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Conserved domains on  [gi|15231353|ref|NP_187354|]
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DEA(D/H)-box RNA helicase family protein [Arabidopsis thaliana]

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 super family cl33924
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
375-776 4.68e-85

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


The actual alignment was detected with superfamily member COG0513:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 276.26  E-value: 4.68e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLreeelqghSKSSPGCPRV 454
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL--------DPSRPRAPQA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 455 IVLVPTAELASQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDE 534
Cdd:COG0513  75 LILAPTRELALQVAEELRKLAK-YLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 535 VDILFgDDEFEAALQNLINSSPVTAQYLFVTATLPLEIyNKLVEVF-PDCEVVMGPRVHRVSNALEEFLVDCSGDDnaek 613
Cdd:COG0513 154 ADRML-DMGFIEDIERILKLLPKERQTLLFSATMPPEI-RKLAKRYlKNPVRIEVAPENATAETIEQRYYLVDKRD---- 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 614 tpetafqnKKTALLQIMEENPVSKTIIFCNKIETCRKVENIFKRvdrkeRQLHVLPFHAALSQESRLTNMQEFTSSQPEe 693
Cdd:COG0513 228 --------KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQK-----RGISAAALHGDLSQGQRERALDAFRNGKIR- 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 694 nslFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARgKGKAFIFVVGKQVGLARRIIERNEKGHPVHDV 773
Cdd:COG0513 294 ---VLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGA-EGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369

                ...
gi 15231353 774 PNA 776
Cdd:COG0513 370 PGF 372
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
164-328 6.87e-03

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 39.89  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  164 KAIPRSGKSAERNEVKRASKVRESRESRRDLDRLEGDDEDVDEVSNPDRFTDNQRAGSRSSYSKGGYAANSRGKGDRLSV 243
Cdd:PRK12678 111 AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGER 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  244 ARDLDSFEGHGRAIDE-VSNPRKFNDNERAESRSSYSRDSSANSRGREDRRFVAKELDTFQGRDKAYDEVYNPRRFTDNE 322
Cdd:PRK12678 191 GRREERGRDGDDRDRRdRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRD 270

                 ....*.
gi 15231353  323 RGLRGG 328
Cdd:PRK12678 271 RRGRRG 276
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
375-776 4.68e-85

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 276.26  E-value: 4.68e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLreeelqghSKSSPGCPRV 454
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL--------DPSRPRAPQA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 455 IVLVPTAELASQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDE 534
Cdd:COG0513  75 LILAPTRELALQVAEELRKLAK-YLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 535 VDILFgDDEFEAALQNLINSSPVTAQYLFVTATLPLEIyNKLVEVF-PDCEVVMGPRVHRVSNALEEFLVDCSGDDnaek 613
Cdd:COG0513 154 ADRML-DMGFIEDIERILKLLPKERQTLLFSATMPPEI-RKLAKRYlKNPVRIEVAPENATAETIEQRYYLVDKRD---- 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 614 tpetafqnKKTALLQIMEENPVSKTIIFCNKIETCRKVENIFKRvdrkeRQLHVLPFHAALSQESRLTNMQEFTSSQPEe 693
Cdd:COG0513 228 --------KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQK-----RGISAAALHGDLSQGQRERALDAFRNGKIR- 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 694 nslFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARgKGKAFIFVVGKQVGLARRIIERNEKGHPVHDV 773
Cdd:COG0513 294 ---VLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGA-EGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369

                ...
gi 15231353 774 PNA 776
Cdd:COG0513 370 PGF 372
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
385-574 1.18e-62

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: 208.45  E-value: 1.18e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEElqghsKSSPGCPRVIVLVPTAELA 464
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP-----KKKGRGPQALVLAPTRELA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 465 SQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDEF 544
Cdd:cd00268  76 MQIAEVARKLGK-GTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRML-DMGF 153
                       170       180       190
                ....*....|....*....|....*....|
gi 15231353 545 EAALQNLINSSPVTAQYLFVTATLPLEIYN 574
Cdd:cd00268 154 EEDVEKILSALPKDRQTLLFSATLPEEVKE 183
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
374-762 2.96e-40

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 153.94  E-value: 2.96e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  374 KTFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQrlreeELQGHSKSSPGCPR 453
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQ-----HLLDFPRRKSGPPR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  454 VIVLVPTAELASQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILD 533
Cdd:PRK11192  76 ILILTPTRELAMQVADQARELAK-HTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  534 EVDILFgDDEFEAALQNLINSSPVTAQYLFVTATLPleiyNKLVEVFpdcevvmgprVHRVSNALEEFLVDCS------- 606
Cdd:PRK11192 155 EADRML-DMGFAQDIETIAAETRWRKQTLLFSATLE----GDAVQDF----------AERLLNDPVEVEAEPSrrerkki 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  607 ------GDDNaektpetafqNKKTALL-QIMEENPVSKTIIFCNKIETCRKVENIFkrvdrKERQLHVLPFHAALSQESR 679
Cdd:PRK11192 220 hqwyyrADDL----------EHKTALLcHLLKQPEVTRSIVFVRTRERVHELAGWL-----RKAGINCCYLEGEMVQAKR 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  680 LTNMQEFTSSqpEENslFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARgKGKAFIFV-------VGK 752
Cdd:PRK11192 285 NEAIKRLTDG--RVN--VLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGR-KGTAISLVeahdhllLGK 359
                        410
                 ....*....|....*
gi 15231353  753 -----QVGLARRIIE 762
Cdd:PRK11192 360 ieryiEEPLKARVID 374
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
400-574 1.24e-35

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: 132.37  E-value: 1.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353   400 IQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEElqghsksspGCPRVIVLVPTAELASQVLANCRSISKsGV 479
Cdd:pfam00270   3 IQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD---------NGPQALVLAPTRELAEQIYEELKKLGK-GL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353   480 PFRSMVVTGGFRQRTQLENLeQGVDVLIATPGRFTYLMNEGILgLSNLRCAILDEVDiLFGDDEFEAALQNLINSSPVTA 559
Cdd:pfam00270  73 GLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKKR 149
                         170
                  ....*....|....*
gi 15231353   560 QYLFVTATLPLEIYN 574
Cdd:pfam00270 150 QILLLSATLPRNLED 164
DEXDc smart00487
DEAD-like helicases superfamily;
389-590 9.70e-33

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 125.68  E-value: 9.70e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353    389 LKEQNFDRPAHIQAMAFSPVIDG-KSCIIADQSGSGKTLAYLVPVIQRLREEelqghsksspGCPRVIVLVPTAELASQV 467
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG----------KGGRVLVLVPTRELAEQW 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353    468 LANCRSISKSgVPFRSMVVTGGFRQRTQLENLEQGV-DVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDEFEA 546
Cdd:smart00487  71 AEELKKLGPS-LGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLL-DGGFGD 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 15231353    547 ALQNLINSSPVTAQYLFVTATLPLEIYNKLVEVFPDCEVVMGPR 590
Cdd:smart00487 149 QLEKLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF 192
PRK12678 PRK12678
transcription termination factor Rho; Provisional
164-328 6.87e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 39.89  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  164 KAIPRSGKSAERNEVKRASKVRESRESRRDLDRLEGDDEDVDEVSNPDRFTDNQRAGSRSSYSKGGYAANSRGKGDRLSV 243
Cdd:PRK12678 111 AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGER 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  244 ARDLDSFEGHGRAIDE-VSNPRKFNDNERAESRSSYSRDSSANSRGREDRRFVAKELDTFQGRDKAYDEVYNPRRFTDNE 322
Cdd:PRK12678 191 GRREERGRDGDDRDRRdRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRD 270

                 ....*.
gi 15231353  323 RGLRGG 328
Cdd:PRK12678 271 RRGRRG 276
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
375-776 4.68e-85

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 276.26  E-value: 4.68e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLreeelqghSKSSPGCPRV 454
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL--------DPSRPRAPQA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 455 IVLVPTAELASQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDE 534
Cdd:COG0513  75 LILAPTRELALQVAEELRKLAK-YLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 535 VDILFgDDEFEAALQNLINSSPVTAQYLFVTATLPLEIyNKLVEVF-PDCEVVMGPRVHRVSNALEEFLVDCSGDDnaek 613
Cdd:COG0513 154 ADRML-DMGFIEDIERILKLLPKERQTLLFSATMPPEI-RKLAKRYlKNPVRIEVAPENATAETIEQRYYLVDKRD---- 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 614 tpetafqnKKTALLQIMEENPVSKTIIFCNKIETCRKVENIFKRvdrkeRQLHVLPFHAALSQESRLTNMQEFTSSQPEe 693
Cdd:COG0513 228 --------KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQK-----RGISAAALHGDLSQGQRERALDAFRNGKIR- 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 694 nslFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARgKGKAFIFVVGKQVGLARRIIERNEKGHPVHDV 773
Cdd:COG0513 294 ---VLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGA-EGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369

                ...
gi 15231353 774 PNA 776
Cdd:COG0513 370 PGF 372
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
385-574 1.18e-62

