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Conserved domains on  [gi|17136814|ref|NP_476927|]
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DEAD box protein 45A [Drosophila melanogaster]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423521)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
9-381 6.19e-129

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 381.80  E-value: 6.19e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH-FALVLTPTHEL 87
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRApQALILAPTREL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  88 AYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDF 167
Cdd:COG0513  84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLDMGF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 168 DESLSIIERCLPKTRQNLFFSATMKDFIKEssifpIASdcfEWSQD-------SDVATVETLDQRYLLCADYDRdmvlIE 240
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRK-----LAK---RYLKNpvrievaPENATAETIEQRYYLVDKRDK----LE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 241 ALRKYREENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDIPSV 320
Cdd:COG0513 231 LLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDV 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136814 321 ELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISIFRfPRDLELLAAIEEEINTKLTEHPID 381
Cdd:COG0513 311 SHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT-PDERRLLRAIEKLIGQKIEEEELP 370
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
9-381 6.19e-129

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 381.80  E-value: 6.19e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH-FALVLTPTHEL 87
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRApQALILAPTREL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  88 AYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDF 167
Cdd:COG0513  84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLDMGF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 168 DESLSIIERCLPKTRQNLFFSATMKDFIKEssifpIASdcfEWSQD-------SDVATVETLDQRYLLCADYDRdmvlIE 240
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRK-----LAK---RYLKNpvrievaPENATAETIEQRYYLVDKRDK----LE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 241 ALRKYREENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDIPSV 320
Cdd:COG0513 231 LLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDV 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136814 321 ELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISIFRfPRDLELLAAIEEEINTKLTEHPID 381
Cdd:COG0513 311 SHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT-PDERRLLRAIEKLIGQKIEEEELP 370
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
9-211 1.81e-116

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: 341.90  E-value: 1.81e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELA 88
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  89 YQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCD--TFSFDNLKYLVVDEADRMLNGD 166
Cdd:cd17955  81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDdtTKVLSRVKFLVLDEADRLLTGS 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17136814 167 FDESLSIIERCLPKTRQNLFFSATMKDFIKESSIFPIAsDCFEWS 211
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGN-KPFFWE 204
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
6-382 1.13e-91

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 287.47  E-value: 1.13e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    6 ANPFQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSeepVSHF---ALVLT 82
Cdd:PRK11776   3 MTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD---VKRFrvqALVLC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   83 PTHELAYQISEQFLVAGQAM-GVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLtGCDTFSFDNLKYLVVDEADR 161
Cdd:PRK11776  80 PTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHL-RKGTLDLDALNTLVLDEADR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  162 MLN-GDFDESLSIIERClPKTRQNLFFSATMKDFIKEssifpIASDCFEWSQDSDVATVE---TLDQRYLLCADYDRDMV 237
Cdd:PRK11776 159 MLDmGFQDAIDAIIRQA-PARRQTLLFSATYPEGIAA-----ISQRFQRDPVEVKVESTHdlpAIEQRFYEVSPDERLPA 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  238 LIEALRKYREENenanVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDI 317
Cdd:PRK11776 233 LQRLLLHHQPES----CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDI 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136814  318 PSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISIFRfPRDLELLAAIEEEINTKLTEHPIDQ 382
Cdd:PRK11776 309 KALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVA-PEEMQRANAIEDYLGRKLNWEPLPS 372
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
31-197 8.02e-56

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: 184.37  E-value: 8.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    31 TPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELAYQISEQFLVAGQAMGVRVCVVS 110
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   111 GGTDQMVESQKLmQRPHIVVAMPGRLADHLtgCDTFSFDNLKYLVVDEADRMLNGDFDESLSIIERCLPKTRQNLFFSAT 190
Cdd:pfam00270  81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLL--QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*..
gi 17136814   191 MKDFIKE 197
Cdd:pfam00270 158 LPRNLED 164
DEXDc smart00487
DEAD-like helicases superfamily;
31-197 9.08e-43

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 151.11  E-value: 9.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814     31 TPIQQKCIPAILAG-QDCIGAAKTGSGKTFAFALPILERLSEEPVSHfALVLTPTHELAYQISEQFLVAGQAMGVRVCVV 109
Cdd:smart00487  10 RPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGR-VLVLVPTRELAEQWAEELKKLGPSLGLKVVGL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    110 SGGTDQMVESQKLMQ-RPHIVVAMPGRLADHLTgCDTFSFDNLKYLVVDEADRMLNGDFDESLSIIERCLPKTRQNLFFS 188
Cdd:smart00487  89 YGGDSKREQLRKLESgKTDILVTTPGRLLDLLE-NDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLLS 167

                   ....*....
gi 17136814    189 ATMKDFIKE 197
Cdd:smart00487 168 ATPPEEIEN 176
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
9-381 6.19e-129

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 381.80  E-value: 6.19e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH-FALVLTPTHEL 87
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRApQALILAPTREL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  88 AYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDF 167
Cdd:COG0513  84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLDMGF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 168 DESLSIIERCLPKTRQNLFFSATMKDFIKEssifpIASdcfEWSQD-------SDVATVETLDQRYLLCADYDRdmvlIE 240
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRK-----LAK---RYLKNpvrievaPENATAETIEQRYYLVDKRDK----LE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 241 ALRKYREENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDIPSV 320
Cdd:COG0513 231 LLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDV 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136814 321 ELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISIFRfPRDLELLAAIEEEINTKLTEHPID 381
Cdd:COG0513 311 SHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT-PDERRLLRAIEKLIGQKIEEEELP 370
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
9-211 1.81e-116

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: 341.90  E-value: 1.81e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELA 88
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  89 YQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCD--TFSFDNLKYLVVDEADRMLNGD 166
Cdd:cd17955  81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDdtTKVLSRVKFLVLDEADRLLTGS 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17136814 167 FDESLSIIERCLPKTRQNLFFSATMKDFIKESSIFPIAsDCFEWS 211
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGN-KPFFWE 204
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
6-382 1.13e-91

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 287.47  E-value: 1.13e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    6 ANPFQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSeepVSHF---ALVLT 82
Cdd:PRK11776   3 MTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD---VKRFrvqALVLC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   83 PTHELAYQISEQFLVAGQAM-GVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLtGCDTFSFDNLKYLVVDEADR 161
Cdd:PRK11776  80 PTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHL-RKGTLDLDALNTLVLDEADR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  162 MLN-GDFDESLSIIERClPKTRQNLFFSATMKDFIKEssifpIASDCFEWSQDSDVATVE---TLDQRYLLCADYDRDMV 237
Cdd:PRK11776 159 MLDmGFQDAIDAIIRQA-PARRQTLLFSATYPEGIAA-----ISQRFQRDPVEVKVESTHdlpAIEQRFYEVSPDERLPA 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  238 LIEALRKYREENenanVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDI 317
Cdd:PRK11776 233 LQRLLLHHQPES----CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDI 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136814  318 PSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISIFRfPRDLELLAAIEEEINTKLTEHPIDQ 382
Cdd:PRK11776 309 KALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVA-PEEMQRANAIEDYLGRKLNWEPLPS 372
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
9-191 1.20e-75

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: 237.21  E-value: 1.20e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELA 88
Cdd:cd17954   2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  89 YQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADRMLNGDFD 168
Cdd:cd17954  82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLNMDFE 161
                       170       180
                ....*....|....*....|...
gi 17136814 169 ESLSIIERCLPKTRQNLFFSATM 191
Cdd:cd17954 162 PEIDKILKVIPRERTTYLFSATM 184
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
18-197 1.40e-74

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: 234.26  E-value: 1.40e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHF----ALVLTPTHELAYQISE 93
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGrgpqALVLAPTRELAMQIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  94 QFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDFDESLSI 173
Cdd:cd00268  81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIER-GKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                       170       180
                ....*....|....*....|....
gi 17136814 174 IERCLPKTRQNLFFSATMKDFIKE 197
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKE 183
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
9-410 2.14e-65

