NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|33859536|ref|NP_034159|]
View 

ATP-dependent RNA helicase DDX4 isoform 2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 230-482 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 33859536 230 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 309
Cdd:cd18052  12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 310 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC 389
Cdd:cd18052  92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 390 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFL 469
Cdd:cd18052 172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                       250
                ....*....|...
gi 33859536 470 KSSYLFVAVGQVG 482
Cdd:cd18052 252 KEDYLFLTVGRVG 264
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 488-617 1.40e-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: 1.40e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 488 VQQTILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 566
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 33859536 567 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 617
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 ...
 230-482 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 33859536 230 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 309
Cdd:cd18052  12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 310 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC 389
Cdd:cd18052  92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 390 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFL 469
Cdd:cd18052 172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                       250
                ....*....|...
gi 33859536 470 KSSYLFVAVGQVG 482
Cdd:cd18052 252 KEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
262-627 1.74e-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: 1.74e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 262 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqePEC 341
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------PQA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 342 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 421
Cdd:COG0513  75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 422 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGDFLKSsYLFVAVGQVGGACRDVQQTILQVGQYSK 500
Cdd:COG0513 155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPENATAETIEQRYYLVDKRDK 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 501 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 580
Cdd:COG0513 229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 33859536 581 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSDNHLAQ 627
Cdd:COG0513 309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRA 355
PTZ00110 PTZ00110
helicase; Provisional
 251-656 6.23e-118

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 364.09  E-value: 6.23e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  251 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITA 330
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INA 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  331 S-RFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIG 409
Cdd:PTZ00110 195 QpLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  410 LKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFVAVGQVG-GACRDV 488
Cdd:PTZ00110 275 LRRVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNI 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  489 QQTILQVGQYSKREKLVEILRNIGDE--RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 566
Cdd:PTZ00110 351 KQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPI 430

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  567 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSdNHLAQPLVKVLSDAQQDVPAWLEE 646
Cdd:PTZ00110 431 MIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK-YRLARDLVKVLREAKQPVPPELEK 509

                        410
                 ....*....|
gi 33859536  647 IAFSTYVPPS 656
Cdd:PTZ00110 510 LSNERSNGTE 519
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 285-464 1.36e-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: 1.36e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536   285 TPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELINQIYLEARKFSFG 364
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD---------KLDNGPQALVLAPTRELAEQIYEELKKLGKG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536   365 TCVRAVVIYGGTQFgHSVRQIVQGCNILCATPGRLMDIIGKEKiGLKQVKYLVLDEADRMLDMGFGPEMKKLISCpgMPs 444
Cdd:pfam00270  72 LGLKVASLLGGDSR-KEQLEKLKGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146

                         170       180
                  ....*....|....*....|
gi 33859536   445 kEQRQTLLFSATFPEEIQRL 464
Cdd:pfam00270 147 -KKRQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 488-617 1.40e-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: 1.40e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 488 VQQTILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 566
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 33859536 567 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 617
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
276-476 2.01e-50

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 174.60  E-value: 2.01e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536    276 IAKAGYTKLTPVQKYSIPIVLAG-RDLMACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqEPECIIVAPTRELINQI 354
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK----------GGRVLVLVPTRELAEQW 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536    355 YLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEM 433
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 33859536    434 KKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFV 476
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLNDPVFID 189
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 499-608 2.47e-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: 2.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536   499 SKREKLVEILRNIGDERTMVFVETKKKADfIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLD 578
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 33859536   579 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 608
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
527-608 2.04e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.84  E-value: 2.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536    527 DFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 606
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 33859536    607 CG 608
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
496-614 6.67e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 94.41  E-value: 6.67e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 496 GQYSKREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKISTTSIHG--DRE------QREREQALGDFRCGK 563
Cdd:COG1111 332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 33859536 564 CPVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNTGRAI 614
Cdd:COG1111 412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
PRK13766 PRK13766
Hef nuclease; Provisional
 500-614 6.15e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.76  E-value: 6.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  500 KREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKIST------TSIHGDREQREREQ--ALGDFRCGKCPVL 567
Cdd:PRK13766 348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGMSQKEQieILDKFRAGEFNVL 427

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 33859536  568 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 614
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 ...
 230-482 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 33859536 230 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 309
Cdd:cd18052  12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 310 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC 389
Cdd:cd18052  92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 390 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFL 469
Cdd:cd18052 172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                       250
                ....*....|...
gi 33859536 470 KSSYLFVAVGQVG 482
Cdd:cd18052 252 KEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
262-627 1.74e-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: 1.74e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 262 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqePEC 341
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------PQA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 342 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 421
Cdd:COG0513  75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 422 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGDFLKSsYLFVAVGQVGGACRDVQQTILQVGQYSK 500
Cdd:COG0513 155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPENATAETIEQRYYLVDKRDK 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 501 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 580
Cdd:COG0513 229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 33859536 581 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSDNHLAQ 627
Cdd:COG0513 309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRA 355
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 262-482 5.21e-145

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: 5.21e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 262 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAS-RFKELQEPE 340
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgRGRRKAYPS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 341 CIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 420
Cdd:cd17967  81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33859536 421 ADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFLKsSYLFVAVGQVG 482
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
PTZ00110 PTZ00110
helicase; Provisional
 251-656 6.23e-118

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 364.09  E-value: 6.23e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  251 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITA 330
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INA 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  331 S-RFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIG 409
Cdd:PTZ00110 195 QpLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  410 LKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFVAVGQVG-GACRDV 488
Cdd:PTZ00110 275 LRRVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNI 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  489 QQTILQVGQYSKREKLVEILRNIGDE--RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 566
Cdd:PTZ00110 351 KQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPI 430

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  567 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSdNHLAQPLVKVLSDAQQDVPAWLEE 646
Cdd:PTZ00110 431 MIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK-YRLARDLVKVLREAKQPVPPELEK 509

                        410
                 ....*....|
gi 33859536  647 IAFSTYVPPS 656
Cdd:PTZ00110 510 LSNERSNGTE 519
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 241-482 7.93e-113

DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350809 [Multi-domain]  Cd Length: 249  Bit Score: 340.09  E-value: 7.93e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 241 FDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL 320
Cdd:cd18051   1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 321 AHMMRDG-----ITASRF--KELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILC 393
Cdd:cd18051  81 SQIYEQGpgeslPSESGYygRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 394 ATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFLkSSY 473
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFL-DNY 239


                ....*....
gi 33859536 474 LFVAVGQVG 482
Cdd:cd18051 240 IFLAVGRVG 248
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 263-655 2.37e-102

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 320.98  E-value: 2.37e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  263 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITASRFKelqePECI 342
Cdd:PRK11776   6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK-----LDVKRFR----VQAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  343 IVAPTRELINQIYLEARKFSFGT-CVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 421
Cdd:PRK11776  77 VLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  422 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGDFLKSSyLFVAVGQVGGAcRDVQQTILQVGQYSK 500
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRqAP-----ARRQTLLFSATYPEGIAAISQRFQRDP-VEVKVESTHDL-PAIEQRFYEVSPDER 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  501 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 580
Cdd:PRK11776 230 LPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33859536  581 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFdTDSDNHLAQplvkVLSDAQQDVPAW--LEEIAFSTYVPP 655
Cdd:PRK11776 310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLV-APEEMQRAN----AIEDYLGRKLNWepLPSLSPLSGVPL 381
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 262-616 1.22e-90

