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Conserved domains on  [gi|262118318|ref|NP_001160006|]
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probable ATP-dependent RNA helicase DDX4 isoform 4 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030645)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 108-360 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: 547.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 108 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGS 187
Cdd:cd18052   12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 188 GKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGC 267
Cdd:cd18052   92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 268 NILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFL 347
Cdd:cd18052  172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                        250
                 ....*....|...
gi 262118318 348 KSNYLFVAVGQVG 360
Cdd:cd18052  252 KEDYLFLTVGRVG 264
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 366-495 5.88e-58

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: 189.64  E-value: 5.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 366 VQQTVLQVGQFSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPV 444
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 262118318 445 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 495
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 ...
 108-360 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: 547.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 108 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGS 187
Cdd:cd18052   12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 188 GKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGC 267
Cdd:cd18052   92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 268 NILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFL 347
Cdd:cd18052  172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                        250
                 ....*....|...
gi 262118318 348 KSNYLFVAVGQVG 360
Cdd:cd18052  252 KEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
140-496 1.65e-156

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 454.22  E-value: 1.65e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 140 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITAsrfkelqePEC 219
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------PQA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 220 IIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEA 299
Cdd:COG0513   75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 300 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLMFSATFPEEIQRLAAEFLKsNYLFVAVGQVGGACRDVQQTVLQVGQFSK 378
Cdd:COG0513  155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDK 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 379 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIE 458
Cdd:COG0513  229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 262118318 459 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 496
Cdd:COG0513  309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT 346
PTZ00110 PTZ00110
helicase; Provisional
 129-530 1.78e-118

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 361.40  E-value: 1.78e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 129 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmhdgITA 208
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INA 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 209 S-RFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIG 287
Cdd:PTZ00110 195 QpLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 288 LKQIKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFVAVGQVG-GACRDV 366
Cdd:PTZ00110 275 LRRVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNI 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 367 QQTVLQVGQFSKREKLVEILRNIGDE--RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPV 444
Cdd:PTZ00110 351 KQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPI 430

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 445 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESdNHLAQPLVKVLTDAQQDVPAWLEE 524
Cdd:PTZ00110 431 MIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK-YRLARDLVKVLREAKQPVPPELEK 509


                 ....*.
gi 262118318 525 IAFSTY 530
Cdd:PTZ00110 510 LSNERS 515
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 163-342 6.73e-62

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: 201.32  E-value: 6.73e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318  163 TPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMhdgitasrfKELQEPECIIVAPTRELVNQIYLEARKFSFG 242
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD---------KLDNGPQALVLAPTRELAEQIYEELKKLGKG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318  243 TCVRAVVIYGGTQLGHSIRQIvQGCNILCATPGRLMDIIGKEKiGLKQIKYLVLDEADRMLDMGFGPEMKKLISCpgMPs 322
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146

                         170       180
                  ....*....|....*....|
gi 262118318  323 kEQRQTLMFSATFPEEIQRL 342
Cdd:pfam00270 147 -KKRQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 366-495 5.88e-58

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: 189.64  E-value: 5.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 366 VQQTVLQVGQFSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPV 444
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 262118318 445 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 495
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
154-357 1.01e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 178.45  E-value: 1.01e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318   154 IAKAGYTKLTPVQKYSIPIILAG-RDLMACAQTGSGKTAAFLLPILAHmmhdgitasrFKELQEPECIIVAPTRELVNQI 232
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA----------LKRGKGGRVLVLVPTRELAEQW 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318   233 YLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGC-NILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEM 311
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 262118318   312 KKLIScpgmPSKEQRQTLMFSATFPEEIQRLAAEFLKsNYLFVAVG 357
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLN-DPVFIDVG 191
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 377-486 1.10e-37

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 134.65  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318  377 SKREKLVEILRNIGDERTMVFVETKKKADfIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLD 456
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 262118318  457 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 486
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
405-486 5.73e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 106.91  E-value: 5.73e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318   405 DFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 484
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 262118318   485 CG 486
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
374-492 1.37e-19

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 92.87  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 374 GQFSKREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKISTTSIHG--DRE------QREREQALGDFRFGK 441
Cdd:COG1111  332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 262118318 442 CPVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNTGRAI 492
Cdd:COG1111  412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
PRK13766 PRK13766
Hef nuclease; Provisional
 378-492 5.02e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.38  E-value: 5.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 378 KREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKIST------TSIHGDREQREREQ--ALGDFRFGKCPVL 445
Cdd:PRK13766 348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGMSQKEQieILDKFRAGEFNVL 427

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 262118318 446 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 492
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 ...
 108-360 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: 547.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 108 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGS 187
Cdd:cd18052   12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 188 GKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGC 267
Cdd:cd18052   92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 268 NILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFL 347
Cdd:cd18052  172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251

                        250
                 ....*....|...
gi 262118318 348 KSNYLFVAVGQVG 360
Cdd:cd18052  252 KEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
140-496 1.65e-156

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 454.22  E-value: 1.65e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 140 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITAsrfkelqePEC 219
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------PQA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 220 IIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEA 299
Cdd:COG0513   75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 300 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLMFSATFPEEIQRLAAEFLKsNYLFVAVGQVGGACRDVQQTVLQVGQFSK 378
Cdd:COG0513  155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDK 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 379 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIE 458
Cdd:COG0513  229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 262118318 459 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 496
Cdd:COG0513  309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT 346
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 140-360 7.39e-149

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: 426.90  E-value: 7.39e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 140 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITAS-RFKELQEPE 218
Cdd:cd17967    1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgRGRRKAYPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 219 CIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDE 298
Cdd:cd17967   81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 262118318 299 ADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFLKsNYLFVAVGQVG 360
Cdd:cd17967  161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
PTZ00110 PTZ00110
helicase; Provisional
 129-530 1.78e-118

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 361.40  E-value: 1.78e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 129 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmhdgITA 208
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INA 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 209 S-RFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIG 287
Cdd:PTZ00110 195 QpLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 288 LKQIKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFVAVGQVG-GACRDV 366
Cdd:PTZ00110 275 LRRVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNI 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 367 QQTVLQVGQFSKREKLVEILRNIGDE--RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPV 444
Cdd:PTZ00110 351 KQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPI 430

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 445 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESdNHLAQPLVKVLTDAQQDVPAWLEE 524
Cdd:PTZ00110 431 MIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK-YRLARDLVKVLREAKQPVPPELEK 509


                 ....*.
gi 262118318 525 IAFSTY 530
Cdd:PTZ00110 510 LSNERS 515
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 119-360 3.67e-117

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: 347.41  E-value: 3.67e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 119 FDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPIL 198
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 199 AHMMHDG-----ITASRF--KELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILC 271
Cdd:cd18051   81 SQIYEQGpgeslPSESGYygRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 272 ATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFLkSNY 351
Cdd:cd18051  161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFL-DNY 239


                 ....*....
gi 262118318 352 LFVAVGQVG 360
Cdd:cd18051  240 IFLAVGRVG 248
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 141-495 5.52e-103

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 318.67  E-value: 5.52e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 141 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmhdgITASRFKelqePECI 220
Cdd:PRK11776   6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK-----LDVKRFR----VQAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 221 IVAPTRELVNQIYLEARKFSFGT-CVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEA 299
Cdd:PRK11776  77 VLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 300 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLMFSATFPEEIQRLAAEFLKsNYLFVAVGQVGGAcRDVQQTVLQVGQFSK 378
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRqAP-----ARRQTLLFSATYPEGIAAISQRFQR-DPVEVKVESTHDL-PAIEQRFYEVSPDER 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 379 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIE 458
Cdd:PRK11776 230 LPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 262118318 459 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 495
Cdd:PRK11776 310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLV 346
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 140-494 9.37e-90

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 283.37  E-value: 9.37e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 140 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMmhdgITASRFKELQePEC 219
Cdd:PRK11192   2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL----LDFPRRKSGP-PRI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 220 IIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEA 299
Cdd:PRK11192  77 LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 300 DRMLDMGFGPEMKKLiscpgmpSKEQR---QTLMFSATFP-EEIQRLAAEFLKsNYLFVAVgqvggacrdvqqtvlqvgQ 375
Cdd:PRK11192 157 DRMLDMGFAQDIETI-------AAETRwrkQTLLFSATLEgDAVQDFAERLLN-DPVEVEA------------------E 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 376 FSKREK-------------------LVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGD 436
Cdd:PRK11192 211 PSRRERkkihqwyyraddlehktalLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKR 290

