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Conserved domains on  [gi|2624742258|emb|CUM57699|]
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unnamed protein product [Debaryomyces tyrocola]

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

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
121-490 9.88e-151

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 437.66  E-value: 9.88e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 121 FDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKGLKVLCISPTREL 198
Cdd:COG0513     4 FADLGLSPPLLKALAElgYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILAPTREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 199 ALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFE 277
Cdd:COG0513    84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRgVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 278 QDIKSVMQQTNhANRQTLMFTATWPKEVRELASTFMNSPVKVSIGDRNelSANKRITQIVEVIEPYDKEKKLLSLLRkyq 357
Cdd:COG0513   164 EDIERILKLLP-KERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPEN--ATAETIEQRYYLVDKRDKLELLRRLLR--- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 358 sgSNKDDKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVIN 437
Cdd:COG0513   238 --DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVIN 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2624742258 438 LTFPLTVEDYVHRIGRTGRAGQTGIAHTLFTEHEKHLsgaLMNVLRGANQPVP 490
Cdd:COG0513   316 YDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRL---LRAIEKLIGQKIE 365
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
121-490 9.88e-151

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 437.66  E-value: 9.88e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 121 FDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKGLKVLCISPTREL 198
Cdd:COG0513     4 FADLGLSPPLLKALAElgYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILAPTREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 199 ALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFE 277
Cdd:COG0513    84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRgVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 278 QDIKSVMQQTNhANRQTLMFTATWPKEVRELASTFMNSPVKVSIGDRNelSANKRITQIVEVIEPYDKEKKLLSLLRkyq 357
Cdd:COG0513   164 EDIERILKLLP-KERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPEN--ATAETIEQRYYLVDKRDKLELLRRLLR--- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 358 sgSNKDDKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVIN 437
Cdd:COG0513   238 --DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVIN 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2624742258 438 LTFPLTVEDYVHRIGRTGRAGQTGIAHTLFTEHEKHLsgaLMNVLRGANQPVP 490
Cdd:COG0513   316 YDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRL---LRAIEKLIGQKIE 365
PTZ00110 PTZ00110
helicase; Provisional
82-511 1.63e-121

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 367.56  E-value: 1.63e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  82 YSQSPALTKLPQSEIDSFLQENEVTVEDPHNLGlRPLLGFDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIG 159
Cdd:PTZ00110   94 YKEHPEVSALSSKEVDEIRKEKEITIIAGENVP-KPVVSFEYTSFPDYILKSLKNagFTEPTPIQVQGWPIALSGRDMIG 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 160 VAETGSGKTFAFGVPAINNILTHNK----KGLKVLCISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSLRD 235
Cdd:PTZ00110  173 IAETGSGKTLAFLLPAIVHINAQPLlrygDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRR 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 236 -ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTnHANRQTLMFTATWPKEVRELASTFMN 314
Cdd:PTZ00110  253 gVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQI-RPDRQTLMWSATWPKEVQSLARDLCK 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 315 S-PVKVSIGDRnELSANKRITQIVEVIEPYDKEKKLLSLLRKYQsgsNKDDKILIFALYKKEATRIENLLVRNSFKVSAV 393
Cdd:PTZ00110  332 EePVHVNVGSL-DLTACHNIKQEVFVVEEHEKRGKLKMLLQRIM---RDGDKILIFVETKKGADFLTKELRLDGWPALCI 407
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 394 HGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRAGQTGIAHTLFTEHEKH 473
Cdd:PTZ00110  408 HGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYR 487
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2624742258 474 LSGALMNVLRGANQPVPDELLKFG-GHTKKKAHSAYGAF 511
Cdd:PTZ00110  488 LARDLVKVLREAKQPVPPELEKLSnERSNGTERRRWGGY 526
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
137-320 4.25e-89

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: 271.62  E-value: 4.25e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 137 FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNK---KGLKVLCISPTRELALQIYDNLVDLTANT 213
Cdd:cd00268    10 FEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKkkgRGPQALVLAPTRELAMQIAEVARKLGKGT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 214 PLKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNhANR 292
Cdd:cd00268    90 GLKVAAIYGGAPIKKQIEALKKgPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKILSALP-KDR 168
                         170       180
                  ....*....|....*....|....*...
gi 2624742258 293 QTLMFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd00268   169 QTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
141-308 3.10e-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: 3.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 141 TPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNIlTHNKKGLKVLCISPTRELALQIYDNLVDLTANTPLKCVAV 220
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL-DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 221 YGGVSKHEQVSSLRDASVVVATPGRLIDLLNDgALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNhANRQTLMFTAT 300
Cdd:pfam00270  80 LGGDSRKEQLEKLKGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLP-KKRQILLLSAT 157

                  ....*...
gi 2624742258 301 WPKEVREL 308
Cdd:pfam00270 158 LPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
135-336 1.14e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 177.30  E-value: 1.14e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  135 SKFPTPTPIQSVSWPYLLSG-KDVIGVAETGSGKTFAFGVPAINNILTHNKKglKVLCISPTRELALQIYDNLVDLTANT 213
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG--RVLVLVPTRELAEQWAEELKKLGPSL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  214 PLKCVAVYGGVSKHEQVSSLR--DASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHaN 291
Cdd:smart00487  82 GLKVVGLYGGDSKREQLRKLEsgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK-N 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2624742258  292 RQTLMFTATWPKEVRELASTFMNSPVKVSIGDRnelsANKRITQI 336
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNDPVFIDVGFT----PLEPIEQF 201
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
121-490 9.88e-151

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 437.66  E-value: 9.88e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 121 FDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKGLKVLCISPTREL 198
Cdd:COG0513     4 FADLGLSPPLLKALAElgYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILAPTREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 199 ALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFE 277
Cdd:COG0513    84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRgVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 278 QDIKSVMQQTNhANRQTLMFTATWPKEVRELASTFMNSPVKVSIGDRNelSANKRITQIVEVIEPYDKEKKLLSLLRkyq 357
Cdd:COG0513   164 EDIERILKLLP-KERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPEN--ATAETIEQRYYLVDKRDKLELLRRLLR--- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 358 sgSNKDDKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVIN 437
Cdd:COG0513   238 --DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVIN 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2624742258 438 LTFPLTVEDYVHRIGRTGRAGQTGIAHTLFTEHEKHLsgaLMNVLRGANQPVP 490
Cdd:COG0513   316 YDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRL---LRAIEKLIGQKIE 365
PTZ00110 PTZ00110
helicase; Provisional
82-511 1.63e-121

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 367.56  E-value: 1.63e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  82 YSQSPALTKLPQSEIDSFLQENEVTVEDPHNLGlRPLLGFDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIG 159
Cdd:PTZ00110   94 YKEHPEVSALSSKEVDEIRKEKEITIIAGENVP-KPVVSFEYTSFPDYILKSLKNagFTEPTPIQVQGWPIALSGRDMIG 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 160 VAETGSGKTFAFGVPAINNILTHNK----KGLKVLCISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSLRD 235
Cdd:PTZ00110  173 IAETGSGKTLAFLLPAIVHINAQPLlrygDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRR 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 236 -ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTnHANRQTLMFTATWPKEVRELASTFMN 314
Cdd:PTZ00110  253 gVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQI-RPDRQTLMWSATWPKEVQSLARDLCK 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 315 S-PVKVSIGDRnELSANKRITQIVEVIEPYDKEKKLLSLLRKYQsgsNKDDKILIFALYKKEATRIENLLVRNSFKVSAV 393
Cdd:PTZ00110  332 EePVHVNVGSL-DLTACHNIKQEVFVVEEHEKRGKLKMLLQRIM---RDGDKILIFVETKKGADFLTKELRLDGWPALCI 407
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 394 HGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRAGQTGIAHTLFTEHEKH 473
Cdd:PTZ00110  408 HGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYR 487
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2624742258 474 LSGALMNVLRGANQPVPDELLKFG-GHTKKKAHSAYGAF 511
Cdd:PTZ00110  488 LARDLVKVLREAKQPVPPELEKLSnERSNGTERRRWGGY 526
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
141-478 8.09e-96

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 298.64  E-value: 8.09e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 141 TPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNIlthNKKGLK----VLCisPTRELALQIYDNLVDLTANTP-L 215
Cdd:PRK11776   28 TPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL---DVKRFRvqalVLC--PTRELADQVAKEIRRLARFIPnI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 216 KCVAVYGGVSKHEQVSSLR-DASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTnHANRQT 294
Cdd:PRK11776  103 KVLTLCGGVPMGPQIDSLEhGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQA-PARRQT 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 295 LMFTATWPKEVRELASTFMNSPVKVSIGDRNELSAnkrITQIVEVIEPYDKEKKLLSLLRKYQSGSnkddkILIFALYKK 374
Cdd:PRK11776  182 LLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA---IEQRFYEVSPDERLPALQRLLLHHQPES-----CVVFCNTKK 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 375 EATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRT 454
Cdd:PRK11776  254 ECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRT 333
                         330       340
                  ....*....|....*....|....
gi 2624742258 455 GRAGQTGIAHTLFTEHEKHLSGAL 478
Cdd:PRK11776  334 GRAGSKGLALSLVAPEEMQRANAI 357
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
137-320 4.25e-89

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: 271.62  E-value: 4.25e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 137 FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNK---KGLKVLCISPTRELALQIYDNLVDLTANT 213
Cdd:cd00268    10 FEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKkkgRGPQALVLAPTRELAMQIAEVARKLGKGT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 214 PLKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNhANR 292
Cdd:cd00268    90 GLKVAAIYGGAPIKKQIEALKKgPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKILSALP-KDR 168
                         170       180
                  ....*....|....*....|....*...
gi 2624742258 293 QTLMFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd00268   169 QTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
119-466 1.28e-85