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 289.54  E-value: 1.22e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  262 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMmrdgITASRFKELQePEC 341
Cdd:PRK11192   2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL----LDFPRRKSGP-PRI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  342 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 421
Cdd:PRK11192  77 LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  422 DRMLDMGFGPEMKKLiscpgmpSKEQR---QTLLFSATFP-EEIQRLAGDFLKSSYLFVAvgqvgGACRDVQQTILQvgQ 497
Cdd:PRK11192 157 DRMLDMGFAQDIETI-------AAETRwrkQTLLFSATLEgDAVQDFAERLLNDPVEVEA-----EPSRRERKKIHQ--W 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  498 Y-------SKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVAT 570
Cdd:PRK11192 223 YyraddleHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVAT 302

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 33859536  571 SVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 616
Cdd:PRK11192 303 DVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 276-615 1.51e-87

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 282.08  E-value: 1.51e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfKELQEPECIIVAPTRELINQIY 355
Cdd:PRK10590  16 VAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHA---KGRRPVRALILTPTRELAAQIG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  356 LEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 435
Cdd:PRK10590  93 ENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRR 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  436 LIScpGMPSKeqRQTLLFSATFPEEIQRLAGDFLKSSyLFVAVGQVGGACRDVQQTILQVGQYSKREKLVEILRNIGDER 515
Cdd:PRK10590 173 VLA--KLPAK--RQNLLFSATFSDDIKALAEKLLHNP-LEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGKGNWQQ 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  516 TMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTID 595
Cdd:PRK10590 248 VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPE 327

                        330       340
                 ....*....|....*....|
gi 33859536  596 EYVHRIGRTGRCGNTGRAIS 615
Cdd:PRK10590 328 DYVHRIGRTGRAAATGEALS 347
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 246-653 1.53e-87

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 283.99  E-value: 1.53e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  246 TILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAH--- 322
Cdd:PLN00206 106 KLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcct 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  323 MMRDGITASRfkelqEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDI 402
Cdd:PLN00206 186 IRSGHPSEQR-----NPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDL 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  403 IGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPskeqrQTLLFSATFPEEIQRLAGDFLKSsYLFVAVGQVG 482
Cdd:PLN00206 261 LSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKD-IILISIGNPN 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  483 GACRDVQQTILQVGQYSKREKLVEILRNIGDER--TMVFVETKKKADFIAtflcqEKISTT------SIHGDREQREREQ 554
Cdd:PLN00206 335 RPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLA-----NAITVVtglkalSIHGEKSMKERRE 409

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  555 ALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSDNhLAQPLVKVLS 634
Cdd:PLN00206 410 VMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRN-LFPELVALLK 488

                        410
                 ....*....|....*....
gi 33859536  635 DAQQDVPawlEEIAFSTYV 653
Cdd:PLN00206 489 SSGAAIP---RELANSRYL 504
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 263-620 1.21e-86

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 280.26  E-value: 1.21e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  263 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFkeLQEPECI 342
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERY--MGEPRAL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  343 IVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQI-VQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 421
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  422 DRMLDMGFGPEMKKLIScpGMPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLfVAVGQVGGACRDVQQTILQVGQYSKR 501
Cdd:PRK01297 247 DRMLDMGFIPQVRQIIR--QTPRKEERQTLLFSATFTDDVMNLAKQWTTDPAI-VEIEPENVASDTVEQHVYAVAGSDKY 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  502 EKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIEN 581
Cdd:PRK01297 324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 33859536  582 VQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTD 620
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGED 442
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 272-470 7.92e-84

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 263.15  E-value: 7.92e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 272 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkelqEPECIIVAPTRELI 351
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGR-----GPQALVLAPTRELA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 352 NQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGP 431
Cdd:cd00268  76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEE 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33859536 432 EMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGDFLK 470
Cdd:cd00268 156 DVEKILSaLP-----KDRQTLLFSATLPEEVKELAKKFLK 190
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 255-616 3.49e-78

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 261.04  E-value: 3.49e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  255 DAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFK 334
Cdd:PRK04537   3 DKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  335 ElqEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKI-GLKQV 413
Cdd:PRK04537  83 E--DPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHAC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  414 KYLVLDEADRMLDMGFGPEMKKLIScpGMPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFVAVGQVGGACRdVQQTIL 493
Cdd:PRK04537 161 EICVLDEADRMFDLGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR-VRQRIY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  494 QVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVA 573
Cdd:PRK04537 238 FPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVA 317

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 33859536  574 ARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 616
Cdd:PRK04537 318 ARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 276-616 1.57e-72

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 241.41  E-value: 1.57e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkELQEPECIIVAPTRELINQIY 355
Cdd:PRK04837  23 LEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDR--KVNQPRALIMAPTRELAVQIH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  356 LEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 435
Cdd:PRK04837 101 ADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRW 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  436 LIScpGMPSKEQRQTLLFSATFPEEIQRLAGDFLKS-SYLFVAVGQVGGacRDVQQTILqvgqY-SKREKLVEILRNIGD 513
Cdd:PRK04837 181 LFR--RMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVEPEQKTG--HRIKEELF----YpSNEEKMRLLQTLIEE 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  514 E---RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDL 590
Cdd:PRK04837 253 EwpdRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDL 332

                        330       340
                 ....*....|....*....|....*.
gi 33859536  591 PSTIDEYVHRIGRTGRCGNTGRAISF 616
Cdd:PRK04837 333 PDDCEDYVHRIGRTGRAGASGHSISL 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 262-618 1.10e-69

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 239.36  E-value: 1.10e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  262 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPEC 341
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD---------PELKAPQI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  342 IIVAPTRELINQIYLEARKFS-FGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 420
Cdd:PRK11634  78 LVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  421 ADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPEEIQRLAGDFLKSSYLfVAVgQVGGACR-DVQQTILQVGQYS 499
Cdd:PRK11634 158 ADEMLRMGFIEDVETIMA--QIP--EGHQTALFSATMPEAIRRITRRFMKEPQE-VRI-QSSVTTRpDISQSYWTVWGMR 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  500 KREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDI 579
Cdd:PRK11634 232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 33859536  580 ENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 618
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 ...
 276-470 7.45e-67

DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 218.39  E-value: 7.45e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITASRFKELQE-PECIIVAPTRELINQI 354
Cdd:cd17966   5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVH-----INAQPPLERGDgPIVLVLAPTRELAQQI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 355 YLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMK 434
Cdd:cd17966  80 QQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 33859536 435 KLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLK 470
Cdd:cd17966 160 KIVD----QIRPDRQTLMWSATWPKEVRRLAEDFLK 191
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 272-469 7.82e-62

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: 7.82e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 272 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitASRFKELQE-PECIIVAPTREL 350
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-----DQRELEKGEgPIAVIVAPTREL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 351 INQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 430
Cdd:cd17952  76 AQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFE 155

