NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|242012580|ref|XP_002427009|]
View 

DEAD box ATP-dependent RNA helicase, putative [Pediculus humanus corporis]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423521)

DEAD/DEAH box-containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0005524
PubMed:  20206133
SCOP:  4000282|3002019

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
130-509 9.32e-166

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 476.56  E-value: 9.32e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 130 INSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMskssfctPE 209
Cdd:COG0513    1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA-------PQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 210 VIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDE 289
Cdd:COG0513   74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 290 ADRMLDMGFISEIKKMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVGGACSDVVQKFFSVSKFQKR 369
Cdd:COG0513  154 ADRMLDMGFIEDIERILKL----LPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 370 NKLIELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKN 449
Cdd:COG0513  230 ELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDD 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 450 VAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYDPlcdsHLAPALVKILSQAGQEIP 509
Cdd:COG0513  310 VSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTP----DERRLLRAIEKLIGQKIE 365
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
130-509 9.32e-166

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 476.56  E-value: 9.32e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 130 INSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMskssfctPE 209
Cdd:COG0513    1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA-------PQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 210 VIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDE 289
Cdd:COG0513   74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 290 ADRMLDMGFISEIKKMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVGGACSDVVQKFFSVSKFQKR 369
Cdd:COG0513  154 ADRMLDMGFIEDIERILKL----LPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 370 NKLIELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKN 449
Cdd:COG0513  230 ELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDD 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 450 VAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYDPlcdsHLAPALVKILSQAGQEIP 509
Cdd:COG0513  310 VSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTP----DERRLLRAIEKLIGQKIE 365
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
88-350 1.10e-146

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: 422.07  E-value: 1.10e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580  88 YIPDDPTEDDNEIFgNHISSGINFEKYDDIEVKVSGKNPPKSINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMS 167
Cdd:cd18052    1 YIPPPPPEDEDEIF-ATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 168 GRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSFC-TPEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTA 246
Cdd:cd18052   80 GRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVqEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 247 VFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISEIKKMINHPTMKSSSQRQTLMFSATF 326
Cdd:cd18052  160 VGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATF 239
                        250       260
                 ....*....|....*....|....*
gi 242012580 327 PSEVQHLAKTFLN-NYLFVVVGIVG 350
Cdd:cd18052  240 PEEIQRLAAEFLKeDYLFLTVGRVG 264
PTZ00110 PTZ00110
helicase; Provisional
121-509 1.89e-115

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 352.54  E-value: 1.89e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 121 VSGKNPPKSINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIM 200
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLR 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 201 SKSSfctPEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFS 280
Cdd:PTZ00110 200 YGDG---PIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLR 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 281 MTEFLILDEADRMLDMGFISEIKKMINhptmKSSSQRQTLMFSATFPSEVQHLAKTFLNNY-LFVVVGIVG-GACSDVVQ 358
Cdd:PTZ00110 277 RVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEpVHVNVGSLDlTACHNIKQ 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 359 KFFSVSKFQKRNKLIELLES--NGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILV 436
Cdd:PTZ00110 353 EVFVVEEHEKRGKLKMLLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMI 432
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242012580 437 ATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYDPlcDSH-LAPALVKILSQAGQEIP 509
Cdd:PTZ00110 433 ATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP--DKYrLARDLVKVLREAKQPVP 504
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
155-333 4.59e-60

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 195.92  E-value: 4.59e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580  155 TPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQimskssfcTPEVIIMTPTRELTIQIFEEARKFSRGT 234
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN--------GPQALVLAPTRELAEQIYEELKKLGKGL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580  235 FLKVALTYGGTAVFHQVEKIKnGCNILVATPGRLLDFVQRgIIDFSMTEFLILDEADRMLDMGFISEIKKMINHPtmksS 314
Cdd:pfam00270  73 GLKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL----P 146
                         170
                  ....*....|....*....
gi 242012580  315 SQRQTLMFSATFPSEVQHL 333
Cdd:pfam00270 147 KKRQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
146-347 1.45e-53

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 180.00  E-value: 1.45e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580   146 INKCQYHKPTPIQKHCIPIIMSG-RDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMskssfctpeVIIMTPTRELTIQIF 224
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGR---------VLVLVPTRELAEQWA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580   225 EEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGC-NILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISEIK 303
Cdd:smart00487  72 EELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLE 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 242012580   304 KMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVG 347
Cdd:smart00487 152 KLLKL----LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVG 191
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
130-509 9.32e-166

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 476.56  E-value: 9.32e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 130 INSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMskssfctPE 209
Cdd:COG0513    1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA-------PQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 210 VIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDE 289
Cdd:COG0513   74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 290 ADRMLDMGFISEIKKMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVGGACSDVVQKFFSVSKFQKR 369
Cdd:COG0513  154 ADRMLDMGFIEDIERILKL----LPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 370 NKLIELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKN 449
Cdd:COG0513  230 ELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDD 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 450 VAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYDPlcdsHLAPALVKILSQAGQEIP 509
Cdd:COG0513  310 VSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTP----DERRLLRAIEKLIGQKIE 365
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
88-350 1.10e-146

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: 422.07  E-value: 1.10e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580  88 YIPDDPTEDDNEIFgNHISSGINFEKYDDIEVKVSGKNPPKSINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMS 167
Cdd:cd18052    1 YIPPPPPEDEDEIF-ATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 168 GRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSFC-TPEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTA 246
Cdd:cd18052   80 GRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVqEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 247 VFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISEIKKMINHPTMKSSSQRQTLMFSATF 326
Cdd:cd18052  160 VGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATF 239
                        250       260
                 ....*....|....*....|....*
gi 242012580 327 PSEVQHLAKTFLN-NYLFVVVGIVG 350
Cdd:cd18052  240 PEEIQRLAAEFLKeDYLFLTVGRVG 264
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
132-350 3.08e-139

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: 401.09  E-value: 3.08e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 132 SFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQI--MSKSSFCTPE 209
Cdd:cd17967    1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPsvGRGRRKAYPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 210 VIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDE 289
Cdd:cd17967   81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242012580 290 ADRMLDMGFISEIKKMINHPTMKSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVG 350
Cdd:cd17967  161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
PTZ00110 PTZ00110
helicase; Provisional
121-509 1.89e-115

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 352.54  E-value: 1.89e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 121 VSGKNPPKSINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIM 200
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLR 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 201 SKSSfctPEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFS 280
Cdd:PTZ00110 200 YGDG---PIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLR 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 281 MTEFLILDEADRMLDMGFISEIKKMINhptmKSSSQRQTLMFSATFPSEVQHLAKTFLNNY-LFVVVGIVG-GACSDVVQ 358
Cdd:PTZ00110 277 RVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWSATWPKEVQSLARDLCKEEpVHVNVGSLDlTACHNIKQ 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 359 KFFSVSKFQKRNKLIELLES--NGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILV 436
Cdd:PTZ00110 353 EVFVVEEHEKRGKLKMLLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMI 432
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242012580 437 ATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYDPlcDSH-LAPALVKILSQAGQEIP 509
Cdd:PTZ00110 433 ATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP--DKYrLARDLVKVLREAKQPVP 504
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
111-350 6.79e-107

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: 319.68  E-value: 6.79e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 111 FEKYDDIEVKVSGKNPPKSINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPII 190
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 191 NKLLEKNQIMSKSSFCT--------PEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILV 262
Cdd:cd18051   81 SQIYEQGPGESLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 263 ATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISEIKKMINHPTMKSSSQRQTLMFSATFPSEVQHLAKTFLNNYL 342
Cdd:cd18051  161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYI 240

                 ....*...
gi 242012580 343 FVVVGIVG 350
Cdd:cd18051  241 FLAVGRVG 248
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
129-487 2.06e-100