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 262118318 437 FRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 494
Cdd:PRK11192 291 LTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 154-493 4.07e-89

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 282.47  E-value: 4.07e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITAsrfKELQEPECIIVAPTRELVNQIY 233
Cdd:PRK10590  16 VAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHA---KGRRPVRALILTPTRELAAQIG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 LEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKK 313
Cdd:PRK10590  93 ENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRR 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 314 LIScpGMPSKeqRQTLMFSATFPEEIQRLAAEFLKsNYLFVAVGQVGGACRDVQQTVLQVGQFSKREKLVEILRNIGDER 393
Cdd:PRK10590 173 VLA--KLPAK--RQNLLFSATFSDDIKALAEKLLH-NPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGKGNWQQ 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 394 TMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTID 473
Cdd:PRK10590 248 VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPE 327

                        330       340
                 ....*....|....*....|
gi 262118318 474 EYVHRIGRTGRCGNTGRAIS 493
Cdd:PRK10590 328 DYVHRIGRTGRAAATGEALS 347
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 124-531 2.17e-88

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 282.83  E-value: 2.17e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 124 TILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAH--- 200
Cdd:PLN00206 106 KLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcct 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 201 MMHDGITASRfkelqEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDI 280
Cdd:PLN00206 186 IRSGHPSEQR-----NPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDL 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 281 IGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPskeqrQTLMFSATFPEEIQRLAAEFLKsNYLFVAVGQVG 360
Cdd:PLN00206 261 LSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAK-DIILISIGNPN 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 361 GACRDVQQTVLQVGQFSKREKLVEILRNIGDER--TMVFVETKKKADFIAtflcqEKISTT------SIHGDREQREREQ 432
Cdd:PLN00206 335 RPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLA-----NAITVVtglkalSIHGEKSMKERRE 409

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 433 ALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDNhLAQPLVKVLT 512
Cdd:PLN00206 410 VMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRN-LFPELVALLK 488

                        410
                 ....*....|....*....
gi 262118318 513 DAQQDVPawlEEIAFSTYI 531
Cdd:PLN00206 489 SSGAAIP---RELANSRYL 504
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 141-494 8.63e-88

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 279.87  E-value: 8.63e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 141 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFkeLQEPECI 220
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERY--MGEPRAL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 221 IVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQI-VQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEA 299
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 300 DRMLDMGFGPEMKKLIScpGMPSKEQRQTLMFSATFPEEIQRLAAEFLkSNYLFVAVGQVGGACRDVQQTVLQVGQFSKR 379
Cdd:PRK01297 247 DRMLDMGFIPQVRQIIR--QTPRKEERQTLLFSATFTDDVMNLAKQWT-TDPAIVEIEPENVASDTVEQHVYAVAGSDKY 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 380 EKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIEN 459
Cdd:PRK01297 324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 262118318 460 VQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 494
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 150-354 2.46e-87

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: 268.54  E-value: 2.46e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 150 LNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRfkelqEPECIIVAPTRELV 229
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGR-----GPQALVLAPTRELA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 230 NQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGP 309
Cdd:cd00268   76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEE 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 262118318 310 EMKKLIS-CPgmpskEQRQTLMFSATFPEEIQRLAAEFLKsNYLFV 354
Cdd:cd00268  156 DVEKILSaLP-----KDRQTLLFSATLPEEVKELAKKFLK-NPVRI 195
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 133-494 2.29e-78

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 257.96  E-value: 2.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 133 DAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFK 212
Cdd:PRK04537   3 DKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 213 ElqEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKI-GLKQI 291
Cdd:PRK04537  83 E--DPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHAC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 292 KYLVLDEADRMLDMGFGPEMKKLIScpGMPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFVAVGQVGGACRdVQQTVL 371
Cdd:PRK04537 161 EICVLDEADRMFDLGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR-VRQRIY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 372 QVGQFSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVA 451
Cdd:PRK04537 238 FPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVA 317

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 262118318 452 ARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 494
Cdd:PRK04537 318 ARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 154-494 2.86e-73

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 240.26  E-value: 2.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRfkELQEPECIIVAPTRELVNQIY 233
Cdd:PRK04837  23 LEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDR--KVNQPRALIMAPTRELAVQIH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 LEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKK 313
Cdd:PRK04837 101 ADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRW 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 314 LIScpGMPSKEQRQTLMFSATFPEEIQRLAAEFLKS-NYLFVAVGQVGGacRDVQQTVlqvgqF--SKREKLVEILRNIG 390
Cdd:PRK04837 181 LFR--RMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVEPEQKTG--HRIKEEL-----FypSNEEKMRLLQTLIE 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 391 DE---RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFD 467
Cdd:PRK04837 252 EEwpdRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYD 331

                        330       340
                 ....*....|....*....|....*..
gi 262118318 468 LPSTIDEYVHRIGRTGRCGNTGRAISF 494
Cdd:PRK04837 332 LPDDCEDYVHRIGRTGRAGASGHSISL 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 140-496 8.96e-70

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 236.67  E-value: 8.96e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 140 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMhdgitasrfKELQEPEC 219
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD---------PELKAPQI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 220 IIVAPTRELVNQIYLEARKFS-FGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDE 298
Cdd:PRK11634  78 LVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 299 ADRMLDMGFGPEMKKLIScpGMPskEQRQTLMFSATFPEEIQRLAAEFLKSNYLfVAVgQVGGACR-DVQQTVLQVGQFS 377
Cdd:PRK11634 158 ADEMLRMGFIEDVETIMA--QIP--EGHQTALFSATMPEAIRRITRRFMKEPQE-VRI-QSSVTTRpDISQSYWTVWGMR 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 378 KREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDI 457
Cdd:PRK11634 232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 262118318 458 ENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 496
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 ...
 154-354 5.63e-69

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: 221.09  E-value: 5.63e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDgitaSRFKELQEPECIIVAPTRELVNQIY 233
Cdd:cd17966    5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQ----PPLERGDGPIVLVLAPTRELAQQIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 LEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKK 313
Cdd:cd17966   81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 262118318 314 LIScpgmPSKEQRQTLMFSATFPEEIQRLAAEFLKsNYLFV 354
Cdd:cd17966  161 IVD----QIRPDRQTLMWSATWPKEVRRLAEDFLK-DYIQV 196
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 129-349 2.17e-62

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: 204.92  E-value: 2.17e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 129 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDgita 208
Cdd:cd17953    2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQ---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 209 SRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDII---GKEK 285
Cdd:cd17953   78 RPVKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262118318 286 IGLKQIKYLVLDEADRMLDMGFGPEMKKLIscpgMPSKEQRQTLMFSATFPEEIQRLAAEFLKS 349
Cdd:cd17953  158 TNLRRVTYVVLDEADRMFDMGFEPQIMKIV----NNIRPDRQTVLFSATFPRKVEALARKVLHK 217
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 163-342 6.73e-62

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: 201.32  E-value: 6.73e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318  163 TPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMhdgitasrfKELQEPECIIVAPTRELVNQIYLEARKFSFG 242
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD---------KLDNGPQALVLAPTRELAEQIYEELKKLGKG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318  243 TCVRAVVIYGGTQLGHSIRQIvQGCNILCATPGRLMDIIGKEKiGLKQIKYLVLDEADRMLDMGFGPEMKKLISCpgMPs 322
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146

                         170       180
                  ....*....|....*....|
gi 262118318  323 kEQRQTLMFSATFPEEIQRL 342
Cdd:pfam00270 147 -KKRQILLLSATLPRNLEDL 165
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 154-354 2.56e-61

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


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 201.66  E-value: 2.56e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILA-GRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFKelqePECIIVAPTRELVNQI 232
Cdd:cd17964    9 LTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSG----VSALIISPTRELALQI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 233 YLEARKF-SFGTCVRAVVIYGGTQLGHSIRQIV-QGCNILCATPGRLMDIIGKEKIG--LKQIKYLVLDEADRMLDMGFG 308
Cdd:cd17964   85 AAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLDMGFR 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 262118318 309 PEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFV 354
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 ...
 154-349 4.47e-61

