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Conserved domains on  [gi|225007636|ref|NP_001139357|]
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ATP-dependent RNA helicase DDX4 isoform 1 [Mus musculus]

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 ...
 256-508 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: 540.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 256 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 335
Cdd:cd18052   12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 336 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC 415
Cdd:cd18052   92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 416 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFL 495
Cdd:cd18052  172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                        250
                 ....*....|...
gi 225007636 496 KSSYLFVAVGQVG 508
Cdd:cd18052  252 KEDYLFLTVGRVG 264
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 514-643 1.95e-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: 1.95e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 514 VQQTILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 592
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225007636 593 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 643
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 ...
 256-508 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: 540.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 256 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 335
Cdd:cd18052   12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 336 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC 415
Cdd:cd18052   92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 416 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFL 495
Cdd:cd18052  172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                        250
                 ....*....|...
gi 225007636 496 KSSYLFVAVGQVG 508
Cdd:cd18052  252 KEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
288-653 3.88e-154

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 453.83  E-value: 3.88e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 288 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqePEC 367
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------PQA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 368 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 447
Cdd:COG0513   75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 448 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGDFLKSsYLFVAVGQVGGACRDVQQTILQVGQYSK 526
Cdd:COG0513  155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPENATAETIEQRYYLVDKRDK 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 527 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 606
Cdd:COG0513  229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 225007636 607 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSDNHLAQ 653
Cdd:COG0513  309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRA 355
PTZ00110 PTZ00110
helicase; Provisional
 277-682 2.37e-117

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 363.71  E-value: 2.37e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 277 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITA 356
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INA 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 357 S-RFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIG 435
Cdd:PTZ00110 195 QpLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 436 LKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFVAVGQVG-GACRDV 514
Cdd:PTZ00110 275 LRRVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNI 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 515 QQTILQVGQYSKREKLVEILRNIGDE--RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 592
Cdd:PTZ00110 351 KQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPI 430

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 593 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSdNHLAQPLVKVLSDAQQDVPAWLEE 672
Cdd:PTZ00110 431 MIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK-YRLARDLVKVLREAKQPVPPELEK 509

                        410
                 ....*....|
gi 225007636 673 IAFSTYVPPS 682
Cdd:PTZ00110 510 LSNERSNGTE 519
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 311-490 1.97e-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: 200.55  E-value: 1.97e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636  311 TPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELINQIYLEARKFSFG 390
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD---------KLDNGPQALVLAPTRELAEQIYEELKKLGKG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636  391 TCVRAVVIYGGTQFgHSVRQIVQGCNILCATPGRLMDIIGKEKiGLKQVKYLVLDEADRMLDMGFGPEMKKLISCpgMPs 470
Cdd:pfam00270  72 LGLKVASLLGGDSR-KEQLEKLKGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146

                         170       180
                  ....*....|....*....|
gi 225007636  471 kEQRQTLLFSATFPEEIQRL 490
Cdd:pfam00270 147 -KKRQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 514-643 1.95e-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: 1.95e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 514 VQQTILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 592
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225007636 593 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 643
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
302-502 2.62e-50

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 174.60  E-value: 2.62e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636   302 IAKAGYTKLTPVQKYSIPIVLAG-RDLMACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqEPECIIVAPTRELINQI 380
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK----------GGRVLVLVPTRELAEQW 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636   381 YLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEM 459
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 225007636   460 KKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFV 502
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLNDPVFID 189
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 525-634 2.58e-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: 137.73  E-value: 2.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636  525 SKREKLVEILRNIGDERTMVFVETKKKADfIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLD 604
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 225007636  605 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 634
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
553-634 2.42e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.45  E-value: 2.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636   553 DFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 632
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 225007636   633 CG 634
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
522-640 7.22e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 94.41  E-value: 7.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 522 GQYSKREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKISTTSIHG--DRE------QREREQALGDFRCGK 589
Cdd:COG1111  332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 225007636 590 CPVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNTGRAI 640
Cdd:COG1111  412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
PRK13766 PRK13766
Hef nuclease; Provisional
 526-640 6.57e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.76  E-value: 6.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 526 KREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKIST------TSIHGDREQREREQ--ALGDFRCGKCPVL 593
Cdd:PRK13766 348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGMSQKEQieILDKFRAGEFNVL 427

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 225007636 594 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 640
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 ...
 256-508 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: 540.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 256 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 335
Cdd:cd18052   12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 336 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC 415
Cdd:cd18052   92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 416 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFL 495
Cdd:cd18052  172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                        250
                 ....*....|...
gi 225007636 496 KSSYLFVAVGQVG 508
Cdd:cd18052  252 KEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
288-653 3.88e-154

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 453.83  E-value: 3.88e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 288 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqePEC 367
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------PQA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 368 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 447
Cdd:COG0513   75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 448 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGDFLKSsYLFVAVGQVGGACRDVQQTILQVGQYSK 526
Cdd:COG0513  155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPENATAETIEQRYYLVDKRDK 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 527 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 606
Cdd:COG0513  229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 225007636 607 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSDNHLAQ 653
Cdd:COG0513  309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRA 355
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 288-508 1.13e-144

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: 421.51  E-value: 1.13e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 288 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAS-RFKELQEPE 366
Cdd:cd17967    1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgRGRRKAYPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 367 CIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 446
Cdd:cd17967   81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225007636 447 ADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFLKsSYLFVAVGQVG 508
Cdd:cd17967  161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
PTZ00110 PTZ00110
helicase; Provisional
 277-682 2.37e-117

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 363.71  E-value: 2.37e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 277 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITA 356
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INA 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 357 S-RFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIG 435
Cdd:PTZ00110 195 QpLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 436 LKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFVAVGQVG-GACRDV 514
Cdd:PTZ00110 275 LRRVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNI 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 515 QQTILQVGQYSKREKLVEILRNIGDE--RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 592
Cdd:PTZ00110 351 KQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPI 430

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 593 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSdNHLAQPLVKVLSDAQQDVPAWLEE 672
Cdd:PTZ00110 431 MIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK-YRLARDLVKVLREAKQPVPPELEK 509

                        410
                 ....*....|
gi 225007636 673 IAFSTYVPPS 682
Cdd:PTZ00110 510 LSNERSNGTE 519
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 267-508 1.57e-112

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: 340.09  E-value: 1.57e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 267 FDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL 346
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 347 AHMMRDG-----ITASRF--KELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILC 419
Cdd:cd18051   81 SQIYEQGpgeslPSESGYygRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 420 ATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFLkSSY 499
Cdd:cd18051  161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFL-DNY 239


                 ....*....
gi 225007636 500 LFVAVGQVG 508
Cdd:cd18051  240 IFLAVGRVG 248
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 289-681 4.58e-102

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 320.98  E-value: 4.58e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 289 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITASRFKelqePECI 368
Cdd:PRK11776   6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK-----LDVKRFR----VQAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 369 IVAPTRELINQIYLEARKFSFGT-CVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 447
Cdd:PRK11776  77 VLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 448 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGDFLKSSyLFVAVGQVGGAcRDVQQTILQVGQYSK 526
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRqAP-----ARRQTLLFSATYPEGIAAISQRFQRDP-VEVKVESTHDL-PAIEQRFYEVSPDER 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 527 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 606
Cdd:PRK11776 230 LPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225007636 607 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFdTDSDNHLAQplvkVLSDAQQDVPAW--LEEIAFSTYVPP 681
Cdd:PRK11776 310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLV-APEEMQRAN----AIEDYLGRKLNWepLPSLSPLSGVPL 381
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 288-642 2.23e-90

