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 389 EARK-FSFgtcVRAVVIYGGTQfghsiRQIVQGCNILCATPGRLMDIIGKEKIGLkqvkyLVLDEADRmldmgFGPEMKK 467
Cdd:cd17918    83 EARKfLPF---INVELVTGGTK-----AQILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHR-----FGVAQRE 144

                         170       180
                  ....*....|....*....|.
gi 1958750291 468 LISCPGMPSkeqrqTLLFSAT 488
Cdd:cd17918   145 ALYNLGATH-----FLEATAT 160
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
 312-495 7.46e-07

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: 50.23  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 312 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPTRELIN-QIY-LE 389
Cdd:cd17920     9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL---LLDGVT------------LVVSPLISLMQdQVDrLQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 390 ARkfsfgtCVRAVVIYGGTQFgHSIRQIVQGC-----NILCATPGRLMDIIGKEKIG----LKQVKYLVLDEADRMLDMG 460
Cdd:cd17920    74 QL------GIRAAALNSTLSP-EEKREVLLRIkngqyKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHCVSQWG 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958750291 461 --FGPEMKKLIS----CPGMPskeqrqTLLFSATFPEEIQR 495
Cdd:cd17920   147 hdFRPDYLRLGRlrraLPGVP------ILALTATATPEVRE 181
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 320-453 1.32e-06

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: 49.12  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 320 QKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD-GITAsrfkelqepecIIVAPTRELIN-QI-YLEARKFSFG 396
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDpGSRA-----------LYLYPTKALAQdQLrSLRELLEQLG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958750291 397 TCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDII----GKEKIGLKQVKYLVLDEA 453
Cdd:cd17923    74 LGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
313-369 1.37e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 52.03  E-value: 1.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750291 313 YTKLTPVQKYSIPIVLAGRDLMACAQTGSGKT-AAFlLPILAHMMRDGITASRFKELQ 369
Cdd:COG1201    22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGLR 78
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 545-654 2.54e-06

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 48.40  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 545 DERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFD--- 621
Cdd:cd18790    27 GERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadk 106

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958750291 622 ---LPSTiDEYVHRIGRTGRCGNtGRAISFFDTESD 654
Cdd:cd18790   107 egfLRSE-TSLIQTIGRAARNVN-GKVILYADKITD 140
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 330-452 6.06e-06

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: 47.19  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 330 GRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkelqepeCIIVAPTRELINQIY--LEARKFSFGTCVRAVVIYGG 407
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------VLYISPLKALINDQErrLEEPLDEIDLEIPVAVRHGD 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958750291 408 TQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIG--LKQVKYLVLDE 452
Cdd:cd17922    73 TSQSEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 543-635 6.98e-06

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: 45.63  E-value: 6.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 543 IGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQA---LGDFRCGKCPVLVATSVAARGLDIENVQHVIn 619
Cdd:cd18799     4 YVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV- 82

                          90
                  ....*....|....*...
gi 1958750291 620 FDLP--STIdEYVHRIGR 635
Cdd:cd18799    83 FLRPteSRT-LFLQMLGR 99
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 538-638 9.25e-06

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: 46.10  E-value: 9.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 538 EILRNIGDERTM-VFVETKKKADFIAT---FLCQEKISTTSI---HG--DREQRER-EQAL--GDFRcgkcpVLVATSVA 605
Cdd:cd18796    30 EVIFLLERHKSTlVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAALkrGDLK-----VVVATSSL 104

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958750291 606 ARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 638
Cdd:cd18796   105 ELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
ResIII pfam04851
Type III restriction enzyme, res subunit;
315-491 1.53e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 45.74  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 315 KLTPVQKYSIPIVLAGRDL--------MAcaqTGSGKT--AAFllpilahmmrdgITASRFKELQEPECIIVAPTRELIN 384
Cdd:pfam04851   3 ELRPYQIEAIENLLESIKNgqkrglivMA---TGSGKTltAAK------------LIARLFKKGPIKKVLFLVPRKDLLE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 385 QIYLEARKFsFGTCVRAVVIYGGTqfghSIRQIVQGCNILCATPGRLMDII--GKEKIGLKQVKYLVLDEADRmldmGFG 462
Cdd:pfam04851  68 QALEEFKKF-LPNYVEIGEIISGD----KKDESVDDNKIVVTTIQSLYKALelASLELLPDFFDVIIIDEAHR----SGA 138