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 33859536 431 PEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFL 469
Cdd:cd17952 156 YQVRSIVG----HVRPDRQTLLFSATFKKKIEQLARDIL 190
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 285-464 1.36e-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: 1.36e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536   285 TPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELINQIYLEARKFSFG 364
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD---------KLDNGPQALVLAPTRELAEQIYEELKKLGKG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536   365 TCVRAVVIYGGTQFgHSVRQIVQGCNILCATPGRLMDIIGKEKiGLKQVKYLVLDEADRMLDMGFGPEMKKLISCpgMPs 444
Cdd:pfam00270  72 LGLKVASLLGGDSR-KEQLEKLKGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146

                         170       180
                  ....*....|....*....|
gi 33859536   445 kEQRQTLLFSATFPEEIQRL 464
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) ...
 251-471 1.03e-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: 1.03e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 251 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITA 330
Cdd:cd17953   2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRH-----IKD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 331 SRF-KELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDII---GKE 406
Cdd:cd17953  77 QRPvKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGR 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33859536 407 KIGLKQVKYLVLDEADRMLDMGFGPEMKKLIscpgMPSKEQRQTLLFSATFPEEIQRLAGDFLKS 471
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 ...
 276-476 3.90e-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: 3.90e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIPIVLA-GRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKelqePECIIVAPTRELINQI 354
Cdd:cd17964   9 LTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSG----VSALIISPTRELALQI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 355 YLEARKF-SFGTCVRAVVIYGGTQFGHSVRQIV-QGCNILCATPGRLMDIIGKEKIG--LKQVKYLVLDEADRMLDMGFG 430
Cdd:cd17964  85 AAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLDMGFR 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 33859536 431 PEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFV 476
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 ...
 276-471 2.06e-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: 2.06e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfKELQEPECIIVAPTRELINQIY 355
Cdd:cd17945   5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEE-TKDDGPYALILAPTRELAQQIE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 356 LEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 435
Cdd:cd17945  84 EETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTK 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 33859536 436 LIScpGMPS------------------KEQRQTLLFSATFPEEIQRLAGDFLKS 471
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 ...
 488-617 1.40e-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: 1.40e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 488 VQQTILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 566
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 33859536 567 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 617
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 249-479 2.41e-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: 2.41e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 249 VEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgI 328
Cdd:cd18049  12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH-----I 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 329 TASRFKELQE-PECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEK 407
Cdd:cd18049  87 NHQPFLERGDgPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK 166

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33859536 408 IGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKsSYLFVAVG 479
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 ...
 272-465 3.81e-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: 3.81e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 272 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqEPECIIVAPTRELI 351
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-------GLRALILAPTRELA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 352 NQIYLEARKFSFGTCVRAVVIYGGTQFG-HSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 430
Cdd:cd17957  74 SQIYRELLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFR 153

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 33859536 431 PEMKKLI-SCpgmpSKEQRQTLLFSATFPEEIQRLA 465
Cdd:cd17957 154 EQTDEILaAC----TNPNLQRSLFSATIPSEVEELA 185
PTZ00424 PTZ00424
helicase 45; Provisional
 262-625 4.70e-54

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 190.81  E-value: 4.70e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  262 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitasrfkeLQEPEC 341
Cdd:PTZ00424  29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD---------LNACQA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  342 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 421
Cdd:PTZ00424 100 LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  422 DRMLDMGFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLAGDFLKSSYLfVAVGQVGGACRDVQQTILQVGQYS-K 500
Cdd:PTZ00424 180 DEMLSRGFKGQIYDVFK--KLPP--DVQVALFSATMPNEILELTTKFMRDPKR-ILVKKDELTLEGIRQFYVAVEKEEwK 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  501 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 580
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 33859536  581 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSDNHL 625
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 ...
 249-479 2.71e-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: 2.71e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 249 VEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgI 328
Cdd:cd18050  50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVH-----I 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 329 TASRFKELQE-PECIIVAPTRELINQIYLEArkFSFGTCVR--AVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGK 405
Cdd:cd18050 125 NHQPYLERGDgPICLVLAPTRELAQQVQQVA--DDYGKSSRlkSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEA 202

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33859536 406 EKIGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKsSYLFVAVG 479
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 ...
 263-476 6.26e-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: 6.26e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 263 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD--GITAsrfkelqepe 340
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDpyGIFA---------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 341 cIIVAPTRELINQIyleARKF-SFGTC--VRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDII---GKEKIGLKQVK 414
Cdd:cd17955  71 -LVLTPTRELAYQI---AEQFrALGAPlgLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTKVLSRVK 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33859536 415 YLVLDEADRMLDMGFGPEMKKLISCpgMPSKeqRQTLLFSATFPEEIQRLAGDFLKSSYLFV 476
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 ...
 276-465 2.01e-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: 2.01e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRdgitasRFKELQEPECIIVAPTRELINQIY 355
Cdd:cd17947   5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY------RPKKKAATRVLVLVPTRELAMQCF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 356 LEARKFS-FGTCVRAVVIyGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVLDEADRMLDMGFGPEM 433
Cdd:cd17947  79 SVLQQLAqFTDITFALAV-GGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADEL 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 33859536 434 KKLI-SCPgmpskEQRQTLLFSATFPEEIQRLA 465
Cdd:cd17947 158 KEILrLCP-----RTRQTMLFSATMTDEVKDLA 185
DEXDc smart00487
DEAD-like helicases superfamily;
276-476 2.01e-50

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 174.60  E-value: 2.01e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536    276 IAKAGYTKLTPVQKYSIPIVLAG-RDLMACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqEPECIIVAPTRELINQI 354
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK----------GGRVLVLVPTRELAEQW 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536    355 YLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEM 433
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 33859536    434 KKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFV 476
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 ...
 262-464 2.07e-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: 2.07e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 262 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitASRFkelqepEC 341
Cdd:cd17954   1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---PQRF------FA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 342 IIVAPTRELINQI--YLEARKFSFGtcVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVL 418
Cdd:cd17954  72 LVLAPTRELAQQIseQFEALGSSIG--LKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVM 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 33859536 419 DEADRMLDMGFGPEMKKLISCpgMPSkeQRQTLLFSATFPEEIQRL 464
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, ...
 276-465 2.75e-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: 2.75e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhMMRDGITASRFKELQepeCIIVAPTRELINQIY 355
Cdd:cd17960   5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLE-ILLKRKANLKKGQVG---ALIISPTRELATQIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 356 LEARKF--SFGTCVRAVVIYGGTQFGHSVRQIV-QGCNILCATPGRLMDIIG--KEKIGLKQVKYLVLDEADRMLDMGFG 430
Cdd:cd17960  81 EVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLGFE 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 33859536 431 PEMKKLISCpgMPskEQRQTLLFSATFPEEIQRLA 465
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 ...
 275-470 6.46e-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: 6.46e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 275 NIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMmrDGITASRFKElQEPECIIVAPTRELINQI 354
Cdd:cd17958   4 EIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL--DLQPIPREQR-NGPGVLVLTPTRELALQI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 355 YLEARKFSFGTcVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMK 434
Cdd:cd17958  81 EAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 33859536 435 KLIscpgMPSKEQRQTLLFSATFPEEIQRLAGDFLK 470
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 ...
 262-459 2.91e-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: 2.91e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 262 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL----AHMMRDGITAsrfkelq 337
Cdd:cd17959   2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIeklkAHSPTVGARA------- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 338 epecIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLV 417
Cdd:cd17959  75 ----LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVV 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 33859536 418 LDEADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPE 459
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) ...
 268-466 4.64e-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: 4.64e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 268 LCQTLNNNIakaGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitASRFKELQEPECIIVAPT 347
Cdd:cd17949   1 LVSHLKSKM---GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSL---EPRVDRSDGTLALVLVPT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 348 RELINQIYLEARKF--SFGTCVRAVVIyGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVLDEADRM 424
Cdd:cd17949  75 RELALQIYEVLEKLlkPFHWIVPGYLI-GGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRL 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 33859536 425 LDMGFGPEMKKLIS---------CPGMPSKEQRQTLLFSATFPEEIQRLAG 466
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 ...
 276-465 3.97e-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: 3.97e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitasRFKELQEPECIIVAPTRELINQIY 355
Cdd:cd17941   5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE-----RWTPEDGLGALIISPTRELAMQIF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 356 LEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQgCNILCATPGRL---MDiigkEKIGL--KQVKYLVLDEADRMLDMGFG 430
Cdd:cd17941  80 EVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLlqhMD----ETPGFdtSNLQMLVLDEADRILDMGFK 154