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: 201.39  E-value: 4.47e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRfKELQEPECIIVAPTRELVNQIY 233
Cdd:cd17945    5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEE-TKDDGPYALILAPTRELAQQIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 LEARKFSFGTCVRAVVIYGGtqlgHSIRQIV----QGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGP 309
Cdd:cd17945   84 EETQKFAKPLGIRVVSIVGG----HSIEEQAfslrNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 262118318 310 EMKKLIScpGMPS------------------KEQRQTLMFSATFPEEIQRLAAEFLKS 349
Cdd:cd17945  160 QVTKILD--AMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRR 215
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 150-347 5.60e-61

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


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 200.33  E-value: 5.60e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 150 LNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMhdgitASRFKELQE-PECIIVAPTREL 228
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-----DQRELEKGEgPIAVIVAPTREL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 229 VNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFG 308
Cdd:cd17952   76 AQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFE 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 262118318 309 PEMKKLIScpgmPSKEQRQTLMFSATFPEEIQRLAAEFL 347
Cdd:cd17952  156 YQVRSIVG----HVRPDRQTLLFSATFKKKIEQLARDIL 190
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 127-357 1.21e-59

DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 198.31  E-value: 1.21e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 127 VEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGI 206
Cdd:cd18049   12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 207 tasrFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKI 286
Cdd:cd18049   92 ----LERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262118318 287 GLKQIKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLMFSATFPEEIQRLAAEFLKsNYLFVAVG 357
Cdd:cd18049  168 NLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLK-DYIHINIG 233
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 150-357 1.49e-58

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: 193.96  E-value: 1.49e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 150 LNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmhdgITASRFKElqEPECIIVAPTRELV 229
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQK-----LGKPRKKK--GLRALILAPTRELA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 230 NQIYLEARKFSFGTCVRAVVIYGGTQLG-HSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFG 308
Cdd:cd17957   74 SQIYRELLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFR 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 262118318 309 PEMKKLI-SCpgmpSKEQRQTLMFSATFPEEIQRLAAEFLKsNYLFVAVG 357
Cdd:cd17957  154 EQTDEILaAC----TNPNLQRSLFSATIPSEVEELARSVMK-DPIRIIVG 198
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 366-495 5.88e-58

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: 189.64  E-value: 5.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 366 VQQTVLQVGQFSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPV 444
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 262118318 445 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 495
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PTZ00424 PTZ00424
helicase 45; Provisional
 140-494 3.93e-55

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 191.58  E-value: 3.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 140 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDgitasrfkeLQEPEC 219
Cdd:PTZ00424  29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD---------LNACQA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 220 IIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEA 299
Cdd:PTZ00424 100 LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 300 DRMLDMGFGPEMKKLIScpGMPSkeQRQTLMFSATFPEEIQRLAAEFLKSNYLfVAVGQVGGACRDVQQTVLQVGQFS-K 378
Cdd:PTZ00424 180 DEMLSRGFKGQIYDVFK--KLPP--DVQVALFSATMPNEILELTTKFMRDPKR-ILVKKDELTLEGIRQFYVAVEKEEwK 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 379 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIE 458
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 262118318 459 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 494
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINF 370
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 127-357 7.03e-54

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: 184.06  E-value: 7.03e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 127 VEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDgi 206
Cdd:cd18050   50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQ-- 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 207 taSRFKELQEPECIIVAPTRELVNQIYLEArkFSFGTCVR--AVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKE 284
Cdd:cd18050  128 --PYLERGDGPICLVLAPTRELAQQVQQVA--DDYGKSSRlkSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAG 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262118318 285 KIGLKQIKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLMFSATFPEEIQRLAAEFLKsNYLFVAVG 357
Cdd:cd18050  204 KTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLR-DYVQINIG 271
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 154-348 3.51e-53

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: 179.76  E-value: 3.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHdgitasRFKELQEPECIIVAPTRELVNQIY 233
Cdd:cd17947    5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY------RPKKKAATRVLVLVPTRELAMQCF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 LEARKFS-FGTCVRAVVIyGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEK-IGLKQIKYLVLDEADRMLDMGFGPEM 311
Cdd:cd17947   79 SVLQQLAqFTDITFALAV-GGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADEL 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 262118318 312 KKLI-SCPgmpskEQRQTLMFSATFPEEIQRLAAEFLK 348
Cdd:cd17947  158 KEILrLCP-----RTRQTMLFSATMTDEVKDLAKLSLN 190
DEXDc smart00487
DEAD-like helicases superfamily;
154-357 1.01e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 178.45  E-value: 1.01e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318   154 IAKAGYTKLTPVQKYSIPIILAG-RDLMACAQTGSGKTAAFLLPILAHmmhdgitasrFKELQEPECIIVAPTRELVNQI 232
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA----------LKRGKGGRVLVLVPTRELAEQW 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318   233 YLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGC-NILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEM 311
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 262118318   312 KKLIScpgmPSKEQRQTLMFSATFPEEIQRLAAEFLKsNYLFVAVG 357
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLN-DPVFIDVG 191
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 153-348 7.87e-52

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: 176.12  E-value: 7.87e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 153 NIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMmhDGITASRFKElQEPECIIVAPTRELVNQI 232
Cdd:cd17958    4 EIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL--DLQPIPREQR-NGPGVLVLTPTRELALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 233 YLEARKFSFGTcVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMK 312
Cdd:cd17958   81 EAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 262118318 313 KLIscpgMPSKEQRQTLMFSATFPEEIQRLAAEFLK 348
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 ...
 140-348 1.37e-51

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: 175.57  E-value: 1.37e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 140 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHM-MHDGITASRfkelqepe 218
Cdd:cd17959    2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkAHSPTVGAR-------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 219 CIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDE 298
Cdd:cd17959   74 ALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDE 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 262118318 299 ADRMLDMGFGPEMKKLIScpGMPskEQRQTLMFSATFPEeiqrLAAEFLK 348
Cdd:cd17959  154 ADRLFEMGFAEQLHEILS--RLP--ENRQTLLFSATLPK----LLVEFAK 195
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 140-342 8.42e-51

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: 173.66  E-value: 8.42e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 140 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDgitASRFkelqepEC 219
Cdd:cd17954    1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---PQRF------FA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 220 IIVAPTRELVNQI--YLEARKFSFGtcVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEK-IGLKQIKYLVL 296
Cdd:cd17954   72 LVLAPTRELAQQIseQFEALGSSIG--LKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVM 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 262118318 297 DEADRMLDMGFGPEMKKLISCpgMPSkeQRQTLMFSATFPEEIQRL 342
Cdd:cd17954  150 DEADRLLNMDFEPEIDKILKV--IPR--ERTTYLFSATMTTKVAKL 191
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 141-354 1.52e-50

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 172.79  E-value: 1.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 141 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHD--GITAsrfkelqepe 218
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDpyGIFA---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 219 cIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDII---GKEKIGLKQIKYLV 295
Cdd:cd17955   71 -LVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTKVLSRVKFLV 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 262118318 296 LDEADRMLDMGFGPEMKKLISCpgMPSKeqRQTLMFSATFPEEIQRLAAEFLKSNYLFV 354
Cdd:cd17955  150 LDEADRLLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 146-354 3.44e-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: 169.69  E-value: 3.44e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 146 LCQTLNNNIakaGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDgitASRFKELQEPECIIVAPT 225
Cdd:cd17949    1 LVSHLKSKM---GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSL---EPRVDRSDGTLALVLVPT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 226 RELVNQIYLEARKF--SFGTCVRAVVIyGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEK-IGLKQIKYLVLDEADRM 302
Cdd:cd17949   75 RELALQIYEVLEKLlkPFHWIVPGYLI-GGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262118318 303 LDMGFGPEMKKLIS---------CPGMPSKEQRQTLMFSATFPEEIQRLaAEFLKSNYLFV 354
Cdd:cd17949  154 LDMGFEKDITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRL-AGLSLKDPVYI 213
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 154-343 1.20e-48

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


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 167.75  E-value: 1.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAhmmhdgITASRFKELQEPE--CIIVAPTRELVNQ 231
Cdd:cd17960    5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLE------ILLKRKANLKKGQvgALIISPTRELATQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 232 IYLEARKF--SFGTCVRAVVIYGGTQLGHSIRQIV-QGCNILCATPGRLMDIIG--KEKIGLKQIKYLVLDEADRMLDMG 306
Cdd:cd17960   79 IYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLG 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 262118318 307 FGPEMKKLISCpgMPskEQRQTLMFSATFPEEIQRLA 343
Cdd:cd17960  159 FEADLNRILSK--LP--KQRRTGLFSATQTDAVEELI 191
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 141-351 2.53e-48