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: 208.45  E-value: 1.18e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEElqghsKSSPGCPRVIVLVPTAELA 464
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP-----KKKGRGPQALVLAPTRELA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 465 SQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDEF 544
Cdd:cd00268  76 MQIAEVARKLGK-GTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRML-DMGF 153
                       170       180       190
                ....*....|....*....|....*....|
gi 15231353 545 EAALQNLINSSPVTAQYLFVTATLPLEIYN 574
Cdd:cd00268 154 EEDVEKILSALPKDRQTLLFSATLPEEVKE 183
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
374-762 2.96e-40

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 153.94  E-value: 2.96e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  374 KTFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQrlreeELQGHSKSSPGCPR 453
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQ-----HLLDFPRRKSGPPR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  454 VIVLVPTAELASQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILD 533
Cdd:PRK11192  76 ILILTPTRELAMQVADQARELAK-HTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  534 EVDILFgDDEFEAALQNLINSSPVTAQYLFVTATLPleiyNKLVEVFpdcevvmgprVHRVSNALEEFLVDCS------- 606
Cdd:PRK11192 155 EADRML-DMGFAQDIETIAAETRWRKQTLLFSATLE----GDAVQDF----------AERLLNDPVEVEAEPSrrerkki 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  607 ------GDDNaektpetafqNKKTALL-QIMEENPVSKTIIFCNKIETCRKVENIFkrvdrKERQLHVLPFHAALSQESR 679
Cdd:PRK11192 220 hqwyyrADDL----------EHKTALLcHLLKQPEVTRSIVFVRTRERVHELAGWL-----RKAGINCCYLEGEMVQAKR 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  680 LTNMQEFTSSqpEENslFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARgKGKAFIFV-------VGK 752
Cdd:PRK11192 285 NEAIKRLTDG--RVN--VLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGR-KGTAISLVeahdhllLGK 359
                        410
                 ....*....|....*
gi 15231353  753 -----QVGLARRIIE 762
Cdd:PRK11192 360 ieryiEEPLKARVID 374
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
598-749 2.24e-37

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: 136.10  E-value: 2.24e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 598 LEEFLVDCSGDDNaektpetafqnKKTALLQIMEENPVSKTIIFCNKIETCRKVENIFKrvdrkERQLHVLPFHAALSQE 677
Cdd:cd18787   1 IKQLYVVVEEEEK-----------KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLE-----ELGIKVAALHGDLSQE 64
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231353 678 SRLTNMQEFTSSQpeenSLFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARgKGKAFIFV 749
Cdd:cd18787  65 ERERALKKFRSGK----VRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGR-KGTAITFV 131
PTZ00110 PTZ00110
helicase; Provisional
375-761 5.20e-37

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 146.46  E-value: 5.20e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEELQghsksSPG-CPR 453
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLL-----RYGdGPI 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  454 VIVLVPTAELASQVLANCRSISKSGvPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILD 533
Cdd:PTZ00110 206 VLVLAPTRELAEQIREQCNKFGASS-KIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLD 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  534 EVDILFgDDEFEAALQNLINSSPVTAQYLFVTATLPLEIyNKLVEVFPDCEVV---MGP----RVHRVSNalEEFLVdcs 606
Cdd:PTZ00110 285 EADRML-DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEV-QSLARDLCKEEPVhvnVGSldltACHNIKQ--EVFVV--- 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  607 gdDNAEKTpetafQNKKTALLQIMEENPvsKTIIFCnkiETCRKVENIFK--RVDrkerQLHVLPFHAALSQESRLTNMQ 684
Cdd:PTZ00110 358 --EEHEKR-----GKLKMLLQRIMRDGD--KILIFV---ETKKGADFLTKelRLD----GWPALCIHGDKKQEERTWVLN 421
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231353  685 EFTSSQpeenSLFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARgARGKGKAFIFVVGKQVGLARRII 761
Cdd:PTZ00110 422 EFKTGK----SPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGR-AGAKGASYTFLTPDKYRLARDLV 493
PTZ00424 PTZ00424
helicase 45; Provisional
375-760 3.10e-36

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 141.50  E-value: 3.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLreeelqghSKSSPGCpRV 454
Cdd:PTZ00424  29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI--------DYDLNAC-QA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  455 IVLVPTAELASQVLANCRSISKSgVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDE 534
Cdd:PTZ00424 100 LILAPTRELAQQIQKVVLALGDY-LKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  535 VDILFGDDeFEAALQNLINSSPVTAQYLFVTATLPLEIYNKLVEVFPDCEVVMGPRVHRVSNALEEFLVDCSGDDnaekt 614
Cdd:PTZ00424 179 ADEMLSRG-FKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEE----- 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  615 petafqNKKTALLQIMEENPVSKTIIFCNkieTCRKVENIFKRVdrKERQLHVLPFHAALSQESRLTNMQEFTSSqpeeN 694
Cdd:PTZ00424 253 ------WKFDTLCDLYETLTITQAIIYCN---TRRKVDYLTKKM--HERDFTVSCMHGDMDQKDRDLIMREFRSG----S 317
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231353  695 SLFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARgKGKAFIFVVGKQVGLARRI 760
Cdd:PTZ00424 318 TRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGR-KGVAINFVTPDDIEQLKEI 382
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
388-594 3.43e-36

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: 136.34  E-value: 3.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 388 ALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQR-LREEELQGHSKSSpgcPRVIVLVPTAELASQ 466
Cdd:cd17948   4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRlLRYKLLAEGPFNA---PRGLVITPSRELAEQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 467 VLANCRSISKsGVPFRSMVVTGGfRQRTQLENLEQG-VDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDEFE 545
Cdd:cd17948  81 IGSVAQSLTE-GLGLKVKVITGG-RTKRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLL-DDSFN 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231353 546 AALQNLINSSPVT-------------AQYLFVTATLPL---EIYNKLVEVfPDCEVVMGPRVHRV 594
Cdd:cd17948 158 EKLSHFLRRFPLAsrrsentdgldpgTQLVLVSATMPSgvgEVLSKVIDV-DSIETVTSDKLHRL 221
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
372-741 6.25e-36

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 140.88  E-value: 6.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  372 SRKTFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEelQGHSKSSPGC 451
Cdd:PRK04837   6 TEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSH--PAPEDRKVNQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  452 PRVIVLVPTAELASQVLANCRSISKSgVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAI 531
Cdd:PRK04837  84 PRALIMAPTRELAVQIHADAEPLAQA-TGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  532 LDEVDILFgDDEFEAALQNLINSSPVTAQYL--FVTATLPLEIYNKLVEVFPDCE-VVMGPRV---HRVSnalEEfLVDC 605
Cdd:PRK04837 163 LDEADRMF-DLGFIKDIRWLFRRMPPANQRLnmLFSATLSYRVRELAFEHMNNPEyVEVEPEQktgHRIK---EE-LFYP 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  606 SGDDnaektpetafqnkKTALLQ-IMEENPVSKTIIFCNKIETCrkvENIFKRVDRKERQLHVLPfhAALSQESRLTNMQ 684
Cdd:PRK04837 238 SNEE-------------KMRLLQtLIEEEWPDRAIIFANTKHRC---EEIWGHLAADGHRVGLLT--GDVAQKKRLRILE 299
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231353  685 EFTSSQPEenslFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTAR-GARG 741
Cdd:PRK04837 300 EFTRGDLD----ILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRaGASG 353
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
400-574 1.24e-35

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: 132.37  E-value: 1.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353   400 IQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEElqghsksspGCPRVIVLVPTAELASQVLANCRSISKsGV 479
Cdd:pfam00270   3 IQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD---------NGPQALVLAPTRELAEQIYEELKKLGK-GL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353   480 PFRSMVVTGGFRQRTQLENLeQGVDVLIATPGRFTYLMNEGILgLSNLRCAILDEVDiLFGDDEFEAALQNLINSSPVTA 559
Cdd:pfam00270  73 GLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKKR 149
                         170
                  ....*....|....*
gi 15231353   560 QYLFVTATLPLEIYN 574
Cdd:pfam00270 150 QILLLSATLPRNLED 164
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
376-746 3.86e-34

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 136.97  E-value: 3.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  376 FAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEELQghSKSSPGCPRVI 455
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPP--KERYMGEPRAL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  456 VLVPTAELASQVLANCRSISK-SGVPFRSMVvtGGFRQRTQLENLE-QGVDVLIATPGRFTYLMNEGILGLSNLRCAILD 533
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKyTGLNVMTFV--GGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLD 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  534 EVDILFgDDEFEAALQNLINSSPVTA--QYLFVTATLPLEIYNKLVEVFPDCEVVMGPRVHRVSNALEEFLVDCSGDDna 611
Cdd:PRK01297 245 EADRML-DMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD-- 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  612 ektpetafqnKKTALLQIMEENPVSKTIIFCNKIETCRKVENIFKRVDRKERQLHvlpfhAALSQESRLTNMQEFTssqp 691
Cdd:PRK01297 322 ----------KYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLS-----GDVPQHKRIKTLEGFR---- 382
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15231353  692 EENSLFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTAR-GARGKGKAF 746
Cdd:PRK01297 383 EGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRaGASGVSISF 438
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
376-574 3.93e-34

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: 129.34  E-value: 3.93e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 376 FAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEELQghsksspgcPRVI 455
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV---------IQAL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 456 VLVPTAELASQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEV 535
Cdd:cd17940  72 ILVPTRELALQTSQVCKELGK-HMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEA 150
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15231353 536 DILFgDDEFEAALQNLINSSPVTAQYLFVTATLPLEIYN 574
Cdd:cd17940 151 DKLL-SQDFQPIIEKILNFLPKERQILLFSATFPLTVKN 188
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
375-763 4.48e-34

