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Conserved domains on  [gi|148231835|ref|NP_001079623|]
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DEAD-box helicase 39A S homeolog [Xenopus laevis]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13028696)

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

CATH:  1.20.1320.20|3.40.50.300
EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0004386|GO:0005524
PubMed:  20206133|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 43-250 3.21e-160

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: 449.87  E-value: 3.21e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  43 SSGFRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTR 122
Cdd:cd17950    1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 123 ELAFQISKEYERFSKYMPTVKVAVFFGGLSIKKDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLE 202
Cdd:cd17950   81 ELAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148231835 203 QLDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFV 250
Cdd:cd17950  161 QLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 261-390 1.41e-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: 169.61  E-value: 1.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 261 LQQYYVKLKDSEKNRKLF-DLLDVLEFNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRI 339
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148231835 340 LVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFV 390
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 43-250 3.21e-160

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: 449.87  E-value: 3.21e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  43 SSGFRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTR 122
Cdd:cd17950    1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 123 ELAFQISKEYERFSKYMPTVKVAVFFGGLSIKKDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLE 202
Cdd:cd17950   81 ELAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148231835 203 QLDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFV 250
Cdd:cd17950  161 QLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
46-398 1.68e-127

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 374.87  E-value: 1.68e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEA-VEGQVSVLVMCHTREL 124
Cdd:COG0513    4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPTREL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 125 AFQISKEYERFSKYMPtVKVAVFFGGLSIKKDEDTIRKScPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLeql 204
Cdd:COG0513   84 ALQVAEELRKLAKYLG-LRVATVYGGVSIGRQIRALKRG-VDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML--- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 205 DM--RRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFVDDETKlTLHGLQQYYVKLKDSEKNRKLFDLLD 282
Cdd:COG0513  159 DMgfIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENA-TAETIEQRYYLVDKRDKLELLRRLLR 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 283 VLEFNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYD 362
Cdd:COG0513  238 DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYD 317

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 148231835 363 MPEDSDTYLHRVARAGRFGTKGLAITFVSDEEDAKI 398
Cdd:COG0513  318 LPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLL 353
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 51-414 2.61e-82

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 260.12  E-value: 2.61e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  51 LKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELAFQISK 130
Cdd:PRK11776  11 LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 131 EYERFSKYMPTVKVAVFFGGLSIKKDEDTIRKScPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMleqLDM--RR 208
Cdd:PRK11776  91 EIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHG-AHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM---LDMgfQD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 209 DVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFVDDETKLTlhGLQQYYVKLKDSEKNRKLFDLLDVLEFNQ 288
Cdd:PRK11776 167 AIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLP--AIEQRFYEVSPDERLPALQRLLLHHQPES 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 289 VVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSD 368
Cdd:PRK11776 245 CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPE 324

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 148231835 369 TYLHRVARAGRFGTKGLAITFVSDEEDAKI--LNDVQDRfEVNVGELP 414
Cdd:PRK11776 325 VHVHRIGRTGRAGSKGLALSLVAPEEMQRAnaIEDYLGR-KLNWEPLP 371
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 261-390 1.41e-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: 169.61  E-value: 1.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 261 LQQYYVKLKDSEKNRKLF-DLLDVLEFNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRI 339
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148231835 340 LVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFV 390
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 68-235 3.93e-46

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: 156.63  E-value: 3.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835   68 SEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELAFQISKEYERFSKYMPtVKVAVF 147
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLG-LKVASL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  148 FGGLSIKKDEDTIRKscPHIVVGTPGRILALVRSKILnLKNVKHFVLDECDKMLEQlDMRRDVQEIFRLTPHEKQCMMFS 227
Cdd:pfam00270  80 LGGDSRKEQLEKLKG--PDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDM-GFGPDLEEILRRLPKKRQILLLS 155