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


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 166.70  E-value: 2.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 141 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPIL--AHMMHDGITAsrfkelqepe 218
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILekIDPKKDVIQA---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 219 cIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDE 298
Cdd:cd17940   71 -LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 262118318 299 ADRMLDMGFGPEMKKLIS-CPgmpskEQRQTLMFSATFPEEIQRLAAEFLKSNY 351
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 ...
 154-354 2.30e-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: 161.37  E-value: 2.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmmhDGITASRFKELQEPECIIVAPTRELVNQIY 233
Cdd:cd17942    5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-----ELLYKLKFKPRNGTGVIIISPTRELALQIY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 LEARKF------SFGTCVravviyGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGL-KQIKYLVLDEADRMLDMG 306
Cdd:cd17942   80 GVAKELlkyhsqTFGIVI------GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILEIG 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 262118318 307 FGPEMKKLISCpgMPSkeQRQTLMFSATFPEEIQRLAAEFLKSNYLFV 354
Cdd:cd17942  154 FEEEMRQIIKL--LPK--RRQTMLFSATQTRKVEDLARISLKKKPLYV 197
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 154-356 1.34e-45

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: 159.38  E-value: 1.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDgitasRFKELQEPECIIVAPTRELVNQIY 233
Cdd:cd17941    5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE-----RWTPEDGLGALIISPTRELAMQIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 LEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQgCNILCATPGRL---MDiigkEKIGL--KQIKYLVLDEADRMLDMGFG 308
Cdd:cd17941   80 EVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLlqhMD----ETPGFdtSNLQMLVLDEADRILDMGFK 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 262118318 309 PEMKKLIScpGMPSKeqRQTLMFSATFPEEIQRLAAEFLKsNYLFVAV 356
Cdd:cd17941  155 ETLDAIVE--NLPKS--RQTLLFSATQTKSVKDLARLSLK-NPEYISV 197
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 154-349 7.96e-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: 154.80  E-value: 7.96e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASrFKELQEPECIIVAPTRELVNQIY 233
Cdd:cd17951    5 LKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLP-FIKGEGPYGLIVCPSRELARQTH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 ---------LEARKFSfgtCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLD 304
Cdd:cd17951   84 evieyyckaLQEGGYP---QLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 262118318 305 MGFGPEMKKLISCpgmpSKEQRQTLMFSATFPEEIQrlaaEFLKS 349
Cdd:cd17951  161 MGFEEDIRTIFSY----FKGQRQTLLFSATMPKKIQ----NFAKS 197
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 150-348 2.03e-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: 153.47  E-value: 2.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 150 LNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMhdgitasrfKELQEPECIIVAPTRELV 229
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL---------TEHRNPSALILTPTRELA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 230 NQIYLEARKFSFGTC-VRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFG 308
Cdd:cd17962   72 VQIEDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQ 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 262118318 309 PEMKKLIScpgmPSKEQRQTLMFSATFPEEIQRLAAEFLK 348
Cdd:cd17962  152 QQVLDILE----NISHDHQTILVSATIPRGIEQLAGQLLQ 187
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 154-350 9.51e-42

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: 150.47  E-value: 9.51e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIP-IILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQI 232
Cdd:cd17946    5 LADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTRELAVQV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 233 --YLEA-RKFsfgTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGK--EKIG-LKQIKYLVLDEADRMLDMG 306
Cdd:cd17946   85 kdHLKAiAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEgnEHLAnLKSLRFLVLDEADRMLEKG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 262118318 307 FGPEMKKLISC---PGMPSKEQRQTLMFSATFPEEIQRLAAEFLKSN 350
Cdd:cd17946  162 HFAELEKILELlnkDRAGKKRKRQTFVFSATLTLDHQLPLKLNSKKK 208
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 141-349 2.10e-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: 2.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 141 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmmhdgitasrfkelQEPECI 220
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------QIVVAL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 221 IVAPTRELVNQIYLEARKFSF---GTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLD 297
Cdd:cd17938   65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 262118318 298 EADRMLDMGFGPEMKKLIS-CPGMPSKEQR-QTLMFSATF-PEEIQRLAAEFLKS 349
Cdd:cd17938  145 EADRLLSQGNLETINRIYNrIPKITSDGKRlQVIVCSATLhSFEVKKLADKIMHF 199
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 377-486 1.10e-37

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 134.65  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318  377 SKREKLVEILRNIGDERTMVFVETKKKADfIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLD 456
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 262118318  457 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 486
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 150-348 2.21e-36

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


Pssm-ID: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 134.24  E-value: 2.21e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 150 LNNNIAKA----GYTKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILahmmhdgitaSRFKE-LQEPECIIV 222
Cdd:cd17963    1 LKPELLKGlyamGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAML----------SRVDPtLKSPQALCL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 223 APTRELVNQIYLEARKFSFGT------CVRAVVIYGGTQLGHsirQIVQGcnilcaTPGRLMDIIGKEKIGLKQIKYLVL 296
Cdd:cd17963   71 APTRELARQIGEVVEKMGKFTgvkvalAVPGNDVPRGKKITA---QIVIG------TPGTVLDWLKKRQLDLKKIKILVL 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 262118318 297 DEADRMLDM-GFGPE---MKKLI--SCpgmpskeqrQTLMFSATFPEEIQRLAAEFLK 348
Cdd:cd17963  142 DEADVMLDTqGHGDQsirIKRMLprNC---------QILLFSATFPDSVRKFAEKIAP 190
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 154-349 6.86e-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: 133.48  E-value: 6.86e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDgiTASRFKElQEPECIIVAPTRELVNQIY 233
Cdd:cd17961    9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKA--KAESGEE-QGTRALILVPTRELAQQVS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 LEARKFSFGTC--VRAVVIYGGTqlgHSIRQIVQ---GCNILCATPGRLMDII-GKEKIGLKQIKYLVLDEADRMLDMGF 307
Cdd:cd17961   86 KVLEQLTAYCRkdVRVVNLSASS---SDSVQRALlaeKPDIVVSTPARLLSHLeSGSLLLLSTLKYLVIDEADLVLSYGY 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 262118318 308 GPEMKKLIS-CPGMPskeqrQTLMFSATFPEEIQRLAAEFLKS 349
Cdd:cd17961  163 EEDLKSLLSyLPKNY-----QTFLMSATLSEDVEALKKLVLHN 200
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 158-351 1.08e-35

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: 132.66  E-value: 1.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 158 GYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFKElqePECIIVAPTRELVNQIYLE-- 235
Cdd:cd17944    9 GVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRA---PKVLVLAPTRELANQVTKDfk 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 236 --ARKFSFgTCvravvIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKK 313
Cdd:cd17944   86 diTRKLSV-AC-----FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 262118318 314 LISCPGMPSKEQR-QTLMFSATFPEEIQRLAAEFLKSNY 351
Cdd:cd17944  160 ILSVSYKKDSEDNpQTLLFSATCPDWVYNVAKKYMKSQY 198
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 146-342 3.34e-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: 132.37  E-value: 3.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 146 LCQTLNNNiakaGYTKLTPVQKYSIPIILAG---------RDLMACAQTGSGKTAAFLLPILAHMMHDGITASRfkelqe 216
Cdd:cd17956    1 LLKNLQNN----GITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLR------ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 217 peCIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGC--------NILCATPGRLMD-IIGKEKIG 287
Cdd:cd17956   71 --ALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDhLNSTPGFT 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262118318 288 LKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQR----------------QTLMFSATF---PEEIQRL 342
Cdd:cd17956  149 LKHLRFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLgsfgdanllersvrplQKLLFSATLtrdPEKLSSL 222
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 154-349 9.55e-32

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: 122.07  E-value: 9.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGitasrfkelQEPECIIVAPTRELVNQIY 233
Cdd:cd17950   17 IVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD---------GQVSVLVICHTRELAFQIS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 LEARKFS-FGTCVRAVVIYGGTQLGHSIRQIVQGC-NILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDmgfGPEM 311
Cdd:cd17950   88 NEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE---QLDM 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 262118318 312 KKLI-----SCPgmpskEQRQTLMFSATFPEEIQRLAAEFLKS 349
Cdd:cd17950  165 RRDVqeifrATP-----HDKQVMMFSATLSKEIRPVCKKFMQD 202
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 153-337 5.07e-30