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 272.07  E-value: 1.28e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 119 LGFDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHN-----KKGLKVLC 191
Cdd:PRK10590    1 MSFDSLGLSPDILRAVAEqgYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphakgRRPVRALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 192 ISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSLRDA-SVVVATPGRLIDLLNDGALSLDSIEYLVLDEADR 270
Cdd:PRK10590   81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGvDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 271 MLEKGFEQDIKSVMQQTNhANRQTLMFTATWPKEVRELASTFMNSPVKVSIGDRNelSANKRITQIVEVIepyDKEKK-- 348
Cdd:PRK10590  161 MLDMGFIHDIRRVLAKLP-AKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN--TASEQVTQHVHFV---DKKRKre 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 349 LLSLLrkyqSGSNKDDKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLD 428
Cdd:PRK10590  235 LLSQM----IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD 310
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2624742258 429 IPNVKVVINLTFPLTVEDYVHRIGRTGRAGQTGIAHTL 466
Cdd:PRK10590  311 IEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSL 348
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
120-495 8.56e-82

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 262.54  E-value: 8.56e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 120 GFDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKG------LKVLC 191
Cdd:PRK01297   88 RFHDFNLAPELMHAIHDlgFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKerymgePRALI 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 192 ISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSL--RDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEAD 269
Cdd:PRK01297  168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 270 RMLEKGFEQDIKSVMQQTNH-ANRQTLMFTATWPKEVRELASTFMNSPVKVSIGDRNElsANKRITQIVEVIEPYDKEKK 348
Cdd:PRK01297  248 RMLDMGFIPQVRQIIRQTPRkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENV--ASDTVEQHVYAVAGSDKYKL 325
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 349 LLSLLRKyqsgsNKDDKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLD 428
Cdd:PRK01297  326 LYNLVTQ-----NPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIH 400
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2624742258 429 IPNVKVVINLTFPLTVEDYVHRIGRTGRAGQTGIAHTLFTEHEKHLSGALMNVL--RGANQPVPDELLK 495
Cdd:PRK01297  401 IDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLgrKISCEMPPAELLK 469
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
140-517 4.72e-78

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 257.08  E-value: 4.72e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 140 PTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNIlTHNKKGLKVLCISPTRELALQIYDNLVDLTANTP-LKCV 218
Cdd:PRK11634   29 PSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL-DPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRgVNVV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 219 AVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNhANRQTLMF 297
Cdd:PRK11634  108 ALYGGQRYDVQLRALRQgPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIP-EGHQTALF 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 298 TATWPKEVRELASTFMNSPVKVSIgdRNELSANKRITQIVEVIEPYDKEKKLLSLLRkyqsgSNKDDKILIFALYKKEAT 377
Cdd:PRK11634  187 SATMPEAIRRITRRFMKEPQEVRI--QSSVTTRPDISQSYWTVWGMRKNEALVRFLE-----AEDFDAAIIFVRTKNATL 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 378 RIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRA 457
Cdd:PRK11634  260 EVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRA 339
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2624742258 458 GQTGIAhTLFTEH-EKHLsgaLMNVLRGANQPVPD------ELL------KFGGHTKKKAHSAygaffkDVDM 517
Cdd:PRK11634  340 GRAGRA-LLFVENrERRL---LRNIERTMKLTIPEvelpnaELLgkrrleKFAAKVQQQLESS------DLDQ 402
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
121-525 1.66e-77

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 250.24  E-value: 1.66e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 121 FDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKGL---KVLCISPT 195
Cdd:PRK11192    3 FSELELDESLLEALQDkgYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSgppRILILTPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 196 RELALQIYDNLVDLTANTPLKCVAVYGGVS--KHEQVSSlRDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLE 273
Cdd:PRK11192   83 RELAMQVADQARELAKHTHLDIATITGGVAymNHAEVFS-ENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 274 KGFEQDIKSVMQQTNHaNRQTLMFTATWPKE-VRELASTFMNSPVKVSI-GDRNElsaNKRITQIVEVIEPYDKEKKLL- 350
Cdd:PRK11192  162 MGFAQDIETIAAETRW-RKQTLLFSATLEGDaVQDFAERLLNDPVEVEAePSRRE---RKKIHQWYYRADDLEHKTALLc 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 351 SLLRKYQSGsnkddKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIP 430
Cdd:PRK11192  238 HLLKQPEVT-----RSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDID 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 431 NVKVVINLTFPLTVEDYVHRIGRTGRAGQTGIAHTLFTEHEKHLSGalmNVLRGANQP----VPDEL---LKFGGHTKKK 503
Cdd:PRK11192  313 DVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLG---KIERYIEEPlkarVIDELrpkTKAPSEKKTG 389
                         410       420
                  ....*....|....*....|..
gi 2624742258 504 AHSAYGAFFKDVDMTKTAKKIK 525
Cdd:PRK11192  390 KPSKKVLAKRAEKKEKEKEKPK 411
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
141-463 6.01e-76

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 245.65  E-value: 6.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 141 TPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKGLK------VLCISPTRELALQIYDNLVDLTANTP 214
Cdd:PRK04837   32 TPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRkvnqprALIMAPTRELAVQIHADAEPLAQATG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 215 LKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHAN-R 292
Cdd:PRK04837  112 LKLGLAYGGDGYDKQLKVLESgVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRWLFRRMPPANqR 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 293 QTLMFTATWPKEVRELASTFMNSPVKVSIgdRNELSANKRITQivEVIEPYDKEKK--LLSLLRKyqsgsNKDDKILIFA 370
Cdd:PRK04837  192 LNMLFSATLSYRVRELAFEHMNNPEYVEV--EPEQKTGHRIKE--ELFYPSNEEKMrlLQTLIEE-----EWPDRAIIFA 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 371 LYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHR 450
Cdd:PRK04837  263 NTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHR 342
                         330
                  ....*....|...
gi 2624742258 451 IGRTGRAGQTGIA 463
Cdd:PRK04837  343 IGRTGRAGASGHS 355
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
116-463 2.49e-74

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 246.02  E-value: 2.49e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 116 RPL--LGFDQIDLD-SRIAGVISK-FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTH------NKK 185
Cdd:PRK04537    4 KPLtdLTFSSFDLHpALLAGLESAgFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRpaladrKPE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 186 GLKVLCISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLND-GALSLDSIEYL 263
Cdd:PRK04537   84 DPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQgVDVIIATPGRLIDYVKQhKVVSLHACEIC 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 264 VLDEADRMLEKGFEQDIKSVMQQT-NHANRQTLMFTATWPKEVRELASTFMNSPVKVSIgdRNELSANKRITQivEVIEP 342
Cdd:PRK04537  164 VLDEADRMFDLGFIKDIRFLLRRMpERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVV--ETETITAARVRQ--RIYFP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 343 YDKEKK--LLSLLRKYQSGsnkddKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLAT 420
Cdd:PRK04537  240 ADEEKQtlLLGLLSRSEGA-----RTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVAT 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2624742258 421 DVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRAGQTGIA 463
Cdd:PRK04537  315 DVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDA 357
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
136-320 9.12e-73

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: 229.56  E-value: 9.12e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 136 KFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNI----LTHNKKGLKVLCISPTRELALQIYDNLVDLTA 211
Cdd:cd17966     9 GFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHInaqpPLERGDGPIVLVLAPTRELAQQIQQEANKFGG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 212 NTPLKCVAVYGGVSKHEQVSSL-RDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNhA 290
Cdd:cd17966    89 SSRLRNTCVYGGAPKGPQIRDLrRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQIR-P 167
                         170       180       190
                  ....*....|....*....|....*....|
gi 2624742258 291 NRQTLMFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd17966   168 DRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
121-322 6.29e-71

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: 225.83  E-value: 6.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 121 FDQIDLDSRIAGVI--SKFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHN---------KKGLKV 189
Cdd:cd17967     2 FEEAGLRELLLENIkrAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGppsvgrgrrKAYPSA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 190 LCISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSL-RDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEA 268
Cdd:cd17967    82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLlRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2624742258 269 DRMLEKGFEQDIKSVMQQTN---HANRQTLMFTATWPKEVRELASTFMNSPVKVSIG 322
Cdd:cd17967   162 DRMLDMGFEPQIRKIVEHPDmppKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
104-315 5.14e-62

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: 204.05  E-value: 5.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 104 EVTVEDPHnlglRPLLGFDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILT 181
Cdd:cd18052    32 EVTGRNPP----PAILTFEEANLCETLLKNIRKagYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 182 HNKKGLK--------VLCISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSL-RDASVVVATPGRLIDLLND 252
Cdd:cd18052   108 EGLTASSfsevqepqALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIeKGCHILVATPGRLLDFIGR 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2624742258 253 GALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTN---HANRQTLMFTATWPKEVRELASTFMNS 315
Cdd:cd18052   188 GKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGmpsKEDRQTLMFSATFPEEIQRLAAEFLKE 253
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
71-494 1.59e-61

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 210.41  E-value: 1.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  71 PTKINASDSTGYSQSPALT-KLPQSEIDSFLQENEVTVEDphNLGLRPLLGFDQIDLDSRIAGVISK--FPTPTPIQSVS 147
Cdd:PLN00206   74 PKRLPATDECFYVRDPGSTsGLSSSQAELLRRKLEIHVKG--EAVPPPILSFSSCGLPPKLLLNLETagYEFPTPIQMQA 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 148 WPYLLSGKDVIGVAETGSGKTFAFGVPAINNI-------LTHNKKGLKVLcISPTRELALQIYDNLVDLTANTPLKCVAV 220
Cdd:PLN00206  152 IPAALSGRSLLVSADTGSGKTASFLVPIISRCctirsghPSEQRNPLAMV-LTPTRELCVQVEDQAKVLGKGLPFKTALV 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 221 YGGVSKHEQVSSLRDA-SVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTnhANRQTLMFTA 299
Cdd:PLN00206  231 VGGDAMPQQLYRIQQGvELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQAL--SQPQVLLFSA 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 300 TWPKEVRELASTFMNSPVKVSIGDRNElsANKRITQIVEVIEPYDKEKKLLSLLrkyQSGSNKDDKILIFALYKKEATRI 379
Cdd:PLN00206  309 TVSPEVEKFASSLAKDIILISIGNPNR--PNKAVKQLAIWVETKQKKQKLFDIL---KSKQHFKPPAVVFVSSRLGADLL 383
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 380 ENLL-VRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRAG 458
Cdd:PLN00206  384 ANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMG 463
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2624742258 459 QTGIAHTLFTEHEKHLSGALMNVLRGANQPVPDELL 494
Cdd:PLN00206  464 EKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELA 499
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
141-308 3.10e-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: 3.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 141 TPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNIlTHNKKGLKVLCISPTRELALQIYDNLVDLTANTPLKCVAV 220
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL-DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 221 YGGVSKHEQVSSLRDASVVVATPGRLIDLLNDgALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNhANRQTLMFTAT 300
Cdd:pfam00270  80 LGGDSRKEQLEKLKGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLP-KKRQILLLSAT 157