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958750291 463 PEMKKLIscpgmpSKEQRQTLL-FSATFPE 491
Cdd:pfam04851 139 SSYRNIL------EYFKPAFLLgLTATPER 162
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 525-649 2.49e-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: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 525 LQVGQYSKREKLVEILRNIGD-ERTMVFVETKKKADFIAtflcqEKISTTSIHGDREQREREQALGDFRCGKCPVLVATS 603
Cdd:cd18789    28 LAAMNPNKLRALEELLKRHEQgDKIIVFTDNVEALYRYA-----KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSK 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958750291 604 VAARGLDI--ENVQHVINFDLPSTiDEYVHRIGRTGRCGNTGRAISFF 649
Cdd:cd18789   103 VGDEGIDLpeANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 331-453 1.20e-04

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 43.79  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 331 RDLMACAQTGSGKT--AAFLLPILAHmmrdgitasRFKELQEPECIIV--APTRELINQiylEARKFSFGTCVRAVVIYG 406
Cdd:cd18034    17 RNTIVVLPTGSGKTliAVMLIKEMGE---------LNRKEKNPKKRAVflVPTVPLVAQ---QAEAIRSHTDLKVGEYSG 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958750291 407 GTQFGHSIRQIVQGC----NILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 453
Cdd:cd18034    85 EMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 331-428 1.66e-04

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: 43.50  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 331 RDLMACAQTGSGKTAAFLLPILaHMMRDGITASRFKelqePECIIVAPTRELINQIYLEAR-KFS-FGTCVraVVIYGGT 408
Cdd:cd18023    18 KNFVVSAPTGSGKTVLFELAIL-RLLKERNPLPWGN----RKVVYIAPIKALCSEKYDDWKeKFGpLGLSC--AELTGDT 90

                          90       100
                  ....*....|....*....|
gi 1958750291 409 QFGhSIRQIvQGCNILCATP 428
Cdd:cd18023    91 EMD-DTFEI-QDADIILTTP 108
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
 312-452 1.93e-04

N-terminal DEXH-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: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 43.51  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 312 GYTKLTPVQKYSIPIVLAGRD-LMACAQTGSGKTAAFLLPIL----AHMMRDG-ITASRFKelqepeCIIVAPTRELINQ 385
Cdd:cd18019    14 GFKSLNRIQSKLFPAAFETDEnLLLCAPTGAGKTNVALLTILreigKHRNPDGtINLDAFK------IVYIAPMKALVQE 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750291 386 IY--LEARKFSFGTCVRAVViyGGTQFghSIRQIVQgCNILCATPGRlMDII---GKEKIGLKQVKYLVLDE 452
Cdd:cd18019    88 MVgnFSKRLAPYGITVAELT--GDQQL--TKEQISE-TQIIVTTPEK-WDIItrkSGDRTYTQLVRLIIIDE 153
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 575-635 5.87e-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: 41.18  E-value: 5.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958750291 575 IHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIEN-----VQHVINFDLpSTIDEYVHRIGR 635
Cdd:cd18811    67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGL-SQLHQLRGRVGR 131
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 339-453 7.79e-04

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 40.37  E-value: 7.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 339 TGSGKTA-AFLLPIlahmmrdgitasrfkELQEPECIIVAPTRELINQIYLEARKFSFGtcvraVVIYggtQFGHSIRQI 417
Cdd:cd17926    27 TGSGKTLtALALIA---------------YLKELRTLIVVPTDALLDQWKERFEDFLGD-----SSIG---LIGGGKKKD 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958750291 418 VQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 453
Cdd:cd17926    84 FDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
 330-393 1.14e-03

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


Pssm-ID: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 40.74  E-value: 1.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958750291 330 GRDLMACAQTGSGKTAAFLLPILAHMMRDGItasrfkelqePECIIVAPTRELINQIYLEARKF 393
Cdd:cd17930     1 PGLVILEAPTGSGKTEAALLWALKLAARGGK----------RRIIYALPTRATINQMYERIREI 54
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 334-455 1.35e-03

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 40.58  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 334 MACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqePECIIVAPTRELINQIYLEARKFsFGTCVRAVVIYGGTQfGHS 413
Cdd:cd18035    20 LIVLPTGLGKTIIAILVAADRLTKKG-----------GKVLILAPSRPLVEQHAENLKRV-LNIPDKITSLTGEVK-PEE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958750291 414 IRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADR 455
Cdd:cd18035    87 RAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
 547-641 1.97e-03