                       170       180       190
                ....*....|....*....|....*....|....*
gi 33859536 431 PEMKKLIScpGMPSKeqRQTLLFSATFPEEIQRLA 465
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 ...
 263-473 6.67e-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: 6.67e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 263 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL--AHMMRDGITAsrfkelqepe 340
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILekIDPKKDVIQA---------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 341 cIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 420
Cdd:cd17940  71 -LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 33859536 421 ADRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGDFLKSSY 473
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 ...
 276-476 6.86e-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: 6.86e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmmrDGITASRFKELQEPECIIVAPTRELINQIY 355
Cdd:cd17942   5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-----ELLYKLKFKPRNGTGVIIISPTRELALQIY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 356 LEARKF------SFGTCVravviyGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGL-KQVKYLVLDEADRMLDMG 428
Cdd:cd17942  80 GVAKELlkyhsqTFGIVI------GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILEIG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 33859536 429 FGPEMKKLISCpgMPSkeQRQTLLFSATFPEEIQRLAGDFLKSSYLFV 476
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 ...
 276-472 1.42e-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: 1.42e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASrFKELQEPECIIVAPTRELINQIY 355
Cdd:cd17951   5 LKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLP-FIKGEGPYGLIVCPSRELARQTH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 356 ---------LEARKFSfgtCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLD 426
Cdd:cd17951  84 evieyyckaLQEGGYP---QLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 33859536 427 MGFGPEMKKLISCpgmpSKEQRQTLLFSATFPEEIQrlagDFLKSS 472
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 ...
 272-470 3.46e-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: 3.46e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 272 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELI 351
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL---------TEHRNPSALILTPTRELA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 352 NQIYLEARKFSFGTC-VRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 430
Cdd:cd17962  72 VQIEDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQ 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33859536 431 PEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGDFLK 470
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 ...
 263-465 7.36e-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: 7.36e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 263 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmmrdgitasrfkelQEPECI 342
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------QIVVAL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 343 IVAPTRELINQIYLEARKFSF---GTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLD 419
Cdd:cd17938  65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 33859536 420 EADRMLDMGFGPEMKKLIS-CPGMPSKEQR-QTLLFSATF-PEEIQRLA 465
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 ...
 276-457 3.36e-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: 3.36e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIP-IVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQI 354
Cdd:cd17946   5 LADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTRELAVQV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 355 --YLEA-RKFsfgTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGK--EKIG-LKQVKYLVLDEADRMLDMG 428
Cdd:cd17946  85 kdHLKAiAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEgnEHLAnLKSLRFLVLDEADRMLEKG 161

                       170       180       190
                ....*....|....*....|....*....|..
gi 33859536 429 FGPEMKKLISC---PGMPSKEQRQTLLFSATF 457
Cdd:cd17946 162 HFAELEKILELlnkDRAGKKRKRQTFVFSATL 193
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 499-608 2.47e-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: 2.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536   499 SKREKLVEILRNIGDERTMVFVETKKKADfIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLD 578
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 33859536   579 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 608
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 ...
 280-473 1.04e-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: 1.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 280 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKElqePECIIVAPTRELINQIYLE-- 357
Cdd:cd17944   9 GVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRA---PKVLVLAPTRELANQVTKDfk 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 358 --ARKFSFgTCvravvIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 435
Cdd:cd17944  86 diTRKLSV-AC-----FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 33859536 436 LISCPGMPSKEQR-QTLLFSATFPEEIQRLAGDFLKSSY 473
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 ...
 276-471 4.27e-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: 4.27e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgiTASRFKElQEPECIIVAPTRELINQIY 355
Cdd:cd17961   9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKA--KAESGEE-QGTRALILVPTRELAQQVS 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 356 LEARKFSFGTC--VRAVVIyggTQFGHSVRQIVQ---GCNILCATPGRLMDII-GKEKIGLKQVKYLVLDEADRMLDMGF 429
Cdd:cd17961  86 KVLEQLTAYCRkdVRVVNL---SASSSDSVQRALlaeKPDIVVSTPARLLSHLeSGSLLLLSTLKYLVIDEADLVLSYGY 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 33859536 430 GPEMKKLIS-CPGMPskeqrQTLLFSATFPEEIQRLAGDFLKS 471
Cdd:cd17961 163 EEDLKSLLSyLPKNY-----QTFLMSATLSEDVEALKKLVLHN 200
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 268-464 3.57e-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: 3.57e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 268 LCQTLNNNiakaGYTKLTPVQKYSIPIVLAG---------RDLMACAQTGSGKTAAFLLPILAhmmrdgITASRFK-ELQ 337
Cdd:cd17956   1 LLKNLQNN----GITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQ------ALSKRVVpRLR 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 338 epeCIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGC--------NILCATPGRLMD-IIGKEKI 408
Cdd:cd17956  71 ---ALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDhLNSTPGF 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33859536 409 GLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQR----------------QTLLFSATF---PEEIQRL 464
Cdd:cd17956 148 TLKHLRFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLgsfgdanllersvrplQKLLFSATLtrdPEKLSSL 222
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 272-465 5.44e-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: 5.44e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 272 LNNNIAKA----GYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILahmmrdgitaSRFKE-LQEPECIIV 344
Cdd:cd17963   1 LKPELLKGlyamGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAML----------SRVDPtLKSPQALCL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 345 APTRELINQIYLEARKFSFGT------CVRAVVIYGGTQFGHsvrQIVQGcnilcaTPGRLMDIIGKEKIGLKQVKYLVL 418
Cdd:cd17963  71 APTRELARQIGEVVEKMGKFTgvkvalAVPGNDVPRGKKITA---QIVIG------TPGTVLDWLKKRQLDLKKIKILVL 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 33859536 419 DEADRMLDM-GFGPE---MKKLI--SCpgmpskeqrQTLLFSATFPEEIQRLA 465
Cdd:cd17963 142 DEADVMLDTqGHGDQsirIKRMLprNC---------QILLFSATFPDSVRKFA 185
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 275-467 5.18e-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: 5.18e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 275 NIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkELQEPECIIVAPTRELINQI 354
Cdd:cd17948   4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEG--PFNAPRGLVITPSRELAEQI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 355 YLEARKFSFGTCVRAVVIYGgtqfGHSVRQIV----QGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 430
Cdd:cd17948  82 GSVAQSLTEGLGLKVKVITG----GRTKRQIRnphfEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 33859536 431 PEMKKLIS-CP-GMPSKEQR-------QTLLFSATFPEEIQRLAGD 467
Cdd:cd17948 158 EKLSHFLRrFPlASRRSENTdgldpgtQLVLVSATMPSGVGEVLSK 203
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 276-471 7.39e-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: 7.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILaHMMRdgitasrfKELQEPECIIVAPTRELINQIY 355
Cdd:cd17950  17 IVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL-QQLE--------PVDGQVSVLVICHTRELAFQIS 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 356 LEARKFS-FGTCVRAVVIYGGTQFGHSVRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDmgfGPEM 433
Cdd:cd17950  88 NEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE---QLDM 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 33859536 434 KKLI-----SCPgmpskEQRQTLLFSATFPEEIQRLAGDFLKS 471
Cdd:cd17950 165 RRDVqeifrATP-----HDKQVMMFSATLSKEIRPVCKKFMQD 202
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 265-469 8.13e-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: 8.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 265 EANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhmmrdgITASRFKELQepeCIIV 344
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQ------RIDTTVRETQ---ALVL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 345 APTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRM 424
Cdd:cd17939  72 APTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEM 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 33859536 425 LDMGFGPEMKKLISCpgMPSKEqrQTLLFSATFPEEIQRLAGDFL 469
Cdd:cd17939 152 LSRGFKDQIYDIFQF--LPPET--QVVLFSATMPHEVLEVTKKFM 192
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 263-470 1.02e-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: 1.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 263 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECI 342
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQID---------TSLKATQAL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 343 IVAPTRELINQI--YLEARKFSFGTCVRAVViyGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 420
Cdd:cd18046  72 VLAPTRELAQQIqkVVMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDE 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 33859536 421 ADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPEEIQRLAGDFLK 470
Cdd:cd18046 150 ADEMLSRGFKDQIYDIFQ--KLP--PDTQVVLLSATMPNDVLEVTTKFMR 195
HELICc smart00490
helicase superfamily c-terminal domain;
527-608 2.04e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.84  E-value: 2.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536    527 DFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 606
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 33859536    607 CG 608
Cdd:smart00490  81 AG 82
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 263-469 7.17e-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: 7.17e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 263 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhmMRDgitasrfKELQEPECI 342
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ--CLD-------IQVRETQAL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 343 IVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEAD 422
Cdd:cd18045  72 ILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEAD 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 33859536 423 RMLDMGFgpemKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFL 469
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, ...
 276-459 4.62e-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: 4.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLlpILAHMMRDgitasrfKELQEPECIIVAPTRELINQIY 355
Cdd:cd17943   5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFV--VIALESLD-------LERRHPQVLILAPTREIAVQIH 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 356 LEARKF-SFGTCVRAVVIYGGTqfghSV---RQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGP 431
Cdd:cd17943  76 DVFKKIgKKLEGLKCEVFIGGT----PVkedKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQK 151