                  ....*...
gi 2624742258 301 WPKEVREL 308
Cdd:pfam00270 158 LPRNLEDL 165
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
135-320 4.07e-60

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: 196.87  E-value: 4.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 135 SKFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTH----NKKGLKVLCISPTRELALQIYDNLVDLT 210
Cdd:cd17952     8 QEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQreleKGEGPIAVIVAPTRELAQQIYLEAKKFG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 211 ANTPLKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTnH 289
Cdd:cd17952    88 KAYNLRVVAVYGGGSKWEQAKALQEgAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVGHV-R 166
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2624742258 290 ANRQTLMFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd17952   167 PDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
PTZ00424 PTZ00424
helicase 45; Provisional
121-463 5.87e-59

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 200.44  E-value: 5.87e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 121 FDQIDLDSRI-AGVIS-KFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNIlTHNKKGLKVLCISPTREL 198
Cdd:PTZ00424   30 FDALKLNEDLlRGIYSyGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI-DYDLNACQALILAPTREL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 199 ALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSLRDA-SVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFE 277
Cdd:PTZ00424  109 AQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGvHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 278 QDIKSVMQQTNhANRQTLMFTATWPKEVRELASTFMNSPVKVSIgDRNELSAnKRITQIVEVIEpyDKEKKLLSLLRKYQ 357
Cdd:PTZ00424  189 GQIYDVFKKLP-PDVQVALFSATMPNEILELTTKFMRDPKRILV-KKDELTL-EGIRQFYVAVE--KEEWKFDTLCDLYE 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 358 SGSNKddKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVIN 437
Cdd:PTZ00424  264 TLTIT--QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVIN 341
                         330       340
                  ....*....|....*....|....*.
gi 2624742258 438 LTFPLTVEDYVHRIGRTGRAGQTGIA 463
Cdd:PTZ00424  342 YDLPASPENYIHRIGRSGRFGRKGVA 367
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
135-322 7.34e-59

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


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 193.57  E-value: 7.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 135 SKFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNK-KGLKVLCISPTRELALQIYDNLVDLTANT 213
Cdd:cd17957     8 SGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKkKGLRALILAPTRELASQIYRELLKLSKGT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 214 PLKCVAVYGG--VSKHEQVSSLRDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHAN 291
Cdd:cd17957    88 GLRIVLLSKSleAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEILAACTNPN 167
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2624742258 292 RQTLMFTATWPKEVRELASTFMNSPVKVSIG 322
Cdd:cd17957   168 LQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
116-319 1.18e-58

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: 193.75  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 116 RPLLGFDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNK----KGLKV 189
Cdd:cd17953     9 KPIQKWSQCGLSEKVLDLIKKlgYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPvkpgEGPIG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 190 LCISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSL-RDASVVVATPGRLIDLL--NDGAL-SLDSIEYLVL 265
Cdd:cd17953    89 LIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELkRGAEIVVCTPGRMIDILtaNNGRVtNLRRVTYVVL 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2624742258 266 DEADRMLEKGFEQDIKSVMQQTnHANRQTLMFTATWPKEVRELASTFMNSPVKV 319
Cdd:cd17953   169 DEADRMFDMGFEPQIMKIVNNI-RPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
95-322 1.88e-58

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


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 194.07  E-value: 1.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  95 EIDSFLQENEVTVEDpHNlGLRPLLGFDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFG 172
Cdd:cd18049     2 EVEQYRRSKEITVRG-HN-CPKPVLNFYEANFPANVMDVIARqnFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 173 VPAINNI----LTHNKKGLKVLCISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSL-RDASVVVATPGRLI 247
Cdd:cd18049    80 LPAIVHInhqpFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLeRGVEICIATPGRLI 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2624742258 248 DLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTnHANRQTLMFTATWPKEVRELASTFMNSPVKVSIG 322
Cdd:cd18049   160 DFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI-RPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
137-320 9.77e-58

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


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 191.38  E-value: 9.77e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 137 FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNI-----LTHNKK--GLKVLCISPTRELALQIYDNLVDL 209
Cdd:cd17945    10 YKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsrlppLDEETKddGPYALILAPTRELAQQIEEETQKF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 210 TANTPLKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVM---- 284
Cdd:cd17945    90 AKPLGIRVVSIVGGHSIEEQAFSLRNgCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKILdamp 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2624742258 285 ---------------QQTNHANRQTLMFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd17945   170 vsnkkpdteeaeklaASGKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
82-322 2.01e-57

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: 192.53  E-value: 2.01e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  82 YSQSPALTKLPQSEIDSFLQENEVTVEDphNLGLRPLLGFDQIDLDSRIAGVI--SKFPTPTPIQSVSWPYLLSGKDVIG 159
Cdd:cd18050    27 YVEHPEVARMTQYDVEELRRKKEITIRG--VGCPKPVFAFHQANFPQYVMDVLldQNFKEPTPIQCQGFPLALSGRDMVG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 160 VAETGSGKTFAFGVPAINNIlTHN---KKGLKVLCI--SPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSL- 233
Cdd:cd18050   105 IAQTGSGKTLAYLLPAIVHI-NHQpylERGDGPICLvlAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLe 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 234 RDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTnHANRQTLMFTATWPKEVRELASTFM 313
Cdd:cd18050   184 RGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI-RPDRQTLMWSATWPKEVRQLAEDFL 262

                  ....*....
gi 2624742258 314 NSPVKVSIG 322
Cdd:cd18050   263 RDYVQINIG 271
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
137-320 4.16e-56

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: 186.31  E-value: 4.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 137 FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKK--GLKVLCISPTRELALQIYDNLVDLTANTP 214
Cdd:cd17947    10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKkaATRVLVLVPTRELAMQCFSVLQQLAQFTD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 215 LKCVAVYGGVSKHEQVSSLRDA-SVVVATPGRLID-LLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTnHANR 292
Cdd:cd17947    90 ITFALAVGGLSLKAQEAALRARpDIVIATPGRLIDhLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEILRLC-PRTR 168
                         170       180
                  ....*....|....*....|....*...
gi 2624742258 293 QTLMFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd17947   169 QTMLFSATMTDEVKDLAKLSLNKPVRVF 196
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
130-319 7.95e-56

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: 185.75  E-value: 7.95e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 130 IAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTH-----NKKGLKVLCISPTRELALQI 202
Cdd:cd17958     1 IMKEIKKqgFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQpipreQRNGPGVLVLTPTRELALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 203 YDNLVDLTANTpLKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIK 281
Cdd:cd17958    81 EAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKgVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2624742258 282 SVMQQTnHANRQTLMFTATWPKEVRELASTFMNSPVKV 319
Cdd:cd17958   160 KILLDI-RPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
333-467 3.96e-55

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: 181.17  E-value: 3.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 333 ITQIVEVIEPYDKEKKLLSLLRKyqsgSNKDDKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAG 412
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLE----KLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSG 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2624742258 413 KTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRAGQTGIAHTLF 467
Cdd:cd18787    77 KVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
120-319 5.29e-54

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: 180.96  E-value: 5.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 120 GFDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKK-GLKVLCISPTR 196
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKkgYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTvGARALILSPTR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 197 ELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSL-RDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKG 275
Cdd:cd17959    82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALaSNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2624742258 276 FEQDIKSVMQQTNhANRQTLMFTATWPKEVRELASTFMNSPVKV 319
Cdd:cd17959   162 FAEQLHEILSRLP-ENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEXDc smart00487
DEAD-like helicases superfamily;
135-336 1.14e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 177.30  E-value: 1.14e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  135 SKFPTPTPIQSVSWPYLLSG-KDVIGVAETGSGKTFAFGVPAINNILTHNKKglKVLCISPTRELALQIYDNLVDLTANT 213
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG--RVLVLVPTRELAEQWAEELKKLGPSL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  214 PLKCVAVYGGVSKHEQVSSLR--DASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHaN 291
Cdd:smart00487  82 GLKVVGLYGGDSKREQLRKLEsgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK-N 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2624742258  292 RQTLMFTATWPKEVRELASTFMNSPVKVSIGDRnelsANKRITQI 336
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNDPVFIDVGFT----PLEPIEQF 201
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
136-318 2.50e-52

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: 177.00  E-value: 2.50e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 136 KFPTPTPIQSVSWPYLLS-GKDVIGVAETGSGKTFAFGVPAINNILT----HNKKGLKVLCISPTRELALQIYDNLVDLT 210
Cdd:cd17964    13 GFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNtkpaGRRSGVSALIISPTRELALQIAAEAKKLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 211 AN-TPLKCVAVYGGVSKHEQVSSLR--DASVVVATPGRLIDLLND--GALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQ 285
Cdd:cd17964    93 QGlRKLRVQSAVGGTSRRAELNRLRrgRPDILVATPGRLIDHLENpgVAKAFTDLDYLVLDEADRLLDMGFRPDLEQILR 172
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2624742258 286 QTNHAN---RQTLMFTATWPKEVRELASTFMNSPVK 318
Cdd:cd17964   173 HLPEKNadpRQTLLFSATVPDEVQQIARLTLKKDYK 208
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
136-300 2.89e-51