C-terminal helicase domain of HrQ family helicases; 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. HrQ 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: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 39.16  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 547 RTMVFVETKKKADFIATFLCQEKIST----TSIHGDR------EQREREQalgDFRCGKCPVLVATSVAARGLDIENVQH 616
Cdd:cd18797    37 KTIVFCRSRKLAELLLRYLKARLVEEgplaSKVASYRagylaeDRREIEA---ELFNGELLGVVATNALELGIDIGGLDA 113

                          90       100
                  ....*....|....*....|....*
gi 1958750291 617 VINFDLPSTIDEYVHRIGRTGRCGN 641
Cdd:cd18797   114 VVLAGYPGSLASLWQQAGRAGRRGK 138
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 575-614 2.33e-03

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 39.17  E-value: 2.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958750291 575 IHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENV 614
Cdd:cd18792    66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA 105
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
 574-637 2.49e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.45  E-value: 2.49e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750291  574 SIHGD--REQR-EREQAL--GDFRCgkcpvLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTG 637
Cdd:PRK09751   306 SHHGSvsKEQRaITEQALksGELRC-----VVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
 336-470 2.70e-03

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: 39.55  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 336 CAQTGSGKTAAFLLPILAHmmrdgitasrFKELQEPECIIVAPTRELINQIYLE-ARKFSFGTCVRAVVIYGGTQfghSI 414
Cdd:cd18021    25 GAPTGSGKTVCAELALLRH----------WRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLGKKVVKLTGETS---TD 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750291 415 RQIVQGCNILCATPGRLmDIIG---KEKIGLKQVKYLVLDEAdRMLDMGFGPEMKKLIS 470
Cdd:cd18021    92 LKLLAKSDVILATPEQW-DVLSrrwKQRKNVQSVELFIADEL-HLIGGENGPVYEVVVS 148
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
 332-504 3.64e-03

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


Pssm-ID: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 39.34  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 332 DLMACAQTGSGKTAAFLLPILaHMMRDGITASRFKELQEPECIIVAPTRELINQI--YLEARKFSFGTCVRAVViyGGTQ 409
Cdd:cd18020    19 NMLICAPTGAGKTNIAMLTIL-HEIRQHVNQGGVIKKDDFKIVYIAPMKALAAEMveKFSKRLAPLGIKVKELT--GDMQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 410 FGhsiRQIVQGCNILCATPGRlMDIIGKEKIG----LKQVKYLVLDEAdRMLDMGFGPEMKKLIScPGMPSKEQRQTLL- 484
Cdd:cd18020    96 LT---KKEIAETQIIVTTPEK-WDVVTRKSSGdvalSQLVRLLIIDEV-HLLHDDRGPVIESLVA-RTLRQVESTQSMIr 169

                         170       180
                  ....*....|....*....|...
gi 1958750291 485 ---FSATFPEEIQrlAGEFLKSN 504
Cdd:cd18020   170 ivgLSATLPNYLD--VADFLRVN 190
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
 312-453 5.82e-03

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 38.78  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 312 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLP--ILAHmMRDGITasrfkelqepecIIVAPTREL-INQI-Y 387
Cdd:cd18018     9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPalLLRR-RGPGLT------------LVVSPLIALmKDQVdA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958750291 388 LEARkfsfgtcVRAVVIYGG---TQFGHSIRQIVQG-CNILCATPGRLMDIIGKEKI-GLKQVKYLVLDEA 453
Cdd:cd18018    76 LPRA-------IKAAALNSSltrEERRRILEKLRAGeVKILYVSPERLVNESFRELLrQTPPISLLVVDEA 139
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
 321-455 7.57e-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: 38.57  E-value: 7.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750291 321 KYSIPIVLA---GRDLMACAQTGSGKTAafllpILAHMMRDGITasRFKELQEPECIIVAPTRELINQiylEARKFS--F 395
Cdd:cd17927     5 NYQLELAQPalkGKNTIICLPTGSGKTF-----VAVLICEHHLK--KFPAGRKGKVVFLANKVPLVEQ---QKEVFRkhF 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750291 396 GTCVRAVV-IYGGTQFGHSIRQIVQGCNILCATPGRLM-DIIGKEKIGLKQVKYLVLDEADR 455
Cdd:cd17927    75 ERPGYKVTgLSGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
 
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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