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 289.54  E-value: 2.23e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 288 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMmrdgITASRFKELQePEC 367
Cdd:PRK11192   2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL----LDFPRRKSGP-PRI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 368 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 447
Cdd:PRK11192  77 LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 448 DRMLDMGFGPEMKKLiscpgmpSKEQR---QTLLFSATFP-EEIQRLAGDFLKSSYLFVAvgqvgGACRDVQQTILQvgQ 523
Cdd:PRK11192 157 DRMLDMGFAQDIETI-------AAETRwrkQTLLFSATLEgDAVQDFAERLLNDPVEVEA-----EPSRRERKKIHQ--W 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 524 Y-------SKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVAT 596
Cdd:PRK11192 223 YyraddleHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVAT 302

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 225007636 597 SVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 642
Cdd:PRK11192 303 DVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 272-679 3.62e-87

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 283.60  E-value: 3.62e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 272 TILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAH--- 348
Cdd:PLN00206 106 KLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcct 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 349 MMRDGITASRfkelqEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDI 428
Cdd:PLN00206 186 IRSGHPSEQR-----NPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDL 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 429 IGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPskeqrQTLLFSATFPEEIQRLAGDFLKSsYLFVAVGQVG 508
Cdd:PLN00206 261 LSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKD-IILISIGNPN 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 509 GACRDVQQTILQVGQYSKREKLVEILRNIGDER--TMVFVETKKKADFIAtflcqEKISTT------SIHGDREQREREQ 580
Cdd:PLN00206 335 RPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLA-----NAITVVtglkalSIHGEKSMKERRE 409

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 581 ALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSDNhLAQPLVKVLS 660
Cdd:PLN00206 410 VMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRN-LFPELVALLK 488

                        410
                 ....*....|....*....
gi 225007636 661 DAQQDVPawlEEIAFSTYV 679
Cdd:PLN00206 489 SSGAAIP---RELANSRYL 504
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 302-641 5.43e-87

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 281.31  E-value: 5.43e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfKELQEPECIIVAPTRELINQIY 381
Cdd:PRK10590  16 VAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHA---KGRRPVRALILTPTRELAAQIG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 382 LEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 461
Cdd:PRK10590  93 ENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRR 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 462 LIScpGMPSKeqRQTLLFSATFPEEIQRLAGDFLKSSyLFVAVGQVGGACRDVQQTILQVGQYSKREKLVEILRNIGDER 541
Cdd:PRK10590 173 VLA--KLPAK--RQNLLFSATFSDDIKALAEKLLHNP-LEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGKGNWQQ 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 542 TMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTID 621
Cdd:PRK10590 248 VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPE 327

                        330       340
                 ....*....|....*....|
gi 225007636 622 EYVHRIGRTGRCGNTGRAIS 641
Cdd:PRK10590 328 DYVHRIGRTGRAAATGEALS 347
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 289-646 2.16e-86

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 280.26  E-value: 2.16e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 289 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFkeLQEPECI 368
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERY--MGEPRAL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 369 IVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQI-VQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 447
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 448 DRMLDMGFGPEMKKLIScpGMPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLfVAVGQVGGACRDVQQTILQVGQYSKR 527
Cdd:PRK01297 247 DRMLDMGFIPQVRQIIR--QTPRKEERQTLLFSATFTDDVMNLAKQWTTDPAI-VEIEPENVASDTVEQHVYAVAGSDKY 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 528 EKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIEN 607
Cdd:PRK01297 324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 225007636 608 VQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTD 646
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGED 442
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 298-496 1.37e-83

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: 263.15  E-value: 1.37e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 298 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkelqEPECIIVAPTRELI 377
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGR-----GPQALVLAPTRELA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 378 NQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGP 457
Cdd:cd00268   76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEE 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 225007636 458 EMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGDFLK 496
Cdd:cd00268  156 DVEKILSaLP-----KDRQTLLFSATLPEEVKELAKKFLK 190
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 281-642 7.15e-78

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 260.65  E-value: 7.15e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 281 DAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFK 360
Cdd:PRK04537   3 DKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 361 ElqEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKI-GLKQV 439
Cdd:PRK04537  83 E--DPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHAC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 440 KYLVLDEADRMLDMGFGPEMKKLIScpGMPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFVAVGQVGGACRdVQQTIL 519
Cdd:PRK04537 161 EICVLDEADRMFDLGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR-VRQRIY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 520 QVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVA 599
Cdd:PRK04537 238 FPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVA 317

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 225007636 600 ARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 642
Cdd:PRK04537 318 ARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 302-642 2.58e-72

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 241.41  E-value: 2.58e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkELQEPECIIVAPTRELINQIY 381
Cdd:PRK04837  23 LEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDR--KVNQPRALIMAPTRELAVQIH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 382 LEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 461
Cdd:PRK04837 101 ADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRW 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 462 LIScpGMPSKEQRQTLLFSATFPEEIQRLAGDFLKS-SYLFVAVGQVGGacRDVQQTILqvgqY-SKREKLVEILRNIGD 539
Cdd:PRK04837 181 LFR--RMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVEPEQKTG--HRIKEELF----YpSNEEKMRLLQTLIEE 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 540 E---RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDL 616
Cdd:PRK04837 253 EwpdRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDL 332

                        330       340
                 ....*....|....*....|....*.
gi 225007636 617 PSTIDEYVHRIGRTGRCGNTGRAISF 642
Cdd:PRK04837 333 PDDCEDYVHRIGRTGRAGASGHSISL 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 288-644 5.78e-69

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 238.21  E-value: 5.78e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 288 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPEC 367
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD---------PELKAPQI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 368 IIVAPTRELINQIYLEARKFS-FGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 446
Cdd:PRK11634  78 LVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 447 ADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPEEIQRLAGDFLKSSYLfVAVgQVGGACR-DVQQTILQVGQYS 525
Cdd:PRK11634 158 ADEMLRMGFIEDVETIMA--QIP--EGHQTALFSATMPEAIRRITRRFMKEPQE-VRI-QSSVTTRpDISQSYWTVWGMR 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 526 KREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDI 605
Cdd:PRK11634 232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 225007636 606 ENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 644
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 ...
 302-496 1.14e-66

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: 218.39  E-value: 1.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITASRFKELQE-PECIIVAPTRELINQI 380
Cdd:cd17966    5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVH-----INAQPPLERGDgPIVLVLAPTRELAQQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 381 YLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMK 460
Cdd:cd17966   80 QQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 225007636 461 KLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLK 496
Cdd:cd17966  160 KIVD----QIRPDRQTLMWSATWPKEVRRLAEDFLK 191
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 298-495 1.15e-61

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: 204.96  E-value: 1.15e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 298 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitASRFKELQE-PECIIVAPTREL 376
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-----DQRELEKGEgPIAVIVAPTREL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 377 INQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 456
Cdd:cd17952   76 AQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFE 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 225007636 457 PEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFL 495
Cdd:cd17952  156 YQVRSIVG----HVRPDRQTLLFSATFKKKIEQLARDIL 190
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 311-490 1.97e-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: 200.55  E-value: 1.97e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636  311 TPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELINQIYLEARKFSFG 390
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD---------KLDNGPQALVLAPTRELAEQIYEELKKLGKG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636  391 TCVRAVVIYGGTQFgHSVRQIVQGCNILCATPGRLMDIIGKEKiGLKQVKYLVLDEADRMLDMGFGPEMKKLISCpgMPs 470
Cdd:pfam00270  72 LGLKVASLLGGDSR-KEQLEKLKGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146

                         170       180
                  ....*....|....*....|
gi 225007636  471 kEQRQTLLFSATFPEEIQRL 490
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) ...
 277-497 1.49e-59