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: 174.73  E-value: 2.89e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 136 KFPTPTPIQSVSWPY-LLSGKDVIGVAETGSGKTFAFGVPAINNILTHNK--------KGLKVLCISPTRELALQIYDNL 206
Cdd:cd17946     9 GFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSsngvggkqKPLRALILTPTRELAVQVKDHL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 207 VDLTANTPLKCVAVYGGVS--KHEQVSSlRDASVVVATPGRLIDLL---NDGALSLDSIEYLVLDEADRMLEKG----FE 277
Cdd:cd17946    89 KAIAKYTNIKIASIVGGLAvqKQERLLK-KRPEIVVATPGRLWELIqegNEHLANLKSLRFLVLDEADRMLEKGhfaeLE 167
                         170       180
                  ....*....|....*....|....*
gi 2624742258 278 QDIK--SVMQQTNHANRQTLMFTAT 300
Cdd:cd17946   168 KILEllNKDRAGKKRKRQTFVFSAT 192
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
121-322 9.87e-51

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: 174.07  E-value: 9.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 121 FDQIDLDSRIAGVI--SKFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILT---------------HN 183
Cdd:cd18051    23 FSDLDLGEIIRNNIelARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEqgpgeslpsesgyygRR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 184 KKGLKVLCISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSL-RDASVVVATPGRLIDLLNDGALSLDSIEY 262
Cdd:cd18051   103 KQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLeRGCHLLVATPGRLVDMLERGKIGLDYCKY 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2624742258 263 LVLDEADRMLEKGFEQDIKSVMQQTN---HANRQTLMFTATWPKEVRELASTFMNSPVKVSIG 322
Cdd:cd18051   183 LVLDEADRMLDMGFEPQIRRIVEQDTmppTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
140-320 2.58e-50

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


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 171.25  E-value: 2.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 140 PTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPaINNILTHNKKGLKVLCISPTRELALQIYDNLVDLTANTPLKCVA 219
Cdd:cd17955    22 PTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP-ILQRLSEDPYGIFALVLTPTRELAYQIAEQFRALGAPLGLRCCV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 220 VYGGVSKHEQVSSL-RDASVVVATPGRLIDLL---NDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNhANRQTL 295
Cdd:cd17955   101 IVGGMDMVKQALELsKRPHIVVATPGRLADHLrssDDTTKVLSRVKFLVLDEADRLLTGSFEDDLATILSALP-PKRQTL 179
                         170       180
                  ....*....|....*....|....*
gi 2624742258 296 MFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd17955   180 LFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
137-320 2.69e-50

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


Pssm-ID: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 171.35  E-value: 2.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 137 FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILtHNKKGLKVLCISPTRELALQIYDNLVDLTANTPLK 216
Cdd:cd17954    20 WKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALL-ENPQRFFALVLAPTRELAQQISEQFEALGSSIGLK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 217 CVAVYGGVSKHEQVSSL-RDASVVVATPGRLID-LLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHaNRQT 294
Cdd:cd17954    99 SAVLVGGMDMMAQAIALaKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRLLNMDFEPEIDKILKVIPR-ERTT 177
                         170       180
                  ....*....|....*....|....*.
gi 2624742258 295 LMFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd17954   178 YLFSATMTTKVAKLQRASLKNPVKIE 203
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
136-320 4.69e-48

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


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 165.06  E-value: 4.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 136 KFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNIL----THNKKGLKVLCISPTRELALQIYDNLVDLTA 211
Cdd:cd17960     9 GFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLkrkaNLKKGQVGALIISPTRELATQIYEVLQSFLE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 212 --NTPLKCVAVYGGVSKHEQVSSLRD--ASVVVATPGRLIDLLN--DGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQ 285
Cdd:cd17960    89 hhLPKLKCQLLIGGTNVEEDVKKFKRngPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLGFEADLNRILS 168
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2624742258 286 QTNHaNRQTLMFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd17960   169 KLPK-QRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
140-319 3.39e-46

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: 160.58  E-value: 3.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 140 PTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKK-------GLKVLCISPTRELALQIYDNLVDLTAN 212
Cdd:cd17951    13 PTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKlpfikgeGPYGLIVCPSRELARQTHEVIEYYCKA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 213 ------TPLKCVAVYGGVSKHEQVSSLRDA-SVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQ 285
Cdd:cd17951    93 lqeggyPQLRCLLCIGGMSVKEQLEVIRKGvHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEEDIRTIFS 172
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2624742258 286 QTNHaNRQTLMFTATWPKEVRELASTFMNSPVKV 319
Cdd:cd17951   173 YFKG-QRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
135-321 5.08e-45

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


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 157.07  E-value: 5.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 135 SKFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNiLTHNK----KGLKVLCISPTRELALQIYDNLVDLT 210
Cdd:cd17941     8 AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEK-LYRERwtpeDGLGALIISPTRELAMQIFEVLRKVG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 211 ANTPLKCVAVYGGVSKHEQVSSLRDASVVVATPGRLIDLLNDGA-LSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNh 289
Cdd:cd17941    87 KYHSFSAGLIIGGKDVKEEKERINRMNILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRILDMGFKETLDAIVENLP- 165
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2624742258 290 ANRQTLMFTATWPKEVRELASTFMNSPVKVSI 321
Cdd:cd17941   166 KSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
126-317 1.10e-43

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: 153.89  E-value: 1.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 126 LDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTH-----NKKGLKVLCISPTREL 198
Cdd:cd17961     1 LDPRLLKAIAKlgWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAkaesgEEQGTRALILVPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 199 ALQIYDNLVDLTA--NTPLKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSL-DSIEYLVLDEADRMLEK 274
Cdd:cd17961    81 AQQVSKVLEQLTAycRKDVRVVNLSASSSDSVQRALLAEkPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2624742258 275 GFEQDIKSVMQQTNhANRQTLMFTATWPKEVRELASTFMNSPV 317
Cdd:cd17961   161 GYEEDLKSLLSYLP-KNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
127-319 2.83e-43

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: 152.48  E-value: 2.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 127 DSRIAGVISK-FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNI-LTHNKkgLKVLCISPTRELALQIYD 204
Cdd:cd17939     6 EDLLRGIYAYgFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRE--TQALVLAPTRELAQQIQK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 205 NLVDLTANTPLKCVAVYGGVSKHEQVSSLR-DASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSV 283
Cdd:cd17939    84 VVKALGDYMGVKVHACIGGTSVREDRRKLQyGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDI 163
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2624742258 284 MQQTNhANRQTLMFTATWPKEVRELASTFMNSPVKV 319
Cdd:cd17939   164 FQFLP-PETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
136-320 1.13e-41

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: 148.28  E-value: 1.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 136 KFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILT---HNKKGLKVLCISPTRELALQIYDNLVDLTAN 212
Cdd:cd17942     9 GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKlkfKPRNGTGVIIISPTRELALQIYGVAKELLKY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 213 TPLKCVAVYGGVSKHEQVSSL-RDASVVVATPGRLID-LLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNhA 290
Cdd:cd17942    89 HSQTFGIVIGGANRKAEAEKLgKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIKLLP-K 167
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2624742258 291 NRQTLMFTATWPKEVRELAS-TFMNSPVKVS 320
Cdd:cd17942   168 RRQTMLFSATQTRKVEDLARiSLKKKPLYVG 198
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
136-320 2.98e-41

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: 147.35  E-value: 2.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 136 KFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKK-----GLKVLCISPTRELALQIYDNLVDLT 210
Cdd:cd17949    10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrsdGTLALVLVPTRELALQIYEVLEKLL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 211 ANTP-LKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLID-LLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQ-- 285
Cdd:cd17949    90 KPFHwIVPGYLIGGEKRKSEKARLRKgVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILEll 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2624742258 286 --QTNHAN--------RQTLMFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd17949   170 ddKRSKAGgekskpsrRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
135-320 6.17e-41

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: 145.87  E-value: 6.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 135 SKFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKgLKVLCISPTRELALQIYDNLVDLTANTP 214
Cdd:cd17943     8 AGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRH-PQVLILAPTREIAVQIHDVFKKIGKKLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 215 -LKCVAVYGGVSKHEQVSSLRDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIK---SVMQqtnhA 290
Cdd:cd17943    87 gLKCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNwifSSLP----K 162
                         170       180       190
                  ....*....|....*....|....*....|
gi 2624742258 291 NRQTLMFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd17943   163 NKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
137-319 8.02e-40

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: 143.21  E-value: 8.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 137 FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILThNKKGLKVLCISPTRELALQIYDNLVDLTANTPLK 216
Cdd:cd17940    19 FEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDP-KKDVIQALILVPTRELALQTSQVCKELGKHMGVK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 217 CVAVYGGVSKHEQVSSLRDA-SVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNhANRQTL 295
Cdd:cd17940    98 VMVTTGGTSLRDDIMRLYQTvHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNFLP-KERQIL 176
                         170       180
                  ....*....|....*....|....
gi 2624742258 296 MFTATWPKEVRELASTFMNSPVKV 319
Cdd:cd17940   177 LFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
135-320 1.87e-37

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: 136.52  E-value: 1.87e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 135 SKFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKGLkVLCISPTRELALQIYDNLVDLTANTP 214
Cdd:cd17962     8 AGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPS-ALILTPTRELAVQIEDQAKELMKGLP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 215 -LKCVAVYGGVSKHEQVSSLRD-ASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHaNR 292
Cdd:cd17962    87 pMKTALLVGGLPLPPQLYRLQQgVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISH-DH 165
                         170       180
                  ....*....|....*....|....*...
gi 2624742258 293 QTLMFTATWPKEVRELASTFMNSPVKVS 320
Cdd:cd17962   166 QTILVSATIPRGIEQLAGQLLQNPVRIT 193
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
140-319 3.93e-37