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 310.58  E-value: 2.06e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 129 SINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLleknqimSKSSFCTp 208
Cdd:PRK11776   2 SMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-------DVKRFRV- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 209 EVIIMTPTRELTIQIFEEARKFSRGTF-LKVaLTY-GGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLI 286
Cdd:PRK11776  74 QALVLCPTRELADQVAKEIRRLARFIPnIKV-LTLcGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 287 LDEADRMLDMGFISEIKKMINH-PTmksssQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVGGAcSDVVQKFFSVSK 365
Cdd:PRK11776 153 LDEADRMLDMGFQDAIDAIIRQaPA-----RRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 366 FQKRNKLIELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGL 445
Cdd:PRK11776 227 DERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGL 306
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 242012580 446 DIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYDP 487
Cdd:PRK11776 307 DIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAP 348
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
132-483 6.90e-98

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 304.04  E-value: 6.90e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 132 SFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIInKLLEKNQIMSKSSfcTP-EV 210
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLL-QHLITRQPHAKGR--RPvRA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 211 IIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEA 290
Cdd:PRK10590  79 LILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 291 DRMLDMGFISEIKKMINhptmKSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVGGACSDVVQKFFSVSKFQKRN 370
Cdd:PRK10590 159 DRMLDMGFIHDIRRVLA----KLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRE 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 371 KLIELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKNV 450
Cdd:PRK10590 235 LLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEEL 314
                        330       340       350
                 ....*....|....*....|....*....|...
gi 242012580 451 AHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATS 483
Cdd:PRK10590 315 PHVVNYELPNVPEDYVHRIGRTGRAAATGEALS 347
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
142-344 6.03e-94

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: 284.72  E-value: 6.03e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 142 LINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSsfctPEVIIMTPTRELTI 221
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRG----PQALVLAPTRELAM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 222 QIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISE 301
Cdd:cd00268   77 QIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEED 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 242012580 302 IKKMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFV 344
Cdd:cd00268  157 VEKILSA----LPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
126-501 7.08e-93

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 291.82  E-value: 7.08e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 126 PPKSINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEkNQIMSKSSF 205
Cdd:PRK01297  82 PQEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQ-TPPPKERYM 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 206 CTPEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIK-NGCNILVATPGRLLDFVQRGIIDFSMTEF 284
Cdd:PRK01297 161 GEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEV 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 285 LILDEADRMLDMGFISEIKKMINHPTMKSssQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVGGACSDVVQKFFSVS 364
Cdd:PRK01297 241 MVLDEADRMLDMGFIPQVRQIIRQTPRKE--ERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVA 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 365 KFQKRNKLIELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARG 444
Cdd:PRK01297 319 GSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRG 398
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 242012580 445 LDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYDPlCDSHLAPALVKIL 501
Cdd:PRK01297 399 IHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGE-DDAFQLPEIEELL 454
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
133-484 2.73e-92

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 288.41  E-value: 2.73e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 133 FNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSfCTPEVII 212
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKV-NQPRALI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 213 MTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADR 292
Cdd:PRK04837  89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 293 MLDMGFISEIKKMINHptMKSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVGGACSDVVQKFFSVSKFQKRNKL 372
Cdd:PRK04837 169 MFDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 373 IELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKNVAH 452
Cdd:PRK04837 247 QTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTH 326
                        330       340       350
                 ....*....|....*....|....*....|..
gi 242012580 453 VVNFDLPKTIDEYVHRIGRTGRVGNRGLATSF 484
Cdd:PRK04837 327 VFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
133-500 1.08e-90

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 284.91  E-value: 1.08e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 133 FNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQimSKSSFctPEVII 212
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPR--RKSGP--PRILI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 213 MTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADR 292
Cdd:PRK11192  79 LTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 293 MLDMGFISEIKKMinhpTMKSSSQRQTLMFSATFPSE-VQHLAKTFLNNYLFVvvgivggacsDV---------VQKFF- 361
Cdd:PRK11192 159 MLDMGFAQDIETI----AAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEV----------EAepsrrerkkIHQWYy 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 362 -SVSKFQKRNKLIELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSV 440
Cdd:PRK11192 225 rADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDV 304
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 441 AARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSfydpLCDSHLAPALVKI 500
Cdd:PRK11192 305 AARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAIS----LVEAHDHLLLGKI 360
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
132-486 4.94e-86

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 278.66  E-value: 4.94e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 132 SFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLleknqimsKSSFCTPEVI 211
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--------DPELKAPQIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 212 IMTPTRELTIQIFEEARKFS---RGtfLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILD 288
Cdd:PRK11634  79 VLAPTRELAVQVAEAMTDFSkhmRG--VNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 289 EADRMLDMGFISEIKKMINhptmKSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVGGACSDVVQKFFSVSKFQK 368
Cdd:PRK11634 157 EADEMLRMGFIEDVETIMA----QIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 369 RNKLIELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIK 448
Cdd:PRK11634 233 NEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVE 312
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 242012580 449 NVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYD 486
Cdd:PRK11634 313 RISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVE 350
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
117-509 2.14e-84

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 271.28  E-value: 2.14e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 117 IEVKVSGKNPPKSINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLlEK 196
Cdd:PLN00206 107 LEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRC-CT 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 197 NQIMSKSSFCTPEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGI 276
Cdd:PLN00206 186 IRSGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHD 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 277 IDFSMTEFLILDEADRMLDMGFISEIKKMInhptmKSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVGGACSDV 356
Cdd:PLN00206 266 IELDNVSVLVLDEVDCMLERGFRDQVMQIF-----QALSQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAV 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 357 VQKFFSVSKFQKRNKLIELLESNGSSK--CLVFVEQKRTTDFIATFLCE-KNFPATSIHGDRDQREREEALRDFKTGKMD 433
Cdd:PLN00206 341 KQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVP 420
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242012580 434 ILVATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYDPLcDSHLAPALVKILSQAGQEIP 509
Cdd:PLN00206 421 VIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE-DRNLFPELVALLKSSGAAIP 495
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
155-509 7.22e-81

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 263.35  E-value: 7.22e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 155 TPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSFcTPEVIIMTPTRELTIQIFEEARKFSRGT 234
Cdd:PRK04537  33 TPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKPE-DPRALILAPTRELAIQIHKDAVKFGADL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 235 FLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFV-QRGIIDFSMTEFLILDEADRMLDMGFISEIKKMINHptMKS 313
Cdd:PRK04537 112 GLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVkQHKVVSLHACEICVLDEADRMFDLGFIKDIRFLLRR--MPE 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 314 SSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVGGACSDVVQKFFSVSKFQKRNKLIELLESNGSSKCLVFVEQKRT 393
Cdd:PRK04537 190 RGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAF 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 394 TDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTG 473
Cdd:PRK04537 270 VERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTA 349
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 242012580 474 RVGNRGLATSFydpLCDSHlAPALVKILSQAGQEIP 509
Cdd:PRK04537 350 RLGEEGDAISF---ACERY-AMSLPDIEAYIEQKIP 381
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
120-340 1.72e-70

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: 224.95  E-value: 1.72e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 120 KVSGKNPPKSINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLleKNQI 199
Cdd:cd17953    1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI--KDQR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 200 MSKSSfCTPEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFV---QRGI 276
Cdd:cd17953   79 PVKPG-EGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRV 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242012580 277 IDFSMTEFLILDEADRMLDMGFISEIKKMINH--PtmksssQRQTLMFSATFPSEVQHLAKTFLNN 340
Cdd:cd17953  158 TNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNirP------DRQTVLFSATFPRKVEALARKVLHK 217
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
142-344 5.04e-69

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: 221.04  E-value: 5.04e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 142 LINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSFCTPEVIIMTPTRELTI 221
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKDDGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 222 QIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISE 301
Cdd:cd17945   81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 242012580 302 IKKMINH--PTMKS--------------SSQRQTLMFSATFPSEVQHLAKTFLNNYLFV 344
Cdd:cd17945  161 VTKILDAmpVSNKKpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
142-347 6.98e-68