                  ....*...
gi 148231835  228 ATLSKEIR 235
Cdd:pfam00270 156 ATLPRNLE 163
DEXDc smart00487
DEAD-like helicases superfamily;
59-264 4.10e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 155.34  E-value: 4.10e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835    59 IVDCGFEHPSEVQHECIPQAILG-MDILCQAKSGMGKTAVFVLATLQQIEAVEGQvSVLVMCHTRELAFQISKEYERFSK 137
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG-RVLVLVPTRELAEQWAEELKKLGP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835   138 YMPtVKVAVFFGGLSIKKDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEQlDMRRDVQEIFRLT 217
Cdd:smart00487  80 SLG-LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDG-GFGDQLEKLLKLL 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 148231835   218 PHEKQCMMFSATLSKEIRPVCRKFMQDPMEVfvdDETKLTLHGLQQY 264
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDPVFI---DVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 272-381 5.06e-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: 109.22  E-value: 5.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  272 EKNRKLFDLLDVLEFNQVVIFVKSVQRCMAlAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMD 351
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 148231835  352 IERVNIVFNYDMPEDSDTYLHRVARAGRFG 381
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
302-381 2.74e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 93.05  E-value: 2.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835   302 LAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFG 381
Cdd:smart00490   3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
266-399 5.17e-11

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 64.39  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 266 VKLKDSEKNRKLFDLLDVLEFNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNL 345
Cdd:COG0514  210 VPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIA 289

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148231835 346 FGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSdEEDAKIL 399
Cdd:COG0514  290 FGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYG-PEDVAIQ 342
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 290-389 9.79e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 44.70  E-value: 9.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 290 VIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERlSRYQQfkDFQR---RILVATNLFGRGMDIERVNIVFNYDMPED 366
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVR-ADVQE--AFQRddlQIVVATVAFGMGINKPNVRFVVHFDIPRN 316

                         90       100
                 ....*....|....*....|...
gi 148231835 367 SDTYLHRVARAGRFGTKGLAITF 389
Cdd:PRK11057 317 IESYYQETGRAGRDGLPAEAMLF 339
 
Name Accession Description Interval E-value
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 43-250 3.21e-160

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: 449.87  E-value: 3.21e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  43 SSGFRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTR 122
Cdd:cd17950    1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 123 ELAFQISKEYERFSKYMPTVKVAVFFGGLSIKKDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLE 202
Cdd:cd17950   81 ELAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148231835 203 QLDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFV 250
Cdd:cd17950  161 QLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
46-398 1.68e-127

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 374.87  E-value: 1.68e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEA-VEGQVSVLVMCHTREL 124
Cdd:COG0513    4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPTREL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 125 AFQISKEYERFSKYMPtVKVAVFFGGLSIKKDEDTIRKScPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLeql 204
Cdd:COG0513   84 ALQVAEELRKLAKYLG-LRVATVYGGVSIGRQIRALKRG-VDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML--- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 205 DM--RRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFVDDETKlTLHGLQQYYVKLKDSEKNRKLFDLLD 282
Cdd:COG0513  159 DMgfIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENA-TAETIEQRYYLVDKRDKLELLRRLLR 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 283 VLEFNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYD 362
Cdd:COG0513  238 DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYD 317

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 148231835 363 MPEDSDTYLHRVARAGRFGTKGLAITFVSDEEDAKI 398
Cdd:COG0513  318 LPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLL 353
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 51-414 2.61e-82

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 260.12  E-value: 2.61e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  51 LKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELAFQISK 130
Cdd:PRK11776  11 LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 131 EYERFSKYMPTVKVAVFFGGLSIKKDEDTIRKScPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMleqLDM--RR 208
Cdd:PRK11776  91 EIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHG-AHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM---LDMgfQD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 209 DVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFVDDETKLTlhGLQQYYVKLKDSEKNRKLFDLLDVLEFNQ 288
Cdd:PRK11776 167 AIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLP--AIEQRFYEVSPDERLPALQRLLLHHQPES 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 289 VVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSD 368
Cdd:PRK11776 245 CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPE 324

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 148231835 369 TYLHRVARAGRFGTKGLAITFVSDEEDAKI--LNDVQDRfEVNVGELP 414
Cdd:PRK11776 325 VHVHRIGRTGRAGSKGLALSLVAPEEMQRAnaIEDYLGR-KLNWEPLP 371
PTZ00424 PTZ00424
helicase 45; Provisional
 33-417 6.27e-80