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: 135.91  E-value: 3.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 140 PTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNIlthnkkglKVLCISPTRELALQIYDNLVDLTA---NTPLK 216
Cdd:cd17938    22 PTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV--------VALILEPSRELAEQTYNCIENFKKyldNPKLR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 217 CVAVYGGVSKHEQVSSLRDAS-VVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDI----KSVMQQTNHAN 291
Cdd:cd17938    94 VALLIGGVKAREQLKRLESGVdIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETInriyNRIPKITSDGK 173
                         170       180       190
                  ....*....|....*....|....*....|
gi 2624742258 292 R-QTLMFTATWPK-EVRELASTFMNSPVKV 319
Cdd:cd17938   174 RlQVIVCSATLHSfEVKKLADKIMHFPTWV 203
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
121-319 6.31e-37

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: 135.27  E-value: 6.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 121 FDQIDLD-SRIAGVIS-KFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNIlTHNKKGLKVLCISPTREL 198
Cdd:cd18046     1 FDDMNLKeSLLRGIYAyGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI-DTSLKATQALVLAPTREL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 199 ALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSLRDA-SVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFE 277
Cdd:cd18046    80 AQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGpHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2624742258 278 QDIKSVMQQTNhANRQTLMFTATWPKEVRELASTFMNSPVKV 319
Cdd:cd18046   160 DQIYDIFQKLP-PDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
120-321 1.29e-36

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: 134.78  E-value: 1.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 120 GFDQIDLDSRIAGVISK--FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFgVPAINNILTHNKKGLKVLCISPTRE 197
Cdd:cd17950     3 GFRDFLLKPELLRAIVDcgFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVF-VLSTLQQLEPVDGQVSVLVICHTRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 198 LALQIYDNLVDLTANTPLKCVAV-YGGVSKHEQVSSLRDAS--VVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEK 274
Cdd:cd17950    82 LAFQISNEYERFSKYMPNVKTAVfFGGVPIKKDIEVLKNKCphIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQ 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2624742258 275 -GFEQDIKSVMQQTNHaNRQTLMFTATWPKEVRELASTFMNSPVKVSI 321
Cdd:cd17950   162 lDMRRDVQEIFRATPH-DKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
142-315 5.13e-35

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


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 130.35  E-value: 5.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 142 PIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNI---LTHNKKGL--KVLCISPTRELALQIYDNLVDLTANTPLK 216
Cdd:cd17944    15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLqedQQPRKRGRapKVLVLAPTRELANQVTKDFKDITRKLSVA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 217 CVavYGGVSKHEQVSSLRDA-SVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHA----N 291
Cdd:cd17944    95 CF--YGGTPYQQQIFAIRNGiDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYKKdsedN 172
                         170       180
                  ....*....|....*....|....
gi 2624742258 292 RQTLMFTATWPKEVRELASTFMNS 315
Cdd:cd17944   173 PQTLLFSATCPDWVYNVAKKYMKS 196
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
344-458 1.57e-34

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: 125.79  E-value: 1.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 344 DKEKKLLSLLRKyqsgsNKDDKILIFALYKKEAtRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVA 423
Cdd:pfam00271   1 EKLEALLELLKK-----ERGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVA 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2624742258 424 ARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRAG 458
Cdd:pfam00271  75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
136-319 7.38e-32

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: 121.14  E-value: 7.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 136 KFPTPTPIQSVSWPYLLSG--KDVIGVAETGSGKTFAFGVPAINNILThNKKGLKVLCISPTRELALQIYDNLVDLTANT 213
Cdd:cd17963    13 GFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDP-TLKSPQALCLAPTRELARQIGEVVEKMGKFT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 214 PLKC-VAVYGGVSKHEQVSSlrdASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLE-KGFEQDIKSVMQQTNHaN 291
Cdd:cd17963    92 GVKVaLAVPGNDVPRGKKIT---AQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDtQGHGDQSIRIKRMLPR-N 167
                         170       180
                  ....*....|....*....|....*...
gi 2624742258 292 RQTLMFTATWPKEVRELASTFMNSPVKV 319
Cdd:cd17963   168 CQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
137-319 3.20e-28

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


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 111.41  E-value: 3.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 137 FPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKgLKVLCISPTRELALQIYDNLVDLTANTPLK 216
Cdd:cd18045    19 FEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRE-TQALILSPTRELAVQIQKVLLALGDYMNVQ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 217 CVAVYGGVSKHEQVSSLRDA-SVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHANrQTL 295
Cdd:cd18045    98 CHACIGGTSVGDDIRKLDYGqHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYLPPAT-QVV 176
                         170       180
                  ....*....|....*....|....
gi 2624742258 296 MFTATWPKEVRELASTFMNSPVKV 319
Cdd:cd18045   177 LVSATLPQDILEMTNKFMTDPIRI 200
HELICc smart00490
helicase superfamily c-terminal domain;
378-458 1.79e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 105.37  E-value: 1.79e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  378 RIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRA 457
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81

                   .
gi 2624742258  458 G 458
Cdd:smart00490  82 G 82
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
142-301 2.57e-27

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: 109.64  E-value: 2.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 142 PIQSVSWPYLLSG---------KDVIGVAETGSGKTFAFGVPAINNILTHNKKGLKVLCISPTRELALQIYDNLVDLTAN 212
Cdd:cd17956    15 PVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKELVQQVYKVFESLCKG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 213 TPLKCVAVYGGVS-KHEQVSSLRD--------ASVVVATPGRLIDLLNDGA-LSLDSIEYLVLDEADRMLEKGFEQDIKS 282
Cdd:cd17956    95 TGLKVVSLSGQKSfKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPgFTLKHLRFLVIDEADRLLNQSFQDWLET 174
                         170
                  ....*....|....*....
gi 2624742258 283 VMQQTNHANRQTLMFTATW 301
Cdd:cd17956   175 VMKALGRPTAPDLGSFGDA 193
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
140-310 9.60e-27

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: 108.22  E-value: 9.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 140 PTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILT--HNKKG----LKVLCISPTRELALQIYDNLVDLTANT 213
Cdd:cd17948    13 PTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRykLLAEGpfnaPRGLVITPSRELAEQIGSVAQSLTEGL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 214 PLKCVAVYGGVSKHEQVSSLR-DASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHANR 292
Cdd:cd17948    93 GLKVKVITGGRTKRQIRNPHFeEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRRFPLASR 172
                         170       180       190
                  ....*....|....*....|....*....|
gi 2624742258 293 ------------QTLMFTATWPKEVRELAS 310
Cdd:cd17948   173 rsentdgldpgtQLVLVSATMPSGVGEVLS 202
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
160-453 1.19e-21

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 98.56  E-value: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 160 VAETGSGKTFAFGvpainNILTHNKKGLKVLCISPTRELALQIYDNLVDLTANTPLkcvavyGGVSKHeqvsslRDASVV 239
Cdd:COG1061   106 VAPTGTGKTVLAL-----ALAAELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLA------GGGKKD------SDAPIT 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 240 VATPGRLIDLLNDGALSlDSIEYLVLDEADRMLEKGFEQdiksVMQQTNHANRqtLMFTATwPK---EVRELASTFMNSP 316
Cdd:COG1061   169 VATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRR----ILEAFPAAYR--LGLTAT-PFrsdGREILLFLFDGIV 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 317 VKVSIGdrnELSANKRITQ--IVEVIEPYDKEKK-------------------LLSLLRKYQSGSNKDDKILIFALYKKE 375
Cdd:COG1061   241 YEYSLK---EAIEDGYLAPpeYYGIRVDLTDERAeydalserlrealaadaerKDKILRELLREHPDDRKTLVFCSSVDH 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 376 ATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLT---FPLTvedYVHRIG 452
Cdd:COG1061   318 AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRptgSPRE---FIQRLG 394

                  .
gi 2624742258 453 R 453
Cdd:COG1061   395 R 395
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
154-277 8.71e-20

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: 85.92  E-value: 8.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 154 GKDVIGVAETGSGKTFAFGVPAINNILthnKKGLKVLCISPTRELALQIYDNLVDLtANTPLKCVAVYGGVSKHEQVSS- 232
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLL---KKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAEEREKNk 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2624742258 233 LRDASVVVATPGRLIDLLN-DGALSLDSIEYLVLDEADRMLEKGFE 277
Cdd:cd00046    77 LGDADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALLIDSRG 122
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
325-469 9.93e-18

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 86.71  E-value: 9.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 325 NELSANKRITQIVEVIEPYDKE----KKLLSLLRKyQSGSNKDDKILIFALYKKEATRIENLLVRNSFKV------SAVH 394
Cdd:COG1111   312 KRLVSDPRFRKAMRLAEEADIEhpklSKLREILKE-QLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKE 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 395 GD--LSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINltfpltvedY---------VHRIGRTGRAGQtGIA 463
Cdd:COG1111   391 GDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIF---------YepvpseirsIQRKGRTGRKRE-GRV 460

                  ....*.
gi 2624742258 464 HTLFTE 469
Cdd:COG1111   461 VVLIAK 466
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
151-467 1.57e-17

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 85.19  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 151 LLSGKDVIGVAETGSGKTFAFGVPAInnILthnkKGLkVLCISPTreLALQiyDNLVD-LTANTpLKCVAVYGGVSKHEQ 229
Cdd:COG0514    29 VLAGRDALVVMPTGGGKSLCYQLPAL--LL----PGL-TLVVSPL--IALM--KDQVDaLRAAG-IRAAFLNSSLSAEER 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 230 VSSLRDAS-----VVVATPGRL-----IDLLNDGALSLdsieyLVLDEA--------DrmlekgFEQD---IKSVMQQtn 288
Cdd:COG0514    97 REVLRALRagelkLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPDyrrLGELRER-- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 289 HANRQTLMFTATWPKEVRE--LASTFMNSPVKVSIG-DRNELsankRITqiVEVIEPYDKEKKLLSLLRKYQSGSnkddk 365
Cdd:COG0514   164 LPNVPVLALTATATPRVRAdiAEQLGLEDPRVFVGSfDRPNL----RLE--VVPKPPDDKLAQLLDFLKEHPGGS----- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 366 ILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATdVA-ARGLDIPNVKVVINLTFPLTV 444
Cdd:COG0514   233 GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSI 311
                         330       340
                  ....*....|....*....|...
gi 2624742258 445 EDYVHRIGRTGRAGQTGIAHTLF 467
Cdd:COG0514   312 EAYYQEIGRAGRDGLPAEALLLY 334
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
139-268 1.14e-15

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: 74.99  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 139 TPTPIQSVSW-PYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKglkVLCISPTRELALQIYDNLVDLTANTPLKC 217
Cdd:cd17921     1 LLNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK---AVYIAPTRALVNQKEADLRERFGPLGKNV 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2624742258 218 VAVYGGVSkhEQVSSLRDASVVVATPGRL-IDLLNDGALSLDSIEYLVLDEA 268
Cdd:cd17921    78 GLLTGDPS--VNKLLLAEADILVATPEKLdLLLRNGGERLIQDVRLVVVDEA 127
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
341-467 9.65e-15

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: 71.09  E-value: 9.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 341 EPYDKEKKLLsLLRKYQSGSNKDDKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLAT 420
Cdd:cd18794     9 RPKDKKDEKL-DLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2624742258 421 dVA-ARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRAGQTGIAHTLF 467
Cdd:cd18794    88 -VAfGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
PRK13766 PRK13766
Hef nuclease; Provisional
326-469 1.59e-13

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 73.37  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 326 ELSANKRITQIVEVIEPYDKE----KKLLSLLRKyQSGSNKDDKILIFALYKKEATRIENLLVRNSFKV------SAVHG 395
Cdd:PRK13766  325 RLVEDPRFRKAVRKAKELDIEhpklEKLREIVKE-QLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDG 403
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2624742258 396 D--LSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVInltF--PLTVE-DYVHRIGRTGRaGQTGIAHTLFTE 469
Cdd:PRK13766  404 DkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI---FyePVPSEiRSIQRKGRTGR-QEEGRVVVLIAK 478
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
104-316 2.98e-13

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: 69.28  E-value: 2.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 104 EVTVEDPHNlglrPLLG---FDQIDL-DSRIAGVISK-FPTPTPIQSVSWPYLLSG--KDVIGVAETGSGKTFAFgVPAI 176
Cdd:cd18048     4 EVLQRDPTS----PLFSvksFEELHLkEELLRGIYAMgFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAF-VLAM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 177 NNILTHNKKGLKVLCISPTRELALQIyDNLVDLTANTPLKCVAVYGGVSKHEQVSSLRDASVVVATPGRLID-LLNDGAL 255
Cdd:cd18048    79 LSRVDALKLYPQCLCLSPTFELALQT-GKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDwCFKLRLI 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2624742258 256 SLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHANRQTLMFTATWPKEVRELASTFMNSP 316
Cdd:cd18048   158 DVTNISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
137-316 1.06e-12

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: 67.05  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 137 FPTPTPIQSVSWPYLLSG--KDVIGVAETGSGKTFAFgvpaINNILTHNKKGLK---VLCISPTRELALQIYDNLVDLTA 211
Cdd:cd18047    21 FNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAF----VLAMLSQVEPANKypqCLCLSPTYELALQTGKVIEQMGK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 212 NTPLKCVAVYGGVSKHEQVSSLRDaSVVVATPGRLID-LLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHA 290
Cdd:cd18047    97 FYPELKLAYAVRGNKLERGQKISE-QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPR 175
                         170       180
                  ....*....|....*....|....*.
gi 2624742258 291 NRQTLMFTATWPKEVRELASTFMNSP 316
Cdd:cd18047   176 NCQMLLFSATFEDSVWKFAQKVVPDP 201
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
140-304 1.66e-12

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: 67.40  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 140 PTPIQSVSWPYLLsgKDVIG------------------VAETGSGKTFAFGVPAINNI----------------LTHNKK 185
Cdd:cd17965    31 PSPIQTLAIKKLL--KTLMRkvtkqtsneepklevfllAAETGSGKTLAYLAPLLDYLkrqeqepfeeaeeeyeSAKDTG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 186 GLKVLCISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQVSSLRDAS---VVVATPGRLIDLLNDGALSLDSIEY 262
Cdd:cd17965   109 RPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLAFKGridILVTTPGKLASLAKSRPKILSRVTH 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2624742258 263 LVLDEADRMLEKGFEQDIKSVMQQTNHANrQTLMFTATWPKE 304
Cdd:cd17965   189 LVVDEADTLFDRSFLQDTTSIIKRAPKLK-HLILCSATIPKE 229
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
144-270 3.84e-12

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: 64.84  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 144 QSVSWPYLLSGKDVIgVAETGSGKTfAFGVPAINNILThnKKGLKVLCISPTRELALQIYDNLVDLTaNTPLKCVAVYGG 223
Cdd:cd18035     7 QVLIAAVALNGNTLI-VLPTGLGKT-IIAILVAADRLT--KKGGKVLILAPSRPLVEQHAENLKRVL-NIPDKITSLTGE 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2624742258 224 VSKHEQVSSLRDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADR 270
Cdd:cd18035    82 VKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
151-463 5.47e-12

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 68.32  E-value: 5.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 151 LLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKglKVLCISPTRELALQIYDNLVDLTANTPLKC-VAVY-GGVSKHE 228
Cdd:COG1205    68 ARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA--TALYLYPTKALARDQLRRLRELAEALGLGVrVATYdGDTPPEE 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 229 QVSSLRDASVVVATPgrliDLLNDGALS--------LDSIEYLVLDEA---------------DRMLEkgfeqdiksVMQ 285
Cdd:COG1205   146 RRWIREHPDIVLTNP----DMLHYGLLPhhtrwarfFRNLRYVVIDEAhtyrgvfgshvanvlRRLRR---------ICR 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 286 QTNhANRQTLMFTATW--PKevrELASTFMNSPVKVsI-------GDRN-------ELSANKRITQIVEVIEpydkekkL 349
Cdd:COG1205   213 HYG-SDPQFILASATIgnPA---EHAERLTGRPVTV-VdedgsprGERTfvlwnppLVDDGIRRSALAEAAR-------L 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 350 LSLLrkYQSGSnkddKILIFA-------LYkkeATRIENLLVRNSF--KVSAVHGDLSQQQRTSALGAFKAGKttlLLAt 420
Cdd:COG1205   281 LADL--VREGL----RTLVFTrsrrgaeLL---ARYARRALREPDLadRVAAYRAGYLPEERREIERGLRSGE---LLG- 347
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2624742258 421 dVAAR-----GLDIPNVKVVINLTFPLTVEDYVHRIGRTGRAGQTGIA 463
Cdd:COG1205   348 -VVSTnalelGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
151-459 1.46e-11

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 66.84  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 151 LLSGKDVIGVAETGSGKTFAfgvpAINNILTHNKKGLKVLCISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHEQv 230
Cdd:COG1204    35 LLEGKNLVVSAPTASGKTLI----AELAILKALLNGGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDE- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 231 sSLRDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEA----DRmlEKGFeqDIKSVMQQTNHANRQT----LMFTATWP 302
Cdd:COG1204   110 -WLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGP--TLEVLLARLRRLNPEAqivaLSATIGNA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 303 KEVRE-LASTFMNS---PVKVSIG----------DRNELSANKRITQIVEVIE--------------PYDKEKKLLSLLR 354
Cdd:COG1204   185 EEIAEwLDAELVKSdwrPVPLNEGvlydgvlrfdDGSRRSKDPTLALALDLLEeggqvlvfvssrrdAESLAKKLADELK 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 355 KYQSGSNKDD--KILIFALYKKEATRIENLLVRN-SFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPN 431
Cdd:COG1204   265 RRLTPEEREEleELAEELLEVSEETHTNEKLADClEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPA 344
                         330       340       350
                  ....*....|....*....|....*....|...
gi 2624742258 432 VKVVINLTF-----PLTVEDYVHRIGRTGRAGQ 459
Cdd:COG1204   345 RRVIIRDTKrggmvPIPVLEFKQMAGRAGRPGY 377
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
154-267 2.10e-11

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: 62.22  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 154 GKDVIGVAETGSGKTFAFGVPAINNILTHNKKGLKVLCISPTRELALQIYDNLvdltaNTPLKCVAVY-------GGVSK 226
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRL-----EEPLDEIDLEipvavrhGDTSQ 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2624742258 227 HEQVSSLRDAS-VVVATPGRLIDLLNDGALS--LDSIEYLVLDE 267
Cdd:cd17922    76 SEKAKQLKNPPgILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
336-452 2.36e-11

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: 61.34  E-value: 2.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 336 IVEVIEPydKEKKLLSLLRKYQSgsnKDDKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTT 415
Cdd:cd18793     5 IEEVVSG--KLEALLELLEELRE---PGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2624742258 416 --LLLATDVAARGLDIPNVKVVINLTFPL--TVE----DYVHRIG 452
Cdd:cd18793    80 rvFLLSTKAGGVGLNLTAANRVILYDPWWnpAVEeqaiDRAHRIG 124
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
341-457 3.95e-11

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: 61.07  E-value: 3.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 341 EPYDKEK--KLLSLLRKYQSgSNKDDKILIFAlyKKEATRI-------ENLLVRNSFKVSAVHG----------DLSQQQ 401
Cdd:cd18802     2 EIVVIPKlqKLIEILREYFP-KTPDFRGIIFV--ERRATAVvlsrllkEHPSTLAFIRCGFLIGrgnssqrkrsLMTQRK 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2624742258 402 RTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRtGRA 457
Cdd:cd18802    79 QKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
337-456 9.10e-11

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: 60.06  E-value: 9.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 337 VEVIEPydKEKKLLSLLRKY--QSGSNKDDKILIFALYKKEATRIENLLVRNSFKVSAV----HGD------LSQQQRTS 404
Cdd:cd18801     4 VEKIHP--KLEKLEEIVKEHfkKKQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASgksskgMSQKEQKE 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2624742258 405 ALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGR 456
Cdd:cd18801    82 VIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
135-206 2.87e-10