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: 217.46  E-value: 6.98e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 142 LINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQImskssfCTPEVIIMTPTRELTI 221
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKK------KGLRALILAPTRELAS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 222 QIFEEARKFSRGTFLKVA-LTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFIS 300
Cdd:cd17957   75 QIYRELLKLSKGTGLRIVlLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFRE 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 242012580 301 EIKKMInhpTMKSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVG 347
Cdd:cd17957  155 QTDEIL---AACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
142-345 2.34e-65

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: 210.73  E-value: 2.34e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 142 LINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSfctPEVIIMTPTRELTI 221
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEG---PIAVIVAPTRELAQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 222 QIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISE 301
Cdd:cd17952   78 QIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQ 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 242012580 302 IKKMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVV 345
Cdd:cd17952  158 VRSIVGH----VRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
PTZ00424 PTZ00424
helicase 45; Provisional
125-487 3.58e-64

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 214.69  E-value: 3.58e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 125 NPPKSINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLleknqimsKSS 204
Cdd:PTZ00424  22 NYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI--------DYD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 205 FCTPEVIIMTPTRELTIQIFEEArkFSRGTFLKVAL--TYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMT 282
Cdd:PTZ00424  94 LNACQALILAPTRELAQQIQKVV--LALGDYLKVRChaCVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 283 EFLILDEADRMLDMGFISEIKKMINhptmKSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVGIVGGACSDVVQKFFS 362
Cdd:PTZ00424 172 KLFILDEADEMLSRGFKGQIYDVFK----KLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVA 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 363 VSKFQ-KRNKLIELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVA 441
Cdd:PTZ00424 248 VEKEEwKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLL 327
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 242012580 442 ARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYDP 487
Cdd:PTZ00424 328 ARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTP 373
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
142-345 1.20e-63

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: 206.45  E-value: 1.20e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 142 LINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSfctPEVIIMTPTRELTI 221
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDG---PIVLVLAPTRELAQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 222 QIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISE 301
Cdd:cd17966   78 QIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQ 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 242012580 302 IKKMINhptmKSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVV 345
Cdd:cd17966  158 IRKIVD----QIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
146-340 2.73e-62

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: 202.87  E-value: 2.73e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 146 INKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKnqimsKSSFCTPEVIIMTPTRELTIQIFE 225
Cdd:cd17947    5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYR-----PKKKAATRVLVLVPTRELAMQCFS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 226 EARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGI-IDFSMTEFLILDEADRMLDMGFISEIKK 304
Cdd:cd17947   80 VLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADELKE 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 242012580 305 MINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNN 340
Cdd:cd17947  160 ILRL----CPRTRQTMLFSATMTDEVKDLAKLSLNK 191
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
132-344 3.05e-60

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: 197.91  E-value: 3.05e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 132 SFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSfctpevI 211
Cdd:cd17959    2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARA------L 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 212 IMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEAD 291
Cdd:cd17959   76 ILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEAD 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242012580 292 RMLDMGFISEIKKMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFV 344
Cdd:cd17959  156 RLFEMGFAEQLHEILSR----LPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
155-333 4.59e-60

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 195.92  E-value: 4.59e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580  155 TPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQimskssfcTPEVIIMTPTRELTIQIFEEARKFSRGT 234
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN--------GPQALVLAPTRELAEQIYEELKKLGKGL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580  235 FLKVALTYGGTAVFHQVEKIKnGCNILVATPGRLLDFVQRgIIDFSMTEFLILDEADRMLDMGFISEIKKMINHPtmksS 314
Cdd:pfam00270  73 GLKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL----P 146
                         170
                  ....*....|....*....
gi 242012580  315 SQRQTLMFSATFPSEVQHL 333
Cdd:pfam00270 147 KKRQILLLSATLPRNLEDL 165
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
140-344 2.02e-59

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


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 195.88  E-value: 2.02e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 140 STLINLINKCQYHKPTPIQKHCIPIIMS-GRDLMGCAQTGSGKTAAFLIPIINKLLeKNQIMSKSSfcTPEVIIMTPTRE 218
Cdd:cd17964    3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLL-NTKPAGRRS--GVSALIISPTRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 219 LTIQIFEEARKFSRG-TFLKVALTYGGTAVFHQVEKI-KNGCNILVATPGRLLDFV--QRGIIDFSMTEFLILDEADRML 294
Cdd:cd17964   80 LALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLenPGVAKAFTDLDYLVLDEADRLL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 242012580 295 DMGFISEIKKMINHPTMKSSSQRQTLMFSATFPSEVQHLAKTFLN-NYLFV 344
Cdd:cd17964  160 DMGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKkDYKFI 210
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
356-485 8.14e-58

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 188.49  E-value: 8.14e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 356 VVQKFFSVSKFQKRNKLI-ELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDI 434
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 242012580 435 LVATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFY 485
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
133-343 3.34e-57

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: 189.74  E-value: 3.34e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 133 FNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKnqimSKSSFCtpevII 212
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSED----PYGIFA----LV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 213 MTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQ---RGIIDFSMTEFLILDE 289
Cdd:cd17955   73 LTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDE 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 242012580 290 ADRMLDMGFISEIKKMINH-PTmksssQRQTLMFSATFPSEVQHLAKTFLNNYLF 343
Cdd:cd17955  153 ADRLLTGSFEDDLATILSAlPP-----KRQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
142-340 1.20e-56

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: 188.17  E-value: 1.20e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 142 LINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLL------EKNQIMSkssfctpevIIMTP 215
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLkrkanlKKGQVGA---------LIISP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 216 TRELTIQIFEEARKFSRGTF--LKVALTYGGTAVFHQVEKIK-NGCNILVATPGRLLDFVQR--GIIDFSMTEFLILDEA 290
Cdd:cd17960   72 TRELATQIYEVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDEA 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 242012580 291 DRMLDMGFISEIKKMINH-PtmkssSQRQTLMFSATFPSEVQHLAKTFLNN 340
Cdd:cd17960  152 DRLLDLGFEADLNRILSKlP-----KQRRTGLFSATQTDAVEELIKAGLRN 197
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
118-347 1.42e-56

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: 189.06  E-value: 1.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 118 EVKVSGKNPPKSINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPII-----NK 192
Cdd:cd18049   11 EITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIvhinhQP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 193 LLEKNQimskssfcTPEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFV 272
Cdd:cd18049   91 FLERGD--------GPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242012580 273 QRGIIDFSMTEFLILDEADRMLDMGFISEIKKMINhptmKSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVG 347
Cdd:cd18049  163 EAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
133-340 1.45e-53

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: 180.19  E-value: 1.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 133 FNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKL-LEKNQImskssfctpEVI 211
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdPKKDVI---------QAL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 212 IMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEAD 291
Cdd:cd17940   72 ILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEAD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 242012580 292 RMLDMGFISEIKKMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNN 340
Cdd:cd17940  152 KLLSQDFQPIIEKILNF----LPKERQILLFSATFPLTVKNFMDRHMHN 196
DEXDc smart00487
DEAD-like helicases superfamily;
146-347 1.45e-53

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 180.00  E-value: 1.45e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580   146 INKCQYHKPTPIQKHCIPIIMSG-RDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMskssfctpeVIIMTPTRELTIQIF 224
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGR---------VLVLVPTRELAEQWA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580   225 EEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGC-NILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISEIK 303
Cdd:smart00487  72 EELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLE 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 242012580   304 KMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVG 347
Cdd:smart00487 152 KLLKL----LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVG 191
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
132-340 2.02e-53

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: 179.82  E-value: 2.02e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 132 SFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMskssFCtpevI 211
Cdd:cd17954    1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRF----FA----L 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 212 IMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQR--GiidFSMT--EFLIL 287
Cdd:cd17954   73 VLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtkG---FSLKslKFLVM 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242012580 288 DEADRMLDMGFISEIKKMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNN 340
Cdd:cd17954  150 DEADRLLNMDFEPEIDKILKV----IPRERTTYLFSATMTTKVAKLQRASLKN 198
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
150-346 6.63e-53