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 252.44  E-value: 6.27e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  33 EVKGSYVSIHSSgFRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQ 112
Cdd:PTZ00424  18 TIESNYDEIVDS-FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 113 VSVLVMCHTRELAFQISKEYERFSKYMpTVKVAVFFGGLSIKKDEDTIrKSCPHIVVGTPGRILALVRSKILNLKNVKHF 192
Cdd:PTZ00424  97 CQALILAPTRELAQQIQKVVLALGDYL-KVRCHACVGGTVVRDDINKL-KAGVHMVVGTPGRVYDMIDKRHLRVDDLKLF 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 193 VLDECDKMLEQlDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFVDDEtKLTLHGLQQYYVKL-KDS 271
Cdd:PTZ00424 175 ILDEADEMLSR-GFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKD-ELTLEGIRQFYVAVeKEE 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 272 EKNRKLFDLLDVLEFNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMD 351
Cdd:PTZ00424 253 WKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGID 332

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148231835 352 IERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDeEDAKILNDVQDRFEVNVGELPDEI 417
Cdd:PTZ00424 333 VQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTP-DDIEQLKEIERHYNTQIEEMPMEV 397
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 46-415 7.11e-77

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 250.92  E-value: 7.11e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELA 125
Cdd:PRK11634   8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 126 FQISKEYERFSKYMPTVKVAVFFGGLSIKKDEDTIRKScPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLeQLD 205
Cdd:PRK11634  88 VQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQG-PQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEML-RMG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 206 MRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFVDDETKlTLHGLQQYYVKLKDSEKNRKLFDLLDVLE 285
Cdd:PRK11634 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVT-TRPDISQSYWTVWGMRKNEALVRFLEAED 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 286 FNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPE 365
Cdd:PRK11634 245 FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148231835 366 DSDTYLHRVARAGRFGTKGLAITFVSDEEdAKILNDVQDRFEVNVGE--LPD 415
Cdd:PRK11634 325 DSESYVHRIGRTGRAGRAGRALLFVENRE-RRLLRNIERTMKLTIPEveLPN 375
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 55-248 2.91e-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: 230.41  E-value: 2.91e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVE----GQVSVLVMCHTRELAFQISK 130
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 131 EYERFSKYMPtVKVAVFFGGLSIKKDEDTIRKsCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEqLDMRRDV 210
Cdd:cd00268   81 VARKLGKGTG-LKVAAIYGGAPIKKQIEALKK-GPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLD-MGFEEDV 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148231835 211 QEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd00268  158 EKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 46-390 1.01e-64

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 213.65  E-value: 1.01e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI----EAVEGQVSVLVMCHT 121
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfpRRKSGPPRILILTPT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 122 RELAFQISKEYERFSKYMpTVKVAVFFGGLSIKKDEDTIRKScPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKML 201
Cdd:PRK11192  83 RELAMQVADQARELAKHT-HLDIATITGGVAYMNHAEVFSEN-QDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 202 eqlDM--RRDVQEIFRLTPHEKQCMMFSATL-SKEIRPVCRKFMQDPMEVFVD---DETKltlhGLQQYYVKLKDSEKNR 275
Cdd:PRK11192 161 ---DMgfAQDIETIAAETRWRKQTLLFSATLeGDAVQDFAERLLNDPVEVEAEpsrRERK----KIHQWYYRADDLEHKT 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 276 KLfdLLDVLEFNQV---VIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDI 352
Cdd:PRK11192 234 AL--LCHLLKQPEVtrsIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDI 311

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 148231835 353 ERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFV 390
Cdd:PRK11192 312 DDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLV 349
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 44-396 3.17e-60

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 203.22  E-value: 3.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  44 SGFRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI-------EAVEGQVSVL 116
Cdd:PRK01297  87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtpppkERYMGEPRAL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 117 VMCHTRELAFQISKEYERFSKYMpTVKVAVFFGGLSIKKDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDE 196
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKYT-GLNVMTFVGGMDFDKQLKQLEARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 197 CDKMLEqLDMRRDVQEIFRLTPH--EKQCMMFSATLSKEIRPVCRKFMQDPMEVFVDDETKlTLHGLQQYYVKLKDSEKN 274
Cdd:PRK01297 246 ADRMLD-MGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENV-ASDTVEQHVYAVAGSDKY 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 275 RKLFDLLDVLEFNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIER 354
Cdd:PRK01297 324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 148231835 355 VNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSdEEDA 396
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAG-EDDA 444
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 46-248 1.31e-59