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 62.81  E-value: 2.87e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2624742258 135 SKFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFA-FgVPAINNILTH-----NKKGLKVLCISPTRELALQIYDNL 206
Cdd:COG1201    20 ARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAaF-LPALDELARRprpgeLPDGLRVLYISPLKALANDIERNL 96
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
160-300 1.03e-08

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: 54.23  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 160 VAETGSGKTFaFGVPAINNILTHnkkglKVLCISPTRELALQIYDNLVDLTANTPLKcvAVYGGVSKHeqvssLRDASVV 239
Cdd:cd17926    24 VLPTGSGKTL-TALALIAYLKEL-----RTLIVVPTDALLDQWKERFEDFLGDSSIG--LIGGGKKKD-----FDDANVV 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2624742258 240 VATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQdiksVMQQTNHANRqtLMFTAT 300
Cdd:cd17926    91 VATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSE----ILKELNAKYR--LGLTAT 145
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
415-466 1.05e-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: 51.94  E-value: 1.05e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2624742258 415 TLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRAGQT-GIAHTL 466
Cdd:cd18785    24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDeGEVILF 76
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
155-268 3.87e-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: 53.42  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 155 KDVIGVAETGSGKTF-------AFGVpaINNILTHNKKglKVLCISPTRELALQIYDNLvdlTANTPLKCVAVYGGVSKH 227
Cdd:cd18034    17 RNTIVVLPTGSGKTLiavmlikEMGE--LNRKEKNPKK--RAVFLVPTVPLVAQQAEAI---RSHTDLKVGEYSGEMGVD 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2624742258 228 EQVSS-----LRDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEA 268
Cdd:cd18034    90 KWTKErwkeeLEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
144-268 2.20e-07

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: 51.05  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 144 QSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILthNKKGLKVLCISPTRELALQIYDNLVDLTANTPLKC-VAVYG 222
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL--RDPGSRALYLYPTKALAQDQLRSLRELLEQLGLGIrVATYD 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2624742258 223 GVSKHEQVSSLRD--ASVVVATPgrliDLLNDGAL--------SLDSIEYLVLDEA 268
Cdd:cd17923    83 GDTPREERRAIIRnpPRILLTNP----DMLHYALLphhdrwarFLRNLRYVVLDEA 134
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
345-469 5.88e-07

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: 49.17  E-value: 5.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 345 KEKKLLSLLRKYQSGsnkdDKILIFALYKKEATRIENLLvrnsfKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAA 424
Cdd:cd18789    35 KLRALEELLKRHEQG----DKIIVFTDNVEALYRYAKRL-----LKPFITGETPQSEREEILQNFREGEYNTLVVSKVGD 105
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2624742258 425 RGLDIPNVKVVINLTFPL-TVEDYVHRIGRTGRAGQTGIAHTLFTE 469
Cdd:cd18789   106 EGIDLPEANVAIQISGHGgSRRQEAQRLGRILRPKKGGGKNAFFYS 151
PRK01172 PRK01172
ATP-dependent DNA helicase;
154-462 9.95e-07

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 51.42  E-value: 9.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 154 GKDVIGVAETGSGKTFAfgvpAINNILTHNKKGLKVLCISPTRELALQIYDNLVDLTaNTPLKCVAVYGGVSkhEQVSSL 233
Cdd:PRK01172   37 GENVIVSVPTAAGKTLI----AYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSRLR-SLGMRVKISIGDYD--DPPDFI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 234 RDASVVVATPGRLIDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIKSVMQQTNHANRQTLM--FTATwPKEVRELA-- 309
Cdd:PRK01172  110 KRYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARYVNPDARIlaLSAT-VSNANELAqw 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 310 -------STFMNSPVKVSIGDRNELSANkritqiveviepyDKEKKLLSLLRKYQSGSNKDDKILIFALYKKEATRIENL 382
Cdd:PRK01172  189 lnaslikSNFRPVPLKLGILYRKRLILD-------------GYERSQVDINSLIKETVNDGGQVLVFVSSRKNAEDYAEM 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 383 LVR-----NSFKVSAV--------------------HGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVI- 436
Cdd:PRK01172  256 LIQhfpefNDFKVSSEnnnvyddslnemlphgvafhHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVr 335
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2624742258 437 NLT-------FPLTVEDYVHRIGRTGRAG--QTGI 462
Cdd:PRK01172  336 DITrygnggiRYLSNMEIKQMIGRAGRPGydQYGI 370
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
345-460 1.16e-06

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 51.38  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 345 KEKKLLSLLRKYQSgsnKDDKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTT--LLLATDV 422
Cdd:COG0553   534 KLEALLELLEELLA---EGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKA 610
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2624742258 423 AARGLDIPNVKVVINLTFP--LTVEDyvHRIGRTGRAGQT 460
Cdd:COG0553   611 GGEGLNLTAADHVIHYDLWwnPAVEE--QAIDRAHRIGQT 648
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
151-319 1.34e-06

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 49.07  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 151 LLSGKDVIGVAETGSGKTFAFGVPAinniltHNKKGLkVLCISPTreLALQiyDNLVDLTANTPLKCVAVYGGVSKHEQV 230
Cdd:cd17920    24 VLAGRDVLVVMPTGGGKSLCYQLPA------LLLDGV-TLVVSPL--ISLM--QDQVDRLQQLGIRAAALNSTLSPEEKR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 231 SSLR-----DASVVVATPGRL-----IDLLNdGALSLDSIEYLVLDEADRMLEKG--FEQD---IKSVMQQTNHAnrQTL 295
Cdd:cd17920    93 EVLLrikngQYKLLYVTPERLlspdfLELLQ-RLPERKRLALIVVDEAHCVSQWGhdFRPDylrLGRLRRALPGV--PIL 169
                         170       180
                  ....*....|....*....|....*.
gi 2624742258 296 MFTATWPKEVRE--LASTFMNSPVKV 319
Cdd:cd17920   170 ALTATATPEVREdiLKRLGLRNPVIF 195
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
315-469 3.73e-06

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 46.87  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 315 SPVKVSIGDRNELSANKRITQIVEVIEpydkekkllsllrkyqsgsnKDDKILIFALYKKEATRI-ENLLVRNSFKVSAV 393
Cdd:cd18796    10 LPVAPEIFPWAGESGADAYAEVIFLLE--------------------RHKSTLVFTNTRSQAERLaQRLRELCPDRVPPD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 394 -----HGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRAGQTGIAHTLFT 468
Cdd:cd18796    70 fialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLVP 149

                  .
gi 2624742258 469 E 469
Cdd:cd18796   150 T 150
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
383-459 4.53e-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: 46.57  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 383 LVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVInltfpltVED-------YVHRI-GRT 454
Cdd:cd18811    57 RFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMV-------IEDaerfglsQLHQLrGRV 129

                  ....*
gi 2624742258 455 GRAGQ 459
Cdd:cd18811   130 GRGDH 134
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
151-267 4.90e-06

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: 46.94  E-value: 4.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 151 LLSGKDVIGVAETGSGKTFAFGVPAINNILthnkKGLKVLCISPTRELALQIYDNLVDLtaNTPLKCVAVYGGvSKHEQV 230
Cdd:cd18028    14 LLKGENLLISIPTASGKTLIAEMAMVNTLL----EGGKALYLVPLRALASEKYEEFKKL--EEIGLKVGISTG-DYDEDD 86
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2624742258 231 SSLRDASVVVATPGRLIDLLNDGALSLDSIEYLVLDE 267
Cdd:cd18028    87 EWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
151-300 8.67e-06

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: 46.26  E-value: 8.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 151 LLSGkDVigvaetGSGKTFAFGVPAINNIlthnKKGLKVLCISPTRELALQIYDNLVDLTANTPLKCVAvyGGvsKHEQV 230
Cdd:cd17918    40 LLSG-DV------GSGKTLVALGAALLAY----KNGKQVAILVPTEILAHQHYEEARKFLPFINVELVT--GG--TKAQI 104
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2624742258 231 SSlrDASVVVATPGrlidLLNDGALSLDSiEYLVLDEADRMlekgfeqdikSVMQQ---TNHANRQTLMFTAT 300
Cdd:cd17918   105 LS--GISLLVGTHA----LLHLDVKFKNL-DLVIVDEQHRF----------GVAQRealYNLGATHFLEATAT 160
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
147-275 8.78e-06

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


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 46.55  E-value: 8.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 147 SWPY-LLSGKDVIGVAETGSGKTfAFGVPAInniLTHNKKGLKVLCISPTRELALQIYDNLVDL--TANTPLKCVAVYGG 223
Cdd:cd17924    24 TWAKrLLRGKSFAIIAPTGVGKT-TFGLATS---LYLASKGKRSYLIFPTKSLVKQAYERLSKYaeKAGVEVKILVYHSR 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2624742258 224 VSKHEQVSSL-----RDASVVVATPGRLIDllNDGALSLDSIEYLVLDEADRMLEKG 275
Cdd:cd17924   100 LKKKEKEELLekiekGDFDILVTTNQFLSK--NFDLLSNKKFDFVFVDDVDAVLKSS 154
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
152-459 1.18e-05

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 48.35  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  152 LSGKDVIGVAETGSGKTFAFGVPAINNilthnkKGLkVLCISPTRELalqIYDNLVDL-TANTPlkcvAVY--GGVSKHE 228
Cdd:PLN03137   473 MSGYDVFVLMPTGGGKSLTYQLPALIC------PGI-TLVISPLVSL---IQDQIMNLlQANIP----AASlsAGMEWAE 538
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  229 QVSSLRDAS-------VVVATPGRLI--DLLNDGALSLDSIEYL---VLDEADRMLEKG--FEQDIKS--VMQQtNHANR 292
Cdd:PLN03137   539 QLEILQELSseyskykLLYVTPEKVAksDSLLRHLENLNSRGLLarfVIDEAHCVSQWGhdFRPDYQGlgILKQ-KFPNI 617
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  293 QTLMFTATWPKEVRE---LASTFMNSPVKVSIGDRNELSANkritqivevIEPydKEKKLLSLLRKYQSGSNKDDKILIF 369
Cdd:PLN03137   618 PVLALTATATASVKEdvvQALGLVNCVVFRQSFNRPNLWYS---------VVP--KTKKCLEDIDKFIKENHFDECGIIY 686
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258  370 ALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVH 449
Cdd:PLN03137   687 CLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQ 766
                          330
                   ....*....|
gi 2624742258  450 RIGRTGRAGQ 459
Cdd:PLN03137   767 ECGRAGRDGQ 776
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
151-270 1.25e-05