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 223.19  E-value: 2.14e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELA 88
Cdd:PRK11634   8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   89 YQISEQFLVAGQAM-GVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDF 167
Cdd:PRK11634  88 VQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKR-GTLDLSKLSGLVLDEADEMLRMGF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  168 DESLSIIERCLPKTRQNLFFSATMKDFIKESSiFPIASDCFEWSQDSDVATVETLDQRYLLCADYDRDmvliEALRKYRE 247
Cdd:PRK11634 167 IEDVETIMAQIPEGHQTALFSATMPEAIRRIT-RRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKN----EALVRFLE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  248 ENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDIPSVELVMNHM 327
Cdd:PRK11634 242 AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYD 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  328 LPRTPKEYIHRVGRTARAGRKGMSIsIFRFPRDLELLAAIEEEIntKLT----EHP----IDQRMVERIFMQVnvtrres 399
Cdd:PRK11634 322 IPMDSESYVHRIGRTGRAGRAGRAL-LFVENRERRLLRNIERTM--KLTipevELPnaelLGKRRLEKFAAKV------- 391
                        410
                 ....*....|.
gi 17136814  400 EMQLDNNDFDE 410
Cdd:PRK11634 392 QQQLESSDLDQ 402
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
9-386 3.18e-63

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 212.50  E-value: 3.18e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFA----LVLTPT 84
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGppriLILTPT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   85 HELAYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLtgcDTFSFD--NLKYLVVDEADRM 162
Cdd:PRK11192  83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYI---KEENFDcrAVETLILDEADRM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  163 LNGDFDeslSIIERCLPKTR---QNLFFSATM-----KDFIKEssifpIASDCFEWSQDSDVATVETLDQRYLLCADYDR 234
Cdd:PRK11192 160 LDMGFA---QDIETIAAETRwrkQTLLFSATLegdavQDFAER-----LLNDPVEVEAEPSRRERKKIHQWYYRADDLEH 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  235 DMVLIEALRKyREENENAnvMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARG 314
Cdd:PRK11192 232 KTALLCHLLK-QPEVTRS--IVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARG 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136814  315 LDIPSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISIFRfPRDLELLAAIEeeintKLTEHPIDQRMVE 386
Cdd:PRK11192 309 IDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVE-AHDHLLLGKIE-----RYIEEPLKARVID 374
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
9-364 3.72e-62

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 210.43  E-value: 3.72e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEE--------PVShfALV 80
Cdd:PRK10590   3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphakgrrPVR--ALI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   81 LTPTHELAYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADhLTGCDTFSFDNLKYLVVDEAD 160
Cdd:PRK10590  81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEAD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  161 RMLNGDFDESLSIIERCLPKTRQNLFFSATMKDFIKEssifpIASDCFEWSQDSDVATVETLDQ---RYLLCADYDRDMv 237
Cdd:PRK10590 160 RMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKA-----LAEKLLHNPLEIEVARRNTASEqvtQHVHFVDKKRKR- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  238 liEALRKYREENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDI 317
Cdd:PRK10590 234 --ELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDI 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17136814  318 PSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISIF-----RFPRDLELL 364
Cdd:PRK10590 312 EELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVcvdehKLLRDIEKL 363
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
9-488 6.28e-62

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 212.89  E-value: 6.28e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERL-------SEEPVSHFALVL 81
Cdd:PRK04537  11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALIL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   82 TPTHELAYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADR 161
Cdd:PRK04537  91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDEADR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  162 MLNGDFDESLSIIERCLPK--TRQNLFFSATMKDFIKESSifpiasdcFEWSQDSDVATVET-------LDQRYLLCADY 232
Cdd:PRK04537 171 MFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELA--------YEHMNEPEKLVVETetitaarVRQRIYFPADE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  233 DRDMVLIEALRKyreeNENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAA 312
Cdd:PRK04537 243 EKQTLLLGLLSR----SEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  313 RGLDIPSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISiFRFPRDLELLAAIEEEINTKLTEHPIDQRMVERIFMQV 392
Cdd:PRK04537 319 RGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAIS-FACERYAMSLPDIEAYIEQKIPVEPVTAELLTPLPRPP 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  393 NVTRRESEMQLDNND---------FDER-AQNYRR---KTWIMEGKDPDQMEALYRKKQKDKLREIRRKRKL-----QHA 454
Cdd:PRK04537 398 RVPVEGEEADDEAGDsvgtifreaREQRaAEEQRRgggRSGPGGGSRSGSVGGGGRRDGAGADGKPRPRRKPrvegeADA 477
                        490       500       510
                 ....*....|....*....|....*....|....
gi 17136814  455 EPAASEEGKALLQDERFKSVDSARFEKKGKGRSR 488
Cdd:PRK04537 478 AAAGAETPVVAAAAAQAPGVVAADGERAPRKRRR 511
PTZ00110 PTZ00110
helicase; Provisional
9-376 1.32e-59

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 205.78  E-value: 1.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFA-----LVLTP 83
Cdd:PTZ00110 132 FEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGdgpivLVLAP 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   84 THELAYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTfsfdNLK---YLVVDEAD 160
Cdd:PTZ00110 212 TRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVT----NLRrvtYLVLDEAD 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  161 RMLNGDFDESL-SIIERCLPKtRQNLFFSAT--------MKDFIKESSI-FPIASdcfewsqdSDVATVETLDQRYLLCA 230
Cdd:PTZ00110 288 RMLDMGFEPQIrKIVSQIRPD-RQTLMWSATwpkevqslARDLCKEEPVhVNVGS--------LDLTACHNIKQEVFVVE 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  231 DYDRDMVLIEALRKYReeNENANVMIFTNTKKYCQLLSmtlKNMEIDNV---CLHGFMRQKERVAALSRFKSNQIRTLIA 307
Cdd:PTZ00110 359 EHEKRGKLKMLLQRIM--RDGDKILIFVETKKGADFLT---KELRLDGWpalCIHGDKKQEERTWVLNEFKTGKSPIMIA 433
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136814  308 TDVAARGLDIPSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISIF-----RFPRDL-ELLAAIEEEINTKLT 376
Cdd:PTZ00110 434 TDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLtpdkyRLARDLvKVLREAKQPVPPELE 508
PTZ00424 PTZ00424
helicase 45; Provisional
9-381 1.46e-59

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 201.98  E-value: 1.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELA 88
Cdd:PTZ00424  30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   89 YQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDFD 168
Cdd:PTZ00424 110 QQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDK-RHLRVDDLKLFILDEADEMLSRGFK 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  169 ESLSIIERCLPKTRQNLFFSATMKDFIKESSIfPIASDCFEWSQDSDVATVETLDQRYLLCadyDRDMVLIEALRKYREE 248
Cdd:PTZ00424 189 GQIYDVFKKLPPDVQVALFSATMPNEILELTT-KFMRDPKRILVKKDELTLEGIRQFYVAV---EKEEWKFDTLCDLYET 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  249 NENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDIPSVELVMNHML 328
Cdd:PTZ00424 265 LTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDL 344
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17136814  329 PRTPKEYIHRVGRTARAGRKGMSISiFRFPRDLELLAAIEEEINTKLTEHPID 381
Cdd:PTZ00424 345 PASPENYIHRIGRSGRFGRKGVAIN-FVTPDDIEQLKEIERHYNTQIEEMPME 396
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
18-197 1.17e-57