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: 192.90  E-value: 1.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELA 125
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 126 FQISKEYERFSKYMpTVKVAVFFGGLSIKkdEDTIRKSCP-HIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEQl 204
Cdd:cd17940   81 LQTSQVCKELGKHM-GVKVMVTTGGTSLR--DDIMRLYQTvHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQ- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148231835 205 DMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd17940  157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 51-403 2.41e-59

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 200.42  E-value: 2.41e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  51 LKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQ------VSVLVMCHTREL 124
Cdd:PRK10590   8 LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALILTPTREL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 125 AFQISKEYERFSKYMPtVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLeql 204
Cdd:PRK10590  88 AAQIGENVRDYSKYLN-IRSLVVFGGVSINPQMMKLRGGV-DVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML--- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 205 DMR--RDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFVDDETKLTLHGLQqyYVKLKDSEKNRKLF-DLL 281
Cdd:PRK10590 163 DMGfiHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQ--HVHFVDKKRKRELLsQMI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 282 DVLEFNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNY 361
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 148231835 362 DMPEDSDTYLHRVARAGRFGTKGLAITFVSDEEDaKILNDVQ 403
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEH-KLLRDIE 361
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 46-393 8.98e-57

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 192.49  E-value: 8.98e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLAT---LQQIEAVEG----QVSVLVM 118
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATfhyLLSHPAPEDrkvnQPRALIM 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 119 CHTRELAFQISKEYERFSKyMPTVKVAVFFGGLSIKKDEDTIRKScPHIVVGTPGRILALVRSKILNLKNVKHFVLDECD 198
Cdd:PRK04837  90 APTRELAVQIHADAEPLAQ-ATGLKLGLAYGGDGYDKQLKVLESG-VDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 199 KMLEqLDMRRDVQEIFRLTPHEKQ--CMMFSATLSKEIRPVCRKFMQDPMEVFVDDETKlTLHGLQQYyvklkdseknrk 276
Cdd:PRK04837 168 RMFD-LGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQK-TGHRIKEE------------ 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 277 lfdlldvlefnqvvIFVKSVQRCMALAQLLIEQNFPAIAI--------------------HR------NMSQEERLSRYQ 330
Cdd:PRK04837 234 --------------LFYPSNEEKMRLLQTLIEEEWPDRAIifantkhrceeiwghlaadgHRvglltgDVAQKKRLRILE 299

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148231835 331 QFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDE 393
Cdd:PRK04837 300 EFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 362
PTZ00110 PTZ00110
helicase; Provisional
 4-391 1.64e-55

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 192.30  E-value: 1.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835   4 QDVENelLDYEEDDEPQAPAETAVpIARKEVKGSYVSIHSSGFRDFLLKpellrSIVDCGFEHPSEVQHECIPQAILGMD 83
Cdd:PTZ00110  98 PEVSA--LSSKEVDEIRKEKEITI-IAGENVPKPVVSFEYTSFPDYILK-----SLKNAGFTEPTPIQVQGWPIALSGRD 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  84 ILCQAKSGMGKTAVFVLATLQQIEAV------EGQVsVLVMCHTRELAFQISKEYERFSKyMPTVKVAVFFGGLSIKKDE 157
Cdd:PTZ00110 170 MIGIAETGSGKTLAFLLPAIVHINAQpllrygDGPI-VLVLAPTRELAEQIREQCNKFGA-SSKIRNTVAYGGVPKRGQI 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 158 DTIRKSCpHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLE---QLDMRRDVQEIfrlTPhEKQCMMFSATLSKEI 234
Cdd:PTZ00110 248 YALRRGV-EILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDmgfEPQIRKIVSQI---RP-DRQTLMWSATWPKEV 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 235 ----RPVCRkfmQDPMEVFVDDETKLTLHGLQQYYVKLKDSEKNRKLFDLLDVL--EFNQVVIFVKSVQRCMALAQLLIE 308
Cdd:PTZ00110 323 qslaRDLCK---EEPVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRImrDGDKILIFVETKKGADFLTKELRL 399