                       170       180
                ....*....|....*....|....*...
gi 33859536 432 EMKKLIScpGMPskEQRQTLLFSATFPE 459
Cdd:cd17943 152 DVNWIFS--SLP--KNKQVIAFSATYPK 175
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 249-465 2.72e-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: 2.72e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 249 VEVSGHD-APP--AILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILahm 323
Cdd:cd18048   3 VEVLQRDpTSPlfSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML--- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 324 mrdgitaSRFKELQE-PECIIVAPTRELINQ---IYLEARKFsfgtCVRAVVIYG--GTQFGHSVRQIVQgcnILCATPG 397
Cdd:cd18048  80 -------SRVDALKLyPQCLCLSPTFELALQtgkVVEEMGKF----CVGIQVIYAirGNRPGKGTDIEAQ---IVIGTPG 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 398 RLMDIIGKEK-IGLKQVKYLVLDEADRMLDM-GFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLA 465
Cdd:cd18048 146 TVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKR--SMPK--ECQMLLFSATFEDSVWAFA 211
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 275-468 1.08e-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: 1.08e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 275 NIAKAGYTKL------TPVQKYSIPIVLAGR----------------DLMACAQTGSGKTAAFLLPILAHMMRDGITASR 332
Cdd:cd17965  16 KEILKGSNKTdeeikpSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPFE 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 333 FKELQE--------PECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGtqFGHSVRQIVQ----GCNILCATPGRLM 400
Cdd:cd17965  96 EAEEEYesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSG--FGPSYQRLQLafkgRIDILVTTPGKLA 173

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33859536 401 DIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLAGDF 468
Cdd:cd17965 174 SLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIK--RAPK--LKHLILCSATIPKEFDKTLRKL 237
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
496-614 6.67e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 94.41  E-value: 6.67e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 496 GQYSKREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKISTTSIHG--DRE------QREREQALGDFRCGK 563
Cdd:COG1111 332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 33859536 564 CPVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNTGRAI 614
Cdd:COG1111 412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
280-618 1.86e-19

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 92.13  E-value: 1.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 280 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPtreLI----NQI- 354
Cdd:COG0514  14 GYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPAL---LLPGLT------------LVVSP---LIalmkDQVd 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 355 YLEARKfsfgtcVRAVVIyggtqfgHS------VRQIVQGCN-----ILCATPGRLM-----DIIGKEKIGLkqvkyLVL 418
Cdd:COG0514  76 ALRAAG------IRAAFL-------NSslsaeeRREVLRALRagelkLLYVAPERLLnprflELLRRLKISL-----FAI 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 419 DEA--------DrmldmgFGPE---MKKLI-SCPGMPskeqrqTLLFSATFPEE-----IQRLAgdfLKSSYLFVavgqv 481
Cdd:COG0514 138 DEAhcisqwghD------FRPDyrrLGELReRLPNVP------VLALTATATPRvradiAEQLG---LEDPRVFV----- 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 482 GGACRD-VQQTILQVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFR 560
Cdd:COG0514 198 GSFDRPnLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFL 277

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 561 CGKCPVLVATSvaARGL--DIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 618
Cdd:COG0514 278 RDEVDVIVATI--AFGMgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYG 335
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
297-618 7.45e-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: 7.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 297 AGRDLMACAQTGSGKTAAFLLpILAHMMRDGITasrfkelqepecIIVAPTRELINQIYLEARKFsfgtcvravviYGGT 376
Cdd:COG1061  99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGKRV------------LVLVPRRELLEQWAEELRRF-----------LGDP 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 377 QFGHSVRQIvqGCNILCATPGRLMDIIGKEKIGlKQVKYLVLDEADRmldmGFGPEMKKLIScpgmpSKEQRQTLLFSAT 456
Cdd:COG1061 155 LAGGGKKDS--DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILE-----AFPAAYRLGLTAT 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 457 ------FPEEIQRLAG--------DFLKSSYL----FVAV-------GQVGGACRDVQQTILQVGQYSKREKLVEILRNI 511
Cdd:COG1061 223 pfrsdgREILLFLFDGivyeyslkEAIEDGYLappeYYGIrvdltdeRAEYDALSERLREALAADAERKDKILRELLREH 302

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 512 GD-ERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDL 590
Cdd:COG1061 303 PDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP 382