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: 178.25  E-value: 6.63e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 150 QYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKL-LEKnqimskssfCTPE----VIIMTPTRELTIQIF 224
Cdd:cd17941    9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyRER---------WTPEdglgALIISPTRELAMQIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 225 EEARKFSRGTFLKVALTYGGTAVFHQVEKIkNGCNILVATPGRLLDFVQRGI-IDFSMTEFLILDEADRMLDMGFISEIK 303
Cdd:cd17941   80 EVLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRILDMGFKETLD 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 242012580 304 KMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVV 346
Cdd:cd17941  159 AIVEN----LPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
118-347 2.20e-52

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


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 179.44  E-value: 2.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 118 EVKVSGKNPPKSINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKN 197
Cdd:cd18050   49 EITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQP 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 198 QIMSKSSfctPEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGII 277
Cdd:cd18050  129 YLERGDG---PICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT 205
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 278 DFSMTEFLILDEADRMLDMGFISEIKKMINhptmKSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVVVG 347
Cdd:cd18050  206 NLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
146-345 1.12e-51

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: 174.96  E-value: 1.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 146 INKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEknQIMSKSSFCTPEVIIMTPTRELTIQIFE 225
Cdd:cd17958    5 IKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDL--QPIPREQRNGPGVLVLTPTRELALQIEA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 226 EARKFS-RGtfLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISEIKK 304
Cdd:cd17958   83 ECSKYSyKG--LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 242012580 305 MINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVV 345
Cdd:cd17958  161 ILLD----IRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
144-345 1.30e-51

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: 175.47  E-value: 1.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 144 NLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSFCTpeVIIMTPTRELTIQI 223
Cdd:cd17949    4 HLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDGTL--ALVLVPTRELALQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 224 FEEARKF-SRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQR-GIIDFSMTEFLILDEADRMLDMGFISE 301
Cdd:cd17949   82 YEVLEKLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKD 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242012580 302 IKKMIN---------HPTMKSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFVV 345
Cdd:cd17949  162 ITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
152-338 1.68e-51

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: 174.83  E-value: 1.68e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 152 HKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSFCTPEVIIMTPTRELTIQIFEE----A 227
Cdd:cd17951   11 KKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPFIKGEGPYGLIVCPSRELARQTHEVieyyC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 228 RKFSRGTF--LKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISEIKKM 305
Cdd:cd17951   91 KALQEGGYpqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEEDIRTI 170
                        170       180       190
                 ....*....|....*....|....*....|...
gi 242012580 306 INHPTmkssSQRQTLMFSATFPSEVQHLAKTFL 338
Cdd:cd17951  171 FSYFK----GQRQTLLFSATMPKKIQNFAKSAL 199
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
146-340 3.05e-49

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: 168.69  E-value: 3.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 146 INKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIInKLLEKNQIMSKSSfctPEVIIMTPTRELTIQIFE 225
Cdd:cd17942    5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-ELLYKLKFKPRNG---TGVIIISPTRELALQIYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 226 EAR---KFSRGTFLKVAltyGGTAVFHQVEKIKNGCNILVATPGRLLDFVQ--RGIIdFSMTEFLILDEADRMLDMGFIS 300
Cdd:cd17942   81 VAKellKYHSQTFGIVI---GGANRKAEAEKLGKGVNILVATPGRLLDHLQntKGFL-YKNLQCLIIDEADRILEIGFEE 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 242012580 301 EIKKMINhptmKSSSQRQTLMFSATFPSEVQHLAKTFLNN 340
Cdd:cd17942  157 EMRQIIK----LLPKRRQTMLFSATQTRKVEDLARISLKK 192
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
142-326 1.07e-48

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: 168.19  E-value: 1.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 142 LINLINKCQYHKPTPIQKHCIP-IIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSFCTP-EVIIMTPTREL 219
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPlRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 220 TIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRG---IIDFSMTEFLILDEADRMLDM 296
Cdd:cd17946   81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 242012580 297 G-F--ISEIKKMINHPTMKSSSQRQTLMFSATF 326
Cdd:cd17946  161 GhFaeLEKILELLNKDRAGKKRKRQTFVFSATL 193
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
133-334 8.17e-48

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: 164.80  E-value: 8.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 133 FNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIInklleknQIMSkssfctpeVII 212
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------QIVV--------ALI 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 213 MTPTRELTIQIFEEARKFSR---GTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDE 289
Cdd:cd17938   66 LEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDE 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 242012580 290 ADRMLDMGFISEIKKMINH-PTMKSSSQR-QTLMFSATFPS-EVQHLA 334
Cdd:cd17938  146 ADRLLSQGNLETINRIYNRiPKITSDGKRlQVIVCSATLHSfEVKKLA 193
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
146-344 1.83e-46

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: 160.79  E-value: 1.83e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 146 INKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQimskssfcTPEVIIMTPTRELTIQIFE 225
Cdd:cd17962    5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHR--------NPSALILTPTRELAVQIED 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 226 EARKFSRGTF-LKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISEIKK 304
Cdd:cd17962   77 QAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 242012580 305 MINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFV 344
Cdd:cd17962  157 ILEN----ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
156-338 4.60e-44

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: 155.01  E-value: 4.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 156 PIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSfcTPEVIIMTPTRELTIQIFEEARKFSRGtf 235
Cdd:cd17944   15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGR--APKVLVLAPTRELANQVTKDFKDITRK-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 236 LKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISEIKKMINHPTMKSSS 315
Cdd:cd17944   91 LSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYKKDSE 170
                        170       180
                 ....*....|....*....|....
gi 242012580 316 QR-QTLMFSATFPSEVQHLAKTFL 338
Cdd:cd17944  171 DNpQTLLFSATCPDWVYNVAKKYM 194
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
146-340 6.16e-42

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: 149.27  E-value: 6.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 146 INKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSSFctPEVIIMTPTRELTIQIFE 225
Cdd:cd17961    9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQG--TRALILVPTRELAQQVSK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 226 EARKFSRGTFLKVALTYGGTAVFHQVEK--IKNGCNILVATPGRLLDFVQRG-IIDFSMTEFLILDEADRMLDMGFISEI 302
Cdd:cd17961   87 VLEQLTAYCRKDVRVVNLSASSSDSVQRalLAEKPDIVVSTPARLLSHLESGsLLLLSTLKYLVIDEADLVLSYGYEEDL 166
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 242012580 303 KKMINH-PTMKsssqrQTLMFSATFPSEVQHLAKTFLNN 340
Cdd:cd17961  167 KSLLSYlPKNY-----QTFLMSATLSEDVEALKKLVLHN 200
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
146-344 6.31e-39

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: 140.48  E-value: 6.31e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 146 INKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQimskssfcTPEVIIMTPTRELTIQI-- 223
Cdd:cd17943    5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERR--------HPQVLILAPTREIAVQIhd 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 224 -FEEARKFSRGtfLKVALTYGGTAVFHQVEKIKnGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISEI 302
Cdd:cd17943   77 vFKKIGKKLEG--LKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDV 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 242012580 303 KKMINHptmkSSSQRQTLMFSATFPSEVQHLAKTFLNNYLFV 344
Cdd:cd17943  154 NWIFSS----LPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
367-476 2.97e-37

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 133.10  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580  367 QKRNKLIELLESNGSSKCLVFVEQKRTTDfIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLD 446
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 242012580  447 IKNVAHVVNFDLPKTIDEYVHRIGRTGRVG 476
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
132-346 3.79e-37

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: 136.32  E-value: 3.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 132 SFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINklleknQIMSKSSFCtpEVI 211
Cdd:cd17950    3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQ------QLEPVDGQV--SVL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 212 IMTPTRELTIQIFEEARKFSRgtFL---KVALTYGGTAVFHQVEKIKNGC-NILVATPGRLLDFVQRGIIDFSMTEFLIL 287
Cdd:cd17950   75 VICHTRELAFQISNEYERFSK--YMpnvKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242012580 288 DEADRM---LDM-GFISEIKKMINHptmksssQRQTLMFSATFPSEVQHLAKTFLNNYLFVVV 346
Cdd:cd17950  153 DECDKMleqLDMrRDVQEIFRATPH-------DKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
150-344 3.68e-36