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 136.48  E-value: 4.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEELQGHSKSSpgcPRV 454
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRP---VRA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  455 IVLVPTAELASQVLANCRSISKSgVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDE 534
Cdd:PRK10590  79 LILTPTRELAAQIGENVRDYSKY-LNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  535 VDILFgDDEFEAALQNLINSSPVTAQYLFVTATLPLEI---YNKLVEVFPDCEVVmgpRVHRVSNALEEF--LVDcsgdd 609
Cdd:PRK10590 158 ADRML-DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIkalAEKLLHNPLEIEVA---RRNTASEQVTQHvhFVD----- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  610 naektpetafQNKKTALL-QIMEENPVSKTIIFC-NKIETCRKVENIFKrvdrkeRQLHVLPFHAALSQESRLTNMQEFT 687
Cdd:PRK10590 229 ----------KKRKRELLsQMIGKGNWQQVLVFTrTKHGANHLAEQLNK------DGIRSAAIHGNKSQGARTRALADFK 292
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231353  688 SSQPEenslFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARgKGKAFIFVVGKQVGLARRiIER 763
Cdd:PRK10590 293 SGDIR----VLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAA-TGEALSLVCVDEHKLLRD-IEK 362
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
375-746 4.42e-33

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 135.08  E-value: 4.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEElqGHSKSSPGCPRV 454
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRP--ALADRKPEDPRA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  455 IVLVPTAELASQvlancrsISKSGVPF------RSMVVTGGFRQRTQLENLEQGVDVLIATPGRFT-YLMNEGILGLSNL 527
Cdd:PRK04537  88 LILAPTRELAIQ-------IHKDAVKFgadlglRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIdYVKQHKVVSLHAC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  528 RCAILDEVDILFgDDEFEAALQNLINSSP--VTAQYLFVTATLP-------LEIYNKLVEVFPDCEVVMGPRV-HRVSNA 597
Cdd:PRK04537 161 EICVLDEADRMF-DLGFIKDIRFLLRRMPerGTRQTLLFSATLShrvlelaYEHMNEPEKLVVETETITAARVrQRIYFP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  598 LEEflvdcsgddnaektpetafqNKKTALLQIMEENPVSKTIIFCNkieTCRKVENIFKRVDRKERQLHVLPfhAALSQE 677
Cdd:PRK04537 240 ADE--------------------EKQTLLLGLLSRSEGARTMVFVN---TKAFVERVARTLERHGYRVGVLS--GDVPQK 294
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  678 SRLTNMQEFTSSQPEenslFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTAR-GARGKGKAF 746
Cdd:PRK04537 295 KRESLLNRFQKGQLE----ILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARlGEEGDAISF 360
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
376-568 9.68e-33

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: 125.41  E-value: 9.68e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 376 FAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEelqghskssPGCPRVI 455
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSED---------PYGIFAL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 456 VLVPTAELASQVLANCRSISKSgVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRF-TYLMN--EGILGLSNLRCAIL 532
Cdd:cd17955  72 VLTPTRELAYQIAEQFRALGAP-LGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLaDHLRSsdDTTKVLSRVKFLVL 150
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15231353 533 DEVDILFGDDeFEAALQNLINSSPVTAQYLFVTATL 568
Cdd:cd17955 151 DEADRLLTGS-FEDDLATILSALPPKRQTLLFSATL 185
DEXDc smart00487
DEAD-like helicases superfamily;
389-590 9.70e-33

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 125.68  E-value: 9.70e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353    389 LKEQNFDRPAHIQAMAFSPVIDG-KSCIIADQSGSGKTLAYLVPVIQRLREEelqghsksspGCPRVIVLVPTAELASQV 467
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG----------KGGRVLVLVPTRELAEQW 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353    468 LANCRSISKSgVPFRSMVVTGGFRQRTQLENLEQGV-DVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDEFEA 546
Cdd:smart00487  71 AEELKKLGPS-LGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLL-DGGFGD 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 15231353    547 ALQNLINSSPVTAQYLFVTATLPLEIYNKLVEVFPDCEVVMGPR 590
Cdd:smart00487 149 QLEKLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF 192
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
375-572 1.77e-32

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: 126.62  E-value: 1.77e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEELQGHSKSSPGCPRV 454
Cdd:cd18052  44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQA 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 455 IVLVPTAELASQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDE 534
Cdd:cd18052 124 LIVAPTRELANQIFLEARKFSY-GTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15231353 535 VDILFgDDEFEAALQNLINSSPVTA----QYLFVTATLPLEI 572
Cdd:cd18052 203 ADRML-DMGFGPEIRKLVSEPGMPSkedrQTLMFSATFPEEI 243
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
375-749 2.71e-32

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 132.22  E-value: 2.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEELQGHSKSSPgcPRV 454
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEQRN--PLA 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  455 IVLVPTAELASQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDE 534
Cdd:PLN00206 200 MVLTPTRELCVQVEDQAKVLGK-GLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDE 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  535 VDILFGDDEFEAALQnlINSSPVTAQYLFVTATLPleiynklvevfpdcevvmgPRVHRVSNAL-EEFLVDCSGDDNAek 613
Cdd:PLN00206 279 VDCMLERGFRDQVMQ--IFQALSQPQVLLFSATVS-------------------PEVEKFASSLaKDIILISIGNPNR-- 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  614 tPETAFQ---------NKKTALLQIMEEN-----PVsktIIFCNKietcRKVENIFKRVDRKERQLHVLPFHAALSQESR 679
Cdd:PLN00206 336 -PNKAVKqlaiwvetkQKKQKLFDILKSKqhfkpPA---VVFVSS----RLGADLLANAITVVTGLKALSIHGEKSMKER 407
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231353  680 LTNMQEF-TSSQPeenslFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARgKGKAFIFV 749
Cdd:PLN00206 408 REVMKSFlVGEVP-----VIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGE-KGTAIVFV 472
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
385-572 6.56e-32

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: 122.75  E-value: 6.56e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLreeelqGHSKSSPGCPRVIVLVPTAELA 464
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERL------LYRPKKKAATRVLVLVPTRELA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 465 SQVLANCRSISK-SGVpfRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFT-YLMNEGILGLSNLRCAILDEVDILFgDD 542
Cdd:cd17947  75 MQCFSVLQQLAQfTDI--TFALAVGGLSLKAQEAALRARPDIVIATPGRLIdHLRNSPSFDLDSIEILVLDEADRML-EE 151
                       170       180       190
                ....*....|....*....|....*....|
gi 15231353 543 EFEAALQNLINSSPVTAQYLFVTATLPLEI 572
Cdd:cd17947 152 GFADELKEILRLCPRTRQTMLFSATMTDEV 181
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
416-593 9.63e-32

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: 124.41  E-value: 9.63e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 416 IADQSGSGKTLAYLVPVIQRLREEELQ--------GHSKSSPGCPRVIVLVPTAELASQVLANCRSISKSgVPFRSMVVT 487
Cdd:cd17965  66 LAAETGSGKTLAYLAPLLDYLKRQEQEpfeeaeeeYESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHT-VKLGIKTFS 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 488 GGFRQRTQ--LENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDEFEAALQNLINSSPVTAQYLFVT 565
Cdd:cd17965 145 SGFGPSYQrlQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLF-DRSFLQDTTSIIKRAPKLKHLILCS 223
                       170       180
                ....*....|....*....|....*...
gi 15231353 566 ATLPLEIYNKLVEVFPDCEVVMGPRVHR 593
Cdd:cd17965 224 ATIPKEFDKTLRKLFPDVVRIATPRLHA 251
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
375-572 1.34e-31

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: 122.98  E-value: 1.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAfSPVIDGKSCIIA-DQSGSGKTLAYLVPVIQR-LREEELQGHSKSSPGCP 452
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYA-IPIILAGRDLMAcAQTGSGKTAAFLLPIISKlLEDGPPSVGRGRRKAYP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 453 RVIVLVPTAELASQVLANCRSISK-SGVpfRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAI 531
Cdd:cd17967  80 SALILAPTRELAIQIYEEARKFSYrSGV--RSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLV 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15231353 532 LDEVD-ILfgDDEFEAALQNLINSSPVTA----QYLFVTATLPLEI 572
Cdd:cd17967 158 LDEADrML--DMGFEPQIRKIVEHPDMPPkgerQTLMFSATFPREI 201
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
375-776 1.53e-31

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 131.12  E-value: 1.53e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLrEEELQGhsksspgcPRV 454
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL-DPELKA--------PQI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  455 IVLVPTAELASQVLANCRSISKSGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDE 534
Cdd:PRK11634  78 LVLAPTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  535 VDIL----FGDDefeaaLQNLINSSPVTAQYLFVTATLPlEIYNKLVEVFpdcevVMGPRVHRVSNALeeflvdCSGDDN 610
Cdd:PRK11634 158 ADEMlrmgFIED-----VETIMAQIPEGHQTALFSATMP-EAIRRITRRF-----MKEPQEVRIQSSV------TTRPDI 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  611 AEKTPETAFQNKKTALLQIMEENPVSKTIIFCNKIETCRKVENIFKRVDRKErqlhvlpfhAALSQESRLTnMQEFTSSQ 690
Cdd:PRK11634 221 SQSYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNS---------AALNGDMNQA-LREQTLER 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  691 PEENSL-FLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARGkGKAFIFVVGKQVGLARRiIERNEK-GH 768
Cdd:PRK11634 291 LKDGRLdILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRA-GRALLFVENRERRLLRN-IERTMKlTI 368