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: 190.16  E-value: 1.17e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHF---ALVLTPTHELAYQISEQ 94
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAatrVLVLVPTRELAMQCFSV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  95 FLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADRMLNGDF-DESLSI 173
Cdd:cd17947  81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFaDELKEI 160
                       170       180
                ....*....|....*....|....
gi 17136814 174 IERClPKTRQNLFFSATMKDFIKE 197
Cdd:cd17947 161 LRLC-PRTRQTMLFSATMTDEVKD 183
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
9-387 1.22e-56

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 196.29  E-value: 1.22e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH-------FALVL 81
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKerymgepRALII 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   82 TPTHELAYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQR-PHIVVAMPGRLADHLTGCDTFsFDNLKYLVVDEAD 160
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVH-LDMVEVMVLDEAD 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  161 RMLNGDFDESLSIIERCLPKT--RQNLFFSATMKDfikesSIFPIASdcfEWSQDSDVATVE-------TLDQRYLLCAD 231
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTD-----DVMNLAK---QWTTDPAIVEIEpenvasdTVEQHVYAVAG 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  232 YDRDMVLIEALRkyreENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVA 311
Cdd:PRK01297 320 SDKYKLLYNLVT----QNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVA 395
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136814  312 ARGLDIPSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISiFRFPRDLELLAAIEEEINTKLT-EHPIDQ--RMVER 387
Cdd:PRK01297 396 GRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSIS-FAGEDDAFQLPEIEELLGRKIScEMPPAEllKPVPR 473
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
31-197 8.02e-56

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: 184.37  E-value: 8.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    31 TPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELAYQISEQFLVAGQAMGVRVCVVS 110
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   111 GGTDQMVESQKLmQRPHIVVAMPGRLADHLtgCDTFSFDNLKYLVVDEADRMLNGDFDESLSIIERCLPKTRQNLFFSAT 190
Cdd:pfam00270  81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLL--QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*..
gi 17136814   191 MKDFIKE 197
Cdd:pfam00270 158 LPRNLED 164
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
222-355 5.18e-51

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: 170.38  E-value: 5.18e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 222 LDQRYLLCADYDRDMVLieaLRKYREENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQ 301
Cdd:cd18787   1 IKQLYVVVEEEEKKLLL---LLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGK 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17136814 302 IRTLIATDVAARGLDIPSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISIF 355
Cdd:cd18787  78 VRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
18-193 4.02e-50

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: 170.84  E-value: 4.02e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILA-GQDCIGAAKTGSGKTFAFALPILERLSEEP-------VShfALVLTPTHELAY 89
Cdd:cd17964   5 LLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKpagrrsgVS--ALIISPTRELAL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  90 QISEQF-LVAGQAMGVRVCVVSGGTDQMVESQKLM-QRPHIVVAMPGRLADHLTGCDTF-SFDNLKYLVVDEADRMLNGD 166
Cdd:cd17964  83 QIAAEAkKLLQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLENPGVAkAFTDLDYLVLDEADRLLDMG 162
                       170       180       190
                ....*....|....*....|....*....|.
gi 17136814 167 FDESLSIIERCLPK----TRQNLFFSATMKD 193
Cdd:cd17964 163 FRPDLEQILRHLPEknadPRQTLLFSATVPD 193
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
9-380 4.03e-50

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 177.47  E-value: 4.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHF-------ALVL 81
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrkvnqprALIM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   82 TPTHELAYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADR 161
Cdd:PRK04837  90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQ-NHINLGAIQVVVLDEADR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  162 MlngdFDesLSIIE--RCL------PKTRQNLFFSATMKDFIKESSifpiasdcFEWSQDSDVATVETLD------QRYL 227
Cdd:PRK04837 169 M----FD--LGFIKdiRWLfrrmppANQRLNMLFSATLSYRVRELA--------FEHMNNPEYVEVEPEQktghriKEEL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  228 LCADYDRDMVLIEALrkyREENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIA 307
Cdd:PRK04837 235 FYPSNEEKMRLLQTL---IEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVA 311
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136814  308 TDVAARGLDIPSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISI------FRFPrdlellaAIEEEIntkltEHPI 380
Cdd:PRK04837 312 TDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLaceeyaLNLP-------AIETYI-----GHSI 378
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
23-197 4.56e-47

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: 162.46  E-value: 4.56e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  23 TKLGLKGA-----TPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHF----ALVLTPTHELAYQISE 93
Cdd:cd17941   1 TLKGLKEAgfikmTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELAMQIFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  94 QFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRpHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADRMLNGDFDESLSI 173
Cdd:cd17941  81 VLRKVGKYHSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
                       170       180
                ....*....|....*....|....
gi 17136814 174 IERCLPKTRQNLFFSATMKDFIKE 197
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKD 183
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
18-191 5.08e-47

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: 163.56  E-value: 5.08e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIP-AILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH---------FALVLTPTHEL 87
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNgvggkqkplRALILTPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  88 AYQISEQFLVAGQAMGVRVCVVSGGtdqmVESQK----LMQRPHIVVAMPGRLADHLTGCDTF--SFDNLKYLVVDEADR 161
Cdd:cd17946  81 AVQVKDHLKAIAKYTNIKIASIVGG----LAVQKqerlLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADR 156
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17136814 162 ML-NGDFDESLSIIErCLPKT-------RQNLFFSATM 191
Cdd:cd17946 157 MLeKGHFAELEKILE-LLNKDragkkrkRQTFVFSATL 193
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
9-191 1.19e-46

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: 161.70  E-value: 1.19e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERL--SEEPVSHFALVLTPTHE 86
Cdd:cd17959   3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkaHSPTVGARALILSPTRE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  87 LAYQISEQFLVAGQAMGVRVCVVSGGtDQMvESQ--KLMQRPHIVVAMPGRLAdHLTGCDTFSFDNLKYLVVDEADRMLN 164
Cdd:cd17959  83 LALQTLKVTKELGKFTDLRTALLVGG-DSL-EEQfeALASNPDIIIATPGRLL-HLLVEMNLKLSSVEYVVFDEADRLFE 159
                       170       180
                ....*....|....*....|....*..
gi 17136814 165 GDFDESLSIIERCLPKTRQNLFFSATM 191
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATL 186
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
19-190 6.01e-46

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


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 159.45  E-value: 6.01e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  19 VKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHF----ALVLTPTHELAYQIseq 94
Cdd:cd17942   2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQI--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  95 FLVAGQAM--GVRVC-VVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADRMLNGDFDESL 171
Cdd:cd17942  79 YGVAKELLkyHSQTFgIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEM 158
                       170
                ....*....|....*....
gi 17136814 172 SIIERCLPKTRQNLFFSAT 190
Cdd:cd17942 159 RQIIKLLPKRRQTMLFSAT 177
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
9-190 1.43e-44

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: 156.49  E-value: 1.43e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH----------FA 78
Cdd:cd17967   2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypSA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  79 LVLTPTHELAYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDE 158
Cdd:cd17967  82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIER-GRISLSSIKFLVLDE 160
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17136814 159 ADRMLNGDFDESL-SIIERC-LPKT--RQNLFFSAT 190
Cdd:cd17967 161 ADRMLDMGFEPQIrKIVEHPdMPPKgeRQTLMFSAT 196
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
18-191 5.01e-44

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: 155.48  E-value: 5.01e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIG---------AAKTGSGKTFAFALPILERLSEEPVSHF-ALVLTPTHEL 87
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKSTPpyrpgdlcvSAPTGSGKTLAYVLPIVQALSKRVVPRLrALIVVPTKEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  88 AYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQ--------RPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEA 159
Cdd:cd17956  81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVdtsgrylsRVDILVATPGRLVDHLNSTPGFTLKHLRFLVIDEA 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17136814 160 DRMLNGDFDESLSIIERCL--------------------PKTRQNLFFSATM 191
Cdd:cd17956 161 DRLLNQSFQDWLETVMKALgrptapdlgsfgdanllersVRPLQKLLFSATL 212
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
14-193 2.51e-43