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 309 QNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAIT 388
Cdd:PTZ00110 400 DGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYT 479


                 ...
gi 148231835 389 FVS 391
Cdd:PTZ00110 480 FLT 482
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 48-249 2.25e-53

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: 176.75  E-value: 2.25e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  48 DFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELAFQ 127
Cdd:cd17939    1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 128 ISKEYERFSKYMpTVKVAVFFGGLSIkKDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEQlDMR 207
Cdd:cd17939   81 IQKVVKALGDYM-GVKVHACIGGTSV-REDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSR-GFK 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148231835 208 RDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVF 249
Cdd:cd17939  158 DQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 261-390 1.41e-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: 169.61  E-value: 1.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 261 LQQYYVKLKDSEKNRKLF-DLLDVLEFNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRI 339
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148231835 340 LVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFV 390
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 46-425 3.60e-51

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 181.30  E-value: 3.60e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVS-------VLVM 118
Cdd:PRK04537  11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADrkpedprALIL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 119 CHTRELAFQISKEYERFSKYMpTVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRILALVRS-KILNLKNVKHFVLDEC 197
Cdd:PRK04537  91 APTRELAIQIHKDAVKFGADL-GLRFALVYGGVDYDKQRELLQQGV-DVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 198 DKMLEqLDMRRDVQEIFRLTPHE--KQCMMFSATLSKEIRPVCRKFMQDPMEVFVDDETKLTLHGLQQYYVKlKDSEKNR 275
Cdd:PRK04537 169 DRMFD-LGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFP-ADEEKQT 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 276 KLFDLLDVLEFNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERV 355
Cdd:PRK04537 247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 356 NIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSdeedakilndvqDRFEVNvgeLPdeiDISTYIEQ 425
Cdd:PRK04537 327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFAC------------ERYAMS---LP---DIEAYIEQ 378
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 55-248 4.05e-51

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: 170.52  E-value: 4.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELAFQISKEYER 134
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 135 FSKYMPTVKVAVFFGGLSIKKDEDTIRksCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEQlDMRRDVQEIF 214
Cdd:cd17943   81 IGKKLEGLKCEVFIGGTPVKEDKKKLK--GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEG-SFQKDVNWIF 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 148231835 215 RLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd17943  158 SSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 46-248 1.52e-48

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: 164.16  E-value: 1.52e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELA 125
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 126 FQISKEYERFSKYMpTVKVAVFFGGLSIKKDEDTIRkSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEQlD 205
Cdd:cd18046   81 QQIQKVVMALGDYM-GIKCHACIGGTSVRDDAQKLQ-AGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSR-G 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148231835 206 MRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd18046  158 FKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 51-242 1.30e-47

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: 161.98  E-value: 1.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  51 LKPELLRSIVDCGFEHPSEVQHECIPQAI-LGMDILCQAKSGMGKTAVFVLATLQ-----QIEAVEGQVSVLVMCHTREL 124
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQsllntKPAGRRSGVSALIISPTREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 125 AFQISKEYERFSKYMPTVKVAVFFGGLSIKKDEDTIRKSCPHIVVGTPGRILALVR--SKILNLKNVKHFVLDECDKMle 202
Cdd:cd17964   81 ALQIAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRL-- 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 148231835 203 qLDM--RRDVQEIFRLTPHEK----QCMMFSATLSKEIRPVCRKFM 242
Cdd:cd17964  159 -LDMgfRPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTL 203
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 46-248 4.68e-47

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: 160.56  E-value: 4.68e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELA 125
Cdd:cd17954    2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 126 FQISKEYERFSKyMPTVKVAVFFGGLSIKKDEDTIRKScPHIVVGTPGRIL-ALVRSKILNLKNVKHFVLDECDKMLEqL 204
Cdd:cd17954   82 QQISEQFEALGS-SIGLKSAVLVGGMDMMAQAIALAKK-PHVIVATPGRLVdHLENTKGFSLKSLKFLVMDEADRLLN-M 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148231835 205 DMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd17954  159 DFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 34-396 6.93e-47