                       330       340
                ....*....|....*....|....*...
gi 33859536 591 PSTIDEYVHRIGRTGRCGNTGRAISFFD 618
Cdd:COG1061 383 TGSPREFIQRLGRGLRPAPGKEDALVYD 410
PRK13766 PRK13766
Hef nuclease; Provisional
 500-614 6.15e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.76  E-value: 6.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  500 KREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKIST------TSIHGDREQREREQ--ALGDFRCGKCPVL 567
Cdd:PRK13766 348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGMSQKEQieILDKFRAGEFNVL 427

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 33859536  568 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 614
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 498-603 2.24e-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: 2.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 498 YSKREKLVEILRN----IGDERTMVFVET---------------KKKADFIATFLCQEKISTTSIHGDREQREREQALGD 558
Cdd:cd18802   6 IPKLQKLIEILREyfpkTPDFRGIIFVERratavvlsrllkehpSTLAFIRCGFLIGRGNSSQRKRSLMTQRKQKETLDK 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 33859536 559 FRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGR 603
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 ...
 262-465 2.35e-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: 2.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 262 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILAHMMrdgiTASRFKelqep 339
Cdd:cd18047   2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE----PANKYP----- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 340 ECIIVAPTRELINQ---IYLEARKF----SFGTCVRavviygGTQFGHSVRQIVQgcnILCATPGRLMDIIGKEK-IGLK 411
Cdd:cd18047  73 QCLCLSPTYELALQtgkVIEQMGKFypelKLAYAVR------GNKLERGQKISEQ---IVIGTPGTVLDWCSKLKfIDPK 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 33859536 412 QVKYLVLDEADRMLDMGfGPEMKKLISCPGMPskEQRQTLLFSATFPEEIQRLA 465
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 ...
 500-614 4.99e-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: 4.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 500 KREKLVEILRNI-------GDERTMVFVETKKKADFIATFLCQEK--------ISTTSIHGDREQREREQ--ALGDFRCG 562
Cdd:cd18801  10 KLEKLEEIVKEHfkkkqegSDTRVIIFSEFRDSAEEIVNFLSKIRpgiratrfIGQASGKSSKGMSQKEQkeVIEQFRKG 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 33859536 563 KCPVLVATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 614
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 ...
 504-617 1.15e-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: 1.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 504 LVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQ 583
Cdd:cd18794  21 LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVR 100

                        90       100       110
                ....*....|....*....|....*....|....
gi 33859536 584 HVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 617
Cdd:cd18794 101 FVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
276-606 4.88e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 72.24  E-value: 4.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 276 IAKAGYTKLTPVQKYSIP-IVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGItasrfkelqepeCIIVAPTRELINQI 354
Cdd:COG1204  15 LKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK------------ALYIVPLRALASEK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 355 YLEARKF--SFGtcVRAVVIYGGTQfghSVRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEAdRML-DMGFGP 431
Cdd:COG1204  83 YREFKRDfeELG--IKVGVSTGDYD---SDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLIdDESRGP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 432 --EM---KKLISCPGMpskeqrQTLLFSATF--PEEIQR-LAGDFLKSSY------LFVAVGQV-----GGACRD----- 487
Cdd:COG1204 157 tlEVllaRLRRLNPEA------QIVALSATIgnAEEIAEwLDAELVKSDWrpvplnEGVLYDGVlrfddGSRRSKdptla 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 488 -VQQTILQVGQ-----YSKR------EKLVEILRNIGDErtmvfvETKKKADFIATFL--CQEKISTTSI---------- 543
Cdd:COG1204 231 lALDLLEEGGQvlvfvSSRRdaeslaKKLADELKRRLTP------EEREELEELAEELleVSEETHTNEKladclekgva 304

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33859536 544 --HGD--REQRER-EQAlgdFRCGKCPVLVATSVAARGLdieN--VQHVI------NFDLPSTIDEYVHRIGRTGR 606
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 ...
 298-456 8.63e-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: 8.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 298 GRDLMACAQTGSGKTAAFLLPILAHMmrdgitasrfkELQEPECIIVAPTRELINQIYLEARKFsFGTCVRAVVIYGGTQ 377
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLL-----------LKKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSS 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 378 FGHSVRQIVQGCNILCATPGRL-MDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRqtLLFSAT 456
Cdd:cd00046  69 AEEREKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV--ILLSAT 146
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 499-602 7.30e-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: 7.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 499 SKREKLVEILRNI--GDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDF-RCGKCPV-LVATSVAA 574
Cdd:cd18793  11 GKLEALLELLEELrePGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnEDPDIRVfLLSTKAGG 90

                        90       100       110
                ....*....|....*....|....*....|....
gi 33859536 575 RGLDIENVQHVINFDLP--STIDEY----VHRIG 602
Cdd:cd18793  91 VGLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 265-614 9.34e-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: 9.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 265 EANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD-GITAsrfkelqepecII 343
Cdd:COG1205  38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDpGATA-----------LY 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 344 VAPTRELINQIYLEARKF--SFGTCVRAVVIYGGTQfGHSVRQIVQGCNILCATPgrlmDII------GKEKIG--LKQV 413
Cdd:COG1205 107 LYPTKALARDQLRRLRELaeALGLGVRVATYDGDTP-PEERRWIREHPDIVLTNP----DMLhygllpHHTRWArfFRNL 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 414 KYLVLDEA---------------DRMLDMgfgpeMKKLISCPgmpskeqrQTLLFSATF--PEEI-QRLAGDflkssyLF 475
Cdd:COG1205 182 RYVVIDEAhtyrgvfgshvanvlRRLRRI-----CRHYGSDP--------QFILASATIgnPAEHaERLTGR------PV 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 476 VAVGQVGGAC--RDVqqtIL----QVGQYSKREKLVE---ILRNIGDE--RTMVFVETKKKADFIATFL---CQEKISTT 541
Cdd:COG1205 243 TVVDEDGSPRgeRTF---VLwnppLVDDGIRRSALAEaarLLADLVREglRTLVFTRSRRGAELLARYArraLREPDLAD 319

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33859536 542 SIHGDR------EQREREQALgdfRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAI 614
Cdd:COG1205 320 RVAAYRagylpeERREIERGL---RSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 280-618 3.22e-11

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 66.66  E-value: 3.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  280 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPTRELI-NQI-YLE 357
Cdd:PRK11057  22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL---VLDGLT------------LVVSPLISLMkDQVdQLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  358 ARKFSfGTCVRAvviyggTQFGHSVRQIVQGCN-----ILCATPGRLM--DIIgkEKIGLKQVKYLVLDEADRMLDMG-- 428
Cdd:PRK11057  87 ANGVA-AACLNS------TQTREQQLEVMAGCRtgqikLLYIAPERLMmdNFL--EHLAHWNPALLAVDEAHCISQWGhd 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  429 FGPEMKKL----ISCPGMPskeqrqTLLFSATFPEEIQRlagDFLKSSYLFVAVGQVGGACR-DVQQTILQvgqysKREK 503
Cdd:PRK11057 158 FRPEYAALgqlrQRFPTLP------FMALTATADDTTRQ---DIVRLLGLNDPLIQISSFDRpNIRYTLVE-----KFKP 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536  504 LVEILRNIGDERT---MVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 580
Cdd:PRK11057 224 LDQLMRYVQEQRGksgIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKP 303