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


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 152.74  E-value: 2.51e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  14 LRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILE---RLSEEPVSHF---ALVLTPTHEL 87
Cdd:cd17961   1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQkilKAKAESGEEQgtrALILVPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  88 AYQISEQF--LVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADRMLNG 165
Cdd:cd17961  81 AQQVSKVLeqLTAYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSY 160
                       170       180
                ....*....|....*....|....*...
gi 17136814 166 DFDESLSIIERCLPKTRQNLFFSATMKD 193
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSE 188
DEXDc smart00487
DEAD-like helicases superfamily;
31-197 9.08e-43

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 151.11  E-value: 9.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814     31 TPIQQKCIPAILAG-QDCIGAAKTGSGKTFAFALPILERLSEEPVSHfALVLTPTHELAYQISEQFLVAGQAMGVRVCVV 109
Cdd:smart00487  10 RPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGR-VLVLVPTRELAEQWAEELKKLGPSLGLKVVGL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    110 SGGTDQMVESQKLMQ-RPHIVVAMPGRLADHLTgCDTFSFDNLKYLVVDEADRMLNGDFDESLSIIERCLPKTRQNLFFS 188
Cdd:smart00487  89 YGGDSKREQLRKLESgKTDILVTTPGRLLDLLE-NDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLLS 167

                   ....*....
gi 17136814    189 ATMKDFIKE 197
Cdd:smart00487 168 ATPPEEIEN 176
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
12-197 1.46e-40

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: 145.16  E-value: 1.46e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  12 LGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELAYQI 91
Cdd:cd17939   2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  92 SEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDFDESL 171
Cdd:cd17939  82 QKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEMLSRGFKDQI 160
                       170       180
                ....*....|....*....|....*.
gi 17136814 172 SIIERCLPKTRQNLFFSATMKDFIKE 197
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLE 186
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
9-197 1.50e-40

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


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 145.13  E-value: 1.50e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELA 88
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  89 YQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADhLTGCDTFSFDNLKYLVVDEADRMLNGDFD 168
Cdd:cd17940  81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
                       170       180       190
                ....*....|....*....|....*....|...
gi 17136814 169 ESLSIIERCLPKTRQNLFFSAT----MKDFIKE 197
Cdd:cd17940 160 PIIEKILNFLPKERQILLFSATfpltVKNFMDR 192
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
18-191 5.82e-40

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: 143.50  E-value: 5.82e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH--FALVLTPTHELAYQISEQF 95
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKglRALILAPTRELASQIYREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  96 LVAGQAMGVRVCVVSGGT-DQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDF-DESLSI 173
Cdd:cd17957  81 LKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQ-GPIDLSSVEYLVLDEADKLFEPGFrEQTDEI 159
                       170
                ....*....|....*...
gi 17136814 174 IERCLPKTRQNLFFSATM 191
Cdd:cd17957 160 LAACTNPNLQRSLFSATI 177
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
18-197 1.17e-39

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: 143.11  E-value: 1.17e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQL-TKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH------FALVLTPTHELAYQ 90
Cdd:cd17949   1 LVSHLkSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVdrsdgtLALVLVPTRELALQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  91 ISEQFLVAGQAMG-VRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADRMLNGDFDE 169
Cdd:cd17949  81 IYEVLEKLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEK 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17136814 170 SLSII-------------ERCLPKTRQNLFFSATMKDFIKE 197
Cdd:cd17949 161 DITKIlellddkrskaggEKSKPSRRQTVLVSATLTDGVKR 201
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
9-201 1.81e-39

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: 144.34  E-value: 1.81e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERL---------SEEPVSHFAL 79
Cdd:cd18052  45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegltassFSEVQEPQAL 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  80 VLTPTHELAYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLtGCDTFSFDNLKYLVVDEA 159
Cdd:cd18052 125 IVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFI-GRGKISLSKLKYLILDEA 203
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17136814 160 DRMLNGDF-DESLSIIERC--LPKT-RQNLFFSATM--------KDFIKESSIF 201
Cdd:cd18052 204 DRMLDMGFgPEIRKLVSEPgmPSKEdRQTLMFSATFpeeiqrlaAEFLKEDYLF 257
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
18-203 5.72e-39

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: 140.94  E-value: 5.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALP-ILERLSEE---PVSH----FALVLTPTHELA- 88
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEkklPFIKgegpYGLIVCPSRELAr 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  89 --YQISEQF---LVAGQAMGVRVCVVSGGTDqMVESQKLMQRP-HIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRM 162
Cdd:cd17951  81 qtHEVIEYYckaLQEGGYPQLRCLLCIGGMS-VKEQLEVIRKGvHIVVATPGRLMDMLNK-KKINLDICRYLCLDEADRM 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17136814 163 LNGDFDESLSIIERCLPKTRQNLFFSATM----KDFIKESSIFPI 203
Cdd:cd17951 159 IDMGFEEDIRTIFSYFKGQRQTLLFSATMpkkiQNFAKSALVKPV 203
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
3-352 3.52e-38

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 146.47  E-value: 3.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    3 RKEANPFQIL-----GLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH- 76
Cdd:PLN00206 112 KGEAVPPPILsfsscGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHp 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   77 ------FALVLTPTHELAYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDtFSFDN 150
Cdd:PLN00206 192 seqrnpLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHD-IELDN 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  151 LKYLVVDEADRMLNGDFDESLSIIERCLPkTRQNLFFSATMKDFIKESSIfPIASDCFEWSQDSDVATVETLDQRYLLCA 230
Cdd:PLN00206 271 VSVLVLDEVDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFAS-SLAKDIILISIGNPNRPNKAVKQLAIWVE 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  231 DYDRDMVLIEALRKyrEENENANVMIFTNTKKYCQLLSMTL-KNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATD 309
Cdd:PLN00206 349 TKQKKQKLFDILKS--KQHFKPPAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATG 426
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 17136814  310 VAARGLDIPSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSI 352
Cdd:PLN00206 427 VLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAI 469
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
18-190 6.24e-38

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: 137.78  E-value: 6.24e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELAYQISEQFLV 97
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  98 AGQAM-GVRVCVVSGGTDQMVESQKLmQRPHIVVAMPGRLAdHLTGCDTFSFDNLKYLVVDEADRMLNGDFDESLSIIER 176
Cdd:cd17943  81 IGKKLeGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIK-QLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFS 158
                       170
                ....*....|....
gi 17136814 177 CLPKTRQNLFFSAT 190
Cdd:cd17943 159 SLPKNKQVIAFSAT 172
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
22-191 7.20e-38

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: 138.66  E-value: 7.20e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  22 LTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILER-LSEEPVSH----FALVLTPTHELAYQISEQFL 96
Cdd:cd17953  27 IKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHiKDQRPVKPgegpIGLIMAPTRELALQIYVECK 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  97 VAGQAMGVRVCVVSGGT---DQMVEsqkLMQRPHIVVAMPGRLADHLTGCDTfSFDNLK---YLVVDEADRMLNGDFDES 170
Cdd:cd17953 107 KFSKALGLRVVCVYGGSgisEQIAE---LKRGAEIVVCTPGRMIDILTANNG-RVTNLRrvtYVVLDEADRMFDMGFEPQ 182
                       170       180
                ....*....|....*....|.
gi 17136814 171 LSIIERCLPKTRQNLFFSATM 191
Cdd:cd17953 183 IMKIVNNIRPDRQTVLFSATF 203
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
18-191 1.08e-36