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


Pssm-ID: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 133.08  E-value: 3.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 150 QYHKPTPIQKHCIPIIMSG--RDLMGCAQTGSGKTAAFLIPIINKLLEKNQimskssfcTPEVIIMTPTRELTIQIFEEA 227
Cdd:cd17963   13 GFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLK--------SPQALCLAPTRELARQIGEVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 228 RKFSRGTFLKVALTYGGTAVFHQvEKIKNgcNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDM-GF---ISEIK 303
Cdd:cd17963   85 EKMGKFTGVKVALAVPGNDVPRG-KKITA--QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHgdqSIRIK 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 242012580 304 KMINHPTmksssqrQTLMFSATFPSEVQHLAKTFLNNYLFV 344
Cdd:cd17963  162 RMLPRNC-------QILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
153-333 1.84e-35

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: 132.49  E-value: 1.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 153 KPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKnQIMSKSSFCTPEVIIMTPTRELTIQIFEEARKFSR 232
Cdd:cd17948   12 KPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRY-KLLAEGPFNAPRGLVITPSRELAEQIGSVAQSLTE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 233 GTFLKVALTYGGtavfHQVEKIKN----GCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGFISEIKKMINH 308
Cdd:cd17948   91 GLGLKVKVITGG----RTKRQIRNphfeEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRR 166
                        170       180       190
                 ....*....|....*....|....*....|....
gi 242012580 309 ---------PTMKSSSQRQTLMFSATFPSEVQHL 333
Cdd:cd17948  167 fplasrrseNTDGLDPGTQLVLVSATMPSGVGEV 200
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
151-340 3.38e-34

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: 127.83  E-value: 3.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 151 YHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLleknqimsKSSFCTPEVIIMTPTRELTIQIfeEARKF 230
Cdd:cd17939   17 FEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI--------DTTVRETQALVLAPTRELAQQI--QKVVK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 231 SRGTFL--KVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRMLDMGF---ISEIKKM 305
Cdd:cd17939   87 ALGDYMgvKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFkdqIYDIFQF 166
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 242012580 306 INHPTmksssqrQTLMFSATFPSEVQHLAKTFLNN 340
Cdd:cd17939  167 LPPET-------QVVLFSATMPHEVLEVTKKFMRD 194
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
133-340 6.01e-34

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: 127.56  E-value: 6.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 133 FNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLleknqimsKSSFCTPEVII 212
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI--------DTSLKATQALV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 213 MTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADR 292
Cdd:cd18046   73 LAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADE 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 242012580 293 MLDMGF---ISEIKKMINHPTmksssqrQTLMFSATFPSEVQHLAKTFLNN 340
Cdd:cd18046  153 MLSRGFkdqIYDIFQKLPPDT-------QVVLLSATMPNDVLEVTTKFMRD 196
HELICc smart00490
helicase superfamily c-terminal domain;
395-476 7.04e-31

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 114.62  E-value: 7.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580   395 DFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGR 474
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 242012580   475 VG 476
Cdd:smart00490  81 AG 82
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
133-340 8.09e-31

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: 118.72  E-value: 8.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 133 FNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINklleknqiMSKSSFCTPEVII 212
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ--------CLDIQVRETQALI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 213 MTPTRELTIQIFEEArkFSRGTFLKVAL--TYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEA 290
Cdd:cd18045   73 LSPTRELAVQIQKVL--LALGDYMNVQChaCIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEA 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242012580 291 DRMLDMGF---ISEIKKMINHPTmksssqrQTLMFSATFPSEVQHLAKTFLNN 340
Cdd:cd18045  151 DEMLNKGFkeqIYDVYRYLPPAT-------QVVLVSATLPQDILEMTNKFMTD 196
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
142-334 2.26e-29

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: 115.81  E-value: 2.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 142 LINLINKCQYHKPTPIQKHCIPIIMSG---------RDLMGCAQTGSGKTAAFLIPIInklleknQIMSKSSFCTPEVII 212
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIV-------QALSKRVVPRLRALI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 213 MTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQVEKIKNGC--------NILVATPGRLLDFVQRGI-IDFSMTE 283
Cdd:cd17956   74 VVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDHLNSTPgFTLKHLR 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242012580 284 FLILDEADRMLDMGF-------ISEIKKMINHPTMK---------SSSQRQTLMFSATFPSEVQHLA 334
Cdd:cd17956  154 FLVIDEADRLLNQSFqdwletvMKALGRPTAPDLGSfgdanllerSVRPLQKLLFSATLTRDPEKLS 220
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
150-329 9.23e-25

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: 103.23  E-value: 9.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 150 QYHKPTPIQKHCIPIIMsgRDLMG------------------CAQTGSGKTAAFLIPIINKL---------LEKNQIMSK 202
Cdd:cd17965   27 EEIKPSPIQTLAIKKLL--KTLMRkvtkqtsneepklevfllAAETGSGKTLAYLAPLLDYLkrqeqepfeEAEEEYESA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 203 SSFCTPEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFHQ--VEKIKNGCNILVATPGRLLDFVQRGIIDFS 280
Cdd:cd17965  105 KDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQrlQLAFKGRIDILVTTPGKLASLAKSRPKILS 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 242012580 281 MTEFLILDEADRMLDMGFISEIKKMInhptmKSSSQRQTLMF-SATFPSE 329
Cdd:cd17965  185 RVTHLVVDEADTLFDRSFLQDTTSII-----KRAPKLKHLILcSATIPKE 229
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
119-335 2.42e-20

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: 90.08  E-value: 2.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 119 VKVSGKNPPK---SINSFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSG--RDLMGCAQTGSGKTAAFLIPIINKl 193
Cdd:cd18048    3 VEVLQRDPTSplfSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 194 leknqIMSKSSFctPEVIIMTPTRELTIQ---IFEEARKFSRGTFLKVALTYGGTAVFHQVEKikngcNILVATPGRLLD 270
Cdd:cd18048   82 -----VDALKLY--PQCLCLSPTFELALQtgkVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEA-----QIVIGTPGTVLD 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242012580 271 FV-QRGIIDFSMTEFLILDEADRMLDMGFISEIKKMINHPTMKSSsqrQTLMFSATFPSEVQHLAK 335
Cdd:cd18048  150 WCfKLRLIDVTNISVFVLDEADVMINVQGHSDHSVRVKRSMPKEC---QMLLFSATFEDSVWAFAE 212
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
358-471 1.13e-18

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: 82.64  E-value: 1.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 358 QKFFSVSKFQKrnkLIELL----ESNGSSKCLVFVEQKRTTDFIATFL-----CEKNFPATSI--HGDRDQRER------ 420
Cdd:cd18802    1 EEIVVIPKLQK---LIEILreyfPKTPDFRGIIFVERRATAVVLSRLLkehpsTLAFIRCGFLigRGNSSQRKRslmtqr 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242012580 421 --EEALRDFKTGKMDILVATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGR 471
Cdd:cd18802   78 kqKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
177-486 2.33e-18

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 88.16  E-value: 2.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 177 TGSGKT--AAFlipIINKLLEKNQimskssfctpeVIIMTPTRELTIQIFEEARKFsrgtfLKVALTYGGtavfhqveKI 254
Cdd:COG1061  109 TGTGKTvlALA---LAAELLRGKR-----------VLVLVPRRELLEQWAEELRRF-----LGDPLAGGG--------KK 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 255 KNGCNILVATPGRL-----LDFVQRgiiDFSMtefLILDEADRMLDMGFiseiKKMINHptmksSSQRQTLMFSAT-FPS 328
Cdd:COG1061  162 DSDAPITVATYQSLarrahLDELGD---RFGL---VIIDEAHHAGAPSY----RRILEA-----FPAAYRLGLTATpFRS 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 329 EVQHLAKTFLNN--------------YL--FVVVGIVGG---------ACSDVVQKFFSVSKFQKRNKLIELLESNGS-S 382
Cdd:COG1061  227 DGREILLFLFDGivyeyslkeaiedgYLapPEYYGIRVDltderaeydALSERLREALAADAERKDKILRELLREHPDdR 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 383 KCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKNVAHVVNFDLPKTI 462
Cdd:COG1061  307 KTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSP 386
                        330       340
                 ....*....|....*....|....
gi 242012580 463 DEYVHRIGRTGRVGNRGLATSFYD 486
Cdd:COG1061  387 REFIQRLGRGLRPAPGKEDALVYD 410
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
368-474 1.46e-17

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 85.94  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 368 KRNKLIEL----LESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHG--DRD------QREREEALRDFKTGKMDIL 435
Cdd:COG1111  336 KLSKLREIlkeqLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGEFNVL 415
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 242012580 436 VATSVAARGLDIKNVAHVVNFDL-PKTIdEYVHRIGRTGR 474
Cdd:COG1111  416 VATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR 454
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
367-487 4.04e-17

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 84.04  E-value: 4.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 367 QKRNKLIELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSvaARGL- 445
Cdd:COG0514  216 DKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AFGMg 293
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 242012580 446 -DIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYDP 487
Cdd:COG0514  294 iDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGP 336
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
132-335 8.68e-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: 70.52  E-value: 8.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 132 SFNEAGLCSTLINLINKCQYHKPTPIQKHCIPIIMSG--RDLMGCAQTGSGKTAAFLIPIINKLleknQIMSKSSFCtpe 209
Cdd:cd18047    2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV----EPANKYPQC--- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 210 vIIMTPTRELTIQ---IFEEARKFsrgtFLKVALTYGGTAvfHQVEK-IKNGCNILVATPGRLLDF-VQRGIIDFSMTEF 284
Cdd:cd18047   75 -LCLSPTYELALQtgkVIEQMGKF----YPELKLAYAVRG--NKLERgQKISEQIVIGTPGTVLDWcSKLKFIDPKKIKV 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 242012580 285 LILDEADRMLDMGFISEIKKMINHPTMKSSsqrQTLMFSATFPSEVQHLAK 335
Cdd:cd18047  148 FVLDEADVMIATQGHQDQSIRIQRMLPRNC---QMLLFSATFEDSVWKFAQ 195
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
368-470 6.23e-13

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: 65.96  E-value: 6.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 368 KRNKLIELLESNGSS--KCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMD--ILVATSVAAR 443
Cdd:cd18793   12 KLEALLELLEELREPgeKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGV 91
                         90       100       110
                 ....*....|....*....|....*....|...
gi 242012580 444 GLDIKNVAHVVNFDLP--KTIDEY----VHRIG 470
Cdd:cd18793   92 GLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
360-485 7.80e-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: 65.69  E-value: 7.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 360 FFSVS-KFQKRNKLIELLESNGSSK---CLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDIL 435
Cdd:cd18794    5 FYSVRpKDKKDEKLDLLKRIKVEHLggsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 242012580 436 VATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFY 485
Cdd:cd18794   85 VATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
PRK13766 PRK13766
Hef nuclease; Provisional
368-474 1.24e-12

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 70.67  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 368 KRNKLIEL----LESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHG--DRD------QREREEALRDFKTGKMDIL 435
Cdd:PRK13766 348 KLEKLREIvkeqLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaSKDgdkgmsQKEQIEILDKFRAGEFNVL 427
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 242012580 436 VATSVAARGLDIKNVAHVVNFD-LPKTIdEYVHRIGRTGR 474
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR 466
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
174-325 6.48e-12

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 63.19  E-value: 6.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 174 CAQTGSGKTAAFLIPIINKLLEKNqimskssfctPEVIIMTPTRELTIQIFEEARKFSRGTfLKVALTYGGTAVFHQVEK 253
Cdd:cd00046    7 TAPTGSGKTLAALLAALLLLLKKG----------KKVLVLVPTKALALQTAERLRELFGPG-IRVAVLVGGSSAEEREKN 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242012580 254 IKNGCNILVATPGRLLDFVQR-GIIDFSMTEFLILDEADRMLDMGFISEIKKMINHPTMKSSSQRqtLMFSAT 325
Cdd:cd00046   76 KLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV--ILLSAT 146
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
368-475 1.78e-11

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 66.79  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 368 KRNKLIELLESNGSS--KCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGK--MDILVATSVAAR 443
Cdd:COG0553  534 KLEALLELLEELLAEgeKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGE 613
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 242012580 444 GLDIKNVAHVVNFDLP-------KTIDEyVHRIGRTGRV 475
Cdd:COG0553  614 GLNLTAADHVIHYDLWwnpaveeQAIDR-AHRIGQTRDV 651
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
372-474 7.09e-11

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: 60.36  E-value: 7.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 372 LIELLESngSSKCLVFVEQKRTTDFIAT---FLCEKNFPATSI---HG--DRDQREREEAlrDFKTGKMDILVATSVAAR 443
Cdd:cd18796   31 VIFLLER--HKSTLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEVEA--ALKRGDLKVVVATSSLEL 106
                         90       100       110
                 ....*....|....*....|....*....|.
gi 242012580 444 GLDIKNVAHVVNFDLPKTIDEYVHRIGRTGR 474
Cdd:cd18796  107 GIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
165-481 5.10e-10

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 62.16  E-value: 5.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 165 IMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQimskssfCTpeVIIMTPTRELTIQIFEEARKFSRGTFLKV-ALTYG 243
Cdd:COG1205   68 ARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG-------AT--ALYLYPTKALARDQLRRLRELAEALGLGVrVATYD 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 244 GTAVFHQVEKIKNGCNILVATPgrllDFVQRGIID--------FSMTEFLILDEA---------------DRMLDMgfis 300
Cdd:COG1205  139 GDTPPEERRWIREHPDIVLTNP----DMLHYGLLPhhtrwarfFRNLRYVVIDEAhtyrgvfgshvanvlRRLRRI---- 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 301 eIKKMINHPTMksssqrqtLMFSATFPSEVQHLAKtflnnyLF---VVVgiVGGACS------------DVVQKFFSVSK 365
Cdd:COG1205  211 -CRHYGSDPQF--------ILASATIGNPAEHAER------LTgrpVTV--VDEDGSprgertfvlwnpPLVDDGIRRSA 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 366 FQKRNKLIELLESNGsSKCLVFVEQKRTTDFIATFLceKNFPATSIHGDR--------DQREREEALRDFKTGKMDILVA 437
Cdd:COG1205  274 LAEAARLLADLVREG-LRTLVFTRSRRGAELLARYA--RRALREPDLADRvaayragyLPEERREIERGLRSGELLGVVS 350
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 242012580 438 TSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLA 481
Cdd:COG1205  351 TNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
153-325 7.37e-10

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: 58.20  E-value: 7.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 153 KPTPIQKHCIPIIMSG------RDLMGCAQTGSGKTAAFLIPIINKLLEKNQimskssfctpeVIIMTPTRELTIQIFEE 226
Cdd:cd17918   15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYKNGKQ-----------VAILVPTEILAHQHYEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 227 ARKFSrgTFLKVALTYGGTAvfhqvEKIKNGCNILVATPGRLLDFVQrgiidFSMTEFLILDEADRmldmgFISEIKKMI 306
Cdd:cd17918   84 ARKFL--PFINVELVTGGTK-----AQILSGISLLVGTHALLHLDVK-----FKNLDLVIVDEQHR-----FGVAQREAL 146
                        170
                 ....*....|....*....
gi 242012580 307 NhptmkSSSQRQTLMFSAT 325
Cdd:cd17918  147 Y-----NLGATHFLEATAT 160
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
363-487 9.27e-10

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 61.27  E-value: 9.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 363 VSKFQKRNKLIELLESNGSSKCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAA 442
Cdd:PRK11057 218 VEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFG 297
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 242012580 443 RGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFYDP 487
Cdd:PRK11057 298 MGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDP 342
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
155-290 1.14e-09

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 57.66  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 155 TPIQKHCI-PIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQImskssfctpeVIIMTPTRELTIQIFEEARKFSRG 233
Cdd:cd17921    3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK----------AVYIAPTRALVNQKEADLRERFGP 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242012580 234 TFLKVALTYGGTAVFHQVEkikNGCNILVATP----GRLLDFVQRGIIDFSMtefLILDEA 290
Cdd:cd17921   73 LGKNVGLLTGDPSVNKLLL---AEADILVATPekldLLLRNGGERLIQDVRL---VVVDEA 127
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
372-474 3.15e-09

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: 55.44  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 372 LIELLESNGS---SKCLVFVEQKRTTDFIATFLcEKNFP---ATSIHGDRD--------QREREEALRDFKTGKMDILVA 437
Cdd:cd18801   18 VKEHFKKKQEgsdTRVIIFSEFRDSAEEIVNFL-SKIRPgirATRFIGQASgksskgmsQKEQKEVIEQFRKGGYNVLVA 96
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 242012580 438 TSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGR 474
Cdd:cd18801   97 TSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
364-484 5.61e-09

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: 54.95  E-value: 5.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 364 SKFQKRNKLIELLESNGssKCLVFVEQKRTTDFIATFLcekNFPAtsIHGDRDQREREEALRDFKTGKMDILVATSVAAR 443
Cdd:cd18789   34 NKLRALEELLKRHEQGD--KIIVFTDNVEALYRYAKRL---LKPF--ITGETPQSEREEILQNFREGEYNTLVVSKVGDE 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 242012580 444 GLDI--KNVAHVVNFdLPKTIDEYVHRIGRTGRVGNRGLATSF 484
Cdd:cd18789  107 GIDLpeANVAIQISG-HGGSRRQEAQRLGRILRPKKGGGKNAF 148
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
177-290 1.09e-08

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: 55.35  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 177 TGSGKTaafLIPI--INKLLEKNQIMSKSSfctPEVIIMTPTRELTIQIFEEARKFsrgTFLKVALTYGGTAVFHQVEKI 254
Cdd:cd18034   25 TGSGKT---LIAVmlIKEMGELNRKEKNPK---KRAVFLVPTVPLVAQQAEAIRSH---TDLKVGEYSGEMGVDKWTKER 95
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 242012580 255 KNGC----NILVATPGRLLDFVQRGIIDFSMTEFLILDEA 290
Cdd:cd18034   96 WKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
431-479 3.08e-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: 50.78  E-value: 3.08e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 242012580 431 KMDILVATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRG 479
Cdd:cd18785   22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
383-471 1.42e-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: 47.17  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 383 KCLVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQRERE-EALRDFKTG--KMDILVATSVAARGLDIKNVAHVVnFDLP 459
Cdd:cd18799    8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV-FLRP 86
                         90
                 ....*....|...
gi 242012580 460 -KTIDEYVHRIGR 471
Cdd:cd18799   87 tESRTLFLQMLGR 99
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
150-196 1.46e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 51.26  E-value: 1.46e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 242012580 150 QYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKT-AAFLiPIINKLLEK 196
Cdd:COG1201   21 RFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFL-PALDELARR 67
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
175-478 2.01e-06

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 50.12  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 175 AQTGSGKTAAFLIpIINKLLeKNQIMSKssfctpeVIIMTPTRELTIQIFEEAR-------------KFSR-------GT 234
Cdd:cd09639    6 APTGYGKTEAALL-WALHSL-KSQKADR-------VIIALPTRATINAMYRRAKeafgetglyhssiLSSRikemgdsEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 235 FLK-VALTYGGTAVFHQveKIKNGCNILVATPGRLLDFVQRGIIDFSM-TEFLILDEADRMLD--MGFIS---EIKKMIN 307
Cdd:cd09639   77 FEHlFPLYIHSNDTLFL--DPITVCTIDQVLKSVFGEFGHYEFTLASIaNSLLIFDEVHFYDEytLALILavlEVLKDND 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 308 HPTMksssqrqtLMfSATFPSevqhLAKTFLNNYLFVVVGIvGGACSDVVQKFF------SVSKFQKRNKLIEllESNGS 381
Cdd:cd09639  155 VPIL--------LM-SATLPK----FLKEYAEKIGYVEENE-PLDLKPNERAPFikiesdKVGEISSLERLLE--FIKKG 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 382 SKCLVFVEQKRTTDFIATFLCEKN--FPATSIHG-----DRDQRErEEALRDFKTGKMDILVATSVAARGLDIknvahvv 454
Cdd:cd09639  219 GSVAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSrftekDRAKKE-AELLLEFKKSEKFVIVATQVIEASLDI------- 290
                        330       340
                 ....*....|....*....|....*...
gi 242012580 455 NFDL----PKTIDEYVHRIGRTGRVGNR 478
Cdd:cd09639  291 SVDVmiteLAPIDSLIQRLGRLHRYGEK 318
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
155-476 2.14e-06

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 50.28  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 155 TPIQKHCIP-IIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKnqimskssfctPEVIIMTPTRELTIQIFEEARKFSRG 233
Cdd:COG1204   24 YPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNG-----------GKALYIVPLRALASEKYREFKRDFEE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 234 TFLKVALTYGGtavFHQVEKIKNGCNILVATPGRLLDFVQRG---IIDFSMtefLILDEA------DRmldmGFISE--I 302
Cdd:COG1204   93 LGIKVGVSTGD---YDSDDEWLGRYDILVATPEKLDSLLRNGpswLRDVDL---VVVDEAhliddeSR----GPTLEvlL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 303 KKMinhptMKSSSQRQTLMFSATFPSeVQHLAKtFLNNYLFV--------VVGIVggacSDVVQKFFSVSKFQKRNKL-- 372
Cdd:COG1204  163 ARL-----RRLNPEAQIVALSATIGN-AEEIAE-WLDAELVKsdwrpvplNEGVL----YDGVLRFDDGSRRSKDPTLal 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 373 -IELLESNGSskCLVFVEQKRTT--------DFIATFLCEKN-----FPATSIHGDRDQREREEALRD------------ 426
Cdd:COG1204  232 aLDLLEEGGQ--VLVFVSSRRDAeslakklaDELKRRLTPEEreeleELAEELLEVSEETHTNEKLADclekgvafhhag 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242012580 427 ------------FKTGKMDILVATSVAARG--LDIKNVahVV-----NFDLPKTIDEYVHRIGRTGRVG 476
Cdd:COG1204  310 lpselrrlvedaFREGLIKVLVATPTLAAGvnLPARRV--IIrdtkrGGMVPIPVLEFKQMAGRAGRPG 376
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
166-292 4.73e-06

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: 47.43  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 166 MSGRDLMGCAQTGSGKTaaflipIINKLLEKNQIMSKSSFCTPEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGT 245
Cdd:cd17927   15 LKGKNTIICLPTGSGKT------FVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDT 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 242012580 246 AVFHQVEKIKNGCNILVATPGRLLDFVQRGII----DFSMtefLILDEADR 292
Cdd:cd17927   89 SENVSVEQIVESSDVIIVTPQILVNDLKSGTIvslsDFSL---LVFDECHN 136
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
385-460 7.56e-06

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 46.47  E-value: 7.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242012580 385 LVFVEQKRTTDFIATFLCEKNFPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKNVAHVVNFDLPK 460
Cdd:cd18790   31 LVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADK 106
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
411-484 8.96e-06

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: 45.80  E-value: 8.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 411 IHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKNvAHVVnfdlpktIDEYVHRIGRT------GRVGnRGLATSF 484
Cdd:cd18811   67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPN-ATVM-------VIEDAERFGLSqlhqlrGRVG-RGDHQSY 137
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
362-482 1.34e-05

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: 44.94  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 362 SVSKFQKRNKLIELLESNGSsKCLVFVEQKRTTDFIATF----LCEKNFPATSIHGDR---DQREREEALRDFKTGKMDI 434
Cdd:cd18797   17 RGSARREAARLFADLVRAGV-KTIVFCRSRKLAELLLRYlkarLVEEGPLASKVASYRagyLAEDRREIEAELFNGELLG 95
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 242012580 435 LVATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLAT 482
Cdd:cd18797   96 VVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
PRK13767 PRK13767
ATP-dependent helicase; Provisional
150-198 1.64e-05