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 33859536  581 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 618
Cdd:PRK11057 304 NVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 284-421 2.06e-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: 2.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 284 LTPVQKYSI-PIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITasrfkelqepeCIIVAPTRELINQIYLEARKFS 362
Cdd:cd17921   2 LNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK-----------AVYIAPTRALVNQKEADLRERF 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 363 FGTCVRAVVIYGGTQFGhsvRQIVQGCNILCATPGRLMDIIGKEKI-GLKQVKYLVLDEA 421
Cdd:cd17921  71 GPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 499-604 5.64e-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: 5.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 499 SKREKLVEILRNI--GDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGK-CPV-LVATSVAA 574
Cdd:COG0553 533 AKLEALLELLEELlaEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLKAGG 612

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 33859536 575 RGLdieNVQ---HVINFDLP-------STIDEyVHRIGRT 604
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 ...
 566-606 5.67e-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: 5.67e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 33859536 566 VLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 606
Cdd:cd18785  25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
 305-603 1.20e-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: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 305 AQTGSGKTAAFLLPILAHMMRDGitASRFkelqepecIIVAPTRELINQIYLEARKFSFGtcvrAVVIYGGTQFGHSVRQ 384
Cdd:COG1203 154 APTGGGKTEAALLFALRLAAKHG--GRRI--------IYALPFTSIINQTYDRLRDLFGE----DVLLHHSLADLDLLEE 219

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 385 IVQGCN---------------ILCATPGRLMDII-----GKEKIGLKQV-KYLVLDEADrMLDMGFGPEMKKLIscpgmp 443
Cdd:COG1203 220 EEEYESearwlkllkelwdapVVVTTIDQLFESLfsnrkGQERRLHNLAnSVIILDEVQ-AYPPYMLALLLRLL------ 292

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 444 sKEQRQ----TLLFSATFPEEIQrlagDFLKSSYLFV--AVGQVGGACRDVQQTILQV--GQYSkREKLVEILRNI--GD 513
Cdd:COG1203 293 -EWLKNlggsVILMTATLPPLLR----EELLEAYELIpdEPEELPEYFRAFVRKRVELkeGPLS-DEELAELILEAlhKG 366

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 514 ERTMVFVETKKKAdfIATF-LCQEKISTTSIH--------GDREQREREqALGDFRCGKCPVLVATSVAARGLDienvqh 584
Cdd:COG1203 367 KSVLVIVNTVKDA--QELYeALKEKLPDEEVYllhsrfcpADRSEIEKE-IKERLERGKPCILVSTQVVEAGVD------ 437

                       330       340
                ....*....|....*....|...
gi 33859536 585 vINFDL----PSTIDEYVHRIGR 603
Cdd:COG1203 438 -IDFDVvirdLAPLDSLIQRAGR 459
PRK13767 PRK13767
ATP-dependent helicase; Provisional
 281-355 2.66e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 54.12  E-value: 2.66e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33859536  281 YTKLTPVQKYSIPIVLAGRDLMACAQTGSGKT-AAFLLPIlahmmRDGITASRFKELQEP-ECIIVAPTRELINQIY 355
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 ...
 280-463 4.56e-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: 4.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 280 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPTRELIN-QIY-LE 357
Cdd:cd17920   9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL---LLDGVT------------LVVSPLISLMQdQVDrLQ 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 358 ARkfsfgtCVRAVVIYGGTQFgHSVRQIVQGC-----NILCATPGRLMDIIGKEKIG----LKQVKYLVLDEADRMLDMG 428
Cdd:cd17920  74 QL------GIRAAALNSTLSP-EEKREVLLRIkngqyKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHCVSQWG 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 33859536 429 --FGPEMKKLIS----CPGMPskeqrqTLLFSATFPEEIQR 463
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 ...
 283-456 6.70e-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: 6.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 283 KLTPVQKYSIPIVLAG------RDLMACAQTGSGKTAAFLLPILAhmmrdgiTASRFKELqepecIIVAPTRELINQIYL 356
Cdd:cd17918  15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL-------AYKNGKQV-----AILVPTEILAHQHYE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 357 EARK-FSFgtcVRAVVIYGGTQfghsvRQIVQGCNILCATPGRLMDIIGKEKIGLkqvkyLVLDEADRmldmgFGPEMKK 435
Cdd:cd17918  83 EARKfLPF---INVELVTGGTK-----AQILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHR-----FGVAQRE 144

                       170       180
                ....*....|....*....|.
gi 33859536 436 LISCPGMPSkeqrqTLLFSAT 456
Cdd:cd17918 145 ALYNLGATH-----FLEATAT 160
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
281-337 1.29e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 52.03  E-value: 1.29e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 33859536 281 YTKLTPVQKYSIPIVLAGRDLMACAQTGSGKT-AAFlLPILAHMMRDGITASRFKELQ 337
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 ...
 288-421 1.39e-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: 1.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 288 QKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD-GITAsrfkelqepecIIVAPTRELIN-QI-YLEARKFSFG 364
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDpGSRA-----------LYLYPTKALAQdQLrSLRELLEQLG 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33859536 365 TCVRAVVIYGGTQfgHSVRQ--IVQGCNILCATPGRLMDII----GKEKIGLKQVKYLVLDEA 421
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) ...
 513-621 1.70e-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: 1.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 513 DERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFD--- 589
Cdd:cd18790  27 GERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadk 106

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 33859536 590 ---LPSTiDEYVHRIGRTGRCGNtGRAISFFD--TDS 621
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 ...
 298-420 4.82e-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: 4.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 298 GRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkelqepeCIIVAPTRELINQIY--LEARKFSFGTCVRAVVIYGG 375
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------VLYISPLKALINDQErrLEEPLDEIDLEIPVAVRHGD 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 33859536 376 TQFGHSVRQIVQGCNILCATPGRLMDIIGKEKIG--LKQVKYLVLDE 420
Cdd:cd17922  73 TSQSEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 511-603 6.66e-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: 6.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 511 IGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQA---LGDFRCGKCPVLVATSVAARGLDIENVQHVIn 587
Cdd:cd18799   4 YVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV- 82

                        90
                ....*....|....*...
gi 33859536 588 FDLP--STIdEYVHRIGR 603
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 ...
 506-606 8.40e-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: 8.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 506 EILRNIGDERTM-VFVETKKKADFIAT---FLCQEKISTTSI---HG--DREQRER-EQAL--GDFRcgkcpVLVATSVA 573
Cdd:cd18796  30 EVIFLLERHKSTlVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAALkrGDLK-----VVVATSSL 104

                        90       100       110
                ....*....|....*....|....*....|...
gi 33859536 574 ARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 606
Cdd:cd18796 105 ELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 493-617 2.37e-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: 2.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 493 LQVGQYSKREKLVEILRNIGD-ERTMVFVETKKKADFIAtflcqEKISTTSIHGDREQREREQALGDFRCGKCPVLVATS 571
Cdd:cd18789  28 LAAMNPNKLRALEELLKRHEQgDKIIVFTDNVEALYRYA-----KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSK 102