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 117.85  E-value: 5.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 153 NIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRfkELQEPECIIVAPTRELVNQI 232
Cdd:cd17948    4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEG--PFNAPRGLVITPSRELAEQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 233 YLEARKFSFGTCVRAVVIYGGTQLGhSIRQIVQG-CNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEM 311
Cdd:cd17948   82 GSVAQSLTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 262118318 312 KKLIS-CP-GMPSKEQR-------QTLMFSATFPE 337
Cdd:cd17948  161 SHFLRrFPlASRRSENTdgldpgtQLVLVSATMPS 195
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 143-347 5.14e-30

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: 116.65  E-value: 5.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 143 EANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAhmmhdgITASRFKELQepeCIIV 222
Cdd:cd17939    1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQ------RIDTTVRETQ---ALVL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 223 APTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRM 302
Cdd:cd17939   72 APTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEM 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 262118318 303 LDMGFGPEMKKLISCpgMPSKEqrQTLMFSATFPEEIQRLAAEFL 347
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 ...
 141-348 2.51e-29

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 114.85  E-value: 2.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 141 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHdgitasrfkELQEPECI 220
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDT---------SLKATQAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 221 IVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEAD 300
Cdd:cd18046   72 VLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEAD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 262118318 301 RMLDMGFGPEMKKLIScpGMPskEQRQTLMFSATFPEEIQRLAAEFLK 348
Cdd:cd18046  152 EMLSRGFKDQIYDIFQ--KLP--PDTQVVLLSATMPNDVLEVTTKFMR 195
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 141-347 8.56e-29

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: 113.33  E-value: 8.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 141 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAhmMHDgitasrfKELQEPECI 220
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ--CLD-------IQVRETQAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 221 IVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEAD 300
Cdd:cd18045   72 ILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEAD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 262118318 301 RMLDMGFgpemKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFL 347
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, ...
 154-354 1.28e-28

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: 112.74  E-value: 1.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLlpILAHMMHDgitasrfKELQEPECIIVAPTRELVNQIY 233
Cdd:cd17943    5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFV--VIALESLD-------LERRHPQVLILAPTREIAVQIH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 LEARKF-SFGTCVRAVVIYGGTQLGHSIRQIvQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMK 312
Cdd:cd17943   76 DVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 262118318 313 KLIScpGMPskEQRQTLMFSATFPEEIQRLAAEFLkSNYLFV 354
Cdd:cd17943  155 WIFS--SLP--KNKQVIAFSATYPKNLDNLLARYM-RKPVLV 191
HELICc smart00490
helicase superfamily c-terminal domain;
405-486 5.73e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 106.91  E-value: 5.73e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318   405 DFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 484
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 262118318   485 CG 486
Cdd:smart00490  81 AG 82
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 127-343 9.66e-22

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: 94.32  E-value: 9.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 127 VEVSGHD-APP--AILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILahm 201
Cdd:cd18048    3 VEVLQRDpTSPlfSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 202 mhdgitaSRFKELQE-PECIIVAPTRELVNQ---IYLEARKFsfgtCVRAVVIYG--GTQLGHSIRQIVQgcnILCATPG 275
Cdd:cd18048   80 -------SRVDALKLyPQCLCLSPTFELALQtgkVVEEMGKF----CVGIQVIYAirGNRPGKGTDIEAQ---IVIGTPG 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 276 RLMDIIGKEK-IGLKQIKYLVLDEADRMLDM-GFGPEMKKLIScpGMPSkeQRQTLMFSATFPEEIQRLA 343
Cdd:cd18048  146 TVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKR--SMPK--ECQMLLFSATFEDSVWAFA 211
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
158-498 1.01e-19

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 92.51  E-value: 1.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 158 GYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPilAHMMhDGITasrfkelqepecIIVAPtreLV----NQI- 232
Cdd:COG0514   14 GYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLP--ALLL-PGLT------------LVVSP---LIalmkDQVd 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 233 YLEARKfsfgtcVRAVVIyggtqlgHS----------IRQIVQG-CNILCATPGRLM-----DIIGKEKIGLkqikyLVL 296
Cdd:COG0514   76 ALRAAG------IRAAFL-------NSslsaeerrevLRALRAGeLKLLYVAPERLLnprflELLRRLKISL-----FAI 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 297 DEA--------DrmldmgFGPE---MKKLI-SCPGMPskeqrqTLMFSATFPEEIQRLAAEFLKSNYLFVavgQVGGACR 364
Cdd:COG0514  138 DEAhcisqwghD------FRPDyrrLGELReRLPNVP------VLALTATATPRVRADIAEQLGLEDPRV---FVGSFDR 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 365 D-VQQTVLQVGQFSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCP 443
Cdd:COG0514  203 PnLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVD 282

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 262118318 444 VLVATSvaARGL--DIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLE 498
Cdd:COG0514  283 VIVATI--AFGMgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 153-346 1.03e-19

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: 88.97  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 153 NIAKAGYTKL------TPVQKYSIPIILAGR----------------DLMACAQTGSGKTAAFLLPILAHMMHDGITASR 210
Cdd:cd17965   16 KEILKGSNKTdeeikpSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPFE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 211 FKELQE--------PECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTqlGHSIRQIVQ----GCNILCATPGRLM 278
Cdd:cd17965   96 EAEEEYesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGF--GPSYQRLQLafkgRIDILVTTPGKLA 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 262118318 279 DIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLIScpGMPSKEQrqtLMF-SATFPEEIQRLAAEF 346
Cdd:cd17965  174 SLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIK--RAPKLKH---LILcSATIPKEFDKTLRKL 237
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
374-492 1.37e-19

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 92.87  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 374 GQFSKREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKISTTSIHG--DRE------QREREQALGDFRFGK 441
Cdd:COG1111  332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 262118318 442 CPVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNTGRAI 492
Cdd:COG1111  412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
175-497 1.10e-18

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 89.70  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 175 AGRDLMACAQTGSGKTAAFLLpILAHMMHDGITasrfkelqepecIIVAPTRELVNQIYLEARKFsfgtcvravviYGGT 254
Cdd:COG1061   99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGKRV------------LVLVPRRELLEQWAEELRRF-----------LGDP 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 255 QLGHSIRQIvqGCNILCATPGRLMDIIGKEKIGlKQIKYLVLDEADRmldmGFGPEMKKLIScpgmpSKEQRQTLMFSAT 334
Cdd:COG1061  155 LAGGGKKDS--DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILE-----AFPAAYRLGLTAT 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 335 ------FPEEIQRL--------AAEFLKSNYL----FVAV-------GQVGGACRDVQQTVLQVGQFSKREKLVEILRNI 389
Cdd:COG1061  223 pfrsdgREILLFLFdgivyeysLKEAIEDGYLappeYYGIrvdltdeRAEYDALSERLREALAADAERKDKILRELLREH 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 390 GD-ERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDL 468
Cdd:COG1061  303 PDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP 382

                        330       340
                 ....*....|....*....|....*....
gi 262118318 469 PSTIDEYVHRIGRTGRCGNTGRAISFFDL 497
Cdd:COG1061  383 TGSPREFIQRLGRGLRPAPGKEDALVYDF 411
PRK13766 PRK13766
Hef nuclease; Provisional
 378-492 5.02e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.38  E-value: 5.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 378 KREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKIST------TSIHGDREQREREQ--ALGDFRFGKCPVL 445
Cdd:PRK13766 348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGMSQKEQieILDKFRAGEFNVL 427

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 262118318 446 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 492
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 140-343 9.02e-15

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 73.22  E-value: 9.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 140 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILAHMMhdgiTASRFKelqep 217
Cdd:cd18047    2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE----PANKYP----- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 218 ECIIVAPTRELVNQ---IYLEARKFsfgtcvravviYGGTQLGHSIR--QIVQGC----NILCATPGRLMDIIGKEK-IG 287
Cdd:cd18047   73 QCLCLSPTYELALQtgkVIEQMGKF-----------YPELKLAYAVRgnKLERGQkiseQIVIGTPGTVLDWCSKLKfID 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 262118318 288 LKQIKYLVLDEADRMLDMGfGPEMKKLISCPGMPskEQRQTLMFSATFPEEIQRLA 343
Cdd:cd18047  142 PKKIKVFVLDEADVMIATQ-GHQDQSIRIQRMLP--RNCQMLLFSATFEDSVWKFA 194
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 382-495 1.52e-14