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: 200.30  E-value: 1.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 277 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITA 356
Cdd:cd17953    2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRH-----IKD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 357 SRF-KELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDII---GKE 432
Cdd:cd17953   77 QRPvKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGR 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225007636 433 KIGLKQVKYLVLDEADRMLDMGFGPEMKKLIscpgMPSKEQRQTLLFSATFPEEIQRLAGDFLKS 497
Cdd:cd17953  157 VTNLRRVTYVVLDEADRMFDMGFEPQIMKIV----NNIRPDRQTVLFSATFPRKVEALARKVLHK 217
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 302-502 5.58e-59

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: 198.19  E-value: 5.58e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLA-GRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKelqePECIIVAPTRELINQI 380
Cdd:cd17964    9 LTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSG----VSALIISPTRELALQI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 381 YLEARKF-SFGTCVRAVVIYGGTQFGHSVRQIV-QGCNILCATPGRLMDIIGKEKIG--LKQVKYLVLDEADRMLDMGFG 456
Cdd:cd17964   85 AAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLDMGFR 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 225007636 457 PEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFV 502
Cdd:cd17964  165 PDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 302-497 2.93e-58

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: 196.77  E-value: 2.93e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfKELQEPECIIVAPTRELINQIY 381
Cdd:cd17945    5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEE-TKDDGPYALILAPTRELAQQIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 382 LEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 461
Cdd:cd17945   84 EETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTK 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 225007636 462 LIScpGMPS------------------KEQRQTLLFSATFPEEIQRLAGDFLKS 497
Cdd:cd17945  164 ILD--AMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRR 215
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 514-643 1.95e-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: 1.95e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 514 VQQTILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 592
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225007636 593 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 643
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 275-505 3.40e-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: 194.46  E-value: 3.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 275 VEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgI 354
Cdd:cd18049   12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH-----I 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 355 TASRFKELQE-PECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEK 433
Cdd:cd18049   87 NHQPFLERGDgPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225007636 434 IGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKsSYLFVAVG 505
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 ...
 298-491 5.29e-56

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 189.72  E-value: 5.29e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 298 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqEPECIIVAPTRELI 377
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-------GLRALILAPTRELA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 378 NQIYLEARKFSFGTCVRAVVIYGGTQFG-HSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 456
Cdd:cd17957   74 SQIYRELLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFR 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 225007636 457 PEMKKLI-SCpgmpSKEQRQTLLFSATFPEEIQRLA 491
Cdd:cd17957  154 EQTDEILaAC----TNPNLQRSLFSATIPSEVEELA 185
PTZ00424 PTZ00424
helicase 45; Provisional
 288-651 6.74e-54

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 190.81  E-value: 6.74e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 288 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitasrfkeLQEPEC 367
Cdd:PTZ00424  29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD---------LNACQA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 368 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 447
Cdd:PTZ00424 100 LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 448 DRMLDMGFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLAGDFLKSSYLfVAVGQVGGACRDVQQTILQVGQYS-K 526
Cdd:PTZ00424 180 DEMLSRGFKGQIYDVFK--KLPP--DVQVALFSATMPNEILELTTKFMRDPKR-ILVKKDELTLEGIRQFYVAVEKEEwK 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 527 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 606
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 225007636 607 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSDNHL 651
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQL 379
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 275-505 3.61e-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: 179.44  E-value: 3.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 275 VEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgI 354
Cdd:cd18050   50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVH-----I 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 355 TASRFKELQE-PECIIVAPTRELINQIYLEArkFSFGTCVR--AVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGK 431
Cdd:cd18050  125 NHQPYLERGDgPICLVLAPTRELAQQVQQVA--DDYGKSSRlkSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEA 202

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225007636 432 EKIGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKsSYLFVAVG 505
Cdd:cd18050  203 GKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLR-DYVQINIG 271
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 289-502 8.22e-51

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: 175.88  E-value: 8.22e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 289 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD--GITAsrfkelqepe 366
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDpyGIFA---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 367 cIIVAPTRELINQIyleARKF-SFGTC--VRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDII---GKEKIGLKQVK 440
Cdd:cd17955   71 -LVLTPTRELAYQI---AEQFrALGAPlgLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTKVLSRVK 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225007636 441 YLVLDEADRMLDMGFGPEMKKLISCpgMPSKeqRQTLLFSATFPEEIQRLAGDFLKSSYLFV 502
Cdd:cd17955  147 FLVLDEADRLLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 302-491 2.62e-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: 174.37  E-value: 2.62e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRdgitasRFKELQEPECIIVAPTRELINQIY 381
Cdd:cd17947    5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY------RPKKKAATRVLVLVPTRELAMQCF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 382 LEARKFS-FGTCVRAVVIyGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVLDEADRMLDMGFGPEM 459
Cdd:cd17947   79 SVLQQLAqFTDITFALAV-GGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADEL 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 225007636 460 KKLI-SCPgmpskEQRQTLLFSATFPEEIQRLA 491
Cdd:cd17947  158 KEILrLCP-----RTRQTMLFSATMTDEVKDLA 185
DEXDc smart00487
DEAD-like helicases superfamily;
302-502 2.62e-50

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 174.60  E-value: 2.62e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636   302 IAKAGYTKLTPVQKYSIPIVLAG-RDLMACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqEPECIIVAPTRELINQI 380
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK----------GGRVLVLVPTRELAEQW 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636   381 YLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEM 459
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 225007636   460 KKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFV 502
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLNDPVFID 189
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 288-490 2.70e-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: 174.43  E-value: 2.70e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 288 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitASRFkelqepEC 367
Cdd:cd17954    1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---PQRF------FA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 368 IIVAPTRELINQI--YLEARKFSFGtcVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVL 444
Cdd:cd17954   72 LVLAPTRELAQQIseQFEALGSSIG--LKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVM 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 225007636 445 DEADRMLDMGFGPEMKKLISCpgMPSkeQRQTLLFSATFPEEIQRL 490
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, ...
 302-491 3.58e-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: 173.92  E-value: 3.58e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhMMRDGITASRFKELQepeCIIVAPTRELINQIY 381
Cdd:cd17960    5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLE-ILLKRKANLKKGQVG---ALIISPTRELATQIY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 382 LEARKF--SFGTCVRAVVIYGGTQFGHSVRQIV-QGCNILCATPGRLMDIIG--KEKIGLKQVKYLVLDEADRMLDMGFG 456
Cdd:cd17960   81 EVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLGFE 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 225007636 457 PEMKKLISCpgMPskEQRQTLLFSATFPEEIQRLA 491
Cdd:cd17960  161 ADLNRILSK--LP--KQRRTGLFSATQTDAVEELI 191
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 301-496 8.37e-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: 173.03  E-value: 8.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 301 NIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMmrDGITASRFKElQEPECIIVAPTRELINQI 380
Cdd:cd17958    4 EIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL--DLQPIPREQR-NGPGVLVLTPTRELALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 381 YLEARKFSFGTcVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMK 460
Cdd:cd17958   81 EAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 225007636 461 KLIscpgMPSKEQRQTLLFSATFPEEIQRLAGDFLK 496
Cdd:cd17958  160 KIL----LDIRPDRQTIMTSATWPDGVRRLAQSYLK 191
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 288-485 3.74e-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: 171.33  E-value: 3.74e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 288 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL----AHMMRDGITAsrfkelq 363
Cdd:cd17959    2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIeklkAHSPTVGARA------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 364 epecIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLV 443
Cdd:cd17959   75 ----LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVV 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 225007636 444 LDEADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPE 485
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) ...
 294-492 5.97e-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: 5.97e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 294 LCQTLNNNIakaGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitASRFKELQEPECIIVAPT 373
Cdd:cd17949    1 LVSHLKSKM---GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSL---EPRVDRSDGTLALVLVPT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 374 RELINQIYLEARKF--SFGTCVRAVVIyGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVLDEADRM 450
Cdd:cd17949   75 RELALQIYEVLEKLlkPFHWIVPGYLI-GGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225007636 451 LDMGFGPEMKKLIS---------CPGMPSKEQRQTLLFSATFPEEIQRLAG 492
Cdd:cd17949  154 LDMGFEKDITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLAG 204
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 302-491 4.93e-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: 162.46  E-value: 4.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitasRFKELQEPECIIVAPTRELINQIY 381
Cdd:cd17941    5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE-----RWTPEDGLGALIISPTRELAMQIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 382 LEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQgCNILCATPGRL---MDiigkEKIGL--KQVKYLVLDEADRMLDMGFG 456
Cdd:cd17941   80 EVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLlqhMD----ETPGFdtSNLQMLVLDEADRILDMGFK 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 225007636 457 PEMKKLIScpGMPSKeqRQTLLFSATFPEEIQRLA 491
Cdd:cd17941  155 ETLDAIVE--NLPKS--RQTLLFSATQTKSVKDLA 185
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 289-499 8.26e-46