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: 135.14  E-value: 1.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH--------FALVLTPTHELAY 89
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddgpYALILAPTRELAQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  90 QISEQFLVAGQAMGVRVCVVSGGtdQMVESQ--KLMQRPHIVVAMPGRLAD----HLtgcdtFSFDNLKYLVVDEADRML 163
Cdd:cd17945  81 QIEEETQKFAKPLGIRVVSIVGG--HSIEEQafSLRNGCEILIATPGRLLDclerRL-----LVLNQCTYVVLDEADRMI 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17136814 164 NGDFDESLSIIERCLPKT--------------------RQNLFFSATM 191
Cdd:cd17945 154 DMGFEPQVTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATM 201
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
18-197 2.52e-36

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: 133.69  E-value: 2.52e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPV-----SHFALVLTPTHELAYQIS 92
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRElekgeGPIAVIVAPTRELAQQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  93 EQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTfSFDNLKYLVVDEADRMLNGDFDESL- 171
Cdd:cd17952  81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKAT-NLQRVTYLVLDEADRMFDMGFEYQVr 159
                       170       180
                ....*....|....*....|....*.
gi 17136814 172 SIIERCLPKtRQNLFFSATMKDFIKE 197
Cdd:cd17952 160 SIVGHVRPD-RQTLLFSATFKKKIEQ 184
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
31-197 3.45e-36

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: 134.78  E-value: 3.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  31 TPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEE-PVSHF---------------ALVLTPTHELAYQISEQ 94
Cdd:cd18051  45 TPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgPGESLpsesgyygrrkqyplALVLAPTRELASQIYDE 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  95 FLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDFDESL-SI 173
Cdd:cd18051 125 ARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLER-GKIGLDYCKYLVLDEADRMLDMGFEPQIrRI 203
                       170       180
                ....*....|....*....|....*..
gi 17136814 174 IERC-LPKT--RQNLFFSATmkdFIKE 197
Cdd:cd18051 204 VEQDtMPPTgeRQTLMFSAT---FPKE 227
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
18-190 5.48e-36

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: 132.49  E-value: 5.48e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH-----FALVLTPTHELAYQIS 92
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLErgdgpIVLVLAPTRELAQQIQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  93 EQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTfsfdNLK---YLVVDEADRMLNGDFDE 169
Cdd:cd17966  81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKT----NLRrvtYLVLDEADRMLDMGFEP 156
                       170       180
                ....*....|....*....|..
gi 17136814 170 SL-SIIERCLPKtRQNLFFSAT 190
Cdd:cd17966 157 QIrKIVDQIRPD-RQTLMWSAT 177
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
22-197 1.29e-35

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: 131.93  E-value: 1.29e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  22 LTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERL---SEEPVSH--FALVLTPTHELAYQISE--Q 94
Cdd:cd17960   5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGqvGALIISPTRELATQIYEvlQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  95 FLVAGQAMGVRVCVVSGGTDQMVESQKLM-QRPHIVVAMPGRLADHLT-GCDTFSFDNLKYLVVDEADRMLNGDFDESLS 172
Cdd:cd17960  85 SFLEHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSrKADKVKVKSLEVLVLDEADRLLDLGFEADLN 164
                       170       180
                ....*....|....*....|....*
gi 17136814 173 IIERCLPKTRQNLFFSATMKDFIKE 197
Cdd:cd17960 165 RILSKLPKQRRTGLFSATQTDAVEE 189
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
9-191 4.60e-34

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


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 127.56  E-value: 4.60e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELA 88
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  89 YQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDFD 168
Cdd:cd18046  81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINR-RYLRTDYIKMFVLDEADEMLSRGFK 159
                       170       180
                ....*....|....*....|...
gi 17136814 169 ESLSIIERCLPKTRQNLFFSATM 191
Cdd:cd18046 160 DQIYDIFQKLPPDTQVVLLSATM 182
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
9-194 2.69e-33

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: 125.51  E-value: 2.69e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSeepvshfALVLTPTHELA 88
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV-------ALILEPSRELA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  89 YQISEQFLVAGQAM---GVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHL-TGCDTFSfdNLKYLVVDEADRMLN 164
Cdd:cd17938  74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIkTGKLDLS--SVRFFVLDEADRLLS 151
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17136814 165 GDFDESLSIIERCLPKTR------QNLFFSATMKDF 194
Cdd:cd17938 152 QGNLETINRIYNRIPKITsdgkrlQVIVCSATLHSF 187
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
18-190 1.37e-31

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: 120.65  E-value: 1.37e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH------FALVLTPTHELAYQI 91
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPReqrngpGVLVLTPTRELALQI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  92 sEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADhLTGCDTFSFDNLKYLVVDEADRMLNGDFDESL 171
Cdd:cd17958  81 -EAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
                       170
                ....*....|....*....
gi 17136814 172 SIIERCLPKTRQNLFFSAT 190
Cdd:cd17958 159 RKILLDIRPDRQTIMTSAT 177
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
9-198 7.27e-31

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: 118.99  E-value: 7.27e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELA 88
Cdd:cd17950   4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  89 YQISEQFLVAGQAM-GVRVCVVSGGTDQMVESQKLMQR-PHIVVAMPGRLADhLTGCDTFSFDNLKYLVVDEADRMLngd 166
Cdd:cd17950  84 FQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDKML--- 159
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17136814 167 fdESLSI------IERCLPKTRQNLFFSATMKDFIKES 198
Cdd:cd17950 160 --EQLDMrrdvqeIFRATPHDKQVMMFSATLSKEIRPV 195
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
18-191 3.80e-30

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: 116.49  E-value: 3.80e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELAYQISEQFLV 97
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  98 AGQAM-GVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDFDESLSIIER 176
Cdd:cd17962  81 LMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQ-SSVELDNIKIVVVDEADTMLKMGFQQQVLDILE 159
                       170
                ....*....|....*
gi 17136814 177 CLPKTRQNLFFSATM 191
Cdd:cd17962 160 NISHDHQTILVSATI 174
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
239-346 1.09e-29

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: 112.30  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   239 IEALRKYREENENANVMIFTNTKKYCQLlSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDIP 318
Cdd:pfam00271   3 LEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
                          90       100
                  ....*....|....*....|....*...
gi 17136814   319 SVELVMNHMLPRTPKEYIHRVGRTARAG 346
Cdd:pfam00271  82 DVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
9-191 1.70e-27

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: 109.48  E-value: 1.70e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELA 88
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  89 YQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDFD 168
Cdd:cd18045  81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLNKGFK 159
                       170       180
                ....*....|....*....|...
gi 17136814 169 ESLSIIERCLPKTRQNLFFSATM 191
Cdd:cd18045 160 EQIYDVYRYLPPATQVVLVSATL 182
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
18-191 2.77e-27

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 109.76  E-value: 2.77e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPV-------SHFALVLTPTHELAYQ 90
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLlaegpfnAPRGLVITPSRELAEQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  91 ISEQFLVAGQAMGVRVCVVSGG--TDQMVESQklMQRPHIVVAMPGRLADhLTGCDTFSFDNLKYLVVDEADRMLNGDFD 168
Cdd:cd17948  81 IGSVAQSLTEGLGLKVKVITGGrtKRQIRNPH--FEEVDILVATPGALSK-LLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17136814 169 ESLS-IIERC------------LPKTRQNLFFSATM 191
Cdd:cd17948 158 EKLShFLRRFplasrrsentdgLDPGTQLVLVSATM 193
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
14-202 2.89e-27

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: 108.43  E-value: 2.89e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  14 LRPWLVKQLTKLGLKGATPIQQKCIPAILAG--QDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELAYQI 91
Cdd:cd17963   1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  92 SEQFLVAGQAMGVRVCVVSGGTDqmVESQKLMqRPHIVVAMPGRLADHltgCDTFSFD--NLKYLVVDEADRML--NGDF 167
Cdd:cd17963  81 GEVVEKMGKFTGVKVALAVPGND--VPRGKKI-TAQIVIGTPGTVLDW---LKKRQLDlkKIKILVLDEADVMLdtQGHG 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17136814 168 DESLSIIeRCLPKTRQNLFFSATMKDFIKE--SSIFP 202
Cdd:cd17963 155 DQSIRIK-RMLPRNCQILLFSATFPDSVRKfaEKIAP 190
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
18-197 2.53e-26

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: 107.02  E-value: 2.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  18 LVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSH-----FALVLTPTHELAYQIS 92
Cdd:cd18049  35 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLErgdgpICLVLAPTRELAQQVQ 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  93 EQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTgCDTFSFDNLKYLVVDEADRMLNGDFDESL- 171
Cdd:cd18049 115 QVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLE-AGKTNLRRCTYLVLDEADRMLDMGFEPQIr 193
                       170       180       190
                ....*....|....*....|....*....|....
gi 17136814 172 SIIERCLPKtRQNLFFSAT--------MKDFIKE 197
Cdd:cd18049 194 KIVDQIRPD-RQTLMWSATwpkevrqlAEDFLKD 226
HELICc smart00490
helicase superfamily c-terminal domain;
265-346 5.99e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 95.36  E-value: 5.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    265 QLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDIPSVELVMNHMLPRTPKEYIHRVGRTAR 344
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 17136814    345 AG 346
Cdd:smart00490  81 AG 82
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
27-190 3.20e-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: 99.31  E-value: 3.20e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  27 LKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPV-----SHFALVLTPTHELAYQISEQFLVAGQA 101
Cdd:cd18050  82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYlergdGPICLVLAPTRELAQQVQQVADDYGKS 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 102 MGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTfSFDNLKYLVVDEADRMLNGDFDESLSIIERCLPKT 181
Cdd:cd18050 162 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 240

                ....*....
gi 17136814 182 RQNLFFSAT 190
Cdd:cd18050 241 RQTLMWSAT 249
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1-492 6.19e-23

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 102.41  E-value: 6.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   1 MQRKEANPFQILGLRPWlvkqltklglkgatpiQQKCIPAILA-----GQDCIGAAKTGSGKTFAFALPILERLSEEPVs 75
Cdd:COG1061  68 LEAGDEASGTSFELRPY----------------QQEALEALLAalergGGRGLVVAPTGTGKTVLALALAAELLRGKRV- 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  76 hfaLVLTPTHELAYQISEQFLvagqamgvRVCVVSGGTDQMVESQKlmqrpHIVVAMPGRLADHLTGcDTFSfDNLKYLV 155
Cdd:COG1061 131 ---LVLVPRRELLEQWAEELR--------RFLGDPLAGGGKKDSDA-----PITVATYQSLARRAHL-DELG-DRFGLVI 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 156 VDEADRMLNGDFDEslsIIERCLPKTRqnLFFSAT---------------------------MKDFIKESSIFPIASDCF 208
Cdd:COG1061 193 IDEAHHAGAPSYRR---ILEAFPAAYR--LGLTATpfrsdgreillflfdgivyeyslkeaiEDGYLAPPEYYGIRVDLT 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 209 EWSQDSDVATvETLDQRYLLCADYDRDmVLIEALRKYREeneNANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQK 288
Cdd:COG1061 268 DERAEYDALS-ERLREALAADAERKDK-ILRELLREHPD---DRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKK 342
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 289 ERVAALSRFKSNQIRTLIATDVAARGLDIPSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISIF-----RFPRDLEL 363
Cdd:COG1061 343 EREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYdfvgnDVPVLEEL 422
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 364 LAAIEEEINTKLTEHPIDQRmVERIFMQVNVTRRESEMQLDNNDFDERAQNYRRKTWIMEGKDPDQMEALYRKKQKDKLR 443
Cdd:COG1061 423 AKDLRDLAGYRVEFLDEEES-EELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKA 501
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*....
gi 17136814 444 EIRRKRKLQHAEPAASEEGKALLQDERFKSVDSARFEKKGKGRSRATQE 492
Cdd:COG1061 502 EGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEE 550
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
19-195 6.67e-22

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: 93.76  E-value: 6.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  19 VKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPV------SHFALVLTPTHELAYQIS 92
Cdd:cd17944   2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQprkrgrAPKVLVLAPTRELANQVT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  93 EQFLVAGQAMgvRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGcDTFSFDNLKYLVVDEADRMLNGDFDESLS 172
Cdd:cd17944  82 KDFKDITRKL--SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQN-GRLDLTKLKHVVLDEVDQMLDMGFAEQVE 158
                       170       180
                ....*....|....*....|....*...
gi 17136814 173 IIERCLPKTR-----QNLFFSATMKDFI 195
Cdd:cd17944 159 EILSVSYKKDsednpQTLLFSATCPDWV 186
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
1-193 4.29e-20

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


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 89.31  E-value: 4.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   1 MQRKEANP------FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAG--QDCIGAAKTGSGKTFAFALPILERLSEE 72
Cdd:cd18048   6 LQRDPTSPlfsvksFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  73 PVSHFALVLTPTHELAYQISE------QFLVAGQAM-GVRVCVVSGGTDqmVESQklmqrphIVVAMPGRLADHLTGCDT 145
Cdd:cd18048  86 KLYPQCLCLSPTFELALQTGKvveemgKFCVGIQVIyAIRGNRPGKGTD--IEAQ-------IVIGTPGTVLDWCFKLRL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17136814 146 FSFDNLKYLVVDEADRMLN--GDFDESLSiIERCLPKTRQNLFFSATMKD 193
Cdd:cd18048 157 IDVTNISVFVLDEADVMINvqGHSDHSVR-VKRSMPKECQMLLFSATFED 205
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
13-159 4.69e-18

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: 87.58  E-value: 4.69e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  13 GLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPvSHFALVLTPTHELAY-QI 91
Cdd:COG1205  40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP-GATALYLYPTKALARdQL 118
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136814  92 SE-QFLVAGQAMGVRVCVVSGGTDQmVESQKLMQRPHIVVAMP-----GRLADHltgcDTFS--FDNLKYLVVDEA 159
Cdd:COG1205 119 RRlRELAEALGLGVRVATYDGDTPP-EERRWIREHPDIVLTNPdmlhyGLLPHH----TRWArfFRNLRYVVIDEA 189
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
9-195 2.54e-16

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: 77.84  E-value: 2.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   9 FQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAG--QDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHE 86
Cdd:cd18047   3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  87 LAYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLmqRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADRML--N 164
Cdd:cd18047  83 LALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKI--SEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIatQ 160
                       170       180       190
                ....*....|....*....|....*....|.
gi 17136814 165 GDFDESLSiIERCLPKTRQNLFFSATMKDFI 195
Cdd:cd18047 161 GHQDQSIR-IQRMLPRNCQMLLFSATFEDSV 190
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
44-190 3.24e-16

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: 75.52  E-value: 3.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  44 GQDCIGAAKTGSGKTFAFALPILERLSEEPVshFALVLTPTHELAYQISEQFLVAGQaMGVRVCVVSGGTDQMVESQKLM 123
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLKKGK--KVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKL 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136814 124 QRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADRMLNGDFDESLS--IIERCLPKTRQNLFFSAT 190
Cdd:cd00046  78 GDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILdlAVRKAGLKNAQVILLSAT 146
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
238-360 2.64e-15

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 79.00  E-value: 2.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 238 LIEALRKYREENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHG--------FMRQKERVAALSRFKSNQIRTLIATD 309
Cdd:COG1111 340 LREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVLVATS 419
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17136814 310 VAARGLDIPSVELVMNHMLPRTPKEYIHRVGRTARAGRKGMSISIFRFPRD 360
Cdd:COG1111 420 VAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGRVVVLIAKGTRD 470
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
31-196 1.10e-13

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: 70.87  E-value: 1.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  31 TPIQQKCIPAILagQDCIG------------------AAKTGSGKTFAFALPILERL-------------SEEPVSHFA- 78
Cdd:cd17965  32 SPIQTLAIKKLL--KTLMRkvtkqtsneepklevfllAAETGSGKTLAYLAPLLDYLkrqeqepfeeaeeEYESAKDTGr 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  79 ---LVLTPTHELAYQISEQFLVAGQAMGVRVCVVSGGTDQMV-ESQKLMQ-RPHIVVAMPGRLADhLTGCDTFSFDNLKY 153
Cdd:cd17965 110 prsVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYqRLQLAFKgRIDILVTTPGKLAS-LAKSRPKILSRVTH 188
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17136814 154 LVVDEADRMLNGDF-DESLSIIERcLPKTRQNLFFSATM-KDFIK 196
Cdd:cd17965 189 LVVDEADTLFDRSFlQDTTSIIKR-APKLKHLILCSATIpKEFDK 232
PRK13766 PRK13766
Hef nuclease; Provisional
238-349 7.51e-12

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 67.98  E-value: 7.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  238 LIEALRKYREENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHG--------FMRQKERVAALSRFKSNQIRTLIATD 309
Cdd:PRK13766 352 LREIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaskdgdkGMSQKEQIEILDKFRAGEFNVLVSTS 431
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 17136814  310 VAARGLDIPSVELVMnhMLPRTPKE--YIHRVGRTARaGRKG 349
Cdd:PRK13766 432 VAEEGLDIPSVDLVI--FYEPVPSEirSIQRKGRTGR-QEEG 470
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
34-159 7.82e-12

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: 64.14  E-value: 7.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  34 QQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHfALVLTPTHELAY-QISE--QFLVAGQAmGVRVCVVS 110
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSR-ALYLYPTKALAQdQLRSlrELLEQLGL-GIRVATYD 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17136814 111 GGTDQMVESQKLMQRPHIVVAMPGRLadHLT-----GCDTFSFDNLKYLVVDEA 159
Cdd:cd17923  83 GDTPREERRAIIRNPPRILLTNPDML--HYAllphhDRWARFLRNLRYVVLDEA 134
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
238-345 1.11e-11

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 62.61  E-value: 1.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 238 LIEALRKYREENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLH---------------GFMRQKERVAALSRFKSNQI 302
Cdd:cd18802  12 LIEILREYFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRcgfligrgnssqrkrSLMTQRKQKETLDKFRDGEL 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17136814 303 RTLIATDVAARGLDIPSVELVMNHMLPRTPKEYIHRVGRtARA 345
Cdd:cd18802  92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
14-159 1.32e-09

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 60.29  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  14 LRPWLVKQLTKLGLKGATPIQQKCIPA-ILAGQDCIGAAKTGSGKTFAFALPILERLSEepvSHFALVLTPTHELAYQIS 92
Cdd:COG1204   7 PLEKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLN---GGKALYIVPLRALASEKY 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136814  93 EQFLVAGQAMGVRVCVVSGGTDqmvESQKLMQRPHIVVAMPGRLaDHLTGCDTFSFDNLKYLVVDEA 159
Cdd:COG1204  84 REFKRDFEELGIKVGVSTGDYD---SDDEWLGRYDILVATPEKL-DSLLRNGPSWLRDVDLVVVDEA 146
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
237-349 1.64e-09

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 56.21  E-value: 1.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 237 VLIEALRKyREENENANVMIFTNTKKYCQLLSMTLKNMEiDNVCLHGF-----------MRQKERVAALSRFKSNQIRTL 305
Cdd:cd18801  17 IVKEHFKK-KQEGSDTRVIIFSEFRDSAEEIVNFLSKIR-PGIRATRFigqasgksskgMSQKEQKEVIEQFRKGGYNVL 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17136814 306 IATDVAARGLDIPSVELVMNHMLPRTPKEYIHRVGRTARaGRKG 349
Cdd:cd18801  95 VATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQG 137
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
44-158 2.44e-09

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: 56.44  E-value: 2.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  44 GQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALV-LTPTHELAYQISE--QFLVAGQAMGVRVCVVSGGTDQMVESQ 120
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLyISPLKALINDQERrlEEPLDEIDLEIPVAVRHGDTSQSEKAK 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17136814 121 KLMQRPHIVVAMPGRLADHLTGCDTFS-FDNLKYLVVDE 158
Cdd:cd17922  81 QLKNPPGILITTPESLELLLVNKKLRElFAGLRYVVVDE 119
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
31-190 4.75e-09

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 55.73  E-value: 4.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  31 TPIQQKCIPAILAGQD-CIGAAKTGSGKTFAFALPILERLSEEPVShfALVLTPTHELAYQISEQFLVAGQAMGVRVCVV 109
Cdd:cd17921   3 NPIQREALRALYLSGDsVLVSAPTSSGKTLIAELAILRALATSGGK--AVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 110 SGGTdqmVESQKLMQRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADRMLNGDFDESL-SIIERCL--PKTRQNLF 186
Cdd:cd17921  81 TGDP---SVNKLLLAEADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIGDGERGVVLeLLLSRLLriNKNARFVG 157

                ....
gi 17136814 187 FSAT 190
Cdd:cd17921 158 LSAT 161
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
242-354 1.47e-08

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


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 53.37  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 242 LRKYREENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDIPSVE 321
Cdd:cd18794  21 LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVR 100
                        90       100       110
                ....*....|....*....|....*....|....
gi 17136814 322 LVMNHMLPRTPKEYIHRVGrtaRAGRKGM-SISI 354
Cdd:cd18794 101 FVIHYSLPKSMESYYQESG---RAGRDGLpSECI 131
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
28-158 1.49e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 54.34  E-value: 1.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  28 KGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFA------LVLTPTHELAYQIS---EQFLVA 98
Cdd:COG1201  23 GAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRPGELpdglrvLYISPLKALANDIErnlRAPLEE 102
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  99 -GQAMG-----VRVCVVSGGTDQmveSQKLMQR---PHIVVAMPGRLADHLTGCDTFS-FDNLKYLVVDE 158
Cdd:COG1201 103 iGEAAGlplpeIRVGVRTGDTPA---SERQRQRrrpPHILITTPESLALLLTSPDARElLRGVRTVIVDE 169
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
53-190 1.41e-06

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 48.07  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  53 TGSGKTFaFALPILERLSEEPVshfaLVLTPTHELAYQISEQFLVAGqaMGVRVCVVSGGTDQMVESQKlmqrphIVVAM 132
Cdd:cd17926  27 TGSGKTL-TALALIAYLKELRT----LIVVPTDALLDQWKERFEDFL--GDSSIGLIGGGKKKDFDDAN------VVVAT 93
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17136814 133 PGRLADHL-TGCDTFSFDNLkyLVVDEADRmLNGDFDEslSIIERCLPKTRqnLFFSAT 190
Cdd:cd17926  94 YQSLSNLAeEEKDLFDQFGL--LIVDEAHH-LPAKTFS--EILKELNAKYR--LGLTAT 145
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
237-317 4.44e-06

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: 46.32  E-value: 4.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 237 VLIEALRKYREENENanVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQ--IRTLIATDVAARG 314
Cdd:cd18793  15 ALLELLEELREPGEK--VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVG 92

                ...
gi 17136814 315 LDI 317
Cdd:cd18793  93 LNL 95
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
299-346 1.31e-05

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: 43.46  E-value: 1.31e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17136814 299 SNQIRTLIATDVAARGLDIPSVELVMNHMLPRTPKEYIHRVGRTARAG 346
Cdd:cd18785  20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
232-357 1.83e-05

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 44.95  E-value: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 232 YDRDMVLIEALRKyreenenanVMIFTNTKK----YCQLLSMTLKNMEIDN--VCLHGFMRQKERVAALSRFKSNQIRTL 305
Cdd:cd18796  28 YAEVIFLLERHKS---------TLVFTNTRSqaerLAQRLRELCPDRVPPDfiALHHGSLSRELREEVEAALKRGDLKVV 98
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17136814 306 IATDVAARGLDIPSVELVMNHMLPRTPKEYIHRVGrtaRAGRKGMSISIFRF 357
Cdd:cd18796  99 VATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLG---RSGHRPGAASKGRL 147
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
287-349 2.02e-05

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 44.55  E-value: 2.02e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136814 287 QKERVAALSRFKSNQIRTLIATDVAARGLDIP--SVELVMN-HMLPRtpKEYIHRVGRTARAGRKG 349
Cdd:cd18789  80 QSEREEILQNFREGEYNTLVVSKVGDEGIDLPeaNVAIQISgHGGSR--RQEAQRLGRILRPKKGG 143
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
32-350 4.97e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 45.86  E-value: 4.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   32 PIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERlseepvSHFALVLTPTHELAYQISEQFLVAGQAMGvrvCVVSG 111
Cdd:PRK11057  28 PGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL------DGLTLVVSPLISLMKDQVDQLLANGVAAA---CLNST 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  112 GT-DQMVESQKLMQRPHI--VVAMPGRLA-----DHLTGCdtfsfdNLKYLVVDEAD--RMLNGDFD---ESLSIIERCL 178
Cdd:PRK11057  99 QTrEQQLEVMAGCRTGQIklLYIAPERLMmdnflEHLAHW------NPALLAVDEAHciSQWGHDFRpeyAALGQLRQRF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  179 PktrqNLFF---SATMKDFIKEssifpiasdcfewsqdsDVATVETLDQRYLLCADYDRDMV---LIEA------LRKYR 246
Cdd:PRK11057 173 P----TLPFmalTATADDTTRQ-----------------DIVRLLGLNDPLIQISSFDRPNIrytLVEKfkpldqLMRYV 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  247 EENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDIPSVELVMNH 326
Cdd:PRK11057 232 QEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHF 311
                        330       340
                 ....*....|....*....|....
gi 17136814  327 MLPRTPKEYIHrvgRTARAGRKGM 350
Cdd:PRK11057 312 DIPRNIESYYQ---ETGRAGRDGL 332
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
39-186 1.11e-04

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 43.19  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  39 PAILaGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFA--LVLTPTHELAYQISEQFLVAGQAMGVRVCVVSGGTDQM 116
Cdd:cd17927  13 PALK-GKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGkvVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSEN 91
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136814 117 VESQKLMQRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADRML-NGDFDESLSIIERCLPKTRQNLF 186
Cdd:cd17927  92 VSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHNTTkNHPYNEIMFRYLDQKLGSSGPLP 162
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
154-348 1.16e-04

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: 44.34  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 154 LVVDEADRMLngdfDESLSIIERCLPKTRQN----LFFSATMKDFIKESS------IFPIASDCFEWSQdsdvatvetld 223
Cdd:cd09639 127 LIFDEVHFYD----EYTLALILAVLEVLKDNdvpiLLMSATLPKFLKEYAekigyvEENEPLDLKPNER----------- 191
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 224 QRYLLCADydRDMVLIEAL-RKYREENENANVMIFTNTKKYCQLLSMTLK--NMEIDNVCLHGFMRQKERVAA----LSR 296
Cdd:cd09639 192 APFIKIES--DKVGEISSLeRLLEFIKKGGSVAIIVNTVDRAQEFYQQLKekGPEEEIMLIHSRFTEKDRAKKeaelLLE 269
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17136814 297 FKSNQIRTLIATDVAARGLDIpSVELVMNHMLPrtPKEYIHRVGRTARAGRK 348
Cdd:cd09639 270 FKKSEKFVIVATQVIEASLDI-SVDVMITELAP--IDSLIQRLGRLHRYGEK 318
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
32-159 3.09e-04

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 42.14  E-value: 3.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  32 PIQQKCIPAILAGQDCIGAAKTGSGKTFAFALP--ILERLseepvshfALVLTPTHELayqISEQflVAG-QAMGVRVCV 108
Cdd:cd17920  15 PGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV--------TLVVSPLISL---MQDQ--VDRlQQLGIRAAA 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136814 109 VSGGTD----QMVESQKLMQRPHIVVAMPGRLADhltgcDTF--------SFDNLKYLVVDEA 159
Cdd:cd17920  82 LNSTLSpeekREVLLRIKNGQYKLLYVTPERLLS-----PDFlellqrlpERKRLALIVVDEA 139
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
282-359 1.52e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.45  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   282 HGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDIPSVELVMNHMLPRTPKEYIHRVGrtaRAGRK--GMSISIFrFPR 359
Cdd:PRK09751  308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIG---RAGHQvgGVSKGLF-FPR 383
ResIII pfam04851
Type III restriction enzyme, res subunit;
34-190 1.87e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 39.19  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814    34 QQKCIPAILAGQD------CIGAAkTGSGKTFAFALPILERLSEEPVSHFaLVLTPTHELAYQISEQFLVAGQAMGVRVC 107
Cdd:pfam04851   8 QIEAIENLLESIKngqkrgLIVMA-TGSGKTLTAAKLIARLFKKGPIKKV-LFLVPRKDLLEQALEEFKKFLPNYVEIGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814   108 VVSGGTDQMVESQKlmqrpHIVVAMPGRLADHLTGCDT-FSFDNLKYLVVDEADRmLNGDFDESlsiIERCLPKTRQnLF 186
Cdd:pfam04851  86 IISGDKKDESVDDN-----KIVVTTIQSLYKALELASLeLLPDFFDVIIIDEAHR-SGASSYRN---ILEYFKPAFL-LG 155

                  ....
gi 17136814   187 FSAT 190
Cdd:pfam04851 156 LTAT 159
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
32-192 2.22e-03

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 39.24  E-value: 2.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  32 PIQQKCIPA-ILAGQDCIGAAKTGSGKTFAFALPILERLSEepvSHFALVLTPTHELAYQISEQFlVAGQAMGVRVCVVS 110
Cdd:cd18028   4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLE---GGKALYLVPLRALASEKYEEF-KKLEEIGLKVGIST 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 111 GGTDqmvESQKLMQRPHIVVAMPGRLaDHLTGCDTFSFDNLKYLVVDE---ADRMLNGDFDESLSIIERCLPKTRQNLFF 187
Cdd:cd18028  80 GDYD---EDDEWLGDYDIIVATYEKF-DSLLRHSPSWLRDVGVVVVDEihlISDEERGPTLESIVARLRRLNPNTQIIGL 155

                ....*
gi 17136814 188 SATMK 192
Cdd:cd18028 156 SATIG 160
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
238-344 3.56e-03

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 38.38  E-value: 3.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814 238 LIEALRKYREENENanVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDI 317
Cdd:cd18790  16 LLGEIRKRVARGER--VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDL 93
                        90       100       110
                ....*....|....*....|....*....|..
gi 17136814 318 PSVELVM-----NHMLPRTPKEYIHRVGRTAR 344
Cdd:cd18790  94 PEVSLVAildadKEGFLRSETSLIQTIGRAAR 125
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
39-158 6.91e-03

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 37.88  E-value: 6.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136814  39 PAIlAGQDCIGAAKTGSGKTFAfALPILE-RLSEEPVSHFALVL-----TPTHELAYQI-SEQFlvagQAMGVRVCVVSG 111
Cdd:cd18073  13 PAM-KGKNTIICAPTGCGKTFV-SLLICEhHLKKFPQGQKGKVVffatkVPVYEQQKSVfSKYF----ERHGYRVTGISG 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17136814 112 GTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDE 158
Cdd:cd18073  87 ATAENVPVEQIIENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDE 133
 
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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