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: 70.70  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 382 LVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQ 461
Cdd:cd18794   21 LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVR 100

                         90       100       110
                 ....*....|....*....|....*....|....
gi 262118318 462 HVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 495
Cdd:cd18794  101 FVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 376-481 4.46e-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: 69.54  E-value: 4.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 376 FSKREKLVEILRN----IGDERTMVFVET---------------KKKADFIATFLCQEKISTTSIHGDREQREREQALGD 436
Cdd:cd18802    6 IPKLQKLIEILREyfpkTPDFRGIIFVERratavvlsrllkehpSTLAFIRCGFLIGRGNSSQRKRSLMTQRKQKETLDK 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 262118318 437 FRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGR 481
Cdd:cd18802   86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 378-492 7.22e-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: 68.92  E-value: 7.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 378 KREKLVEILRNI-------GDERTMVFVETKKKADFIATFLCQEK--------ISTTSIHGDREQREREQ--ALGDFRFG 440
Cdd:cd18801   10 KLEKLEEIVKEHfkkkqegSDTRVIIFSEFRDSAEEIVNFLSKIRpgiratrfIGQASGKSSKGMSQKEQkeVIEQFRKG 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 262118318 441 KCPVLVATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 492
Cdd:cd18801   90 GYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR-KRQGRVV 140
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
154-484 3.86e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 71.85  E-value: 3.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 154 IAKAGYTKLTPVQKYSIP-IILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGItasrfkelqepeCIIVAPTRELVNQI 232
Cdd:COG1204   15 LKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK------------ALYIVPLRALASEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 233 YLEARKF--SFGtcVRAVVIYGGTQlghSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEAdRML-DMGFGP 309
Cdd:COG1204   83 YREFKRDfeELG--IKVGVSTGDYD---SDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLIdDESRGP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 310 --EM---KKLISCPGMpskeqrQTLMFSATF--PEEIQR-LAAEFLKSNYlfVAVGQVGGACRDVQQTVLQVGQFSKREK 381
Cdd:COG1204  157 tlEVllaRLRRLNPEA------QIVALSATIgnAEEIAEwLDAELVKSDW--RPVPLNEGVLYDGVLRFDDGSRRSKDPT 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 382 LVEILRNIGDE-RTMVFVETKKKA-----------------------DFIATFL--CQEKISTTSI------------HG 423
Cdd:COG1204  229 LALALDLLEEGgQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELleVSEETHTNEKladclekgvafhHA 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 262118318 424 D--REQRER-EQAlgdFRFGKCPVLVATSVAARGLdieN--VQHVI------NFDLPSTIDEYVHRIGRTGR 484
Cdd:COG1204  309 GlpSELRRLvEDA---FREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGR 374
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 176-334 1.18e-12

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: 65.50  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 176 GRDLMACAQTGSGKTAAFLLPILAHMmhdgitasrfkELQEPECIIVAPTRELVNQIYLEARKFsFGTCVRAVVIYGGTQ 255
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLL-----------LKKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 256 LGHSIRQIVQGCNILCATPGRL-MDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRqtLMFSAT 334
Cdd:cd00046   69 AEEREKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV--ILLSAT 146
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 377-480 8.41e-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: 62.88  E-value: 8.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 377 SKREKLVEILRNI--GDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDF-RFGKCPV-LVATSVAA 452
Cdd:cd18793   11 GKLEALLELLEELrePGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnEDPDIRVfLLSTKAGG 90

                         90       100       110
                 ....*....|....*....|....*....|....
gi 262118318 453 RGLDIENVQHVINFDLP--STIDEY----VHRIG 480
Cdd:cd18793   91 VGLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 158-496 1.03e-11

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 67.43  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 158 GYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmMHDGITasrfkelqepecIIVAPTREL----VNQiy 233
Cdd:PRK11057  22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL---VLDGLT------------LVVSPLISLmkdqVDQ-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 LEARKFSfGTCVRAvviyggTQLGHSIRQIVQGCN-----ILCATPGRLM--DIIgkEKIGLKQIKYLVLDEADRMLDMG 306
Cdd:PRK11057  85 LLANGVA-AACLNS------TQTREQQLEVMAGCRtgqikLLYIAPERLMmdNFL--EHLAHWNPALLAVDEAHCISQWG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 307 --FGPEMKKL----ISCPGMPskeqrqTLMFSATFPEEIQRLAAEFLksnylfvavgqvggacrDVQQTVLQVGQFSK-- 378
Cdd:PRK11057 156 hdFRPEYAALgqlrQRFPTLP------FMALTATADDTTRQDIVRLL-----------------GLNDPLIQISSFDRpn 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 379 -REKLVE-------ILRNIGDERT---MVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVA 447
Cdd:PRK11057 213 iRYTLVEkfkpldqLMRYVQEQRGksgIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVA 292

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 262118318 448 TSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 496
Cdd:PRK11057 293 TVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 143-492 1.63e-10

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: 64.09  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 143 EANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHD-GITAsrfkelqepecII 221
Cdd:COG1205   38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDpGATA-----------LY 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 222 VAPTRELVNQIYLEARKF--SFGTCVRAVVIYGGTQLghSIRQ-IVQGCNILCATPgrlmDII------GKEKIG--LKQ 290
Cdd:COG1205  107 LYPTKALARDQLRRLRELaeALGLGVRVATYDGDTPP--EERRwIREHPDIVLTNP----DMLhygllpHHTRWArfFRN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 291 IKYLVLDEA---------------DRMLDMgfgpeMKKLISCPgmpskeqrQTLMFSATF--PEEiqrLAAEFLKSNylF 353
Cdd:COG1205  181 LRYVVIDEAhtyrgvfgshvanvlRRLRRI-----CRHYGSDP--------QFILASATIgnPAE---HAERLTGRP--V 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 354 VAVGQVGGAC--RDVqqtVL----QVGQFSKREKLVE---ILRNIGDE--RTMVFVETKKKADFIATFL---CQEKISTT 419
Cdd:COG1205  243 TVVDEDGSPRgeRTF---VLwnppLVDDGIRRSALAEaarLLADLVREglRTLVFTRSRRGAELLARYArraLREPDLAD 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 262118318 420 SIHGDR------EQREREQALgdfRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAI 492
Cdd:COG1205  320 RVAAYRagylpeERREIERGL---RSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 377-482 3.55e-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: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 377 SKREKLVEILRNI--GDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGK-CPV-LVATSVAA 452
Cdd:COG0553  533 AKLEALLELLEELlaEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLKAGG 612

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 262118318 453 RGLdieNVQ---HVINFDLP-------STIDEyVHRIGRT 482
Cdd:COG0553  613 EGL---NLTaadHVIHYDLWwnpaveeQAIDR-AHRIGQT 648
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 162-299 4.23e-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: 56.12  E-value: 4.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 162 LTPVQKYSI-PIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITasrfkelqepeCIIVAPTRELVNQIYLEARKFS 240
Cdd:cd17921    2 LNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK-----------AVYIAPTRALVNQKEADLRERF 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 241 FGTCVRAVVIYGGTQlgHSIRQIvQGCNILCATPGRLMDIIGKEKI-GLKQIKYLVLDEA 299
Cdd:cd17921   71 GPLGKNVGLLTGDPS--VNKLLL-AEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 161-334 2.21e-08

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: 53.96  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 161 KLTPVQKYSIPIILAG------RDLMACAQTGSGKTAAFLLPILAhmmhdgiTASRFKELqepecIIVAPTRELVNQIYL 234
Cdd:cd17918   15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL-------AYKNGKQV-----AILVPTEILAHQHYE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 235 EARK-FSFgtcVRAVVIYGGTQlghsiRQIVQGCNILCATPGRLMDIIGKEKIGLkqikyLVLDEADRmldmgFGPEMKK 313
Cdd:cd17918   83 EARKfLPF---INVELVTGGTK-----AQILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHR-----FGVAQRE 144

                        170       180
                 ....*....|....*....|.
gi 262118318 314 LISCPGMPSkeqrqTLMFSAT 334
Cdd:cd17918  145 ALYNLGATH-----FLEATAT 160
PRK13767 PRK13767
ATP-dependent helicase; Provisional
 159-298 3.35e-08

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 56.43  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 159 YTKLTPVQKYSIPIILAGRDLMACAQTGSGKT-AAFLLPIlahmmHDGITASRFKELQEP-ECIIVAPTRELVNQIY--- 233
Cdd:PRK13767  30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAII-----DELFRLGREGELEDKvYCLYVSPLRALNNDIHrnl 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 234 ---LEArkfsfgtcVRAVVIYGGTQLG---HSIR-----------QIVQGCNILCATPGRLMDIIG----KEKigLKQIK 292
Cdd:PRK13767 105 eepLTE--------IREIAKERGEELPeirVAIRtgdtssyekqkMLKKPPHILITTPESLAILLNspkfREK--LRTVK 174


                 ....*.
gi 262118318 293 YLVLDE 298
Cdd:PRK13767 175 WVIVDE 180
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 444-484 8.04e-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: 49.62  E-value: 8.04e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 262118318 444 VLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 484
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
 183-481 1.96e-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: 53.93  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 183 AQTGSGKTAAFLLPILAHMMHDGitASRFkelqepecIIVAPTRELVNQIYLEARKFSFGtcvrAVVIYGGTQLGHSIRQ 262
Cdd:COG1203  154 APTGGGKTEAALLFALRLAAKHG--GRRI--------IYALPFTSIINQTYDRLRDLFGE----DVLLHHSLADLDLLEE 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 263 IVQGCN---------------ILCATPGRLMDII-----GKEKIgLKQIKY--LVLDEADrMLDMGFGPEMKKLIscpgm 320
Cdd:COG1203  220 EEEYESearwlkllkelwdapVVVTTIDQLFESLfsnrkGQERR-LHNLANsvIILDEVQ-AYPPYMLALLLRLL----- 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 321 psKEQRQT-----LMfSATFPEEIQrlaaEFLKSNYLFVavgqvggaCRDVQQTVLQVGQFSKR-----------EKLVE 384
Cdd:COG1203  293 --EWLKNLggsviLM-TATLPPLLR----EELLEAYELI--------PDEPEELPEYFRAFVRKrvelkegplsdEELAE 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 385 ILRNI--GDERTMVFVETKKKAdfIATF-LCQEKISTTSIH--------GDREQREREqALGDFRFGKCPVLVATSVAAR 453
Cdd:COG1203  358 LILEAlhKGKSVLVIVNTVKDA--QELYeALKEKLPDEEVYllhsrfcpADRSEIEKE-IKERLERGKPCILVSTQVVEA 434

                        330       340       350
                 ....*....|....*....|....*....|..
gi 262118318 454 GLDienvqhvINFDL----PSTIDEYVHRIGR 481
Cdd:COG1203  435 GVD-------IDFDVvirdLAPLDSLIQRAGR 459
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
159-232 2.62e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 53.57  E-value: 2.62e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262118318 159 YTKLTPVQKYSIPIILAGRDLMACAQTGSGKT-AAFlLPILAHMMHDGITASRFKELQepeCIIVAPTRELVNQI 232
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGLR---VLYISPLKALANDI 92
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 166-299 1.46e-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: 48.74  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 166 QKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHD-GITAsrfkelqepecIIVAPTRELVN-QI-YLEARKFSFG 242
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDpGSRA-----------LYLYPTKALAQdQLrSLRELLEQLG 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262118318 243 TCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDII----GKEKIGLKQIKYLVLDEA 299
Cdd:cd17923   74 LGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 177-299 1.57e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 49.19  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 177 RDLMACAQTGSGKT--AAFLLPILAHmmhdgitasRFKELQEPECIIV--APTRELVNQiylEARKFSFGTCVRAVVIYG 252
Cdd:cd18034   17 RNTIVVLPTGSGKTliAVMLIKEMGE---------LNRKEKNPKKRAVflVPTVPLVAQ---QAEAIRSHTDLKVGEYSG 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 262118318 253 GTQLGHSIRQIVQGC----NILCATPGRLMDIIGKEKIGLKQIKYLVLDEA 299
Cdd:cd18034   85 EMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
ResIII pfam04851
Type III restriction enzyme, res subunit;
161-337 2.09e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.05  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318  161 KLTPVQKYSIPIILAGRDL--------MAcaqTGSGKT--AAFllpilahmmhdgITASRFKELQEPECIIVAPTRELVN 230
Cdd:pfam04851   3 ELRPYQIEAIENLLESIKNgqkrglivMA---TGSGKTltAAK------------LIARLFKKGPIKKVLFLVPRKDLLE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318  231 QIYLEARKFsFGTCVRAVVIYGGTqlghSIRQIVQGCNILCATPGRLMDII--GKEKIGLKQIKYLVLDEADRmldmGFG 308
Cdd:pfam04851  68 QALEEFKKF-LPNYVEIGEIISGD----KKDESVDDNKIVVTTIQSLYKALelASLELLPDFFDVIIIDEAHR----SGA 138

                         170       180
                  ....*....|....*....|....*....
gi 262118318  309 PEMKKLISCpgmpSKEQRQtLMFSATFPE 337
Cdd:pfam04851 139 SSYRNILEY----FKPAFL-LGLTATPER 162
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
 158-348 3.25e-06

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: 47.91  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 158 GYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmMHDGITasrfkelqepecIIVAPTRELVN-QIY-LE 235
Cdd:cd17920    9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL---LLDGVT------------LVVSPLISLMQdQVDrLQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 236 ARkfsfgtCVRAVVIyGGTQLGHSIRQIVQGC-----NILCATPGRLMDIIGKEKIG----LKQIKYLVLDEADRMLDMG 306
Cdd:cd17920   74 QL------GIRAAAL-NSTLSPEEKREVLLRIkngqyKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHCVSQWG 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 262118318 307 --FGPEMKKLIS----CPGMPskeqrqTLMFSATFPEEIQRLAAEFLK 348
Cdd:cd17920  147 hdFRPDYLRLGRlrraLPGVP------ILALTATATPEVREDILKRLG 188
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 389-481 3.49e-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: 46.01  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 389 IGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQRERE-QALGDFRFG--KCPVLVATSVAARGLDIENVQHVIn 465
Cdd:cd18799    4 YVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV- 82

                         90
                 ....*....|....*...
gi 262118318 466 FDLP--STIdEYVHRIGR 481
Cdd:cd18799   83 FLRPteSRT-LFLQMLGR 99
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 391-496 4.91e-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: 46.85  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 391 DERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFD--- 467
Cdd:cd18790   27 GERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadk 106

                         90       100       110
                 ....*....|....*....|....*....|..
gi 262118318 468 ---LPSTiDEYVHRIGRTGRCGNtGRAISFFD 496
Cdd:cd18790  107 egfLRSE-TSLIQTIGRAARNVN-GKVILYAD 136
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 371-495 7.45e-06

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: 46.09  E-value: 7.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 371 LQVGQFSKREKLVEILRNIGD-ERTMVFVETKKKADFIAtflcqEKISTTSIHGDREQREREQALGDFRFGKCPVLVATS 449
Cdd:cd18789   28 LAAMNPNKLRALEELLKRHEQgDKIIVFTDNVEALYRYA-----KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSK 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 262118318 450 VAARGLDI--ENVQHVINFDLPSTiDEYVHRIGRTGRCGNTGRAISFF 495
Cdd:cd18789  103 VGDEGIDLpeANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 384-484 9.06e-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: 45.72  E-value: 9.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 384 EILRNIGDERTM-VFVETKKKADFIAT---FLCQEKISTTSI---HG--DREQRER-EQAL--GDFRfgkcpVLVATSVA 451
Cdd:cd18796   30 EVIFLLERHKSTlVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAALkrGDLK-----VVVATSSL 104

                         90       100       110
                 ....*....|....*....|....*....|...
gi 262118318 452 ARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 484
Cdd:cd18796  105 ELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
 158-298 7.83e-05

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: 44.28  E-value: 7.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 158 GYTKLTPVQKYSIPIILAGRD-LMACAQTGSGKTAAFLLPILAHMMHD-----GITASRFKelqepeCIIVAPTRELVNQ 231
Cdd:cd18019   14 GFKSLNRIQSKLFPAAFETDEnLLLCAPTGAGKTNVALLTILREIGKHrnpdgTINLDAFK------IVYIAPMKALVQE 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 262118318 232 IY--LEARKFSFGTCVRAVViyGGTQLghSIRQIVQgCNILCATPGRlMDII---GKEKIGLKQIKYLVLDE 298
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 ...
 177-274 2.00e-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: 42.73  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 177 RDLMACAQTGSGKTAAFLLPILAHMMHDGITASrfkelQEPECIIVAPTRELVNQIYLEAR-KFS-FGTCVraVVIYGGT 254
Cdd:cd18023   18 KNFVVSAPTGSGKTVLFELAILRLLKERNPLPW-----GNRKVVYIAPIKALCSEKYDDWKeKFGpLGLSC--AELTGDT 90

                         90       100
                 ....*....|....*....|
gi 262118318 255 QLGhSIRQIvQGCNILCATP 274
Cdd:cd18023   91 EMD-DTFEI-QDADIILTTP 108
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 185-299 2.28e-04

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 41.52  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 185 TGSGKTA-AFLLPIlahmmhdgitasrfkELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRavVIYGGtqlghsIRQI 263
Cdd:cd17926   27 TGSGKTLtALALIA---------------YLKELRTLIVVPTDALLDQWKERFEDFLGDSSIG--LIGGG------KKKD 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 262118318 264 VQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEA 299
Cdd:cd17926   84 FDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 176-298 2.64e-04

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: 41.80  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 176 GRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRfkelqepeCIIVAPTRELVNQIY--LEARKFSFGTCVRAVVIYGG 253
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------VLYISPLKALINDQErrLEEPLDEIDLEIPVAVRHGD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 262118318 254 TQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIG--LKQIKYLVLDE 298
Cdd:cd17922   73 TSQSEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
 178-350 3.36e-04

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


Pssm-ID: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 42.03  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 178 DLMACAQTGSGKTAAFLLPILaHMMHDGITASRFKELQEPECIIVAPTRELVNQI--YLEARKFSFGTCVRAVViyGGTQ 255
Cdd:cd18020   19 NMLICAPTGAGKTNIAMLTIL-HEIRQHVNQGGVIKKDDFKIVYIAPMKALAAEMveKFSKRLAPLGIKVKELT--GDMQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 256 LGhsiRQIVQGCNILCATPGRlMDIIGKEKIG----LKQIKYLVLDEAdRMLDMGFGPEMKKLIScPGMPSKEQRQTLM- 330
Cdd:cd18020   96 LT---KKEIAETQIIVTTPEK-WDVVTRKSSGdvalSQLVRLLIIDEV-HLLHDDRGPVIESLVA-RTLRQVESTQSMIr 169

                        170       180
                 ....*....|....*....|...
gi 262118318 331 ---FSATFPEEIQrlAAEFLKSN 350
Cdd:cd18020  170 ivgLSATLPNYLD--VADFLRVN 190
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 421-481 5.73e-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: 40.79  E-value: 5.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262118318 421 IHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIEN-----VQHVINFDLpSTIDEYVHRIGR 481
Cdd:cd18811   67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGL-SQLHQLRGRVGR 131
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
 182-316 1.13e-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: 40.32  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 182 CAQTGSGKTAAFLLPILAHmmhdgitasrFKELQEPECIIVAPTRELVNQIYLE-ARKFSFGTCVRAVVIYGGTQLghSI 260
Cdd:cd18021   25 GAPTGSGKTVCAELALLRH----------WRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLGKKVVKLTGETST--DL 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 262118318 261 RQIVQGcNILCATPGRLmDIIG---KEKIGLKQIKYLVLDEAdRMLDMGFGPEMKKLIS 316
Cdd:cd18021   93 KLLAKS-DVILATPEQW-DVLSrrwKQRKNVQSVELFIADEL-HLIGGENGPVYEVVVS 148
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
 174-301 1.21e-03

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 40.49  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 174 LAGRDLMACAQTGSGKTAAFLLPILAHMmhDGITASRFKELqepecIIVAPTRELVNQiylEARKFS--FGTCVRAVV-I 250
Cdd:cd17927   15 LKGKNTIICLPTGSGKTFVAVLICEHHL--KKFPAGRKGKV-----VFLANKVPLVEQ---QKEVFRkhFERPGYKVTgL 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 262118318 251 YGGTQLGHSIRQIVQGCNILCATPGRLM-DIIGKEKIGLKQIKYLVLDEADR 301
Cdd:cd17927   85 SGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 172-301 2.04e-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: 39.42  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 172 IILAGRDL----MACAQTGSGKTAAFLLPILAHMMHDGitasrfkelqePECIIVAPTRELVNQIYLEARKFsFGTCVRA 247
Cdd:cd18035    8 VLIAAVALngntLIVLPTGLGKTIIAILVAADRLTKKG-----------GKVLILAPSRPLVEQHAENLKRV-LNIPDKI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 262118318 248 VVIYGGTQlGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADR 301
Cdd:cd18035   76 TSLTGEVK-PEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 421-460 2.30e-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: 2.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 262118318 421 IHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENV 460
Cdd:cd18792   66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA 105
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
 158-299 2.56e-03

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 39.55  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 158 GYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLP--ILAHmMHDGITasrfkelqepecIIVAPTRELV-NQI-Y 233
Cdd:cd18018    9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPalLLRR-RGPGLT------------LVVSPLIALMkDQVdA 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262118318 234 LEARkfsfgtcVRAVVIYGG---TQLGHSIRQIVQG-CNILCATPGRLMDIIGKEKI-GLKQIKYLVLDEA 299
Cdd:cd18018   76 LPRA-------IKAAALNSSltrEERRRILEKLRAGeVKILYVSPERLVNESFRELLrQTPPISLLVVDEA 139
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
 160-253 2.96e-03

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 39.23  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 160 TKLTPVQKYSIPIILAGRDLMACAQTGSGKTAaFllpilahmmhdGITASRFKELQEPECIIVAPTRELVNQIYLEARKF 239
Cdd:cd17924   16 FPPWGAQRTWAKRLLRGKSFAIIAPTGVGKTT-F-----------GLATSLYLASKGKRSYLIFPTKSLVKQAYERLSKY 83

                         90
                 ....*....|....*.
gi 262118318 240 --SFGTCVRAVVIYGG 253
Cdd:cd17924   84 aeKAGVEVKILVYHSR 99
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
 176-239 4.81e-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: 38.43  E-value: 4.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262118318 176 GRDLMACAQTGSGKTAAFLLPILAHmmhdgitASRFKelqEPECIIVAPTRELVNQIYLEARKF 239
Cdd:cd17930    1 PGLVILEAPTGSGKTEAALLWALKL-------AARGG---KRRIIYALPTRATINQMYERIREI 54
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 156-299 5.71e-03

DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 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: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 38.49  E-value: 5.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 156 KAGYTKLTPVQKYSIPIILAgrDLMacaqtGSGKTAAFLLPI-LAHMMHdgitASRFKELQEPECIIVAPTreLVNQIYL 234
Cdd:cd17999    6 QEGINWLAFLNKYNLHGILC--DDM-----GLGKTLQTLCILaSDHHKR----ANSFNSENLPSLVVCPPT--LVGHWVA 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262118318 235 EARKFsFGTCVRAVVIY-GGTQLGHSIRQIVQGCNILCATpgrlMDIIGKEKIGLKQIK--YLVLDEA 299
Cdd:cd17999   73 EIKKY-FPNAFLKPLAYvGPPQERRRLREQGEKHNVIVAS----YDVLRNDIEVLTKIEwnYCVLDEG 135
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
 174-298 6.84e-03

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 38.23  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118318 174 LAGRDLMACAQTGSGKTAAFLLPILAHMmhdgitaSRFKELQEPECIIVaptreLVNQIYL---EARKFS--FGTCVRAV 248
Cdd:cd18036   15 LRGKNTIICAPTGSGKTRVAVYICRHHL-------EKRRSAGEKGRVVV-----LVNKVPLveqQLEKFFkyFRKGYKVT 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 262118318 249 VIYGGTQLGHSIRQIVQGCNILCATP----GRLMDIIGKEKIGLKQIKYLVLDE 298
Cdd:cd18036   83 GLSGDSSHKVSFGQIVKASDVIICTPqiliNNLLSGREEERVYLSDFSLLIFDE 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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