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 162.08  E-value: 8.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 289 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL--AHMMRDGITAsrfkelqepe 366
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILekIDPKKDVIQA---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 367 cIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 446
Cdd:cd17940   71 -LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 225007636 447 ADRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGDFLKSSY 499
Cdd:cd17940  150 ADKLLSQDFQPIIEKILNfLP-----KERQILLFSATFPLTVKNFMDRHMHNPY 198
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 302-502 8.48e-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: 8.48e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmmrDGITASRFKELQEPECIIVAPTRELINQIY 381
Cdd:cd17942    5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-----ELLYKLKFKPRNGTGVIIISPTRELALQIY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 382 LEARKF------SFGTCVravviyGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGL-KQVKYLVLDEADRMLDMG 454
Cdd:cd17942   80 GVAKELlkyhsqTFGIVI------GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILEIG 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 225007636 455 FGPEMKKLISCpgMPSkeQRQTLLFSATFPEEIQRLAGDFLKSSYLFV 502
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 ...
 302-498 1.73e-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: 158.66  E-value: 1.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASrFKELQEPECIIVAPTRELINQIY 381
Cdd:cd17951    5 LKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLP-FIKGEGPYGLIVCPSRELARQTH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 382 ---------LEARKFSfgtCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLD 452
Cdd:cd17951   84 evieyyckaLQEGGYP---QLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 225007636 453 MGFGPEMKKLISCpgmpSKEQRQTLLFSATFPEEIQrlagDFLKSS 498
Cdd:cd17951  161 MGFEEDIRTIFSY----FKGQRQTLLFSATMPKKIQ----NFAKSA 198
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 298-496 4.14e-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: 154.24  E-value: 4.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 298 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELI 377
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL---------TEHRNPSALILTPTRELA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 378 NQIYLEARKFSFGTC-VRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 456
Cdd:cd17962   72 VQIEDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQ 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 225007636 457 PEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLK 496
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 ...
 289-491 8.60e-41

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: 148.24  E-value: 8.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 289 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmmrdgitasrfkelQEPECI 368
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------QIVVAL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 369 IVAPTRELINQIYLEARKFSF---GTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLD 445
Cdd:cd17938   65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 225007636 446 EADRMLDMGFGPEMKKLIS-CPGMPSKEQR-QTLLFSATF-PEEIQRLA 491
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 ...
 302-483 3.91e-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: 3.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIP-IVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQI 380
Cdd:cd17946    5 LADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTRELAVQV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 381 --YLEA-RKFsfgTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGK--EKIG-LKQVKYLVLDEADRMLDMG 454
Cdd:cd17946   85 kdHLKAiAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEgnEHLAnLKSLRFLVLDEADRMLEKG 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 225007636 455 FGPEMKKLISC---PGMPSKEQRQTLLFSATF 483
Cdd:cd17946  162 HFAELEKILELlnkDRAGKKRKRQTFVFSATL 193
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 525-634 2.58e-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: 137.73  E-value: 2.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636  525 SKREKLVEILRNIGDERTMVFVETKKKADfIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLD 604
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 225007636  605 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 634
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 ...
 306-499 1.09e-36

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


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 136.52  E-value: 1.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 306 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKElqePECIIVAPTRELINQIYLE-- 383
Cdd:cd17944    9 GVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRA---PKVLVLAPTRELANQVTKDfk 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 384 --ARKFSFgTCvravvIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 461
Cdd:cd17944   86 diTRKLSV-AC-----FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 225007636 462 LISCPGMPSKEQR-QTLLFSATFPEEIQRLAGDFLKSSY 499
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 ...
 302-497 4.75e-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: 135.02  E-value: 4.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgiTASRFKElQEPECIIVAPTRELINQIY 381
Cdd:cd17961    9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKA--KAESGEE-QGTRALILVPTRELAQQVS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 382 LEARKFSFGTC--VRAVVIyggTQFGHSVRQIVQ---GCNILCATPGRLMDII-GKEKIGLKQVKYLVLDEADRMLDMGF 455
Cdd:cd17961   86 KVLEQLTAYCRkdVRVVNL---SASSSDSVQRALlaeKPDIVVSTPARLLSHLeSGSLLLLSTLKYLVIDEADLVLSYGY 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 225007636 456 GPEMKKLIS-CPGMPskeqrQTLLFSATFPEEIQRLAGDFLKS 497
Cdd:cd17961  163 EEDLKSLLSyLPKNY-----QTFLMSATLSEDVEALKKLVLHN 200
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 294-490 3.95e-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: 133.14  E-value: 3.95e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 294 LCQTLNNNiakaGYTKLTPVQKYSIPIVLAG---------RDLMACAQTGSGKTAAFLLPILAhmmrdgITASRFK-ELQ 363
Cdd:cd17956    1 LLKNLQNN----GITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQ------ALSKRVVpRLR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 364 epeCIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC--------NILCATPGRLMD-IIGKEKI 434
Cdd:cd17956   71 ---ALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDhLNSTPGF 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225007636 435 GLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQR----------------QTLLFSATF---PEEIQRL 490
Cdd:cd17956  148 TLKHLRFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLgsfgdanllersvrplQKLLFSATLtrdPEKLSSL 222
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 298-491 5.93e-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: 128.46  E-value: 5.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 298 LNNNIAKA----GYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILahmmrdgitaSRFKE-LQEPECIIV 370
Cdd:cd17963    1 LKPELLKGlyamGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAML----------SRVDPtLKSPQALCL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 371 APTRELINQIYLEARKFSFGT------CVRAVVIYGGTQFGHsvrQIVQGcnilcaTPGRLMDIIGKEKIGLKQVKYLVL 444
Cdd:cd17963   71 APTRELARQIGEVVEKMGKFTgvkvalAVPGNDVPRGKKITA---QIVIG------TPGTVLDWLKKRQLDLKKIKILVL 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225007636 445 DEADRMLDM-GFGPE---MKKLI--SCpgmpskeqrQTLLFSATFPEEIQRLA 491
Cdd:cd17963  142 DEADVMLDTqGHGDQsirIKRMLprNC---------QILLFSATFPDSVRKFA 185
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 301-493 5.55e-31