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 33859536 572 VAARGLDI--ENVQHVINFDLPSTiDEYVHRIGRTGRCGNTGRAISFF 617
Cdd:cd18789 103 VGDEGIDLpeANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
ResIII pfam04851
Type III restriction enzyme, res subunit;
283-459 3.08e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 44.97  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536   283 KLTPVQKYSIPIVLAGRDL--------MAcaqTGSGKT--AAFllpilahmmrdgITASRFKELQEPECIIVAPTRELIN 352
Cdd:pfam04851   3 ELRPYQIEAIENLLESIKNgqkrglivMA---TGSGKTltAAK------------LIARLFKKGPIKKVLFLVPRKDLLE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536   353 QIYLEARKFsFGTCVRAVVIYGGTqfghSVRQIVQGCNILCATPGRLMDII--GKEKIGLKQVKYLVLDEADRmldmGFG 430
Cdd:pfam04851  68 QALEEFKKF-LPNYVEIGEIISGD----KKDESVDDNKIVVTTIQSLYKALelASLELLPDFFDVIIIDEAHR----SGA 138

                         170       180       190
                  ....*....|....*....|....*....|
gi 33859536   431 PEMKKLIscpgmpSKEQRQTLL-FSATFPE 459
Cdd:pfam04851 139 SSYRNIL------EYFKPAFLLgLTATPER 162
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 299-421 8.17e-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: 8.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 299 RDLMACAQTGSGKT--AAFLLPILAHmmrdgitasRFKELQEPECIIV--APTRELINQiylEARKFSFGTCVRAVVIYG 374
Cdd:cd18034  17 RNTIVVLPTGSGKTliAVMLIKEMGE---------LNRKEKNPKKRAVflVPTVPLVAQ---QAEAIRSHTDLKVGEYSG 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 33859536 375 GTQFGHSVRQIVQGC----NILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 421
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 ...
 280-420 1.60e-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: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 280 GYTKLTPVQKYSIPIVLAGRD-LMACAQTGSGKTAAFLLPIL----AHMMRDG-ITASRFKelqepeCIIVAPTRELINQ 353
Cdd:cd18019  14 GFKSLNRIQSKLFPAAFETDEnLLLCAPTGAGKTNVALLTILreigKHRNPDGtINLDAFK------IVYIAPMKALVQE 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33859536 354 IY--LEARKFSFGTCVRAVViyGGTQFghSVRQIVQgCNILCATPGRlMDII---GKEKIGLKQVKYLVLDE 420
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 ...
 299-396 1.62e-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: 1.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 299 RDLMACAQTGSGKTAAFLLPILaHMMRDGITASRFKelqePECIIVAPTRELINQIYLEAR-KFS-FGTCVraVVIYGGT 376
Cdd:cd18023  18 KNFVVSAPTGSGKTVLFELAIL-RLLKERNPLPWGN----RKVVYIAPIKALCSEKYDDWKeKFGpLGLSC--AELTGDT 90

                        90       100
                ....*....|....*....|
gi 33859536 377 QFGhSVRQIvQGCNILCATP 396
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 ...
 543-603 5.59e-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: 5.59e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33859536 543 IHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIEN-----VQHVINFDLpSTIDEYVHRIGR 603
Cdd:cd18811  67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGL-SQLHQLRGRVGR 131
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
 298-361 1.08e-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: 1.08e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33859536 298 GRDLMACAQTGSGKTAAFLLPILAHMMRDGItasrfkelqePECIIVAPTRELINQIYLEARKF 361
Cdd:cd17930   1 PGLVILEAPTGSGKTEAALLWALKLAARGGK----------RRIIYALPTRATINQMYERIREI 54
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 302-423 1.10e-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: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 302 MACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqePECIIVAPTRELINQIYLEARKFsFGTCVRAVVIYGGTQfGHS 381
Cdd:cd18035  20 LIVLPTGLGKTIIAILVAADRLTKKG-----------GKVLILAPSRPLVEQHAENLKRV-LNIPDKITSLTGEVK-PEE 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 33859536 382 VRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADR 423
Cdd:cd18035  87 RAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 307-421 1.18e-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: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 307 TGSGKTA-AFLLPIlahmmrdgitasrfkELQEPECIIVAPTRELINQIYLEARKFSFGtcvraVVIYggtQFGHSVRQI 385
Cdd:cd17926  27 TGSGKTLtALALIA---------------YLKELRTLIVVPTDALLDQWKERFEDFLGD-----SSIG---LIGGGKKKD 83

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33859536 386 VQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 421
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 ...
 515-609 1.88e-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: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 515 RTMVFVETKKKADFIATFLCQEKIST----TSIHGDR------EQREREQalgDFRCGKCPVLVATSVAARGLDIENVQH 584
Cdd:cd18797  37 KTIVFCRSRKLAELLLRYLKARLVEEgplaSKVASYRagylaeDRREIEA---ELFNGELLGVVATNALELGIDIGGLDA 113

                        90       100
                ....*....|....*....|....*
gi 33859536 585 VINFDLPSTIDEYVHRIGRTGRCGN 609
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 ...
 543-582 2.22e-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: 2.22e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 33859536 543 IHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENV 582
Cdd:cd18792  66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA 105
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
 542-605 2.36e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.45  E-value: 2.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33859536   542 SIHGD--REQR-EREQAL--GDFRCgkcpvLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTG 605
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 ...
 289-423 2.44e-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: 2.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 289 KYSIPIVLA---GRDLMACAQTGSGKTAafllpILAHMMRDGITasRFKELQEPECIIVAPTRELINQiylEARKFS--F 363
Cdd:cd17927   5 NYQLELAQPalkGKNTIICLPTGSGKTF-----VAVLICEHHLK--KFPAGRKGKVVFLANKVPLVEQ---QKEVFRkhF 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33859536 364 GTCVRAVV-IYGGTQFGHSVRQIVQGCNILCATPGRLM-DIIGKEKIGLKQVKYLVLDEADR 423
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 ...
 304-438 2.55e-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: 2.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 304 CAQTGSGKTAAFLLPILAHmmrdgitasrFKELQEPECIIVAPTRELINQIYLE-ARKFSFGTCVRAVVIYGGTQfghSV 382
Cdd:cd18021  25 GAPTGSGKTVCAELALLRH----------WRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLGKKVVKLTGETS---TD 91

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 33859536 383 RQIVQGCNILCATPGRLmDIIG---KEKIGLKQVKYLVLDEAdRMLDMGFGPEMKKLIS 438
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; ...
 300-470 3.25e-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: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 300 DLMACAQTGSGKTAAFLLPILaHMMRDGITASRFKELQEPECIIVAPTRELINQI--YLEARKFSFGTCVRAVViyGGTQ 377
Cdd:cd18020  19 NMLICAPTGAGKTNIAMLTIL-HEIRQHVNQGGVIKKDDFKIVYIAPMKALAAEMveKFSKRLAPLGIKVKELT--GDMQ 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859536 378 FghsVRQIVQGCNILCATPGRlMDIIGKEKIG----LKQVKYLVLDEAdRMLDMGFGPEMKKLIScPGMPSKEQRQTLL- 452
Cdd:cd18020  96 L---TKKEIAETQIIVTTPEK-WDVVTRKSSGdvalSQLVRLLIIDEV-HLLHDDRGPVIESLVA-RTLRQVESTQSMIr 169

                       170       180
                ....*....|....*....|.
gi 33859536 453 ---FSATFPEEIQrlAGDFLK 470
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH