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Conserved domains on  [gi|1958750301|ref|XP_038958116|]
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probable ATP-dependent RNA helicase DDX4 isoform X11 [Rattus norvegicus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030645)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
228-480 0e+00

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


:

Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 543.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 228 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 307
Cdd:cd18052    12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 308 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC 387
Cdd:cd18052    92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 388 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFL 467
Cdd:cd18052   172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251
                         250
                  ....*....|...
gi 1958750301 468 KSNYLFVAVGQVG 480
Cdd:cd18052   252 KEDYLFLTVGRVG 264
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
486-615 1.21e-57

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


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 191.18  E-value: 1.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 486 VQQSILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 564
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958750301 565 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 615
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 ...
228-480 0e+00

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 543.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 228 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 307
Cdd:cd18052    12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 308 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC 387
Cdd:cd18052    92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 388 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFL 467
Cdd:cd18052   172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251
                         250
                  ....*....|...
gi 1958750301 468 KSNYLFVAVGQVG 480
Cdd:cd18052   252 KEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
260-625 3.10e-156

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 458.07  E-value: 3.10e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 260 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqePEC 339
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------PQA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 340 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 419
Cdd:COG0513    75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 420 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVGGACRDVQQSILQVGQYSK 498
Cdd:COG0513   155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 499 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 578
Cdd:COG0513   229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1958750301 579 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNHLAQ 625
Cdd:COG0513   309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRA 355
PTZ00110 PTZ00110
helicase; Provisional
121-654 4.00e-120

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 369.87  E-value: 4.00e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 121 DTQTRSRGFSKRGGYpdgNDSEASGPFrrGGRDSEYDQDQGSQRGGglFGSRKPAASDSGGYKGlneevvtGSGKNSWKS 200
Cdd:PTZ00110    4 TDGSSSNGSVSSGPS---NNYNSYGPY--PDSSNPYGNYQANHQDN--YGGFRPGYGNYSGGYG-------GFGMNSYGS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 201 EAEGGESSDIQGPKVTYIPPPPPEdedsIFAHYQ-TGINFDKYDTILVE-----VSGHDAPPAILTFEEANLCQTLNNNI 274
Cdd:PTZ00110   70 STLGKRLQPIDWKSINLVPFEKNF----YKEHPEvSALSSKEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 275 AKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITAS-RFKELQEPECIIVAPTRELINQIY 353
Cdd:PTZ00110  146 KNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INAQpLLRYGDGPIVLVLAPTRELAEQIR 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 433
Cdd:PTZ00110  221 EQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRK 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 434 LIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKSNYLFVAVGQVG-GACRDVQQSILQVGQYSKREKLVEILRNIGDE 512
Cdd:PTZ00110  301 IVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRD 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 513 --RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPS 590
Cdd:PTZ00110  377 gdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPN 456
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958750301 591 TIDEYVHRIGRTGRCGNTGRAISFFdTESDNHLAQPLVKVLSDAQQDVPAWLEEIAFSSYAPPS 654
Cdd:PTZ00110  457 QIEDYVHRIGRTGRAGAKGASYTFL-TPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTE 519
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
283-462 9.65e-61

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 200.93  E-value: 9.65e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 283 TPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELINQIYLEARKFSFG 362
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD---------KLDNGPQALVLAPTRELAEQIYEELKKLGKG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 363 TCVRAVVIYGGTQFGHSIRQIvQGCNILCATPGRLMDIIGKEKiGLKQVKYLVLDEADRMLDMGFGPEMKKLISCpgMPs 442
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146
                         170       180
                  ....*....|....*....|
gi 1958750301 443 kEQRQTLLFSATFPEEIQRL 462
Cdd:pfam00270 147 -KKRQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
486-615 1.21e-57

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 191.18  E-value: 1.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 486 VQQSILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 564
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958750301 565 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 615
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
274-477 1.17e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 177.68  E-value: 1.17e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301  274 IAKAGYTKLTPVQKYSIPIVLAG-RDLMACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqEPECIIVAPTRELINQI 352
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK----------GGRVLVLVPTRELAEQW 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301  353 YLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEM 431
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958750301  432 KKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVG 477
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLN-DPVFIDVG 191
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
497-606 4.12e-38

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 136.96  E-value: 4.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 497 SKREKLVEILRNIGDERTMVFVETKKKADfIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLD 576
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1958750301 577 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 606
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
525-606 3.28e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.07  E-value: 3.28e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301  525 DFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 604
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1958750301  605 CG 606
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
494-612 9.11e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 94.03  E-value: 9.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 494 GQYSKREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKISTTSIHG--DRE------QREREQALGDFRCGK 561
Cdd:COG1111   332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958750301 562 CPVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNTGRAI 612
Cdd:COG1111   412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
PRK13766 PRK13766
Hef nuclease; Provisional
498-612 6.10e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.76  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 498 KREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKIST------TSIHGDREQREREQ--ALGDFRCGKCPVL 565
Cdd:PRK13766  348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGMSQKEQieILDKFRAGEFNVL 427
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958750301 566 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 612
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 ...
228-480 0e+00

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 543.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 228 SIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGS 307
Cdd:cd18052    12 EIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 308 GKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC 387
Cdd:cd18052    92 GKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGC 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 388 NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFL 467
Cdd:cd18052   172 HILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251
                         250
                  ....*....|...
gi 1958750301 468 KSNYLFVAVGQVG 480
Cdd:cd18052   252 KEDYLFLTVGRVG 264
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
260-625 3.10e-156

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 458.07  E-value: 3.10e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 260 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqePEC 339
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------PQA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 340 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 419
Cdd:COG0513    75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 420 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVGGACRDVQQSILQVGQYSK 498
Cdd:COG0513   155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 499 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 578
Cdd:COG0513   229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1958750301 579 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNHLAQ 625
Cdd:COG0513   309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRA 355
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
260-480 3.60e-146

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 424.59  E-value: 3.60e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 260 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAS-RFKELQEPE 338
Cdd:cd17967     1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgRGRRKAYPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 339 CIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 418
Cdd:cd17967    81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750301 419 ADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVG 480
Cdd:cd17967   161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
PTZ00110 PTZ00110
helicase; Provisional
121-654 4.00e-120

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 369.87  E-value: 4.00e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 121 DTQTRSRGFSKRGGYpdgNDSEASGPFrrGGRDSEYDQDQGSQRGGglFGSRKPAASDSGGYKGlneevvtGSGKNSWKS 200
Cdd:PTZ00110    4 TDGSSSNGSVSSGPS---NNYNSYGPY--PDSSNPYGNYQANHQDN--YGGFRPGYGNYSGGYG-------GFGMNSYGS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 201 EAEGGESSDIQGPKVTYIPPPPPEdedsIFAHYQ-TGINFDKYDTILVE-----VSGHDAPPAILTFEEANLCQTLNNNI 274
Cdd:PTZ00110   70 STLGKRLQPIDWKSINLVPFEKNF----YKEHPEvSALSSKEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 275 AKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITAS-RFKELQEPECIIVAPTRELINQIY 353
Cdd:PTZ00110  146 KNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-----INAQpLLRYGDGPIVLVLAPTRELAEQIR 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 433
Cdd:PTZ00110  221 EQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRK 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 434 LIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKSNYLFVAVGQVG-GACRDVQQSILQVGQYSKREKLVEILRNIGDE 512
Cdd:PTZ00110  301 IVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRD 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 513 --RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPS 590
Cdd:PTZ00110  377 gdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPN 456
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958750301 591 TIDEYVHRIGRTGRCGNTGRAISFFdTESDNHLAQPLVKVLSDAQQDVPAWLEEIAFSSYAPPS 654
Cdd:PTZ00110  457 QIEDYVHRIGRTGRAGAKGASYTFL-TPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTE 519
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
239-480 3.00e-113

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


Pssm-ID: 350809 [Multi-domain]  Cd Length: 249  Bit Score: 341.25  E-value: 3.00e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 239 FDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL 318
Cdd:cd18051     1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 319 AHMMRDG-----ITASRF--KELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILC 391
Cdd:cd18051    81 SQIYEQGpgeslPSESGYygRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 392 ATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFLkSNY 471
Cdd:cd18051   161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFL-DNY 239

                  ....*....
gi 1958750301 472 LFVAVGQVG 480
Cdd:cd18051   240 IFLAVGRVG 248
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
261-653 1.56e-103

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 323.68  E-value: 1.56e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 261 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITASRFKelqePECI 340
Cdd:PRK11776    6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK-----LDVKRFR----VQAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 341 IVAPTRELINQIYLEARKFSFGT-CVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 419
Cdd:PRK11776   77 VLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 420 DRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVGGAcRDVQQSILQVGQYSK 498
Cdd:PRK11776  157 DRMLDMGFQDAIDAIIRqAP-----ARRQTLLFSATYPEGIAAISQRFQR-DPVEVKVESTHDL-PAIEQRFYEVSPDER 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 499 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 578
Cdd:PRK11776  230 LPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958750301 579 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFdTESDNHLAQplvkVLSDAQQDVPAW--LEEIAFSSYAPP 653
Cdd:PRK11776  310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLV-APEEMQRAN----AIEDYLGRKLNWepLPSLSPLSGVPL 381
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
260-614 1.83e-90

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 288.76  E-value: 1.83e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 260 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMmrdgITASRFKELQePEC 339
Cdd:PRK11192    2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL----LDFPRRKSGP-PRI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 340 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 419
Cdd:PRK11192   77 LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 420 DRMLDMGFGPEMKKLiscpgmpSKEQR---QTLLFSATFP-EEIQRLAGEFLKsNYLFVAVgqvgGACRDVQQSILQvgQ 495
Cdd:PRK11192  157 DRMLDMGFAQDIETI-------AAETRwrkQTLLFSATLEgDAVQDFAERLLN-DPVEVEA----EPSRRERKKIHQ--W 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 496 Y-------SKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVAT 568
Cdd:PRK11192  223 YyraddleHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVAT 302
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1958750301 569 SVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 614
Cdd:PRK11192  303 DVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
274-654 1.19e-88

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 284.78  E-value: 1.19e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfKELQEPECIIVAPTRELINQIY 353
Cdd:PRK10590   16 VAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHA---KGRRPVRALILTPTRELAAQIG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 433
Cdd:PRK10590   93 ENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 434 LIScpGMPSKeqRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVGGACRDVQQSILQVGQYSKREKLVEILRNIGDER 513
Cdd:PRK10590  173 VLA--KLPAK--RQNLLFSATFSDDIKALAEKLLH-NPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGKGNWQQ 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 514 TMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTID 593
Cdd:PRK10590  248 VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPE 327
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750301 594 EYVHRIGRTGRCGNTGRAISFFDTesDNHlaqplvKVLSDAQQDVPAWLEEIAFSSYAP-PS 654
Cdd:PRK10590  328 DYVHRIGRTGRAAATGEALSLVCV--DEH------KLLRDIEKLLKKEIPRIAIPGYEPdPS 381
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
244-639 2.60e-87

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 283.22  E-value: 2.60e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 244 TILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAH--- 320
Cdd:PLN00206  106 KLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcct 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 321 MMRDGITASRfkelqEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDI 400
Cdd:PLN00206  186 IRSGHPSEQR-----NPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDL 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 401 IGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPskeqrQTLLFSATFPEEIQRLAGEFLKsNYLFVAVGQVG 480
Cdd:PLN00206  261 LSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAK-DIILISIGNPN 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 481 GACRDVQQSILQVGQYSKREKLVEILRNIGDER--TMVFVETKKKADFIAtflcqEKISTT------SIHGDREQREREQ 552
Cdd:PLN00206  335 RPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLA-----NAITVVtglkalSIHGEKSMKERRE 409
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 553 ALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNhLAQPLVKVLS 632
Cdd:PLN00206  410 VMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRN-LFPELVALLK 488

                  ....*..
gi 1958750301 633 DAQQDVP 639
Cdd:PLN00206  489 SSGAAIP 495
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
261-614 3.25e-87

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 281.80  E-value: 3.25e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 261 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFkeLQEPECI 340
Cdd:PRK01297   89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERY--MGEPRAL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 341 IVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQI-VQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 419
Cdd:PRK01297  167 IIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 420 DRMLDMGFGPEMKKLIScpGMPSKEQRQTLLFSATFPEEIQRLAGEFLkSNYLFVAVGQVGGACRDVQQSILQVGQYSKR 499
Cdd:PRK01297  247 DRMLDMGFIPQVRQIIR--QTPRKEERQTLLFSATFTDDVMNLAKQWT-TDPAIVEIEPENVASDTVEQHVYAVAGSDKY 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 500 EKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIEN 579
Cdd:PRK01297  324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1958750301 580 VQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 614
Cdd:PRK01297  404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
270-474 1.02e-84

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 265.07  E-value: 1.02e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 270 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkelqEPECIIVAPTRELI 349
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGR-----GPQALVLAPTRELA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 350 NQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGP 429
Cdd:cd00268    76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEE 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958750301 430 EMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGEFLKsNYLFV 474
Cdd:cd00268   156 DVEKILSaLP-----KDRQTLLFSATLPEEVKELAKKFLK-NPVRI 195
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
253-614 2.14e-78

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 261.42  E-value: 2.14e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 253 DAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFK 332
Cdd:PRK04537    3 DKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 333 ElqEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKI-GLKQV 411
Cdd:PRK04537   83 E--DPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHAC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 412 KYLVLDEADRMLDMGFGPEMKKLIScpGMPSKEQRQTLLFSATFPEEIQRLAGEFLKSNYLFVAVGQVGGACRdVQQSIL 491
Cdd:PRK04537  161 EICVLDEADRMFDLGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR-VRQRIY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 492 QVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVA 571
Cdd:PRK04537  238 FPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVA 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1958750301 572 ARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISF 614
Cdd:PRK04537  318 ARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
274-614 5.07e-73

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 242.57  E-value: 5.07e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkELQEPECIIVAPTRELINQIY 353
Cdd:PRK04837   23 LEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDR--KVNQPRALIMAPTRELAVQIH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 433
Cdd:PRK04837  101 ADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRW 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 434 LIScpGMPSKEQRQTLLFSATFPEEIQRLAGEFLKS-NYLFVAVGQVGGacRDVQQSILqvgqY-SKREKLVEILRNIGD 511
Cdd:PRK04837  181 LFR--RMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVEPEQKTG--HRIKEELF----YpSNEEKMRLLQTLIEE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 512 E---RTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDL 588
Cdd:PRK04837  253 EwpdRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDL 332
                         330       340
                  ....*....|....*....|....*.
gi 1958750301 589 PSTIDEYVHRIGRTGRCGNTGRAISF 614
Cdd:PRK04837  333 PDDCEDYVHRIGRTGRAGASGHSISL 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
260-616 1.73e-69

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 238.98  E-value: 1.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 260 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPEC 339
Cdd:PRK11634    7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD---------PELKAPQI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 340 IIVAPTRELINQIYLEARKFS-FGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 418
Cdd:PRK11634   78 LVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 419 ADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPEEIQRLAGEFLKSNYLfVAVgQVGGACR-DVQQSILQVGQYS 497
Cdd:PRK11634  158 ADEMLRMGFIEDVETIMA--QIP--EGHQTALFSATMPEAIRRITRRFMKEPQE-VRI-QSSVTTRpDISQSYWTVWGMR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 498 KREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDI 577
Cdd:PRK11634  232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1958750301 578 ENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFD 616
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 ...
274-474 2.97e-67

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


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 219.55  E-value: 2.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITASRFKELQE-PECIIVAPTRELINQI 352
Cdd:cd17966     5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVH-----INAQPPLERGDgPIVLVLAPTRELAQQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 353 YLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMK 432
Cdd:cd17966    80 QQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958750301 433 KLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFV 474
Cdd:cd17966   160 KIVD----QIRPDRQTLMWSATWPKEVRRLAEDFLK-DYIQV 196
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
274-474 5.63e-61

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


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 203.20  E-value: 5.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLA-GRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKelqePECIIVAPTRELINQI 352
Cdd:cd17964     9 LTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSG----VSALIISPTRELALQI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 353 YLEARKF-SFGTCVRAVVIYGGTQFGHSIRQIV-QGCNILCATPGRLMDIIGKEKIG--LKQVKYLVLDEADRMLDMGFG 428
Cdd:cd17964    85 AAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLDMGFR 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958750301 429 PEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFLKSNYLFV 474
Cdd:cd17964   165 PDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
270-467 6.27e-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: 202.65  E-value: 6.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 270 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitASRFKELQE-PECIIVAPTREL 348
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-----DQRELEKGEgPIAVIVAPTREL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 349 INQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 428
Cdd:cd17952    76 AQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFE 155
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958750301 429 PEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFL 467
Cdd:cd17952   156 YQVRSIVG----HVRPDRQTLLFSATFKKKIEQLARDIL 190
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
283-462 9.65e-61

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 200.93  E-value: 9.65e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 283 TPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELINQIYLEARKFSFG 362
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD---------KLDNGPQALVLAPTRELAEQIYEELKKLGKG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 363 TCVRAVVIYGGTQFGHSIRQIvQGCNILCATPGRLMDIIGKEKiGLKQVKYLVLDEADRMLDMGFGPEMKKLISCpgMPs 442
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146
                         170       180
                  ....*....|....*....|
gi 1958750301 443 kEQRQTLLFSATFPEEIQRL 462
Cdd:pfam00270 147 -KKRQILLLSATLPRNLEDL 165
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
249-469 1.21e-60

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


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 202.61  E-value: 1.21e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 249 VSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgITA 328
Cdd:cd17953     2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRH-----IKD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 329 SRF-KELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDII---GKE 404
Cdd:cd17953    77 QRPvKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGR 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958750301 405 KIGLKQVKYLVLDEADRMLDMGFGPEMKKLIscpgMPSKEQRQTLLFSATFPEEIQRLAGEFLKS 469
Cdd:cd17953   157 VTNLRRVTYVVLDEADRMFDMGFEPQIMKIV----NNIRPDRQTVLFSATFPRKVEALARKVLHK 217
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
274-469 6.09e-59

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 198.31  E-value: 6.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfKELQEPECIIVAPTRELINQIY 353
Cdd:cd17945     5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEE-TKDDGPYALILAPTRELAQQIE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKFSFGTCVRAVVIYGGtqfgHSIRQIV----QGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGP 429
Cdd:cd17945    84 EETQKFAKPLGIRVVSIVGG----HSIEEQAfslrNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750301 430 EMKKLIScpGMPS------------------KEQRQTLLFSATFPEEIQRLAGEFLKS 469
Cdd:cd17945   160 QVTKILD--AMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRR 215
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
486-615 1.21e-57

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 191.18  E-value: 1.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 486 VQQSILQVGQYSKREKL-VEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPV 564
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958750301 565 LVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 615
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
247-477 4.12e-57

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


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 193.69  E-value: 4.12e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 247 VEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgI 326
Cdd:cd18049    12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH-----I 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 327 TASRFKELQE-PECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEK 405
Cdd:cd18049    87 NHQPFLERGDgPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750301 406 IGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVG 477
Cdd:cd18049   167 TNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLK-DYIHINIG 233
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
270-477 6.23e-57

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


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 192.03  E-value: 6.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 270 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITAsrfkelqEPECIIVAPTRELI 349
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-------GLRALILAPTRELA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 350 NQIYLEARKFSFGTCVRAVVIYGGT--QFGHSIRQIvQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGF 427
Cdd:cd17957    74 SQIYRELLKLSKGTGLRIVLLSKSLeaKAKDGPKSI-TKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGF 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958750301 428 GPEMKKLI-SCpgmpSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVG 477
Cdd:cd17957   153 REQTDEILaAC----TNPNLQRSLFSATIPSEVEELARSVMK-DPIRIIVG 198
PTZ00424 PTZ00424
helicase 45; Provisional
260-623 7.96e-54

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 190.42  E-value: 7.96e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 260 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitasrfkeLQEPEC 339
Cdd:PTZ00424   29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD---------LNACQA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 340 IIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 419
Cdd:PTZ00424  100 LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 420 DRMLDMGFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLAGEFLKSNYLfVAVGQVGGACRDVQQSILQVGQYS-K 498
Cdd:PTZ00424  180 DEMLSRGFKGQIYDVFK--KLPP--DVQVALFSATMPNEILELTTKFMRDPKR-ILVKKDELTLEGIRQFYVAVEKEEwK 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 499 REKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIE 578
Cdd:PTZ00424  255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1958750301 579 NVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNHL 623
Cdd:PTZ00424  335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQL 379
DEXDc smart00487
DEAD-like helicases superfamily;
274-477 1.17e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 177.68  E-value: 1.17e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301  274 IAKAGYTKLTPVQKYSIPIVLAG-RDLMACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqEPECIIVAPTRELINQI 352
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK----------GGRVLVLVPTRELAEQW 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301  353 YLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEM 431
Cdd:smart00487  71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958750301  432 KKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVG 477
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLN-DPVFIDVG 191
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
247-477 3.86e-51

DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 179.05  E-value: 3.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 247 VEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHmmrdgI 326
Cdd:cd18050    50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVH-----I 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 327 TASRFKELQE-PECIIVAPTRELINQIYLEArkFSFGTCVR--AVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGK 403
Cdd:cd18050   125 NHQPYLERGDgPICLVLAPTRELAQQVQQVA--DDYGKSSRlkSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEA 202
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958750301 404 EKIGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLKsNYLFVAVG 477
Cdd:cd18050   203 GKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLR-DYVQINIG 271
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
274-468 8.80e-51

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 175.14  E-value: 8.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRdgitasRFKELQEPECIIVAPTRELINQIY 353
Cdd:cd17947     5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY------RPKKKAATRVLVLVPTRELAMQCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKFS-FGTCVRAVVIyGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVLDEADRMLDMGFGPEM 431
Cdd:cd17947    79 SVLQQLAqFTDITFALAV-GGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADEL 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958750301 432 KKLI-SCPgmpskEQRQTLLFSATFPEEIQRLAGEFLK 468
Cdd:cd17947   158 KEILrLCP-----RTRQTMLFSATMTDEVKDLAKLSLN 190
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
261-474 1.41e-50

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


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 175.11  E-value: 1.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 261 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD--GITAsrfkelqepe 338
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDpyGIFA---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 339 cIIVAPTRELINQIyleARKF-SFGTC--VRAVVIYGGTQFghsIRQ---IVQGCNILCATPGRLMDII---GKEKIGLK 409
Cdd:cd17955    71 -LVLTPTRELAYQI---AEQFrALGAPlgLRCCVIVGGMDM---VKQaleLSKRPHIVVATPGRLADHLrssDDTTKVLS 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958750301 410 QVKYLVLDEADRMLDMGFGPEMKKLISCpgMPSKeqRQTLLFSATFPEEIQRLAGEFLKSNYLFV 474
Cdd:cd17955   144 RVKFLVLDEADRLLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
273-468 2.56e-50

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 174.19  E-value: 2.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 273 NIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMmrDGITASRFKElQEPECIIVAPTRELINQI 352
Cdd:cd17958     4 EIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL--DLQPIPREQR-NGPGVLVLTPTRELALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 353 YLEARKFSFGTcVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMK 432
Cdd:cd17958    81 EAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958750301 433 KLIscpgMPSKEQRQTLLFSATFPEEIQRLAGEFLK 468
Cdd:cd17958   160 KIL----LDIRPDRQTIMTSATWPDGVRRLAQSYLK 191
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
260-462 2.78e-50

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 174.04  E-value: 2.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 260 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitASRFkelqepEC 339
Cdd:cd17954     1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---PQRF------FA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 340 IIVAPTRELINQI--YLEARKFSFGtcVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVL 416
Cdd:cd17954    72 LVLAPTRELAQQIseQFEALGSSIG--LKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVM 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958750301 417 DEADRMLDMGFGPEMKKLISCpgMPSkeQRQTLLFSATFPEEIQRL 462
Cdd:cd17954   150 DEADRLLNMDFEPEIDKILKV--IPR--ERTTYLFSATMTTKVAKL 191
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
274-463 5.15e-50

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


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 173.15  E-value: 5.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhMMRDGITASRFKELQepeCIIVAPTRELINQIY 353
Cdd:cd17960     5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLE-ILLKRKANLKKGQVG---ALIISPTRELATQIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKF--SFGTCVRAVVIYGGTQFGHSIRQIV-QGCNILCATPGRLMDIIG--KEKIGLKQVKYLVLDEADRMLDMGFG 428
Cdd:cd17960    81 EVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLGFE 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958750301 429 PEMKKLISCpgMPskEQRQTLLFSATFPEEIQRLA 463
Cdd:cd17960   161 ADLNRILSK--LP--KQRRTGLFSATQTDAVEELI 191
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
260-457 2.21e-49

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 171.72  E-value: 2.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 260 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL----AHMMRDGITAsrfkelq 335
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIeklkAHSPTVGARA------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 336 epecIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLV 415
Cdd:cd17959    75 ----LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVV 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958750301 416 LDEADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPE 457
Cdd:cd17959   151 FDEADRLFEMGFAEQLHEILS--RLP--ENRQTLLFSATLPK 188
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
266-468 4.19e-49

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


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 171.23  E-value: 4.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 266 LCQTLNNNIakaGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitASRFKELQEPECIIVAPT 345
Cdd:cd17949     1 LVSHLKSKM---GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSL---EPRVDRSDGTLALVLVPT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 346 RELINQIYLEARKF--SFGTCVRAVVIyGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEK-IGLKQVKYLVLDEADRM 422
Cdd:cd17949    75 RELALQIYEVLEKLlkPFHWIVPGYLI-GGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRL 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958750301 423 LDMGFGPEMKKLIS---------CPGMPSKEQRQTLLFSATFPEEIQRLAGEFLK 468
Cdd:cd17949   154 LDMGFEKDITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLK 208
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
261-471 4.39e-47

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


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 165.16  E-value: 4.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 261 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL--AHMMRDGITAsrfkelqepe 338
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILekIDPKKDVIQA---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 339 cIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 418
Cdd:cd17940    71 -LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958750301 419 ADRMLDMGFGPEMKKLIS-CPgmpskEQRQTLLFSATFPEEIQRLAGEFLKSNY 471
Cdd:cd17940   150 ADKLLSQDFQPIIEKILNfLP-----KERQILLFSATFPLTVKNFMDRHMHNPY 198
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
274-476 1.47e-46

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


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 163.61  E-value: 1.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgitasRFKELQEPECIIVAPTRELINQIY 353
Cdd:cd17941     5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE-----RWTPEDGLGALIISPTRELAMQIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQgCNILCATPGRL---MDiigkEKIGL--KQVKYLVLDEADRMLDMGFG 428
Cdd:cd17941    80 EVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLlqhMD----ETPGFdtSNLQMLVLDEADRILDMGFK 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958750301 429 PEMKKLIScpGMPSKeqRQTLLFSATFPEEIQRLAGEFLKsNYLFVAV 476
Cdd:cd17941   155 ETLDAIVE--NLPKS--RQTLLFSATQTKSVKDLARLSLK-NPEYISV 197
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
274-474 7.24e-46

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


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 161.76  E-value: 7.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmmrDGITASRFKELQEPECIIVAPTRELINQIY 353
Cdd:cd17942     5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-----ELLYKLKFKPRNGTGVIIISPTRELALQIY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKF------SFGTCVravviyGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGL-KQVKYLVLDEADRMLDMG 426
Cdd:cd17942    80 GVAKELlkyhsqTFGIVI------GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILEIG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958750301 427 FGPEMKKLISCpgMPSkeQRQTLLFSATFPEEIQRLAGEFLKSNYLFV 474
Cdd:cd17942   154 FEEEMRQIIKL--LPK--RRQTMLFSATQTRKVEDLARISLKKKPLYV 197
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
274-469 2.45e-44

DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350709 [Multi-domain]  Cd Length: 206  Bit Score: 157.89  E-value: 2.45e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASrFKELQEPECIIVAPTRELINQIY 353
Cdd:cd17951     5 LKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLP-FIKGEGPYGLIVCPSRELARQTH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 ---------LEARKFSfgtCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLD 424
Cdd:cd17951    84 evieyyckaLQEGGYP---QLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958750301 425 MGFGPEMKKLISCpgmpSKEQRQTLLFSATFPEEIQrlagEFLKS 469
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 ...
270-468 1.06e-43

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


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 155.78  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 270 LNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECIIVAPTRELI 349
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL---------TEHRNPSALILTPTRELA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 350 NQIYLEARKFSFGTC-VRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 428
Cdd:cd17962    72 VQIEDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQ 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958750301 429 PEMKKLIScpgmPSKEQRQTLLFSATFPEEIQRLAGEFLK 468
Cdd:cd17962   152 QQVLDILE----NISHDHQTILVSATIPRGIEQLAGQLLQ 187
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
261-463 1.14e-40

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


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 147.85  E-value: 1.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 261 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmmrdgitasrfkelQEPECI 340
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------QIVVAL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 341 IVAPTRELINQIYLEARKFSF---GTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLD 417
Cdd:cd17938    65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958750301 418 EADRMLDMGFGPEMKKLIS-CPGMPSKEQR-QTLLFSATF-PEEIQRLA 463
Cdd:cd17938   145 EADRLLSQGNLETINRIYNrIPKITSDGKRlQVIVCSATLhSFEVKKLA 193
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
274-455 3.71e-40

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


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 147.39  E-value: 3.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIP-IVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQI 352
Cdd:cd17946     5 LADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTRELAVQV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 353 --YLEA-RKFsfgTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGK--EKIG-LKQVKYLVLDEADRMLDMG 426
Cdd:cd17946    85 kdHLKAiAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEgnEHLAnLKSLRFLVLDEADRMLEKG 161
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958750301 427 FGPEMKKLISC---PGMPSKEQRQTLLFSATF 455
Cdd:cd17946   162 HFAELEKILELlnkDRAGKKRKRQTFVFSATL 193
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
497-606 4.12e-38

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 136.96  E-value: 4.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 497 SKREKLVEILRNIGDERTMVFVETKKKADfIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLD 576
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1958750301 577 IENVQHVINFDLPSTIDEYVHRIGRTGRCG 606
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
278-471 3.62e-37

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


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 137.67  E-value: 3.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 278 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKElqePECIIVAPTRELINQIYLE-- 355
Cdd:cd17944     9 GVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRA---PKVLVLAPTRELANQVTKDfk 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 356 --ARKFSFgTCvravvIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKK 433
Cdd:cd17944    86 diTRKLSV-AC-----FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958750301 434 LISCPGMPSKEQR-QTLLFSATFPEEIQRLAGEFLKSNY 471
Cdd:cd17944   160 ILSVSYKKDSEDNpQTLLFSATCPDWVYNVAKKYMKSQY 198
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
274-469 4.61e-36

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 134.63  E-value: 4.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDgiTASRFKElQEPECIIVAPTRELINQIY 353
Cdd:cd17961     9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKA--KAESGEE-QGTRALILVPTRELAQQVS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKFSFGTC--VRAVVIyggTQFGHSIRQIVQ---GCNILCATPGRLMDII-GKEKIGLKQVKYLVLDEADRMLDMGF 427
Cdd:cd17961    86 KVLEQLTAYCRkdVRVVNL---SASSSDSVQRALlaeKPDIVVSTPARLLSHLeSGSLLLLSTLKYLVIDEADLVLSYGY 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958750301 428 GPEMKKLIS-CPGMPskeqrQTLLFSATFPEEIQRLAGEFLKS 469
Cdd:cd17961   163 EEDLKSLLSyLPKNY-----QTFLMSATLSEDVEALKKLVLHN 200
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
266-462 1.76e-35

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 133.91  E-value: 1.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 266 LCQTLNNNiakaGYTKLTPVQKYSIPIVLAG---------RDLMACAQTGSGKTAAFLLPILAhmmrdgITASRFK-ELQ 335
Cdd:cd17956     1 LLKNLQNN----GITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQ------ALSKRVVpRLR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 336 epeCIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGC--------NILCATPGRLMD-IIGKEKI 406
Cdd:cd17956    71 ---ALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDhLNSTPGF 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958750301 407 GLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQR----------------QTLLFSATF---PEEIQRL 462
Cdd:cd17956   148 TLKHLRFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLgsfgdanllersvrplQKLLFSATLtrdPEKLSSL 222
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
270-468 4.34e-34

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


Pssm-ID: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 128.85  E-value: 4.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 270 LNNNIAKA----GYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILahmmrdgitaSRFKE-LQEPECIIV 342
Cdd:cd17963     1 LKPELLKGlyamGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAML----------SRVDPtLKSPQALCL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 343 APTRELINQIYLEARKFSFGT------CVRAVVIYGGTQFGHsirQIVQGcnilcaTPGRLMDIIGKEKIGLKQVKYLVL 416
Cdd:cd17963    71 APTRELARQIGEVVEKMGKFTgvkvalAVPGNDVPRGKKITA---QIVIG------TPGTVLDWLKKRQLDLKKIKILVL 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750301 417 DEADRMLDM-GFGPE---MKKLI--SCpgmpskeqrQTLLFSATFPEEIQRLAGEFLK 468
Cdd:cd17963   142 DEADVMLDTqGHGDQsirIKRMLprNC---------QILLFSATFPDSVRKFAEKIAP 190
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
273-457 1.56e-30

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 119.78  E-value: 1.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 273 NIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkELQEPECIIVAPTRELINQI 352
Cdd:cd17948     4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEG--PFNAPRGLVITPSRELAEQI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 353 YLEARKFSFGTCVRAVVIYGgtqfGHSIRQIV----QGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFG 428
Cdd:cd17948    82 GSVAQSLTEGLGLKVKVITG----GRTKRQIRnphfEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958750301 429 PEMKKLIS-CP-GMPSKEQR-------QTLLFSATFPE 457
Cdd:cd17948   158 EKLSHFLRrFPlASRRSENTdgldpgtQLVLVSATMPS 195
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
274-469 1.17e-29

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 116.68  E-value: 1.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILaHMMRdgitasrfKELQEPECIIVAPTRELINQIY 353
Cdd:cd17950    17 IVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL-QQLE--------PVDGQVSVLVICHTRELAFQIS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKFS-FGTCVRAVVIYGGTQFGHSIRQIVQGC-NILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDmgfGPEM 431
Cdd:cd17950    88 NEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE---QLDM 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958750301 432 KKLI-----SCPgmpskEQRQTLLFSATFPEEIQRLAGEFLKS 469
Cdd:cd17950   165 RRDVqeifrATP-----HDKQVMMFSATLSKEIRPVCKKFMQD 202
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
263-467 2.19e-29

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 115.50  E-value: 2.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 263 EANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhmmrdgITASRFKELQepeCIIV 342
Cdd:cd17939     1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQ------RIDTTVRETQ---ALVL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 343 APTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRM 422
Cdd:cd17939    72 APTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEM 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958750301 423 LDMGFGPEMKKLISCpgMPSKEqrQTLLFSATFPEEIQRLAGEFL 467
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 ...
261-468 6.70e-29

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


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 114.47  E-value: 6.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 261 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMrdgitasrfKELQEPECI 340
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQID---------TSLKATQAL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 341 IVAPTRELINQI--YLEARKFSFGTCVRAVViyGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDE 418
Cdd:cd18046    72 VLAPTRELAQQIqkVVMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDE 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958750301 419 ADRMLDMGFGPEMKKLIScpGMPskEQRQTLLFSATFPEEIQRLAGEFLK 468
Cdd:cd18046   150 ADEMLSRGFKDQIYDIFQ--KLP--PDTQVVLLSATMPNDVLEVTTKFMR 195
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
261-467 1.95e-28

DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 112.95  E-value: 1.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 261 FEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAhmMRDgitasrfKELQEPECI 340
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ--CLD-------IQVRETQAL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 341 IVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEAD 420
Cdd:cd18045    72 ILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEAD 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958750301 421 RMLDMGFgpemKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEFL 467
Cdd:cd18045   152 EMLNKGF----KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFM 194
HELICc smart00490
helicase superfamily c-terminal domain;
525-606 3.28e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.07  E-value: 3.28e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301  525 DFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 604
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1958750301  605 CG 606
Cdd:smart00490  81 AG 82
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
274-474 6.38e-27

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 108.12  E-value: 6.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLlpILAHMMRDgitasrfKELQEPECIIVAPTRELINQIY 353
Cdd:cd17943     5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFV--VIALESLD-------LERRHPQVLILAPTREIAVQIH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 354 LEARKF-SFGTCVRAVVIYGGTQFGHSIRQIvQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMK 432
Cdd:cd17943    76 DVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958750301 433 KLIScpGMPskEQRQTLLFSATFPEEIQRLAGEFLkSNYLFV 474
Cdd:cd17943   155 WIFS--SLP--KNKQVIAFSATYPKNLDNLLARYM-RKPVLV 191
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
247-463 3.40e-21

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


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 92.78  E-value: 3.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 247 VEVSGHD-APP--AILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILahm 321
Cdd:cd18048     3 VEVLQRDpTSPlfSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 322 mrdgitaSRFKELQE-PECIIVAPTRELINQ---IYLEARKFsfgtCVRAVVIYG--GTQFGHSIRQIVQgcnILCATPG 395
Cdd:cd18048    80 -------SRVDALKLyPQCLCLSPTFELALQtgkVVEEMGKF----CVGIQVIYAirGNRPGKGTDIEAQ---IVIGTPG 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 396 RLMDIIGKEK-IGLKQVKYLVLDEADRMLDM-GFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLA 463
Cdd:cd18048   146 TVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKR--SMPK--ECQMLLFSATFEDSVWAFA 211
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
273-466 3.81e-20

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 90.51  E-value: 3.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 273 NIAKAGYTKL------TPVQKYSIPIVLAGR----------------DLMACAQTGSGKTAAFLLPILAHMMRDGITASR 330
Cdd:cd17965    16 KEILKGSNKTdeeikpSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPFE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 331 FKELQE--------PECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGtqFGHSIRQIVQ----GCNILCATPGRLM 398
Cdd:cd17965    96 EAEEEYesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSG--FGPSYQRLQLafkgRIDILVTTPGKLA 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750301 399 DIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLIScpGMPSkeQRQTLLFSATFPEEIQRLAGEF 466
Cdd:cd17965   174 SLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIK--RAPK--LKHLILCSATIPKEFDKTLRKL 237
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
278-618 5.93e-20

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 93.67  E-value: 5.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 278 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPtreLI----NQI- 352
Cdd:COG0514    14 GYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPAL---LLPGLT------------LVVSP---LIalmkDQVd 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 353 YLEARKfsfgtcVRAVVIYGG---TQFGHSIRQIVQG-CNILCATPGRLM-----DIIGKEKIGLkqvkyLVLDEA---- 419
Cdd:COG0514    76 ALRAAG------IRAAFLNSSlsaEERREVLRALRAGeLKLLYVAPERLLnprflELLRRLKISL-----FAIDEAhcis 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 420 ----DrmldmgFGPE---MKKLI-SCPGMPskeqrqTLLFSATFPEE-----IQRLAgefLKSNYLFVavgqvGGACRD- 485
Cdd:COG0514   145 qwghD------FRPDyrrLGELReRLPNVP------VLALTATATPRvradiAEQLG---LEDPRVFV-----GSFDRPn 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 486 VQQSILQVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVL 565
Cdd:COG0514   205 LRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVI 284
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958750301 566 VATSvaARGL--DIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTE 618
Cdd:COG0514   285 VATI--AFGMgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
494-612 9.11e-20

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 94.03  E-value: 9.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 494 GQYSKREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKISTTSIHG--DRE------QREREQALGDFRCGK 561
Cdd:COG1111   332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958750301 562 CPVLVATSVAARGLDIENVQHVINFDL-PSTIdEYVHRIGRTGRcGNTGRAI 612
Cdd:COG1111   412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
295-616 2.48e-19

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 92.01  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 295 AGRDLMACAQTGSGKTAAFLLpILAHMMRDGITasrfkelqepecIIVAPTRELINQIYLEARKFsfgtcvravviYGGT 374
Cdd:COG1061    99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGKRV------------LVLVPRRELLEQWAEELRRF-----------LGDP 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 375 QFGHSIRQIvqGCNILCATPGRLMDIIGKEKIGlKQVKYLVLDEADRmldmGFGPEMKKLIScpgmpSKEQRQTLLFSAT 454
Cdd:COG1061   155 LAGGGKKDS--DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILE-----AFPAAYRLGLTAT 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 455 ------FPEEIQRLAG--------EFLKSNYL----FVAV-------GQVGGACRDVQQSILQVGQYSKREKLVEILRNI 509
Cdd:COG1061   223 pfrsdgREILLFLFDGivyeyslkEAIEDGYLappeYYGIrvdltdeRAEYDALSERLREALAADAERKDKILRELLREH 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 510 GD-ERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDL 588
Cdd:COG1061   303 PDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP 382
                         330       340
                  ....*....|....*....|....*...
gi 1958750301 589 PSTIDEYVHRIGRTGRCGNTGRAISFFD 616
Cdd:COG1061   383 TGSPREFIQRLGRGLRPAPGKEDALVYD 410
PRK13766 PRK13766
Hef nuclease; Provisional
498-612 6.10e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.76  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 498 KREKLVEILRNI----GDERTMVFVETKKKADFIATFLCQEKIST------TSIHGDREQREREQ--ALGDFRCGKCPVL 565
Cdd:PRK13766  348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGMSQKEQieILDKFRAGEFNVL 427
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958750301 566 VATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 612
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 ...
260-463 2.05e-14

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


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 72.45  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 260 TFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAG--RDLMACAQTGSGKTAAFLLPILAHMMrdgiTASRFKelqep 337
Cdd:cd18047     2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE----PANKYP----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 338 ECIIVAPTRELINQ---IYLEARKF----SFGTCVRavviyggtqfGHSIRQIVQ-GCNILCATPGRLMDIIGKEK-IGL 408
Cdd:cd18047    73 QCLCLSPTYELALQtgkVIEQMGKFypelKLAYAVR----------GNKLERGQKiSEQIVIGTPGTVLDWCSKLKfIDP 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958750301 409 KQVKYLVLDEADRMLDMGfGPEMKKLISCPGMPskEQRQTLLFSATFPEEIQRLA 463
Cdd:cd18047   143 KKIKVFVLDEADVMIATQ-GHQDQSIRIQRMLP--RNCQMLLFSATFEDSVWKFA 194
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
496-601 2.23e-14

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 70.70  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 496 YSKREKLVEILRN----IGDERTMVFVET---------------KKKADFIATFLCQEKISTTSIHGDREQREREQALGD 556
Cdd:cd18802     6 IPKLQKLIEILREyfpkTPDFRGIIFVERratavvlsrllkehpSTLAFIRCGFLIGRGNSSQRKRSLMTQRKQKETLDK 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958750301 557 FRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGR 601
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 ...
498-612 6.90e-14

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 69.31  E-value: 6.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 498 KREKLVEILRNI-------GDERTMVFVETKKKADFIATFLCQEK--------ISTTSIHGDREQREREQ--ALGDFRCG 560
Cdd:cd18801    10 KLEKLEEIVKEHfkkkqegSDTRVIIFSEFRDSAEEIVNFLSKIRpgiratrfIGQASGKSSKGMSQKEQkeVIEQFRKG 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958750301 561 KCPVLVATSVAARGLDIENVQHVINFD-LPSTIdEYVHRIGRTGRcGNTGRAI 612
Cdd:cd18801    90 GYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR-KRQGRVV 140
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
502-615 1.17e-13

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 68.39  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 502 LVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQ 581
Cdd:cd18794    21 LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVR 100
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958750301 582 HVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFF 615
Cdd:cd18794   101 FVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
274-604 2.73e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 73.01  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 274 IAKAGYTKLTPVQKYSIP-IVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGItasrfkelqepeCIIVAPTRELINQI 352
Cdd:COG1204    15 LKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK------------ALYIVPLRALASEK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 353 YLEARKF--SFGtcVRAVVIYGGTQfghSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEAdRML-DMGFGP 429
Cdd:COG1204    83 YREFKRDfeELG--IKVGVSTGDYD---SDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLIdDESRGP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 430 --EM---KKLISCPGMpskeqrQTLLFSATF--PEEIQR-LAGEFLKSNY----LFVAVgqvggacrdVQQSILQVGQYS 497
Cdd:COG1204   157 tlEVllaRLRRLNPEA------QIVALSATIgnAEEIAEwLDAELVKSDWrpvpLNEGV---------LYDGVLRFDDGS 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 498 KREKLVEI---LRNIGDE-RTMVFVETKKKA-----------------------DFIATFL--CQEKISTTSI------- 541
Cdd:COG1204   222 RRSKDPTLalaLDLLEEGgQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELleVSEETHTNEKladclek 301
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750301 542 -----HGD--REQRER-EQAlgdFRCGKCPVLVATSVAARGLdieN--VQHVI------NFDLPSTIDEYVHRIGRTGR 604
Cdd:COG1204   302 gvafhHAGlpSELRRLvEDA---FREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGR 374
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
296-454 8.92e-13

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 66.27  E-value: 8.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 296 GRDLMACAQTGSGKTAAFLLPILAHMmrdgitasrfkELQEPECIIVAPTRELINQIYLEARKFsFGTCVRAVVIYGGTQ 375
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLL-----------LKKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 376 FGHSIRQIVQGCNILCATPGRL-MDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRqtLLFSAT 454
Cdd:cd00046    69 AEEREKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV--ILLSAT 146
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
263-612 1.73e-12

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 70.63  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 263 EANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD-GITAsrfkelqepecII 341
Cdd:COG1205    38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDpGATA-----------LY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 342 VAPTRELINQIYLEARKF--SFGTCVRAVVIYGGTQFghSIRQ-IVQGCNILCATPgrlmDII------GKEKIG--LKQ 410
Cdd:COG1205   107 LYPTKALARDQLRRLRELaeALGLGVRVATYDGDTPP--EERRwIREHPDIVLTNP----DMLhygllpHHTRWArfFRN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 411 VKYLVLDEA---------------DRMLDMgfgpeMKKLISCPgmpskeqrQTLLFSATF--PEEI-QRLAGEflksnyL 472
Cdd:COG1205   181 LRYVVIDEAhtyrgvfgshvanvlRRLRRI-----CRHYGSDP--------QFILASATIgnPAEHaERLTGR------P 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 473 FVAVGQVGGAC--RDV---QQSILQVGQY-SKREKLVEILRNIGDE--RTMVFVETKKKADFIATFL---CQEKISTTSI 541
Cdd:COG1205   242 VTVVDEDGSPRgeRTFvlwNPPLVDDGIRrSALAEAARLLADLVREglRTLVFTRSRRGAELLARYArraLREPDLADRV 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958750301 542 HGDR------EQREREQALgdfRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAI 612
Cdd:COG1205   322 AAYRagylpeERREIERGL---RSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
497-600 7.27e-12

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 63.26  E-value: 7.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 497 SKREKLVEILRNI--GDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDF-RCGKCPV-LVATSVAA 572
Cdd:cd18793    11 GKLEALLELLEELrePGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnEDPDIRVfLLSTKAGG 90
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958750301 573 RGLDIENVQHVINFDLP--STIDEY----VHRIG 600
Cdd:cd18793    91 VGLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
278-638 4.48e-11

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 65.89  E-value: 4.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 278 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPTRELI-NQI-YLE 355
Cdd:PRK11057   22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL---VLDGLT------------LVVSPLISLMkDQVdQLL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 356 ARKFSfGTCVRAvviyggTQFGHSIRQIVQGCN-----ILCATPGRLM--DIIgkEKIGLKQVKYLVLDEADRMLDMG-- 426
Cdd:PRK11057   87 ANGVA-AACLNS------TQTREQQLEVMAGCRtgqikLLYIAPERLMmdNFL--EHLAHWNPALLAVDEAHCISQWGhd 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 427 FGPEMKKL----ISCPGMPskeqrqTLLFSATFPE----EIQRLAGeflksnylfvavgqvggacrdVQQSILQVGQYSK 498
Cdd:PRK11057  158 FRPEYAALgqlrQRFPTLP------FMALTATADDttrqDIVRLLG---------------------LNDPLIQISSFDR 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 499 ---REKLVE-------ILRNIGDERT---MVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVL 565
Cdd:PRK11057  211 pniRYTLVEkfkpldqLMRYVQEQRGksgIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIV 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958750301 566 VATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNHLAQPLVKVLSDAQQDV 638
Cdd:PRK11057  291 VATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDI 363
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
282-419 1.24e-09

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 58.04  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 282 LTPVQKYSI-PIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRDGITasrfkelqepeCIIVAPTRELINQIYLEARKFs 360
Cdd:cd17921     2 LNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK-----------AVYIAPTRALVNQKEADLRER- 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 361 FGTCVRAVVIYGGtQFGHSIRQIvQGCNILCATPGRLMDIIGKEKI-GLKQVKYLVLDEA 419
Cdd:cd17921    70 FGPLGKNVGLLTG-DPSVNKLLL-AEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
497-602 5.61e-09

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 59.47  E-value: 5.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 497 SKREKLVEILRNI--GDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGK-CPV-LVATSVAA 572
Cdd:COG0553   533 AKLEALLELLEELlaEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLKAGG 612
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958750301 573 RGLdieNVQ---HVINFDLP-------STIDEyVHRIGRT 602
Cdd:COG0553   613 EGL---NLTaadHVIHYDLWwnpaveeQAIDR-AHRIGQT 648
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
303-601 5.34e-08

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 55.86  E-value: 5.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 303 AQTGSGKTAAFLLPILAHMMRDGitASRFkelqepecIIVAPTRELINQIYLEARKFSFGtcvrAVVIYGGTQFGHSIRQ 382
Cdd:COG1203   154 APTGGGKTEAALLFALRLAAKHG--GRRI--------IYALPFTSIINQTYDRLRDLFGE----DVLLHHSLADLDLLEE 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 383 IVQGCN---------------ILCATPGRLMDII-----GKEKIGLKQV-KYLVLDEADrMLDMGFGPEMKKLIscpgmp 441
Cdd:COG1203   220 EEEYESearwlkllkelwdapVVVTTIDQLFESLfsnrkGQERRLHNLAnSVIILDEVQ-AYPPYMLALLLRLL------ 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 442 sKEQRQ----TLLFSATFPEEIQrlagEFLKSNYLFV--AVGQVGGACRDVQQSILQV--GQYSkREKLVEILRNI--GD 511
Cdd:COG1203   293 -EWLKNlggsVILMTATLPPLLR----EELLEAYELIpdEPEELPEYFRAFVRKRVELkeGPLS-DEELAELILEAlhKG 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 512 ERTMVFVETKKKAdfIATF-LCQEKISTTSIH--------GDREQREREqALGDFRCGKCPVLVATSVAARGLDienvqh 582
Cdd:COG1203   367 KSVLVIVNTVKDA--QELYeALKEKLPDEEVYllhsrfcpADRSEIEKE-IKERLERGKPCILVSTQVVEAGVD------ 437
                         330       340
                  ....*....|....*....|...
gi 1958750301 583 vINFDL----PSTIDEYVHRIGR 601
Cdd:COG1203   438 -IDFDVvirdLAPLDSLIQRAGR 459
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
564-604 6.17e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 50.40  E-value: 6.17e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958750301 564 VLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 604
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
PRK13767 PRK13767
ATP-dependent helicase; Provisional
279-353 2.64e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 54.12  E-value: 2.64e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958750301 279 YTKLTPVQKYSIPIVLAGRDLMACAQTGSGKT-AAFLLPIlahmmRDGITASRFKELQEP-ECIIVAPTRELINQIY 353
Cdd:PRK13767   30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAII-----DELFRLGREGELEDKvYCLYVSPLRALNNDIH 101
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
281-454 6.67e-07

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 50.11  E-value: 6.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 281 KLTPVQKYSIPIVLAG------RDLMACAQTGSGKTAAFLLPILAhmmrdgiTASRFKELqepecIIVAPTRELINQIYL 354
Cdd:cd17918    15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL-------AYKNGKQV-----AILVPTEILAHQHYE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 355 EARK-FSFgtcVRAVVIYGGTQfghsiRQIVQGCNILCATPGRLMDIIGKEKIGLkqvkyLVLDEADRmldmgFGPEMKK 433
Cdd:cd17918    83 EARKfLPF---INVELVTGGTK-----AQILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHR-----FGVAQRE 144
                         170       180
                  ....*....|....*....|.
gi 1958750301 434 LISCPGMPSkeqrqTLLFSAT 454
Cdd:cd17918   145 ALYNLGATH-----FLEATAT 160
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
278-461 7.05e-07

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 50.23  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 278 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILahmMRDGITasrfkelqepecIIVAPTRELIN-QIY-LE 355
Cdd:cd17920     9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL---LLDGVT------------LVVSPLISLMQdQVDrLQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 356 ARkfsfgtCVRAVVIYGGTQFgHSIRQIVQGC-----NILCATPGRLMDIIGKEKIG----LKQVKYLVLDEADRMLDMG 426
Cdd:cd17920    74 QL------GIRAAALNSTLSP-EEKREVLLRIkngqyKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHCVSQWG 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958750301 427 --FGPEMKKLIS----CPGMPskeqrqTLLFSATFPEEIQR 461
Cdd:cd17920   147 hdFRPDYLRLGRlrraLPGVP------ILALTATATPEVRE 181
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
286-419 1.25e-06

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 49.12  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 286 QKYSIPIVLAGRDLMACAQTGSGKTAAFLLPILAHMMRD-GITAsrfkelqepecIIVAPTRELIN-QI-YLEARKFSFG 362
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDpGSRA-----------LYLYPTKALAQdQLrSLRELLEQLG 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958750301 363 TCVRAVVIYGGTQFGHSIRQIVQGCNILCATPGRLMDII----GKEKIGLKQVKYLVLDEA 419
Cdd:cd17923    74 LGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
279-335 1.28e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 52.03  E-value: 1.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750301 279 YTKLTPVQKYSIPIVLAGRDLMACAQTGSGKT-AAFlLPILAHMMRDGITASRFKELQ 335
Cdd:COG1201    22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGLR 78
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
511-620 2.40e-06

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 48.40  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 511 DERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFD--- 587
Cdd:cd18790    27 GERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadk 106
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958750301 588 ---LPSTiDEYVHRIGRTGRCGNtGRAISFFDTESD 620
Cdd:cd18790   107 egfLRSE-TSLIQTIGRAARNVN-GKVILYADKITD 140
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
296-418 5.74e-06

DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 47.19  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 296 GRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRfkelqepeCIIVAPTRELINQIY--LEARKFSFGTCVRAVVIYGG 373
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------VLYISPLKALINDQErrLEEPLDEIDLEIPVAVRHGD 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958750301 374 TQFGHSIRQIVQGCNILCATPGRLMDIIGKEKIG--LKQVKYLVLDE 418
Cdd:cd17922    73 TSQSEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
509-601 6.63e-06

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 45.63  E-value: 6.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 509 IGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQA---LGDFRCGKCPVLVATSVAARGLDIENVQHVIn 585
Cdd:cd18799     4 YVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV- 82
                          90
                  ....*....|....*...
gi 1958750301 586 FDLP--STIdEYVHRIGR 601
Cdd:cd18799    83 FLRPteSRT-LFLQMLGR 99
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
504-604 1.02e-05

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 46.10  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 504 EILRNIGDERTM-VFVETKKKADFIAT---FLCQEKISTTSI---HG--DREQRER-EQAL--GDFRcgkcpVLVATSVA 571
Cdd:cd18796    30 EVIFLLERHKSTlVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAALkrGDLK-----VVVATSSL 104
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958750301 572 ARGLDIENVQHVINFDLPSTIDEYVHRIGRTGR 604
Cdd:cd18796   105 ELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
ResIII pfam04851
Type III restriction enzyme, res subunit;
281-457 1.45e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 45.74  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 281 KLTPVQKYSIPIVLAGRDL--------MAcaqTGSGKT--AAFllpilahmmrdgITASRFKELQEPECIIVAPTRELIN 350
Cdd:pfam04851   3 ELRPYQIEAIENLLESIKNgqkrglivMA---TGSGKTltAAK------------LIARLFKKGPIKKVLFLVPRKDLLE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 351 QIYLEARKFsFGTCVRAVVIYGGTqfghSIRQIVQGCNILCATPGRLMDII--GKEKIGLKQVKYLVLDEADRmldmGFG 428
Cdd:pfam04851  68 QALEEFKKF-LPNYVEIGEIISGD----KKDESVDDNKIVVTTIQSLYKALelASLELLPDFFDVIIIDEAHR----SGA 138
                         170       180       190
                  ....*....|....*....|....*....|
gi 1958750301 429 PEMKKLIscpgmpSKEQRQTLL-FSATFPE 457
Cdd:pfam04851 139 SSYRNIL------EYFKPAFLLgLTATPER 162
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
491-615 2.36e-05

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 44.93  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 491 LQVGQYSKREKLVEILRNIGD-ERTMVFVETKKKADFIAtflcqEKISTTSIHGDREQREREQALGDFRCGKCPVLVATS 569
Cdd:cd18789    28 LAAMNPNKLRALEELLKRHEQgDKIIVFTDNVEALYRYA-----KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSK 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958750301 570 VAARGLDI--ENVQHVINFDLPSTiDEYVHRIGRTGRCGNTGRAISFF 615
Cdd:cd18789   103 VGDEGIDLpeANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
297-419 1.14e-04

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 43.79  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 297 RDLMACAQTGSGKT--AAFLLPILAHmmrdgitasRFKELQEPECIIV--APTRELINQiylEARKFSFGTCVRAVVIYG 372
Cdd:cd18034    17 RNTIVVLPTGSGKTliAVMLIKEMGE---------LNRKEKNPKKRAVflVPTVPLVAQ---QAEAIRSHTDLKVGEYSG 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958750301 373 GTQFGHSIRQIVQGC----NILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 419
Cdd:cd18034    85 EMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
297-394 1.57e-04

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 43.50  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 297 RDLMACAQTGSGKTAAFLLPILaHMMRDGITASRFKelqePECIIVAPTRELINQIYLEAR-KFS-FGTCVraVVIYGGT 374
Cdd:cd18023    18 KNFVVSAPTGSGKTVLFELAIL-RLLKERNPLPWGN----RKVVYIAPIKALCSEKYDDWKeKFGpLGLSC--AELTGDT 90
                          90       100
                  ....*....|....*....|
gi 1958750301 375 QFGhSIRQIvQGCNILCATP 394
Cdd:cd18023    91 EMD-DTFEI-QDADIILTTP 108
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
278-418 1.83e-04

N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 43.51  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 278 GYTKLTPVQKYSIPIVLAGRD-LMACAQTGSGKTAAFLLPIL----AHMMRDG-ITASRFKelqepeCIIVAPTRELINQ 351
Cdd:cd18019    14 GFKSLNRIQSKLFPAAFETDEnLLLCAPTGAGKTNVALLTILreigKHRNPDGtINLDAFK------IVYIAPMKALVQE 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750301 352 IY--LEARKFSFGTCVRAVViyGGTQFghSIRQIVQgCNILCATPGRlMDII---GKEKIGLKQVKYLVLDE 418
Cdd:cd18019    88 MVgnFSKRLAPYGITVAELT--GDQQL--TKEQISE-TQIIVTTPEK-WDIItrkSGDRTYTQLVRLIIIDE 153
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
541-601 5.56e-04

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 41.18  E-value: 5.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958750301 541 IHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIEN-----VQHVINFDLpSTIDEYVHRIGR 601
Cdd:cd18811    67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGL-SQLHQLRGRVGR 131
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
305-419 7.39e-04

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 40.37  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 305 TGSGKTA-AFLLPIlahmmrdgitasrfkELQEPECIIVAPTRELINQIYLEARKFSFGtcvraVVIYggtQFGHSIRQI 383
Cdd:cd17926    27 TGSGKTLtALALIA---------------YLKELRTLIVVPTDALLDQWKERFEDFLGD-----SSIG---LIGGGKKKD 83
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958750301 384 VQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEA 419
Cdd:cd17926    84 FDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
296-359 1.08e-03

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


Pssm-ID: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 40.74  E-value: 1.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958750301 296 GRDLMACAQTGSGKTAAFLLPILAHMMRDGItasrfkelqePECIIVAPTRELINQIYLEARKF 359
Cdd:cd17930     1 PGLVILEAPTGSGKTEAALLWALKLAARGGK----------RRIIYALPTRATINQMYERIREI 54
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
300-421 1.28e-03

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 40.58  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 300 MACAQTGSGKTAAFLLPILAHMMRDGitasrfkelqePECIIVAPTRELINQIYLEARKFsFGTCVRAVVIYGGTQfGHS 379
Cdd:cd18035    20 LIVLPTGLGKTIIAILVAADRLTKKG-----------GKVLILAPSRPLVEQHAENLKRV-LNIPDKITSLTGEVK-PEE 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958750301 380 IRQIVQGCNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADR 421
Cdd:cd18035    87 RAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
513-607 1.87e-03

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 39.16  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 513 RTMVFVETKKKADFIATFLCQEKIST----TSIHGDR------EQREREQalgDFRCGKCPVLVATSVAARGLDIENVQH 582
Cdd:cd18797    37 KTIVFCRSRKLAELLLRYLKARLVEEgplaSKVASYRagylaeDRREIEA---ELFNGELLGVVATNALELGIDIGGLDA 113
                          90       100
                  ....*....|....*....|....*
gi 1958750301 583 VINFDLPSTIDEYVHRIGRTGRCGN 607
Cdd:cd18797   114 VVLAGYPGSLASLWQQAGRAGRRGK 138
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
541-580 2.21e-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: 2.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958750301 541 IHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENV 580
Cdd:cd18792    66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA 105
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
540-603 2.34e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.45  E-value: 2.34e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750301  540 SIHGD--REQR-EREQAL--GDFRCgkcpvLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTG 603
Cdd:PRK09751   306 SHHGSvsKEQRaITEQALksGELRC-----VVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
302-436 2.56e-03

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 39.55  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 302 CAQTGSGKTAAFLLPILAHmmrdgitasrFKELQEPECIIVAPTRELINQIYLE-ARKFSFGTCVRAVVIYGGTQfghSI 380
Cdd:cd18021    25 GAPTGSGKTVCAELALLRH----------WRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLGKKVVKLTGETS---TD 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750301 381 RQIVQGCNILCATPGRLmDIIG---KEKIGLKQVKYLVLDEAdRMLDMGFGPEMKKLIS 436
Cdd:cd18021    92 LKLLAKSDVILATPEQW-DVLSrrwKQRKNVQSVELFIADEL-HLIGGENGPVYEVVVS 148
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
298-470 3.44e-03

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


Pssm-ID: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 39.34  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 298 DLMACAQTGSGKTAAFLLPILaHMMRDGITASRFKELQEPECIIVAPTRELINQI--YLEARKFSFGTCVRAVViyGGTQ 375
Cdd:cd18020    19 NMLICAPTGAGKTNIAMLTIL-HEIRQHVNQGGVIKKDDFKIVYIAPMKALAAEMveKFSKRLAPLGIKVKELT--GDMQ 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 376 FGhsiRQIVQGCNILCATPGRlMDIIGKEKIG----LKQVKYLVLDEAdRMLDMGFGPEMKKLIScPGMPSKEQRQTLL- 450
Cdd:cd18020    96 LT---KKEIAETQIIVTTPEK-WDVVTRKSSGdvalSQLVRLLIIDEV-HLLHDDRGPVIESLVA-RTLRQVESTQSMIr 169
                         170       180
                  ....*....|....*....|...
gi 1958750301 451 ---FSATFPEEIQrlAGEFLKSN 470
Cdd:cd18020   170 ivgLSATLPNYLD--VADFLRVN 190
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
278-419 5.51e-03

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


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 38.78  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 278 GYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLP--ILAHmMRDGITasrfkelqepecIIVAPTREL-INQI-Y 353
Cdd:cd18018     9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPalLLRR-RGPGLT------------LVVSPLIALmKDQVdA 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958750301 354 LEARkfsfgtcVRAVVIYGG---TQFGHSIRQIVQG-CNILCATPGRLMDIIGKEKI-GLKQVKYLVLDEA 419
Cdd:cd18018    76 LPRA-------IKAAALNSSltrEERRRILEKLRAGeVKILYVSPERLVNESFRELLrQTPPISLLVVDEA 139
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
287-421 7.16e-03

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 38.57  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750301 287 KYSIPIVLA---GRDLMACAQTGSGKTAafllpILAHMMRDGITasRFKELQEPECIIVAPTRELINQiylEARKFS--F 361
Cdd:cd17927     5 NYQLELAQPalkGKNTIICLPTGSGKTF-----VAVLICEHHLK--KFPAGRKGKVVFLANKVPLVEQ---QKEVFRkhF 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750301 362 GTCVRAVV-IYGGTQFGHSIRQIVQGCNILCATPGRLM-DIIGKEKIGLKQVKYLVLDEADR 421
Cdd:cd17927    75 ERPGYKVTgLSGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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