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 121.32  E-value: 5.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 301 NIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkELQEPECIIVAPTRELINQI 380
Cdd:cd17948    4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEG--PFNAPRGLVITPSRELAEQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 381 YLEARKFSFGTCVRAVVIYGgtqfGHSVRQIV----QGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 456
Cdd:cd17948   82 GSVAQSLTEGLGLKVKVITG----GRTKRQIRnphfEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 225007636 457 PEMKKLIS-CP-GMPSKEQR-------QTLLFSATFPEEIQRLAGD 493
Cdd:cd17948  158 EKLSHFLRrFPlASRRSENTdgldpgtQLVLVSATMPSGVGEVLSK 203
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 291-495 7.66e-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: 113.96  E-value: 7.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 291 EANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhmmrdgITASRFKELQepeCIIV 370
Cdd:cd17939    1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQ------RIDTTVRETQ---ALVL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 371 APTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRM 450
Cdd:cd17939   72 APTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEM 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 225007636 451 LDMGFGPEMKKLISCpgMPSKEqrQTLLFSATFPEEIQRLAGDFL 495
Cdd:cd17939  152 LSRGFKDQIYDIFQF--LPPET--QVVLFSATMPHEVLEVTKKFM 192
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 302-497 7.82e-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: 114.36  E-value: 7.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILaHMMRdgitasrfKELQEPECIIVAPTRELINQIY 381
Cdd:cd17950   17 IVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL-QQLE--------PVDGQVSVLVICHTRELAFQIS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 382 LEARKFS-FGTCVRAVVIYGGTQFGHSVRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDmgfGPEM 459
Cdd:cd17950   88 NEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE---QLDM 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 225007636 460 KKLI-----SCPgmpskEQRQTLLFSATFPEEIQRLAGDFLKS 497
Cdd:cd17950  165 RRDVqeifrATP-----HDKQVMMFSATLSKEIRPVCKKFMQD 202
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 289-496 1.08e-28

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: 113.69  E-value: 1.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 289 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECI 368
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQID---------TSLKATQAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 369 IVAPTRELINQI--YLEARKFSFGTCVRAVViyGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 446
Cdd:cd18046   72 VLAPTRELAQQIqkVVMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDE 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 225007636 447 ADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPEEIQRLAGDFLK 496
Cdd:cd18046  150 ADEMLSRGFKDQIYDIFQ--KLP--PDTQVVLLSATMPNDVLEVTTKFMR 195
HELICc smart00490
helicase superfamily c-terminal domain;
553-634 2.42e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.45  E-value: 2.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636   553 DFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 632
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 225007636   633 CG 634
Cdd:smart00490  81 AG 82
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 289-495 7.48e-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: 111.41  E-value: 7.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 289 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhmMRDgitasrfKELQEPECI 368
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ--CLD-------IQVRETQAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 369 IVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEAD 448
Cdd:cd18045   72 ILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEAD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 225007636 449 RMLDMGFgpemKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFL 495
Cdd:cd18045  152 EMLNKGF----KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFM 194
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 302-485 4.86e-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: 108.51  E-value: 4.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLlpILAHMMRDgitasrfKELQEPECIIVAPTRELINQIY 381
Cdd:cd17943    5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFV--VIALESLD-------LERRHPQVLILAPTREIAVQIH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 382 LEARKF-SFGTCVRAVVIYGGTqfghSV---RQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGP 457
Cdd:cd17943   76 DVFKKIgKKLEGLKCEVFIGGT----PVkedKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQK 151

                        170       180
                 ....*....|....*....|....*...
gi 225007636 458 EMKKLIScpGMPskEQRQTLLFSATFPE 485
Cdd:cd17943  152 DVNWIFS--SLP--KNKQVIAFSATYPK 175
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 275-491 2.85e-21

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 93.16  E-value: 2.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 275 VEVSGHD-APP--AILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILahm 349
Cdd:cd18048    3 VEVLQRDpTSPlfSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 350 mrdgitaSRFKELQE-PECIIVAPTRELINQ---IYLEARKFsfgtCVRAVVIYG--GTQFGHSVRQIVQgcnILCATPG 423
Cdd:cd18048   80 -------SRVDALKLyPQCLCLSPTFELALQtgkVVEEMGKF----CVGIQVIYAirGNRPGKGTDIEAQ---IVIGTPG 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 424 RLMDIIGKEK-IGLKQVKYLVLDEADRMLDM-GFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLA 491
Cdd:cd18048  146 TVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKR--SMPK--ECQMLLFSATFEDSVWAFA 211
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 301-494 1.14e-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: 92.05  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 301 NIAKAGYTKL------TPVQKYSIPIVLAGR----------------DLMACAQTGSGKTAAFLLPILAHMMRDGITASR 358
Cdd:cd17965   16 KEILKGSNKTdeeikpSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPFE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 359 FKELQE--------PECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGtqFGHSVRQIVQ----GCNILCATPGRLM 426
Cdd:cd17965   96 EAEEEYesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSG--FGPSYQRLQLafkgRIDILVTTPGKLA 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225007636 427 DIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLAGDF 494
Cdd:cd17965  174 SLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIK--RAPK--LKHLILCSATIPKEFDKTLRKL 237
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
522-640 7.22e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 94.41  E-value: 7.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 522 GQYSKREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKISTTSIHG--DRE------QREREQALGDFRCGK 589
Cdd:COG1111  332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 225007636 590 CPVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNTGRAI 640
Cdd:COG1111  412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
306-644 1.99e-19

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 92.13  E-value: 1.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 306 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPtreLI----NQI- 380
Cdd:COG0514   14 GYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPAL---LLPGLT------------LVVSP---LIalmkDQVd 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 381 YLEARKfsfgtcVRAVVIyggtqfgHS------VRQIVQGCN-----ILCATPGRLM-----DIIGKEKIGLkqvkyLVL 444
Cdd:COG0514   76 ALRAAG------IRAAFL-------NSslsaeeRREVLRALRagelkLLYVAPERLLnprflELLRRLKISL-----FAI 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 445 DEA--------DrmldmgFGPE---MKKLI-SCPGMPskeqrqTLLFSATFPEE-----IQRLAgdfLKSSYLFVavgqv 507
Cdd:COG0514  138 DEAhcisqwghD------FRPDyrrLGELReRLPNVP------VLALTATATPRvradiAEQLG---LEDPRVFV----- 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 508 GGACRD-VQQTILQVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFR 586
Cdd:COG0514  198 GSFDRPnLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFL 277

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 587 CGKCPVLVATSvaARGL--DIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 644
Cdd:COG0514  278 RDEVDVIVATI--AFGMgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYG 335
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
323-644 8.00e-19

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 90.85  E-value: 8.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 323 AGRDLMACAQTGSGKTAAFLLpILAHMMRDGITasrfkelqepecIIVAPTRELINQIYLEARKFsfgtcvravviYGGT 402
Cdd:COG1061   99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGKRV------------LVLVPRRELLEQWAEELRRF-----------LGDP 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 403 QFGHSVRQIvqGCNILCATPGRLMDIIGKEKIGlKQVKYLVLDEADRmldmGFGPEMKKLIScpgmpSKEQRQTLLFSAT 482
Cdd:COG1061  155 LAGGGKKDS--DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILE-----AFPAAYRLGLTAT 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 483 ------FPEEIQRLAG--------DFLKSSYL----FVAV-------GQVGGACRDVQQTILQVGQYSKREKLVEILRNI 537
Cdd:COG1061  223 pfrsdgREILLFLFDGivyeyslkEAIEDGYLappeYYGIrvdltdeRAEYDALSERLREALAADAERKDKILRELLREH 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 538 GD-ERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDL 616
Cdd:COG1061  303 PDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP 382

                        330       340
                 ....*....|....*....|....*...
gi 225007636 617 PSTIDEYVHRIGRTGRCGNTGRAISFFD 644
Cdd:COG1061  383 TGSPREFIQRLGRGLRPAPGKEDALVYD 410
PRK13766 PRK13766
Hef nuclease; Provisional
 526-640 6.57e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.76  E-value: 6.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 526 KREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKIST------TSIHGDREQREREQ--ALGDFRCGKCPVL 593
Cdd:PRK13766 348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGMSQKEQieILDKFRAGEFNVL 427

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 225007636 594 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 640
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 524-629 2.33e-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: 2.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 524 YSKREKLVEILRN----IGDERTMVFVET---------------KKKADFIATFLCQEKISTTSIHGDREQREREQALGD 584
Cdd:cd18802    6 IPKLQKLIEILREyfpkTPDFRGIIFVERratavvlsrllkehpSTLAFIRCGFLIGRGNSSQRKRSLMTQRKQKETLDK 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 225007636 585 FRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGR 629
Cdd:cd18802   86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 288-491 2.46e-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: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 288 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILAHMMrdgiTASRFKelqep 365
Cdd:cd18047    2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE----PANKYP----- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 366 ECIIVAPTRELINQ---IYLEARKF----SFGTCVRavviygGTQFGHSVRQIVQgcnILCATPGRLMDIIGKEK-IGLK 437
Cdd:cd18047   73 QCLCLSPTYELALQtgkVIEQMGKFypelKLAYAVR------GNKLERGQKISEQ---IVIGTPGTVLDWCSKLKfIDPK 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 225007636 438 QVKYLVLDEADRMLDMGfGPEMKKLISCPGMPskEQRQTLLFSATFPEEIQRLA 491
Cdd:cd18047  144 KIKVFVLDEADVMIATQ-GHQDQSIRIQRMLP--RNCQMLLFSATFEDSVWKFA 194
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 526-640 5.73e-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: 69.69  E-value: 5.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 526 KREKLVEILRNI-------GDERTMVFVETKKKADFIATFLCQEK--------ISTTSIHGDREQREREQ--ALGDFRCG 588
Cdd:cd18801   10 KLEKLEEIVKEHfkkkqegSDTRVIIFSEFRDSAEEIVNFLSKIRpgiratrfIGQASGKSSKGMSQKEQkeVIEQFRKG 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225007636 589 KCPVLVATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 640
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 ...
 530-643 1.25e-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: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 530 LVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQ 609
Cdd:cd18794   21 LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVR 100

                         90       100       110
                 ....*....|....*....|....*....|....
gi 225007636 610 HVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 643
Cdd:cd18794  101 FVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
302-632 5.19e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 72.24  E-value: 5.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 302 IAKAGYTKLTPVQKYSIP-IVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGItasrfkelqepeCIIVAPTRELINQI 380
Cdd:COG1204   15 LKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK------------ALYIVPLRALASEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 381 YLEARKF--SFGtcVRAVVIYGGTQfghSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEAdRML-DMGFGP 457
Cdd:COG1204   83 YREFKRDfeELG--IKVGVSTGDYD---SDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLIdDESRGP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 458 --EM---KKLISCPGMpskeqrQTLLFSATF--PEEIQR-LAGDFLKSSY------LFVAVGQV-----GGACRD----- 513
Cdd:COG1204  157 tlEVllaRLRRLNPEA------QIVALSATIgnAEEIAEwLDAELVKSDWrpvplnEGVLYDGVlrfddGSRRSKdptla 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 514 -VQQTILQVGQ-----YSKR------EKLVEILRNIGDErtmvfvETKKKADFIATFL--CQEKISTTSI---------- 569
Cdd:COG1204  231 lALDLLEEGGQvlvfvSSRRdaeslaKKLADELKRRLTP------EEREELEELAEELleVSEETHTNEKladclekgva 304

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225007636 570 --HGD--REQRER-EQAlgdFRCGKCPVLVATSVAARGLdieN--VQHVI------NFDLPSTIDEYVHRIGRTGR 632
Cdd:COG1204  305 fhHAGlpSELRRLvEDA---FREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGR 374
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 324-482 8.99e-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: 8.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 324 GRDLMACAQTGSGKTAAFLLPILAHMmrdgitasrfkELQEPECIIVAPTRELINQIYLEARKFsFGTCVRAVVIYGGTQ 403
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLL-----------LKKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 404 FGHSVRQIVQGCNILCATPGRL-MDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRqtLLFSAT 482
Cdd:cd00046   69 AEEREKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV--ILLSAT 146
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 525-628 7.61e-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: 7.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 525 SKREKLVEILRNI--GDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDF-RCGKCPV-LVATSVAA 600
Cdd:cd18793   11 GKLEALLELLEELrePGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnEDPDIRVfLLSTKAGG 90

                         90       100       110
                 ....*....|....*....|....*....|....
gi 225007636 601 RGLDIENVQHVINFDLP--STIDEY----VHRIG 628
Cdd:cd18793   91 VGLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 291-640 9.91e-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: 68.32  E-value: 9.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 291 EANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD-GITAsrfkelqepecII 369
Cdd:COG1205   38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDpGATA-----------LY 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 370 VAPTRELINQIYLEARKF--SFGTCVRAVVIYGGTQfGHSVRQIVQGCNILCATPgrlmDII------GKEKIG--LKQV 439
Cdd:COG1205  107 LYPTKALARDQLRRLRELaeALGLGVRVATYDGDTP-PEERRWIREHPDIVLTNP----DMLhygllpHHTRWArfFRNL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 440 KYLVLDEA---------------DRMLDMgfgpeMKKLISCPgmpskeqrQTLLFSATF--PEEI-QRLAGDflkssyLF 501
Cdd:COG1205  182 RYVVIDEAhtyrgvfgshvanvlRRLRRI-----CRHYGSDP--------QFILASATIgnPAEHaERLTGR------PV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 502 VAVGQVGGAC--RDVqqtIL----QVGQYSKREKLVE---ILRNIGDE--RTMVFVETKKKADFIATFL---CQEKISTT 567
Cdd:COG1205  243 TVVDEDGSPRgeRTF---VLwnppLVDDGIRRSALAEaarLLADLVREglRTLVFTRSRRGAELLARYArraLREPDLAD 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225007636 568 SIHGDR------EQREREQALgdfRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAI 640
Cdd:COG1205  320 RVAAYRagylpeERREIERGL---RSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 306-644 3.41e-11

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 66.66  E-value: 3.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 306 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPTRELI-NQI-YLE 383
Cdd:PRK11057  22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL---VLDGLT------------LVVSPLISLMkDQVdQLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 384 ARKFSfGTCVRAvviyggTQFGHSVRQIVQGCN-----ILCATPGRLM--DIIgkEKIGLKQVKYLVLDEADRMLDMG-- 454
Cdd:PRK11057  87 ANGVA-AACLNS------TQTREQQLEVMAGCRtgqikLLYIAPERLMmdNFL--EHLAHWNPALLAVDEAHCISQWGhd 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 455 FGPEMKKL----ISCPGMPskeqrqTLLFSATFPEEIQRlagDFLKSSYLFVAVGQVGGACR-DVQQTILQvgqysKREK 529
Cdd:PRK11057 158 FRPEYAALgqlrQRFPTLP------FMALTATADDTTRQ---DIVRLLGLNDPLIQISSFDRpNIRYTLVE-----KFKP 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 530 LVEILRNIGDERT---MVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 606
Cdd:PRK11057 224 LDQLMRYVQEQRGksgIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKP 303

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 225007636 607 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 644
Cdd:PRK11057 304 NVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 310-447 2.15e-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: 57.27  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 310 LTPVQKYSI-PIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITasrfkelqepeCIIVAPTRELINQIYLEARKFS 388
Cdd:cd17921    2 LNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK-----------AVYIAPTRALVNQKEADLRERF 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 389 FGTCVRAVVIYGGTQFGhsvRQIVQGCNILCATPGRLMDIIGKEKI-GLKQVKYLVLDEA 447
Cdd:cd17921   71 GPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 525-630 5.96e-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: 5.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 525 SKREKLVEILRNI--GDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGK-CPV-LVATSVAA 600
Cdd:COG0553  533 AKLEALLELLEELlaEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLKAGG 612

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 225007636 601 RGLdieNVQ---HVINFDLP-------STIDEyVHRIGRT 630
Cdd:COG0553  613 EGL---NLTaadHVIHYDLWwnpaveeQAIDR-AHRIGQT 648
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 592-632 5.89e-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: 5.89e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 225007636 592 VLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 632
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
 331-629 1.26e-07

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: 55.09  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 331 AQTGSGKTAAFLLPILAHMMRDGitASRFkelqepecIIVAPTRELINQIYLEARKFSFGtcvrAVVIYGGTQFGHSVRQ 410
Cdd:COG1203  154 APTGGGKTEAALLFALRLAAKHG--GRRI--------IYALPFTSIINQTYDRLRDLFGE----DVLLHHSLADLDLLEE 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 411 IVQGCN---------------ILCATPGRLMDII-----GKEKIGLKQV-KYLVLDEADrMLDMGFGPEMKKLIscpgmp 469
Cdd:COG1203  220 EEEYESearwlkllkelwdapVVVTTIDQLFESLfsnrkGQERRLHNLAnSVIILDEVQ-AYPPYMLALLLRLL------ 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 470 sKEQRQ----TLLFSATFPEEIQrlagDFLKSSYLFV--AVGQVGGACRDVQQTILQV--GQYSkREKLVEILRNI--GD 539
Cdd:COG1203  293 -EWLKNlggsVILMTATLPPLLR----EELLEAYELIpdEPEELPEYFRAFVRKRVELkeGPLS-DEELAELILEAlhKG 366

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 540 ERTMVFVETKKKAdfIATF-LCQEKISTTSIH--------GDREQREREqALGDFRCGKCPVLVATSVAARGLDienvqh 610
Cdd:COG1203  367 KSVLVIVNTVKDA--QELYeALKEKLPDEEVYllhsrfcpADRSEIEKE-IKERLERGKPCILVSTQVVEAGVD------ 437

                        330       340
                 ....*....|....*....|...
gi 225007636 611 vINFDL----PSTIDEYVHRIGR 629
Cdd:COG1203  438 -IDFDVvirdLAPLDSLIQRAGR 459
PRK13767 PRK13767
ATP-dependent helicase; Provisional
 307-381 2.80e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 54.12  E-value: 2.80e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225007636 307 YTKLTPVQKYSIPIVLAGRDLMACAQTGSGKT-AAFLLPIlahmmRDGITASRFKELQEP-ECIIVAPTRELINQIY 381
Cdd:PRK13767  30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAII-----DELFRLGREGELEDKvYCLYVSPLRALNNDIH 101
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
 306-489 4.76e-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: 51.00  E-value: 4.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 306 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPTRELIN-QIY-LE 383
Cdd:cd17920    9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL---LLDGVT------------LVVSPLISLMQdQVDrLQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 384 ARkfsfgtCVRAVVIYGGTQFgHSVRQIVQGC-----NILCATPGRLMDIIGKEKIG----LKQVKYLVLDEADRMLDMG 454
Cdd:cd17920   74 QL------GIRAAALNSTLSP-EEKREVLLRIkngqyKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHCVSQWG 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 225007636 455 --FGPEMKKLIS----CPGMPskeqrqTLLFSATFPEEIQR 489
Cdd:cd17920  147 hdFRPDYLRLGRlrraLPGVP------ILALTATATPEVRE 181
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 309-482 6.99e-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: 6.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 309 KLTPVQKYSIPIVLAG------RDLMACAQTGSGKTAAFLLPILAhmmrdgiTASRFKELqepecIIVAPTRELINQIYL 382
Cdd:cd17918   15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL-------AYKNGKQV-----AILVPTEILAHQHYE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 383 EARK-FSFgtcVRAVVIYGGTQfghsvRQIVQGCNILCATPGRLMDIIGKEKIGLkqvkyLVLDEADRmldmgFGPEMKK 461
Cdd:cd17918   83 EARKfLPF---INVELVTGGTK-----AQILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHR-----FGVAQRE 144

                        170       180
                 ....*....|....*....|.
gi 225007636 462 LISCPGMPSkeqrqTLLFSAT 482
Cdd:cd17918  145 ALYNLGATH-----FLEATAT 160
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
307-363 1.36e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 52.03  E-value: 1.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 225007636 307 YTKLTPVQKYSIPIVLAGRDLMACAQTGSGKT-AAFlLPILAHMMRDGITASRFKELQ 363
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGLR 78
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 314-447 1.45e-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: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 314 QKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD-GITAsrfkelqepecIIVAPTRELIN-QI-YLEARKFSFG 390
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDpGSRA-----------LYLYPTKALAQdQLrSLRELLEQLG 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225007636 391 TCVRAVVIYGGTQfgHSVRQ--IVQGCNILCATPGRLMDII----GKEKIGLKQVKYLVLDEA 447
Cdd:cd17923   74 LGIRVATYDGDTP--REERRaiIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 539-647 1.77e-06

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 48.78  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 539 DERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFD--- 615
Cdd:cd18790   27 GERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadk 106

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 225007636 616 ---LPSTiDEYVHRIGRTGRCGNtGRAISFFD--TDS 647
Cdd:cd18790  107 egfLRSE-TSLIQTIGRAARNVN-GKVILYADkiTDS 141
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 324-446 5.02e-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: 5.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 324 GRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkelqepeCIIVAPTRELINQIY--LEARKFSFGTCVRAVVIYGG 401
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------VLYISPLKALINDQErrLEEPLDEIDLEIPVAVRHGD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 225007636 402 TQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIG--LKQVKYLVLDE 446
Cdd:cd17922   73 TSQSEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 537-629 6.93e-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: 6.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 537 IGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQA---LGDFRCGKCPVLVATSVAARGLDIENVQHVIn 613
Cdd:cd18799    4 YVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV- 82

                         90
                 ....*....|....*...
gi 225007636 614 FDLP--STIdEYVHRIGR 629
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 ...
 532-632 9.27e-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: 9.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 532 EILRNIGDERTM-VFVETKKKADFIAT---FLCQEKISTTSI---HG--DREQRER-EQAL--GDFRcgkcpVLVATSVA 599
Cdd:cd18796   30 EVIFLLERHKSTlVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAALkrGDLK-----VVVATSSL 104

                         90       100       110
                 ....*....|....*....|....*....|...
gi 225007636 600 ARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 632
Cdd:cd18796  105 ELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 519-643 2.47e-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: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 519 LQVGQYSKREKLVEILRNIGD-ERTMVFVETKKKADFIAtflcqEKISTTSIHGDREQREREQALGDFRCGKCPVLVATS 597
Cdd:cd18789   28 LAAMNPNKLRALEELLKRHEQgDKIIVFTDNVEALYRYA-----KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSK 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 225007636 598 VAARGLDI--ENVQHVINFDLPSTiDEYVHRIGRTGRCGNTGRAISFF 643
Cdd:cd18789  103 VGDEGIDLpeANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
ResIII pfam04851
Type III restriction enzyme, res subunit;
309-485 3.21e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 44.97  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636  309 KLTPVQKYSIPIVLAGRDL--------MAcaqTGSGKT--AAFllpilahmmrdgITASRFKELQEPECIIVAPTRELIN 378
Cdd:pfam04851   3 ELRPYQIEAIENLLESIKNgqkrglivMA---TGSGKTltAAK------------LIARLFKKGPIKKVLFLVPRKDLLE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636  379 QIYLEARKFsFGTCVRAVVIYGGTqfghSVRQIVQGCNILCATPGRLMDII--GKEKIGLKQVKYLVLDEADRmldmGFG 456
Cdd:pfam04851  68 QALEEFKKF-LPNYVEIGEIISGD----KKDESVDDNKIVVTTIQSLYKALelASLELLPDFFDVIIIDEAHR----SGA 138

                         170       180       190
                  ....*....|....*....|....*....|
gi 225007636  457 PEMKKLIscpgmpSKEQRQTLL-FSATFPE 485
Cdd:pfam04851 139 SSYRNIL------EYFKPAFLLgLTATPER 162
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 325-447 8.53e-05

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: 44.18  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 325 RDLMACAQTGSGKT--AAFLLPILAHmmrdgitasRFKELQEPECIIV--APTRELINQiylEARKFSFGTCVRAVVIYG 400
Cdd:cd18034   17 RNTIVVLPTGSGKTliAVMLIKEMGE---------LNRKEKNPKKRAVflVPTVPLVAQ---QAEAIRSHTDLKVGEYSG 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225007636 401 GTQFGHSVRQIVQGC----NILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 447
Cdd:cd18034   85 EMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
 306-446 1.67e-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: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 306 GYTKLTPVQKYSIPIVLAGRD-LMACAQTGSGKTAAFLLPIL----AHMMRDG-ITASRFKelqepeCIIVAPTRELINQ 379
Cdd:cd18019   14 GFKSLNRIQSKLFPAAFETDEnLLLCAPTGAGKTNVALLTILreigKHRNPDGtINLDAFK------IVYIAPMKALVQE 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225007636 380 IY--LEARKFSFGTCVRAVViyGGTQFghSVRQIVQgCNILCATPGRlMDII---GKEKIGLKQVKYLVLDE 446
Cdd:cd18019   88 MVgnFSKRLAPYGITVAELT--GDQQL--TKEQISE-TQIIVTTPEK-WDIItrkSGDRTYTQLVRLIIIDE 153
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 325-422 1.69e-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: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 325 RDLMACAQTGSGKTAAFLLPILaHMMRDGITASRFKelqePECIIVAPTRELINQIYLEAR-KFS-FGTCVraVVIYGGT 402
Cdd:cd18023   18 KNFVVSAPTGSGKTVLFELAIL-RLLKERNPLPWGN----RKVVYIAPIKALCSEKYDDWKeKFGpLGLSC--AELTGDT 90

                         90       100
                 ....*....|....*....|
gi 225007636 403 QFGhSVRQIvQGCNILCATP 422
Cdd:cd18023   91 EMD-DTFEI-QDADIILTTP 108
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 569-629 5.83e-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: 5.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225007636 569 IHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIEN-----VQHVINFDLpSTIDEYVHRIGR 629
Cdd:cd18811   67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGL-SQLHQLRGRVGR 131
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
 324-387 1.13e-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: 1.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225007636 324 GRDLMACAQTGSGKTAAFLLPILAHMMRDGItasrfkelqePECIIVAPTRELINQIYLEARKF 387
Cdd:cd17930    1 PGLVILEAPTGSGKTEAALLWALKLAARGGK----------RRIIYALPTRATINQMYERIREI 54
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 328-449 1.14e-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: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 328 MACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqePECIIVAPTRELINQIYLEARKFsFGTCVRAVVIYGGTQfGHS 407
Cdd:cd18035   20 LIVLPTGLGKTIIAILVAADRLTKKG-----------GKVLILAPSRPLVEQHAENLKRV-LNIPDKITSLTGEVK-PEE 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 225007636 408 VRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADR 449
Cdd:cd18035   87 RAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 333-447 1.23e-03

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: 39.98  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 333 TGSGKTA-AFLLPIlahmmrdgitasrfkELQEPECIIVAPTRELINQIYLEARKFSFGtcvraVVIYggtQFGHSVRQI 411
Cdd:cd17926   27 TGSGKTLtALALIA---------------YLKELRTLIVVPTDALLDQWKERFEDFLGD-----SSIG---LIGGGKKKD 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 225007636 412 VQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 447
Cdd:cd17926   84 FDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
 541-635 1.96e-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: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 541 RTMVFVETKKKADFIATFLCQEKIST----TSIHGDR------EQREREQalgDFRCGKCPVLVATSVAARGLDIENVQH 610
Cdd:cd18797   37 KTIVFCRSRKLAELLLRYLKARLVEEgplaSKVASYRagylaeDRREIEA---ELFNGELLGVVATNALELGIDIGGLDA 113

                         90       100
                 ....*....|....*....|....*
gi 225007636 611 VINFDLPSTIDEYVHRIGRTGRCGN 635
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 ...
 569-608 2.31e-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: 2.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 225007636 569 IHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENV 608
Cdd:cd18792   66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA 105
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
 568-631 2.47e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.45  E-value: 2.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225007636  568 SIHGD--REQR-EREQAL--GDFRCgkcpvLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTG 631
Cdd:PRK09751  306 SHHGSvsKEQRaITEQALksGELRC-----VVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
 315-449 2.54e-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: 39.72  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 315 KYSIPIVLA---GRDLMACAQTGSGKTAafllpILAHMMRDGITasRFKELQEPECIIVAPTRELINQiylEARKFS--F 389
Cdd:cd17927    5 NYQLELAQPalkGKNTIICLPTGSGKTF-----VAVLICEHHLK--KFPAGRKGKVVFLANKVPLVEQ---QKEVFRkhF 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225007636 390 GTCVRAVV-IYGGTQFGHSVRQIVQGCNILCATPGRLM-DIIGKEKIGLKQVKYLVLDEADR 449
Cdd:cd17927   75 ERPGYKVTgLSGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
 330-464 2.66e-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: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 330 CAQTGSGKTAAFLLPILAHmmrdgitasrFKELQEPECIIVAPTRELINQIYLE-ARKFSFGTCVRAVVIYGGTQfghSV 408
Cdd:cd18021   25 GAPTGSGKTVCAELALLRH----------WRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLGKKVVKLTGETS---TD 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 225007636 409 RQIVQGCNILCATPGRLmDIIG---KEKIGLKQVKYLVLDEAdRMLDMGFGPEMKKLIS 464
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; ...
 326-496 3.39e-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: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 326 DLMACAQTGSGKTAAFLLPILaHMMRDGITASRFKELQEPECIIVAPTRELINQI--YLEARKFSFGTCVRAVViyGGTQ 403
Cdd:cd18020   19 NMLICAPTGAGKTNIAMLTIL-HEIRQHVNQGGVIKKDDFKIVYIAPMKALAAEMveKFSKRLAPLGIKVKELT--GDMQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225007636 404 FghsVRQIVQGCNILCATPGRlMDIIGKEKIG----LKQVKYLVLDEAdRMLDMGFGPEMKKLIScPGMPSKEQRQTLL- 478
Cdd:cd18020   96 L---TKKEIAETQIIVTTPEK-WDVVTRKSSGdvalSQLVRLLIIDEV-HLLHDDRGPVIESLVA-RTLRQVESTQSMIr 169

                        170       180
                 ....*....|....*....|.
gi 225007636 479 ---FSATFPEEIQrlAGDFLK 496
Cdd:cd18020  170 ivgLSATLPNYLD--VADFLR 188
 
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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