                 ....*...
gi 15231353  769 PVHDVPNA 776
Cdd:PRK11634 369 PEVELPNA 376
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
375-578 2.50e-30

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: 118.56  E-value: 2.50e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRlreeeLQGHSKSSpGCpRV 454
Cdd:cd17959   2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEK-----LKAHSPTV-GA-RA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 455 IVLVPTAELASQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDE 534
Cdd:cd17959  75 LILSPTRELALQTLKVTKELGK-FTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDE 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15231353 535 VDILFGDDeFEAALQNLINSSPVTAQYLFVTATLPleiyNKLVE 578
Cdd:cd17959 154 ADRLFEMG-FAEQLHEILSRLPENRQTLLFSATLP----KLLVE 192
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
385-569 2.78e-30

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: 118.34  E-value: 2.78e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLreeELQGHSKSSPGCPRVIVLVPTAELA 464
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL---DLQPIPREQRNGPGVLVLTPTRELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 465 SQVLANCRSISKSGvpFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDEF 544
Cdd:cd17958  78 LQIEAECSKYSYKG--LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRML-DMGF 154
                       170       180
                ....*....|....*....|....*
gi 15231353 545 EAALQNLINSSPVTAQYLFVTATLP 569
Cdd:cd17958 155 EPQIRKILLDIRPDRQTIMTSATWP 179
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
385-576 1.04e-29

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: 117.73  E-value: 1.04e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQNFDRPAHIQAMAFSP-VIDGKSCIIADQSGSGKTLAYLVPVIQR-LREEELQGHSKSSPGcPRVIVLVPTAE 462
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERlLSQKSSNGVGGKQKP-LRALILTPTRE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 463 LASQVLANCRSISKSGvPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNL---RCAILDEVDILF 539
Cdd:cd17946  80 LAVQVKDHLKAIAKYT-NIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLkslRFLVLDEADRML 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15231353 540 GD---DEFEAALqNLINSSPVTA----QYLFVTATLPLEIYNKL 576
Cdd:cd17946 159 EKghfAELEKIL-ELLNKDRAGKkrkrQTFVFSATLTLDHQLPL 201
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
386-572 3.19e-29

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: 115.76  E-value: 3.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 386 MKALKEQNFDRPAHIQAMAFSPVI-DGKSCIIADQSGSGKTLAYLVPVIQRLreeeLQGHSKSSPGCPRVIVLVPTAELA 464
Cdd:cd17964   6 LKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSL----LNTKPAGRRSGVSALIISPTRELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 465 SQVLANCRSISKSGVPFRSMVVTGGFRQRTQLENLE-QGVDVLIATPGRFT-YLMNEGILG-LSNLRCAILDEVDILFgD 541
Cdd:cd17964  82 LQIAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIdHLENPGVAKaFTDLDYLVLDEADRLL-D 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15231353 542 DEFEAALQNLI----NSSPVTAQYLFVTATLPLEI 572
Cdd:cd17964 161 MGFRPDLEQILrhlpEKNADPRQTLLFSATVPDEV 195
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
386-572 7.94e-29

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: 114.22  E-value: 7.94e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 386 MKALKEQNFDRPAHIQaMAFSPVI-DGKSCIIADQSGSGKTLAYLVPVIQRLREeelqghSKSSPGcPRVIVLVPTAELA 464
Cdd:cd17957   2 LNNLEESGYREPTPIQ-MQAIPILlHGRDLLACAPTGSGKTLAFLIPILQKLGK------PRKKKG-LRALILAPTRELA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 465 SQVLANCRSISKsGVPFRSMVVTGGFR-QRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDE 543
Cdd:cd17957  74 SQIYRELLKLSK-GTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLF-EPG 151
                       170       180       190
                ....*....|....*....|....*....|.
gi 15231353 544 FEAALQNLIN--SSPVTaQYLFVTATLPLEI 572
Cdd:cd17957 152 FREQTDEILAacTNPNL-QRSLFSATIPSEV 181
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
372-760 1.32e-28

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 119.91  E-value: 1.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  372 SRKTFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLreeelqghsksSPGC 451
Cdd:PRK11776   2 SMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-----------DVKR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  452 PRV--IVLVPTAELASQVLANCRSISksgvpfRSM----VVT--GGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILG 523
Cdd:PRK11776  71 FRVqaLVLCPTRELADQVAKEIRRLA------RFIpnikVLTlcGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  524 LSNLRCAILDEVD-ILfgDDEFEAALQNLINSSPVTAQYLFVTATLPLEIyNKLVEvfpdcevvmgprvhRVSNALEEFL 602
Cdd:PRK11776 145 LDALNTLVLDEADrML--DMGFQDAIDAIIRQAPARRQTLLFSATYPEGI-AAISQ--------------RFQRDPVEVK 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  603 VDCSGDDNA------EKTPetafqNKKTALLQIM--EENPVSkTIIFCNKIETCRKVenifkrVDR-KERQLHVLPFHAA 673
Cdd:PRK11776 208 VESTHDLPAieqrfyEVSP-----DERLPALQRLllHHQPES-CVVFCNTKKECQEV------ADAlNAQGFSALALHGD 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  674 LSQESRLTNMQEF---TSSqpeenslFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARgARGKGKAFIFVV 750
Cdd:PRK11776 276 LEQRDRDQVLVRFanrSCS-------VLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGR-AGSKGLALSLVA 347
                        410
                 ....*....|
gi 15231353  751 GKQVGLARRI 760
Cdd:PRK11776 348 PEEMQRANAI 357
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
386-567 2.10e-27

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: 110.14  E-value: 2.10e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 386 MKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLReeELQGHSKSSPGCprvIVLVPTAELAS 465
Cdd:cd17942   2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLY--KLKFKPRNGTGV---IIISPTRELAL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 466 QVLANCRSISKSGVPFRSMVVtGGFRQRTQLENLEQGVDVLIATPGR-FTYLMNEGILGLSNLRCAILDEVD-ILfgDDE 543
Cdd:cd17942  77 QIYGVAKELLKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRlLDHLQNTKGFLYKNLQCLIIDEADrIL--EIG 153
                       170       180
                ....*....|....*....|....
gi 15231353 544 FEAALQNLINSSPVTAQYLFVTAT 567
Cdd:cd17942 154 FEEEMRQIIKLLPKRRQTMLFSAT 177
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
374-569 3.92e-27

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: 110.16  E-value: 3.92e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 374 KTFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPViqrLREEELQGHSKSSPGcPR 453
Cdd:cd17953  12 QKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPM---FRHIKDQRPVKPGEG-PI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 454 VIVLVPTAELASQVLANCRSISKSgVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYL--MNEG-ILGLSNLRCA 530
Cdd:cd17953  88 GLIMAPTRELALQIYVECKKFSKA-LGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDIltANNGrVTNLRRVTYV 166
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15231353 531 ILDEVDILFgDDEFEAALQNLINSSPVTAQYLFVTATLP 569
Cdd:cd17953 167 VLDEADRMF-DMGFEPQIMKIVNNIRPDRQTVLFSATFP 204
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
385-572 1.01e-26

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: 108.23  E-value: 1.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREeelQGHSKSSPGcPRVIVLVPTAELA 464
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINA---QPPLERGDG-PIVLVLAPTRELA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 465 SQVLANCRSISKSGvPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDEF 544
Cdd:cd17966  77 QQIQQEANKFGGSS-RLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRML-DMGF 154
                       170       180
                ....*....|....*....|....*...
gi 15231353 545 EAALQNLINSSPVTAQYLFVTATLPLEI 572
Cdd:cd17966 155 EPQIRKIVDQIRPDRQTLMWSATWPKEV 182
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
389-572 1.71e-26

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: 107.25  E-value: 1.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 389 LKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEelqghSKSspgcPRVIVLVPTAELASQVL 468
Cdd:cd17962   5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTE-----HRN----PSALILTPTRELAVQIE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 469 ANCRSISKSGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDEFEAAL 548
Cdd:cd17962  76 DQAKELMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTML-KMGFQQQV 154
                       170       180
                ....*....|....*....|....
gi 15231353 549 QNLINSSPVTAQYLFVTATLPLEI 572
Cdd:cd17962 155 LDILENISHDHQTILVSATIPRGI 178
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
375-572 1.78e-25

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: 105.89  E-value: 1.78e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFsPVIDGKSCIIA-DQSGSGKTLAYLVPVIQRLREeelQGHSKSSPGC-- 451
Cdd:cd18051  22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAI-PIIKSKRDLMAcAQTGSGKTAAFLLPILSQIYE---QGPGESLPSEsg 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 452 --------PRVIVLVPTAELASQVLANCRSIS-KSGVpfRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGIL 522
Cdd:cd18051  98 yygrrkqyPLALVLAPTRELASQIYDEARKFAyRSRV--RPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKI 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15231353 523 GLSNLRCAILDEVDILFgDDEFEAALQNLI--NSSPVTA--QYLFVTATLPLEI 572
Cdd:cd18051 176 GLDYCKYLVLDEADRML-DMGFEPQIRRIVeqDTMPPTGerQTLMFSATFPKEI 228
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
376-580 1.85e-25