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 48.01  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 151 LLSGKDVIGVAETGSGKTFAfGVPAINNILTHNKKglkvlCI--SPTRELALQIYDNLVDltantplkcvaVYGGvskhE 228
Cdd:COG4581    37 LEAGRSVLVAAPTGSGKTLV-AEFAIFLALARGRR-----SFytAPIKALSNQKFFDLVE-----------RFGA----E 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2624742258 229 QVSSL-------RDASVVVATPGRLIDLLNDGALSLDSIEYLVLDE----ADR 270
Cdd:COG4581    96 NVGLLtgdasvnPDAPIVVMTTEILRNMLYREGADLEDVGVVVMDEfhylADP 148
PRK13767 PRK13767
ATP-dependent helicase; Provisional
134-206 1.47e-05

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 47.96  E-value: 1.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2624742258 134 ISKFPTPTPIQSVSWPYLLSGKDVIGVAETGSGKTFAFGVPAINNILTHNKKGL---KVLC--ISPTRELALQIYDNL 206
Cdd:PRK13767   27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGEledKVYClyVSPLRALNNDIHRNL 104
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
152-458 1.50e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.79  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 152 LSGKDVIGVAETGSGKTFAFGVPA-INNILThnkkglkvLCISPTRELalqIYDNLVDLTANTpLKCVAVYGGVSKHEQV 230
Cdd:PRK11057   38 LSGRDCLVVMPTGGGKSLCYQIPAlVLDGLT--------LVVSPLISL---MKDQVDQLLANG-VAAACLNSTQTREQQL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 231 SSLR-----DASVVVATPGRL-----IDLLNDGALSLdsieyLVLDEADRMLEKG--FEQDIKSVMQQTNHANRQTLM-F 297
Cdd:PRK11057  106 EVMAgcrtgQIKLLYIAPERLmmdnfLEHLAHWNPAL-----LAVDEAHCISQWGhdFRPEYAALGQLRQRFPTLPFMaL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 298 TATWPKEVRE--LASTFMNSP-VKVSIGDRnelsANKRITqIVEVIEPYDKekkllsLLRKYQSGSNKDDKIlifalYKK 374
Cdd:PRK11057  181 TATADDTTRQdiVRLLGLNDPlIQISSFDR----PNIRYT-LVEKFKPLDQ------LMRYVQEQRGKSGII-----YCN 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 375 EATRIENLLVR---NSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRI 451
Cdd:PRK11057  245 SRAKVEDTAARlqsRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQET 324

                  ....*..
gi 2624742258 452 GRTGRAG 458
Cdd:PRK11057  325 GRAGRDG 331
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
362-453 2.18e-05

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: 43.70  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 362 KDDKILIFALYKKEATRIENLLVRNSFKVSAVHGDLSQQQRT-SALGAFKAGKTTL--LLATDVAARGLDIPNVKVVINL 438
Cdd:cd18799     5 VEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGELKPpiLVTVDLLTTGVDIPEVDNVVFL 84
                          90
                  ....*....|....*..
gi 2624742258 439 --TFPLTVedYVHRIGR 453
Cdd:cd18799    85 rpTESRTL--FLQMLGR 99
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
151-307 2.25e-05

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


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 45.32  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 151 LLSGKDVIGVAETGSGKTFAFGVPAInnILTHNKKGLKVLcISPTreLALQIydnlvDLTANTP--LKCVAVYGGVSKHE 228
Cdd:cd18018    24 LLSGRSTLVVLPTGAGKSLCYQLPAL--LLRRRGPGLTLV-VSPL--IALMK-----DQVDALPraIKAAALNSSLTREE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 229 QVSSLR-----DASVVVATPGRlidLLNDG----ALSLDSIEYLVLDEADRMLEKG--FEQD---IKSVMQQTNhANRQT 294
Cdd:cd18018    94 RRRILEklragEVKILYVSPER---LVNESfrelLRQTPPISLLVVDEAHCISEWShnFRPDylrLCRVLRELL-GAPPV 169
                         170
                  ....*....|...
gi 2624742258 295 LMFTATWPKEVRE 307
Cdd:cd18018   170 LALTATATKRVVE 182
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
374-478 2.45e-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: 44.57  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 374 KEATRIENLLVRnsFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVInltfpltVED------- 446
Cdd:cd18792    49 ALAEELKELVPE--ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMI-------IEDadrfgls 119
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2624742258 447 YVHRI-GRTGRAGQTGIAHTLFTEHEKHLSGAL 478
Cdd:cd18792   120 QLHQLrGRVGRGKHQSYCYLLYPDPKKLTETAK 152
ResIII pfam04851
Type III restriction enzyme, res subunit;
160-300 3.89e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 44.20  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 160 VAETGSGKTF-AFGVPAinnILTHNKKGLKVLCISPTRELALQIYDNLVDLTANTPLKCVAVYGGvskhEQVSSLRDASV 238
Cdd:pfam04851  29 VMATGSGKTLtAAKLIA---RLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGD----KKDESVDDNKI 101
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2624742258 239 VVATPGRL--IDLLNDGALSLDSIEYLVLDEADRMLEKGFEQDIksvmqqtNHANRQTLM-FTAT 300
Cdd:pfam04851 102 VVTTIQSLykALELASLELLPDFFDVIIIDEAHRSGASSYRNIL-------EYFKPAFLLgLTAT 159
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
394-455 6.01e-05

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 46.07  E-value: 6.01e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2624742258  394 HGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTG 455
Cdd:PRK09751   308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
336-456 2.88e-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: 41.91  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 336 IVEV-IEPYDKEKKLLSLLRKYQSGsnkddkILIFA--LYKKE-ATRIENLLVRNSFKVSAVHGDlsqqqRTSALGAFKA 411
Cdd:cd18798     2 IVDVyIEDSDSLEKLLELVKKLGDG------GLIFVsiDYGKEyAEELKEFLERHGIKAELALSS-----TEKNLEKFEE 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2624742258 412 GKTTLLLAT----DVAARGLDIPN-VKVVINLTFPLTVedYVHRIGRTGR 456
Cdd:cd18798    71 GEIDVLIGVasyyGVLVRGIDLPErIKYAIFYGVPVTT--YIQASGRTSR 118
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
152-270 3.80e-04

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: 41.65  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 152 LSGKDVIGVAETGSGKTFAFGVPAIN---NILTHNKKglKVLCISPTRELALQIYDNLVDLTANTPLKCVAVYGGVSKHE 228
Cdd:cd17927    15 LKGKNTIICLPTGSGKTFVAVLICEHhlkKFPAGRKG--KVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENV 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2624742258 229 QVSSL-RDASVVVATPGRLIDLLNDGAL-SLDSIEYLVLDEADR 270
Cdd:cd17927    93 SVEQIvESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDECHN 136
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
374-472 5.36e-04

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: 40.40  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 374 KEATRIENLLvrNSFKVSAVHGDLSQQQRTSALGAFKAGKTTLLLATDVAARGLDIPNVKVVInltfpltVED------- 446
Cdd:cd18810    40 KLATQLRQLV--PEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTII-------IERadkfgla 110
                          90       100
                  ....*....|....*....|....*...
gi 2624742258 447 --YVHRiGRTGRAGQTGIAHTLFTEHEK 472
Cdd:cd18810   111 qlYQLR-GRVGRSKERAYAYFLYPDQKK 137
CMS1 pfam14617
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant ...
225-266 1.65e-03

U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant CMS1-like proteins. The family has similarity to the DEAD-box helicases.


Pssm-ID: 373164  Cd Length: 250  Bit Score: 40.23  E-value: 1.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2624742258 225 SKH----EQVSSLRDASVVVA--TPGRLIDLLNDGALSLDSIEYLVLD 266
Cdd:pfam14617 159 AKHikleEHITYCKASRIGIGvgTPGRIADLLENESLSVDNLKYIILD 206
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
339-459 3.03e-03

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 38.39  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 339 VIEPYDKEKKLLSLLRKYQSGSN-------KDDKILIFA-------LYKKEATRIENLLVRNSFKVSAVHGDLSQQQRTS 404
Cdd:cd18797     4 LWNPPLLDRKDGERGSARREAARlfadlvrAGVKTIVFCrsrklaeLLLRYLKARLVEEGPLASKVASYRAGYLAEDRRE 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2624742258 405 ALGAFKAGKTTLLLATDVAARGLDIPNVKVVINLTFPLTVEDYVHRIGRTGRAGQ 459
Cdd:cd18797    84 IEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGK 138
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
164-312 5.53e-03

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 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: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 38.32  E-value: 5.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 164 GSGKTfafgVPAINNILTHNKKGLK--VLCISPTrelalqiydnlvDLTAN--------TP-LKCVAVYGGVSKHEQVSS 232
Cdd:cd18012    33 GLGKT----LQTLALLLSRKEEGRKgpSLVVAPT------------SLIYNweeeaakfAPeLKVLVIHGTKRKREKLRA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624742258 233 LRDASVVVATPG---RLIDLLNDGalsldSIEYLVLDEAdrmlekgfeQDIKsvmqqtNHANRQTlmftatwpKEVRELA 309
Cdd:cd18012    97 LEDYDLVITSYGllrRDIELLKEV-----KFHYLVLDEA---------QNIK------NPQTKTA--------KAVKALK 148

                  ...
gi 2624742258 310 STF 312
Cdd:cd18012   149 ADH 151
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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