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 47.57  E-value: 1.64e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 242012580 150 QYHKPTPIQKHCIPIIMSGRDLMGCAQTGSGKT-AAFLIpIINKLLEKNQ 198
Cdd:PRK13767  29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLA-IIDELFRLGR 77
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
167-290 1.97e-05

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: 45.27  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 167 SGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSkssfctpevIIMTPTRELTIQIFEEARKFSRGTFLKVAL-TYGGT 245
Cdd:cd17923   14 AGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRA---------LYLYPTKALAQDQLRSLRELLEQLGLGIRVaTYDGD 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 242012580 246 AVFHQVEKI-KNGCNILVATPGRL----LDFVQRGIIDFSMTEFLILDEA 290
Cdd:cd17923   85 TPREERRAIiRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
177-326 5.34e-05

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: 43.45  E-value: 5.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 177 TGSGKTaAFLIPIINKLLEKNqimskssfctpeVIIMTPTRELTIQIFEEARKFSRGTFLKVaLTYGgtavfhqVEKIKN 256
Cdd:cd17926   27 TGSGKT-LTALALIAYLKELR------------TLIVVPTDALLDQWKERFEDFLGDSSIGL-IGGG-------KKKDFD 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 257 GCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADRmLDMGFISEIKKMINHPTMksssqrqtLMFSATF 326
Cdd:cd17926   86 DANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH-LPAKTFSEILKELNAKYR--------LGLTATP 146
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
411-450 6.93e-05

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: 43.41  E-value: 6.93e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 242012580 411 IHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKNV 450
Cdd:cd18792   66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA 105
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
411-481 8.51e-05

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 43.10  E-value: 8.51e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242012580 411 IHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRI-GRTGRVGNRGLA 481
Cdd:cd18810   57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYA 128
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
370-518 1.10e-04

C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 43.06  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 370 NKLIELLESNGSSkCLVFV---EQKRTTDFIATFLCEKNFPATSIHgdrdqREREEALRDFKTGKMDILVATS----VAA 442
Cdd:cd18798   14 EKLLELVKKLGDG-GLIFVsidYGKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVAsyygVLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 443 RGLDI-KNVAHVVNFDLPKTidEYVHRIGRTGRVGN----RGLATSFYDplcDSHLAPALVKILSQAgqeIPDFLLEFKE 517
Cdd:cd18798   88 RGIDLpERIKYAIFYGVPVT--TYIQASGRTSRLYAggltKGLSVVLVD---DPELFEALKKRLKLI---LDEFIFKELE 159

                 .
gi 242012580 518 T 518
Cdd:cd18798  160 E 160
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
157-265 1.24e-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: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 157 IQKHCIP-IIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQimskSSFCTPEVIIMTPTRELTIQIFEEAR-KFSRGT 234
Cdd:cd18023    5 IQSEVFPdLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNP----LPWGNRKVVYIAPIKALCSEKYDDWKeKFGPLG 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 242012580 235 FLKVALTygGTAVFHQVEKIKNgCNILVATP 265
Cdd:cd18023   81 LSCAELT--GDTEMDDTFEIQD-ADIILTTP 108
ResIII pfam04851
Type III restriction enzyme, res subunit;
177-327 2.13e-04

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 41.89  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580  177 TGSGKT--AAFLIpiinKLLEKNQIMSKssfctpeVIIMTPTRELTIQIFEEARKFSRGTFLKVALTYGGTAVFhqvekI 254
Cdd:pfam04851  32 TGSGKTltAAKLI----ARLFKKGPIKK-------VLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDE-----S 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242012580  255 KNGCNILVATPGRLLDFVQRGIIDFSMTEF--LILDEADRMLDMGFiSEIKKMINHPTMksssqrqtLMFSATFP 327
Cdd:pfam04851  96 VDDNKIVVTTIQSLYKALELASLELLPDFFdvIIIDEAHRSGASSY-RNILEYFKPAFL--------LGLTATPE 161
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
168-289 5.60e-04

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


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 40.64  E-value: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 168 GRDLMGCAQTGSGKTAAFLIPIINKLLEKNQimskSSFctpEVIIMTPTRELTIQIFEEARKFSRGTFL--KVALTYGGT 245
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPE----KGV---QVLYISPLKALINDQERRLEEPLDEIDLeiPVAVRHGDT 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 242012580 246 AvfhQVEK---IKNGCNILVATPGRL-LDFVQRGII-DFSMTEFLILDE 289
Cdd:cd17922   74 S---QSEKakqLKNPPGILITTPESLeLLLVNKKLReLFAGLRYVVVDE 119
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
411-440 7.59e-04

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 42.34  E-value: 7.59e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 242012580 411 IHGDRDQREREEALRDFKTGKMDILVATSV 440
Cdd:COG1200  509 LHGRMKPAEKDAVMAAFKAGEIDVLVATTV 538
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
175-292 1.25e-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: 40.19  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 175 AQTGSGKTAAFLIPIINKLLEKNQimskssfctpEVIIMTPTRELTIQIFEEARKFSRGTFLKVALTygGTAVFHQVEKI 254
Cdd:cd18035   23 LPTGLGKTIIAILVAADRLTKKGG----------KVLILAPSRPLVEQHAENLKRVLNIPDKITSLT--GEVKPEERAER 90
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 242012580 255 KNGCNILVATPGRLLDFVQRGIIDFSMTEFLILDEADR 292
Cdd:cd18035   91 WDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
153-289 1.49e-03

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 40.15  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580 153 KPTPIQKHCIPIIMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQIMSKSsfctpEVIIMTPTRELTIQIFEEARKFSR 232
Cdd:cd18036    2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKG-----RVVVLVNKVPLVEQQLEKFFKYFR 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242012580 233 GTFlKVALTYGGTAVFHQVEKIKNGCNILVATPGRLLDFVQRGII-------DFSMtefLILDE 289
Cdd:cd18036   77 KGY-KVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREeervylsDFSL---LIFDE 136
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
411-440 1.56e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 41.29  E-value: 1.56e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 242012580 411 IHGDRDQREREEALRDFKTGKMDILVATSV 440
Cdd:PRK10917 511 LHGRMKPAEKDAVMAAFKAGEIDILVATTV 540
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
406-487 1.80e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.45  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242012580  406 FPATSIHGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTG-RVGnrGLATSF 484
Cdd:PRK09751  302 FIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGL 379

                  ...
gi 242012580  485 YDP 487
Cdd:PRK09751  380 FFP 382
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
412-485 4.41e-03

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 39.88  E-value: 4.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242012580  412 HGDRDQREREEALRDFKTGKMDILVATSVAARGLDIKNVAHVVNFDLPKTIDEYVHRIGRTGRVGNRGLATSFY 485
Cdd:PLN03137  711 HGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYY 784
PRK05580 PRK05580
primosome assembly protein PriA; Validated
414-458 6.41e-03

primosome assembly protein PriA; Validated


Pssm-ID: 235514 [Multi-domain]  Cd Length: 679  Bit Score: 39.37  E-value: 6.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 242012580 414 DRD----QREREEALRDFKTGKMDILVATSVAARGLDIKNV--AHVVNFDL 458
Cdd:PRK05580 459 DRDttrrKGALEQLLAQFARGEADILIGTQMLAKGHDFPNVtlVGVLDADL 509
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
165-243 9.16e-03

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 37.31  E-value: 9.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242012580 165 IMSGRDLMGCAQTGSGKTAAFLIPIINKLLEKNQimskssfctpeVIIMTPTRELTIQIFEEARKFSRgTFLKVALTYG 243
Cdd:cd18028   14 LLKGENLLISIPTASGKTLIAEMAMVNTLLEGGK-----------ALYLVPLRALASEKYEEFKKLEE-IGLKVGISTG 80
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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