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: 105.48  E-value: 1.85e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 376 FAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEELQGHSKSspgcPRVI 455
Cdd:cd18049  26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDG----PICL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 456 VLVPTAELASQVLANCRSISKSgVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEV 535
Cdd:cd18049 102 VLAPTRELAQQVQQVAAEYGRA-CRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEA 180
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15231353 536 DILFgDDEFEAALQNLINSSPVTAQYLFVTATLPLEIyNKLVEVF 580
Cdd:cd18049 181 DRML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEV-RQLAEDF 223
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
385-569 2.46e-25

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: 104.59  E-value: 2.46e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQ-NFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLreEELQGHSKSSPGCpRVIVLVPTAEL 463
Cdd:cd17949   1 LVSHLKSKmGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL--LSLEPRVDRSDGT-LALVLVPTREL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 464 ASQVLANCRSISKsgvPFRSMV---VTGGFRQRTQLENLEQGVDVLIATPGRFTY-LMNEGILGLSNLRCAILDEVDIL- 538
Cdd:cd17949  78 ALQIYEVLEKLLK---PFHWIVpgyLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLl 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15231353 539 ---FGDD--------EFEAALQNLINSSPVTAQYLFVTATLP 569
Cdd:cd17949 155 dmgFEKDitkilellDDKRSKAGGEKSKPSRRQTVLVSATLT 196
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
400-574 3.35e-25

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: 103.77  E-value: 3.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 400 IQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLrEEELQGHSKSSPgcPRVIVLVPTAELASQVLANCRSISksgv 479
Cdd:cd17944  16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKL-QEDQQPRKRGRA--PKVLVLAPTRELANQVTKDFKDIT---- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 480 pfRSMVVT---GGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDEFEAALQNLIN--- 553
Cdd:cd17944  89 --RKLSVAcfyGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQML-DMGFAEQVEEILSvsy 165
                       170       180
                ....*....|....*....|...
gi 15231353 554 --SSPVTAQYLFVTATLPLEIYN 574
Cdd:cd17944 166 kkDSEDNPQTLLFSATCPDWVYN 188
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
375-568 8.65e-25

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: 102.78  E-value: 8.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 375 TFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREeelqghsksSPGCPRV 454
Cdd:cd17954   1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLE---------NPQRFFA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 455 IVLVPTAELASQVLANCRSISkSGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTY-LMNEGILGLSNLRCAILD 533
Cdd:cd17954  72 LVLAPTRELAQQISEQFEALG-SSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMD 150
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15231353 534 EVDILFgDDEFEAALQNLINSSPVTAQ-YLFvTATL 568
Cdd:cd17954 151 EADRLL-NMDFEPEIDKILKVIPRERTtYLF-SATM 184
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
376-568 8.93e-25

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: 102.78  E-value: 8.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 376 FAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLReeelqghsksspgcprVI 455
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV----------------AL 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 456 VLVPTAELASQVLANCRSISK--SGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILD 533
Cdd:cd17938  65 ILEPSRELAEQTYNCIENFKKylDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15231353 534 EVDILFGDDEfEAALQNLINSSPVTA------QYLFVTATL 568
Cdd:cd17938 145 EADRLLSQGN-LETINRIYNRIPKITsdgkrlQVIVCSATL 184
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
385-572 1.57e-24

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: 101.72  E-value: 1.57e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREE-ELQGHSKsspgcPRVIVLVPTAEL 463
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQrELEKGEG-----PIAVIVAPTREL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 464 ASQVLANCRSISKSgVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDE 543
Cdd:cd17952  76 AQQIYLEAKKFGKA-YNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMF-DMG 153
                       170       180
                ....*....|....*....|....*....
gi 15231353 544 FEAALQNLINSSPVTAQYLFVTATLPLEI 572
Cdd:cd17952 154 FEYQVRSIVGHVRPDRQTLLFSATFKKKI 182
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
378-572 2.37e-24

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: 101.25  E-value: 2.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 378 EIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRL--REEELQghsksspgcprVI 455
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdtTVRETQ-----------AL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 456 VLVPTAELASQVLANCRSI-SKSGVpfRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDE 534
Cdd:cd17939  70 VLAPTRELAQQIQKVVKALgDYMGV--KVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDE 147
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15231353 535 VDILFgDDEFEAALQNLINSSPVTAQYLFVTATLPLEI 572
Cdd:cd17939 148 ADEML-SRGFKDQIYDIFQFLPPETQVVLFSATMPHEV 184
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
385-574 5.23e-24

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: 100.49  E-value: 5.23e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEElqghsKSSPGC----PRVIVLVPT 460
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQE-----KKLPFIkgegPYGLIVCPS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 461 AELASQ----VLANCRSISKSGVP-FRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEV 535
Cdd:cd17951  76 RELARQthevIEYYCKALQEGGYPqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEA 155
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15231353 536 DILFgDDEFEAALQNLINSSPVTAQYLFVTATLPLEIYN 574
Cdd:cd17951 156 DRMI-DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQN 193
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
387-568 5.44e-24

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: 100.35  E-value: 5.44e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 387 KALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEELqghSKSSPGCPRVIVLVPTAELASQ 466
Cdd:cd17961   7 KAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKA---ESGEEQGTRALILVPTRELAQQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 467 VLANCRSISKSGVPFRSMVVTGGF----RQRTQLENLEqgvDVLIATPGRFTYLMNEGILGL-SNLRCAILDEVDIL--F 539
Cdd:cd17961  84 VSKVLEQLTAYCRKDVRVVNLSASssdsVQRALLAEKP---DIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVlsY 160
                       170       180
                ....*....|....*....|....*....
gi 15231353 540 GddeFEAALQNLINSSPVTAQYLFVTATL 568
Cdd:cd17961 161 G---YEEDLKSLLSYLPKNYQTFLMSATL 186
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
386-576 5.79e-24

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: 100.03  E-value: 5.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 386 MKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEELQghsksspgcPRVIVLVPTAELAS 465
Cdd:cd17943   2 LEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRH---------PQVLILAPTREIAV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 466 QVLANCRSISKSGVPFRSMVVTGGfrqRTQLENLEQ--GVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDE 543
Cdd:cd17943  73 QIHDVFKKIGKKLEGLKCEVFIGG---TPVKEDKKKlkGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLM-EGS 148
                       170       180       190
                ....*....|....*....|....*....|...
gi 15231353 544 FEAALQNLINSSPVTAQYLFVTATLPLEIYNKL 576
Cdd:cd17943 149 FQKDVNWIFSSLPKNKQVIAFSATYPKNLDNLL 181
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
385-580 2.59e-23

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: 100.47  E-value: 2.59e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREeelQGHSKSSPGcPRVIVLVPTAELA 464
Cdd:cd18050  73 VMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINH---QPYLERGDG-PICLVLAPTRELA 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 465 SQVLANCRSISKSGvPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDEF 544
Cdd:cd18050 149 QQVQQVADDYGKSS-RLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML-DMGF 226
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15231353 545 EAALQNLINSSPVTAQYLFVTATLPLEIyNKLVEVF 580
Cdd:cd18050 227 EPQIRKIVDQIRPDRQTLMWSATWPKEV-RQLAEDF 261
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
621-737 2.99e-23

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: 94.97  E-value: 2.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353   621 NKKTALLQIMEENPVSKTIIFCNKIETCrKVENIFKRvdrkeRQLHVLPFHAALSQESRLTNMQEFtssqPEENSLFLVC 700
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTL-EAELLLEK-----EGIKVARLHGDLSQEEREEILEDF----RKGKIDVLVA 70
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15231353   701 TDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTAR 737
Cdd:pfam00271  71 TDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGR 107
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
387-567 2.15e-22

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: 95.43  E-value: 2.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 387 KALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRL---REEELQGhskssPGCprvIVLVPTAEL 463
Cdd:cd17941   3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyreRWTPEDG-----LGA---LIISPTREL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 464 ASQVLANCRSISKSGVpFRSMVVTGGFRQRTQLENLEQgVDVLIATPGRFTYLMNEGI-LGLSNLRCAILDEVDILFgDD 542
Cdd:cd17941  75 AMQIFEVLRKVGKYHS-FSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRIL-DM 151
                       170       180
                ....*....|....*....|....*
gi 15231353 543 EFEAALQNLINSSPVTAQYLFVTAT 567
Cdd:cd17941 152 GFKETLDAIVENLPKSRQTLLFSAT 176
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
376-572 4.72e-22

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: 94.84  E-value: 4.72e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 376 FAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQ----RLREeelqghsksspgc 451
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQcldiQVRE------------- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 452 PRVIVLVPTAELASQVLANCRSISK-SGVPFRSMVvtGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCA 530
Cdd:cd18045  68 TQALILSPTRELAVQIQKVLLALGDyMNVQCHACI--GGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKML 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15231353 531 ILDEVDILFGdDEFEAALQNLINSSPVTAQYLFVTATLPLEI 572
Cdd:cd18045 146 VLDEADEMLN-KGFKEQIYDVYRYLPPATQVVLVSATLPQDI 186
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
385-560 1.42e-21

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: 93.92  E-value: 1.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQNFDRPAHIQAMAFSPVIDGKSCI-IAdQSGSGKTLAYLVPVIQRLREEELQGHSKSSPGcPRVIVLVPTAEL 463
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIgIA-ETGSGKTAAFLIPLLVYISRLPPLDEETKDDG-PYALILAPTREL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 464 ASQVLANCRSISKsGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDILFgDDE 543
Cdd:cd17945  79 AQQIEEETQKFAK-PLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMI-DMG 156
                       170
                ....*....|....*..
gi 15231353 544 FEAALQNLINSSPVTAQ 560
Cdd:cd17945 157 FEPQVTKILDAMPVSNK 173
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
386-556 3.23e-21

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: 92.25  E-value: 3.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 386 MKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLreeeLQGHSKSSPGCPRVIVLVPTAELAS 465
Cdd:cd17960   2 LDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEIL----LKRKANLKKGQVGALIISPTRELAT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 466 QVLANCRSISKSGVP-FRSMVVTGGFRQRTQLENL-EQGVDVLIATPGRFTYL--MNEGILGLSNLRCAILDEVDILFgD 541
Cdd:cd17960  78 QIYEVLQSFLEHHLPkLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLL-D 156
                       170
                ....*....|....*
gi 15231353 542 DEFEAALQNLINSSP 556
Cdd:cd17960 157 LGFEADLNRILSKLP 171
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
376-572 1.45e-20

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: 90.58  E-value: 1.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 376 FAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLrEEELQGhsksspgcPRVI 455
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI-DTSLKA--------TQAL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 456 VLVPTAELASQVLancRSISKSG--VPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILD 533
Cdd:cd18046  72 VLAPTRELAQQIQ---KVVMALGdyMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLD 148
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15231353 534 EVDILFGDDeFEAALQNLINSSPVTAQYLFVTATLPLEI 572
Cdd:cd18046 149 EADEMLSRG-FKDQIYDIFQKLPPDTQVVLLSATMPNDV 186
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
385-568 6.70e-19

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: 86.53  E-value: 6.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 385 MMKALKEQNFDRPAHIQA----------MAFSPVIDGKSCIIAdQSGSGKTLAYLVPVIQRLReeelqghSKSSPgCPRV 454
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAavipwllpssKSTPPYRPGDLCVSA-PTGSGKTLAYVLPIVQALS-------KRVVP-RLRA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 455 IVLVPTAELASQVLANCRSISKsGVPFRSMVVTGG--FRQRTQLE------NLEQGVDVLIATPGRftyLM-----NEGI 521
Cdd:cd17956  72 LIVVPTKELVQQVYKVFESLCK-GTGLKVVSLSGQksFKKEQKLLlvdtsgRYLSRVDILVATPGR---LVdhlnsTPGF 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231353 522 LgLSNLRCAILDEVDILFG-------------------DDEFEAALQNLINSSPVTAQYLFVTATL 568
Cdd:cd17956 148 T-LKHLRFLVIDEADRLLNqsfqdwletvmkalgrptaPDLGSFGDANLLERSVRPLQKLLFSATL 212
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
382-587 8.29e-19

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: 85.32  E-value: 8.29e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 382 SEDMMKALKEQNFDRPAHIQAMAFsPVI--DGKSCIIAD-QSGSGKTLAYLVPVIQRLREEELqghsksspgCPRVIVLV 458
Cdd:cd17963   2 KPELLKGLYAMGFNKPSKIQETAL-PLIlsDPPENLIAQsQSGTGKTAAFVLAMLSRVDPTLK---------SPQALCLA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 459 PTAELASQVLANCRSISKsgvpFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDIL 538
Cdd:cd17963  72 PTRELARQIGEVVEKMGK----FTGVKVALAVPGNDVPRGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVM 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15231353 539 FGDDEFEAALQNLINSSPVTAQYLFVTATLPLEIYNKLVEVFPDCEVVM 587
Cdd:cd17963 148 LDTQGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
411-567 1.96e-17

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: 79.75  E-value: 1.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 411 GKSCIIADQSGSGKTLAYLVPVIQRLREEElqghsksspgcPRVIVLVPTAELASQVLANCRSISKSGVPFRsmVVTGGF 490
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLKKG-----------KKVLVLVPTKALALQTAERLRELFGPGIRVA--VLVGGS 67
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231353 491 RQRTQLENLEQGVDVLIATPGRF-TYLMNEGILGLSNLRCAILDEVD-ILFGDDEFEAALQNLINSSPVTAQYLFVTAT 567
Cdd:cd00046  68 SAEEREKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHaLLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
HELICc smart00490
helicase superfamily c-terminal domain;
661-737 2.17e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 77.25  E-value: 2.17e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231353    661 KERQLHVLPFHAALSQESRLTNMQEFtssqPEENSLFLVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTAR 737
Cdd:smart00490   8 KELGIKVARLHGGLSQEEREEILDKF----NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
376-572 3.50e-17

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: 80.85  E-value: 3.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 376 FAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLreeelqghsKSSPGCPRVI 455
Cdd:cd17950   4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL---------EPVDGQVSVL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 456 VLVPTAELASQVLANCRSISKSGVPFRSMVVTGGFRQRTQLENLEQGV-DVLIATPGRFTYLMNEGILGLSNLRCAILDE 534
Cdd:cd17950  75 VICHTRELAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDE 154
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15231353 535 VDILFGDDEFEAALQNLINSSPVTAQYLFVTATLPLEI 572
Cdd:cd17950 155 CDKMLEQLDMRRDVQEIFRATPHDKQVMMFSATLSKEI 192
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
370-586 1.35e-15

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: 76.98  E-value: 1.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 370 FFSRKTFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVI-DGKSCIIA-DQSGSGKTLAYLVPVIQRLREEELQghsks 447
Cdd:cd18048  14 LFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLaDPPQNLIAqSQSGTGKTAAFVLAMLSRVDALKLY----- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 448 spgcPRVIVLVPTAELASQVLANCRSISKSGVPFRSMVVTGGFR--QRTQLEnleqgVDVLIATPGR-FTYLMNEGILGL 524
Cdd:cd18048  89 ----PQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRpgKGTDIE-----AQIVIGTPGTvLDWCFKLRLIDV 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231353 525 SNLRCAILDEVDILFGDDEFEAALQNLINSSPVTAQYLFVTATLPLEIYNKLVEVFPDCEVV 586
Cdd:cd18048 160 TNISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNII 221
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
387-750 1.80e-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: 71.02  E-value: 1.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 387 KALKEQNFDRP-AHiQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEelqghskssPGCpRVIVLVPTAELAS 465
Cdd:COG1205  47 AALKKRGIERLySH-QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED---------PGA-TALYLYPTKALAR 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 466 QVLANCRS-ISKSGVPFRSMVVTGG--FRQRTQLenLEQGvDVLIATPgrftYLMNEGILG--------LSNLRCAILDE 534
Cdd:COG1205 116 DQLRRLRElAEALGLGVRVATYDGDtpPEERRWI--REHP-DIVLTNP----DMLHYGLLPhhtrwarfFRNLRYVVIDE 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 535 VDI---LFGddefeAALQNLI----------NSSPvtaQYLFVTATL--PLEIYNKLVEVfpDCEVV------MGPRVHr 593
Cdd:COG1205 189 AHTyrgVFG-----SHVANVLrrlrricrhyGSDP---QFILASATIgnPAEHAERLTGR--PVTVVdedgspRGERTF- 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 594 vsnaleeFLVDCSGDDNAEKTPETAFqnkkTALL--QIMEENpvSKTIIFCNKIetcRKVENIFKRVDRKERQ----LHV 667
Cdd:COG1205 258 -------VLWNPPLVDDGIRRSALAE----AARLlaDLVREG--LRTLVFTRSR---RGAELLARYARRALREpdlaDRV 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 668 LPFHAALSQESRltnmQEFtssqpeENSLF------LVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARG 741
Cdd:COG1205 322 AAYRAGYLPEER----REI------ERGLRsgellgVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQD 391

                ....*....
gi 15231353 742 kgkAFIFVV 750
Cdd:COG1205 392 ---SLVVLV 397
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
421-763 3.97e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 69.67  E-value: 3.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 421 GSGKTLAYLVpVIQRLREeelqghsksspgCPRVIVLVPTAELASQVLANCRSIsksgvpFRSMVVTGGFRQRTQlenle 500
Cdd:COG1061 110 GTGKTVLALA-LAAELLR------------GKRVLVLVPRRELLEQWAEELRRF------LGDPLAGGGKKDSDA----- 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 501 qgvDVLIATPGRFTYLMNEGILGlSNLRCAILDEVDiLFGDDEFEAALQNLinsspvTAQYLF-VTAT--------LPLE 571
Cdd:COG1061 166 ---PITVATYQSLARRAHLDELG-DRFGLVIIDEAH-HAGAPSYRRILEAF------PAAYRLgLTATpfrsdgreILLF 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 572 IYNKLVEVFP-----DCEVVMGPRVHRVSNALEEFLVDcsgDDNAEKTPETAF----QNKKTALLQIMEENP-VSKTIIF 641
Cdd:COG1061 235 LFDGIVYEYSlkeaiEDGYLAPPEYYGIRVDLTDERAE---YDALSERLREALaadaERKDKILRELLREHPdDRKTLVF 311
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 642 CNKIETCRKVENIFkrvdrKERQLHVLPFHAALSQESRLTNMQEFTSSQPEenslFLVCTDRASRGIDFSGVDHVVLFDF 721
Cdd:COG1061 312 CSSVDHAEALAELL-----NEAGIRAAVVTGDTPKKEREEILEAFRDGELR----ILVTVDVLNEGVDVPRLDVAILLRP 382
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 15231353 722 PRDPSEYVRRVGRTARGARGKGKAFIF-VVGKQVGLARRIIER 763
Cdd:COG1061 383 TGSPREFIQRLGRGLRPAPGKEDALVYdFVGNDVPVLEELAKD 425
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
635-749 2.30e-10

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: 57.33  E-value: 2.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 635 VSKTIIFCNKIETCRKVENIFKrvdrkerqlhvlpfhaalsqesrltnmqeftssqpeenslFLVCTDRASRGIDFSGVD 714
Cdd:cd18785   3 VVKIIVFTNSIEHAEEIASSLE----------------------------------------ILVATNVLGEGIDVPSLD 42
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15231353 715 HVVLFDFPRDPSEYVRRVGRTARGARGKGKAFIFV 749
Cdd:cd18785  43 TVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
399-569 7.25e-10

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 58.81  E-value: 7.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 399 HIQAMAFSPVID-GKSCIIADQSGSGKTL-AYLVpVIQRLREEElqghsksspgcPRVIVLVPTAELASQVLANCRSISK 476
Cdd:cd17921   4 PIQREALRALYLsGDSVLVSAPTSSGKTLiAELA-ILRALATSG-----------GKAVYIAPTRALVNQKEADLRERFG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 477 SGvPFRSMVVTGGFrqrTQLENLEQGVDVLIATPGRF-TYLMNEGILGLSNLRCAILDEVDILfGDDE----FEAALQNL 551
Cdd:cd17921  72 PL-GKNVGLLTGDP---SVNKLLLAEADILVATPEKLdLLLRNGGERLIQDVRLVVVDEAHLI-GDGErgvvLELLLSRL 146
                       170
                ....*....|....*...
gi 15231353 552 INSSPvTAQYLFVTATLP 569
Cdd:cd17921 147 LRINK-NARFVGLSATLP 163
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
374-586 2.50e-09

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: 57.81  E-value: 2.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 374 KTFAEIGCSEDMMKALKEQNFDRPAHIQAMAFSPVI--DGKSCIIADQSGSGKTLAYLVPVIqrlreeelqghSKSSPGC 451
Cdd:cd18047   1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLAML-----------SQVEPAN 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 452 --PRVIVLVPTAELAsqvLANCRSISKSGVPFRSMVVTGGFRQrtqlENLEQGV----DVLIATPGR-FTYLMNEGILGL 524
Cdd:cd18047  70 kyPQCLCLSPTYELA---LQTGKVIEQMGKFYPELKLAYAVRG----NKLERGQkiseQIVIGTPGTvLDWCSKLKFIDP 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231353 525 SNLRCAILDEVDILF---GDDEFEAALQNLInssPVTAQYLFVTATLPLEIYNKLVEVFPDCEVV 586
Cdd:cd18047 143 KKIKVFVLDEADVMIatqGHQDQSIRIQRML---PRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
401-658 3.82e-08

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 56.83  E-value: 3.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 401 QAMAF-SPVIDGKSCIIADQSGSGKTL-AYLvPVIQRLREEelqghsksspgcPRVIVLVPTAELASQVLANCRS-ISKS 477
Cdd:COG1204  27 QAEALeAGLLEGKNLVVSAPTASGKTLiAEL-AILKALLNG------------GKALYIVPLRALASEKYREFKRdFEEL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 478 GVpfRSMVVTGGFRQRTqlENLEQgVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDiLFGDDE----FEAALQNLIN 553
Cdd:COG1204  94 GI--KVGVSTGDYDSDD--EWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAH-LIDDESrgptLEVLLARLRR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 554 SSPvTAQYLFVTATLPleiyNklVEVFP---DCEVVmgpRVHRVSNALEEFLVdcsgDDNAEKTPETAFQNKKTAL---L 627
Cdd:COG1204 168 LNP-EAQIVALSATIG----N--AEEIAewlDAELV---KSDWRPVPLNEGVL----YDGVLRFDDGSRRSKDPTLalaL 233
                       250       260       270
                ....*....|....*....|....*....|.
gi 15231353 628 QIMEENpvSKTIIFCNKIetcRKVENIFKRV 658
Cdd:COG1204 234 DLLEEG--GQVLVFVSSR---RDAESLAKKL 259
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
622-726 1.41e-07

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: 50.94  E-value: 1.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 622 KKTALLQIMEE--NPVSKTIIFCNKIETCRKVENIFKrvdrkERQLHVLPFHAALSQESRLTNMQEFtsSQPEENSLFLV 699
Cdd:cd18793  12 KLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALR-----ERGIKYLRLDGSTSSKERQKLVDRF--NEDPDIRVFLL 84
                        90       100
                ....*....|....*....|....*..
gi 15231353 700 CTDRASRGIDFSGVDHVVLFDFPRDPS 726
Cdd:cd18793  85 STKAGGVGLNLTAANRVILYDPWWNPA 111
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
401-534 8.70e-07

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: 50.12  E-value: 8.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 401 QAMAFSPVIDGKSCIIADQSGSGKTLAYLVpviqrLREEELQGHSKSSPGcpRVIVLVPTAELASQVLANCRSISKSgVP 480
Cdd:cd17927   7 QLELAQPALKGKNTIICLPTGSGKTFVAVL-----ICEHHLKKFPAGRKG--KVVFLANKVPLVEQQKEVFRKHFER-PG 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15231353 481 FRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEGIL-GLSNLRCAILDE 534
Cdd:cd17927  79 YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDE 133
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
398-534 9.45e-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: 49.89  E-value: 9.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 398 AHiQAMAFSPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEelqghskssPGcPRVIVLVPTAELASQVLANCRS-ISK 476
Cdd:cd17923   3 SH-QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD---------PG-SRALYLYPTKALAQDQLRSLRElLEQ 71
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231353 477 SGVPFRSMVVTGGFRQRTQLENLEQGVDVLIATPGRFTYLM----NEGILGLSNLRCAILDE 534
Cdd:cd17923  72 LGLGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDE 133
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
421-535 4.46e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 48.03  E-value: 4.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 421 GSGKTL-AYLVpviqrLREEELQGHSKSSPGCpRVIVLVPTAELASQvlaNCRSIsKSGVPFRSMVVTGG-----FRQRT 494
Cdd:cd18034  26 GSGKTLiAVML-----IKEMGELNRKEKNPKK-RAVFLVPTVPLVAQ---QAEAI-RSHTDLKVGEYSGEmgvdkWTKER 95
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15231353 495 QLENLEQgVDVLIATPGRFTYLMNEGILGLSNLRCAILDEV 535
Cdd:cd18034  96 WKEELEK-YDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
411-571 2.19e-05

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: 45.65  E-value: 2.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 411 GKSCIIADQSGSGKTLAYLVPVIQRLREEELQGhsksspgcPRVIVLVPTAELASQVLANCRSISKSGVPFRSMVV-TG- 488
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKG--------VQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVrHGd 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 489 ---GFRQRtQLENLEqgvDVLIATPGRFTYLM-NEGILG-LSNLRCAILDEVDILFGDD---EFEAALQNLINSSPVTAQ 560
Cdd:cd17922  73 tsqSEKAK-QLKNPP---GILITTPESLELLLvNKKLRElFAGLRYVVVDEIHALLGSKrgvQLELLLERLRKLTGRPLR 148
                       170
                ....*....|..
gi 15231353 561 YLFVTATL-PLE 571
Cdd:cd17922 149 RIGLSATLgNLE 160
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
625-722 2.20e-05

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 47.91  E-value: 2.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 625 ALLQIMEENPVS--KTIIFCNKIETCRKVENIFKrvdrkERQLHVLPFHAALSQESRLTNMQEFTssQPEENSLFLVCTD 702
Cdd:COG0553 537 ALLELLEELLAEgeKVLVFSQFTDTLDLLEERLE-----ERGIEYAYLHGGTSAEERDELVDRFQ--EGPEAPVFLISLK 609
                        90       100
                ....*....|....*....|
gi 15231353 703 RASRGIDFSGVDHVVLFDFP 722
Cdd:COG0553 610 AGGEGLNLTAADHVIHYDLW 629
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
408-535 8.81e-05

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 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: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 44.68  E-value: 8.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 408 VIDGKSCIIADQSGSGKT---LAYLVPVIQ---------RLREEELQGHSKSSPGcPRVIVLVPTAelasqVLANCRS-I 474
Cdd:cd18005  16 YKNGRGGILGDDMGLGKTvqvIAFLAAVLGktgtrrdreNNRPRFKKKPPASSAK-KPVLIVAPLS-----VLYNWKDeL 89
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231353 475 SKSGvPFRSMVVTGGFRQRTQLENLEQG-VDVLIATpgrFTYLMNEgILGLSNLR--CAILDEV 535
Cdd:cd18005  90 DTWG-HFEVGVYHGSRKDDELEGRLKAGrLEVVVTT---YDTLRRC-IDSLNSINwsAVIADEA 148
PRK00254 PRK00254
ski2-like helicase; Provisional
378-568 2.59e-04

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 44.42  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  378 EIGCSEDMMKALKEQNFDRPAHIQAMAF-SPVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEElqghsksspgcPRVIV 456
Cdd:PRK00254   5 ELRVDERIKRVLKERGIEELYPPQAEALkSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREG-----------GKAVY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  457 LVPTAELASQVLANCRSISKSGVpfRSMVVTGGFRQRtqlENLEQGVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVD 536
Cdd:PRK00254  74 LVPLKALAEEKYREFKDWEKLGL--RVAMTTGDYDST---DEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIH 148
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15231353  537 iLFGDDEFEAALQNLINSSPVTAQYLFVTATL 568
Cdd:PRK00254 149 -LIGSYDRGATLEMILTHMLGRAQILGLSATV 179
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
616-734 3.50e-04

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 43.98  E-value: 3.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 616 ETAFQNKKTALLQIMEENPVSKTIIFCNkieTCRKVENIFKRVdrKERQLHVLPFHAALSQESRLTNMQEFTssqpEENS 695
Cdd:COG0514 211 PKPPDDKLAQLLDFLKEHPGGSGIVYCL---SRKKVEELAEWL--REAGIRAAAYHAGLDAEEREANQDRFL----RDEV 281
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15231353 696 LFLVCTdraSR---GIDFSGVDHVVLFDFPRDPSEYVRRVGR 734
Cdd:COG0514 282 DVIVAT---IAfgmGIDKPDVRFVIHYDLPKSIEAYYQEIGR 320
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
411-534 3.59e-04

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins 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: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 42.17  E-value: 3.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 411 GKSCIIADQSGSGKTL---AYlvpviqrlreeeLQGHSKSSPGCPRVIVLVPTAelasqVLAN-CRSISKSGVPFRSMVV 486
Cdd:cd17919  19 GPGGILADEMGLGKTLqaiAF------------LAYLLKEGKERGPVLVVCPLS-----VLENwEREFEKWTPDLRVVVY 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15231353 487 TGGFRQRTQLENLEQGV--DVLIATpgrFTYLMNE-GILGLSNLRCAILDE 534
Cdd:cd17919  82 HGSQRERAQIRAKEKLDkfDVVLTT---YETLRRDkASLRKFRWDLVVVDE 129
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
421-534 3.62e-04

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: 42.02  E-value: 3.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 421 GSGKTLAYLVPVIQRLREEElqghsksspgcpRVIVLVPTAELASQVLANCRsisKSGVPFRSMVVTGGFRqrtqlENLE 500
Cdd:cd17918  46 GSGKTLVALGAALLAYKNGK------------QVAILVPTEILAHQHYEEAR---KFLPFINVELVTGGTK-----AQIL 105
                        90       100       110
                ....*....|....*....|....*....|....
gi 15231353 501 QGVDVLIATpgrfTYLMNEGILGLsNLRCAILDE 534
Cdd:cd17918 106 SGISLLVGT----HALLHLDVKFK-NLDLVIVDE 134
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
401-569 5.57e-04

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: 41.55  E-value: 5.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 401 QAMAF-SPVIDGKSCIIADQSGSGKTLAYLVPVIQRLreeeLQGHsksspgcpRVIVLVPTAELASQVLANCRSISKSGV 479
Cdd:cd18028   6 QAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTL----LEGG--------KALYLVPLRALASEKYEEFKKLEEIGL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 480 pfRSMVVTGGFRQRTqlENLEQgVDVLIATPGRFTYLMNEGILGLSNLRCAILDEVDiLFGDDE----FEAALQNLINSS 555
Cdd:cd18028  74 --KVGISTGDYDEDD--EWLGD-YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIH-LISDEErgptLESIVARLRRLN 147
                       170
                ....*....|....
gi 15231353 556 PvTAQYLFVTATLP 569
Cdd:cd18028 148 P-NTQIIGLSATIG 160
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
511-743 1.41e-03

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 41.65  E-value: 1.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 511 GRFTYLMNegiLGLSNLrcaILDEVDILfgDDE----FEAALQNLI-NSSPVtaqyLFVTATLPleiyNKLVEVFPDCEV 585
Cdd:cd09639 114 HYEFTLAS---IANSLL---IFDEVHFY--DEYtlalILAVLEVLKdNDVPI----LLMSATLP----KFLKEYAEKIGY 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 586 VMGPRVHRVSNALEEFLVDCSGDDNAEktpetafQNKKTALLQimEENPVSKTIIFCNKIETCRKvenIFKRVDRKERQL 665
Cdd:cd09639 178 VEENEPLDLKPNERAPFIKIESDKVGE-------ISSLERLLE--FIKKGGSVAIIVNTVDRAQE---FYQQLKEKGPEE 245
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231353 666 HVLPFHAALSQESRLTNMQEFTSSQPEENSLFLVCTDRASRGIDFSgVDhvVLFDFPRDPSEYVRRVGRTARGARGKG 743
Cdd:cd09639 246 EIMLIHSRFTEKDRAKKEAELLLEFKKSEKFVIVATQVIEASLDIS-VD--VMITELAPIDSLIQRLGRLHRYGEKNG 320
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
636-749 2.05e-03

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: 39.55  E-value: 2.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 636 SKTIIFCNkieTCRKVENIFKRV-DRKERQLHVLPF---HAALSQESRLTnmqeftssqpEENSL------FLVCTDRAS 705
Cdd:cd18796  39 KSTLVFTN---TRSQAERLAQRLrELCPDRVPPDFIalhHGSLSRELREE----------VEAALkrgdlkVVVATSSLE 105
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15231353 706 RGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARGKGKAFIFV 749
Cdd:cd18796 106 LGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLVP 149
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
393-538 2.16e-03

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 40.03  E-value: 2.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 393 NFDRpahIQAMAFSPVIDG-KSCIIADQSGSGKT----LAYLvpviqRLreeeLQGHSKSSPGCPRVIVLVPTAELASQV 467
Cdd:cd18023   1 YFNR---IQSEVFPDLLYSdKNFVVSAPTGSGKTvlfeLAIL-----RL----LKERNPLPWGNRKVVYIAPIKALCSEK 68
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231353 468 LANCR-SISKSGVPFrsMVVTGGfrqrTQLENLE--QGVDVLIATPGRF---TYLMNEGILGLSNLRCAILDEVDIL 538
Cdd:cd18023  69 YDDWKeKFGPLGLSC--AELTGD----TEMDDTFeiQDADIILTTPEKWdsmTRRWRDNGNLVQLVALVLIDEVHII 139
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
407-535 2.29e-03

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


Pssm-ID: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 40.15  E-value: 2.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 407 PVIDGKSCIIADQSGSGKTLAYLVPVIQRLREEELQGHskssPGcpRVIVLVPTAELASQVLancrsiSKSGVPFRSMV- 485
Cdd:cd18036  13 PALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGE----KG--RVVVLVNKVPLVEQQL------EKFFKYFRKGYk 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15231353 486 ---VTGGFRQRTQLENLEQGVDVLIATPGRFTYLMNEG----ILGLSNLRCAILDEV 535
Cdd:cd18036  81 vtgLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGreeeRVYLSDFSLLIFDEC 137
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
622-750 2.66e-03

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: 38.73  E-value: 2.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 622 KKTALLQIM----EENPVSKTIIFCNKIETCRKVENIFKRVDRKERQLHVlpfhAALSQESRLTNMQEFTSSQPEEN--- 694
Cdd:cd18802   8 KLQKLIEILreyfPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRC----GFLIGRGNSSQRKRSLMTQRKQKetl 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231353 695 SLF-------LVCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRtargARGKGKAFIFVV 750
Cdd:cd18802  84 DKFrdgelnlLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR----ARAPNSKYILMV 142
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
627-742 4.74e-03

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: 38.11  E-value: 4.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353 627 LQIMEENPVSKTIIFCNKIETcrkVENIFKRVDRKERQLHVLPF--HAA------LSQESRLTNMQEFtssQPEENSLfL 698
Cdd:cd18801  22 FKKKQEGSDTRVIIFSEFRDS---AEEIVNFLSKIRPGIRATRFigQASgksskgMSQKEQKEVIEQF---RKGGYNV-L 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15231353 699 VCTDRASRGIDFSGVDHVVLFDFPRDPSEYVRRVGRTARGARGK 742
Cdd:cd18801  95 VATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQGR 138
PRK12678 PRK12678
transcription termination factor Rho; Provisional
164-328 6.87e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 39.89  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  164 KAIPRSGKSAERNEVKRASKVRESRESRRDLDRLEGDDEDVDEVSNPDRFTDNQRAGSRSSYSKGGYAANSRGKGDRLSV 243
Cdd:PRK12678 111 AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGER 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231353  244 ARDLDSFEGHGRAIDE-VSNPRKFNDNERAESRSSYSRDSSANSRGREDRRFVAKELDTFQGRDKAYDEVYNPRRFTDNE 322
Cdd:PRK12678 191 GRREERGRDGDDRDRRdRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRD 270

                 ....*.
gi 15231353  323 RGLRGG 328
Cdd:PRK12678 271 RRGRRG 276
 
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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