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 168.43  E-value: 6.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  34 VKGSYVSIHSSGFRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQV 113
Cdd:PLN00206 111 VKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGH 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 114 S-------VLVMCHTRELAFQISKEYERFSKYMPtVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRILALVRSKILNL 186
Cdd:PLN00206 191 PseqrnplAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQGV-ELIVGTPGRLIDLLSKHDIEL 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 187 KNVKHFVLDECDKMLEQlDMRRDVQEIFRLTPhEKQCMMFSATLSKEIRPVCRKFMQDPMEVFVDDETKLTlHGLQQYYV 266
Cdd:PLN00206 269 DNVSVLVLDEVDCMLER-GFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPN-KAVKQLAI 345

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 267 KLKDSEKNRKLFDLLDVLEFNQ--VVIFVKSVQRCMALAQLL-IEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVAT 343
Cdd:PLN00206 346 WVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVAT 425

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148231835 344 NLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDEEDA 396
Cdd:PLN00206 426 GVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRN 478
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 68-235 3.93e-46

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: 156.63  E-value: 3.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835   68 SEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELAFQISKEYERFSKYMPtVKVAVF 147
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLG-LKVASL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  148 FGGLSIKKDEDTIRKscPHIVVGTPGRILALVRSKILnLKNVKHFVLDECDKMLEQlDMRRDVQEIFRLTPHEKQCMMFS 227
Cdd:pfam00270  80 LGGDSRKEQLEKLKG--PDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDM-GFGPDLEEILRRLPKKRQILLLS 155


                  ....*...
gi 148231835  228 ATLSKEIR 235
Cdd:pfam00270 156 ATLPRNLE 163
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 46-247 1.82e-45

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: 156.23  E-value: 1.82e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELA 125
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 126 FQISKEYERFSKYMpTVKVAVFFGGLSIKKDEDTIRKsCPHIVVGTPGRILALVRS---KILNLKNVKHFVLDECDKMLE 202
Cdd:cd17955   81 YQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSK-RPHIVVATPGRLADHLRSsddTTKVLSRVKFLVLDEADRLLT 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 148231835 203 QlDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPME 247
Cdd:cd17955  159 G-SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 55-249 2.07e-45

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: 155.88  E-value: 2.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI---EAVEGQVSVLVMCHTRELAFQISKE 131
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 132 YERFSKYMPtVKVAVFFGGLSIKKDEDTIRkSCPHIVVGTPGRILALVR-SKILNLKNVKHFVLDECDKMLEqLDMRRDV 210
Cdd:cd17947   81 LQQLAQFTD-ITFALAVGGLSLKAQEAALR-ARPDIVIATPGRLIDHLRnSPSFDLDSIEILVLDEADRMLE-EGFADEL 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 148231835 211 QEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVF 249
Cdd:cd17947  158 KEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
DEXDc smart00487
DEAD-like helicases superfamily;
59-264 4.10e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 155.34  E-value: 4.10e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835    59 IVDCGFEHPSEVQHECIPQAILG-MDILCQAKSGMGKTAVFVLATLQQIEAVEGQvSVLVMCHTRELAFQISKEYERFSK 137
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG-RVLVLVPTRELAEQWAEELKKLGP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835   138 YMPtVKVAVFFGGLSIKKDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEQlDMRRDVQEIFRLT 217
Cdd:smart00487  80 SLG-LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDG-GFGDQLEKLLKLL 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 148231835   218 PHEKQCMMFSATLSKEIRPVCRKFMQDPMEVfvdDETKLTLHGLQQY 264
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDPVFI---DVGFTPLEPIEQF 201
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 51-248 4.94e-45

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: 154.66  E-value: 4.94e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  51 LKPELLRSIVDCGFEHPSEVQHECIPqAILG---MDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELAFQ 127
Cdd:cd17963    1 LKPELLKGLYAMGFNKPSKIQETALP-LILSdppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 128 ISKEYERFSKYmPTVKVAvffggLSIK-KDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEQLDM 206
Cdd:cd17963   80 IGEVVEKMGKF-TGVKVA-----LAVPgNDVPRGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTQGH 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148231835 207 RRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd17963  154 GDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 46-248 1.20e-40

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


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 143.62  E-value: 1.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAvegqvsvLVMCHTRELA 125
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVVA-------LILEPSRELA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 126 FQISKEYERFSKYM--PTVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEQ 203
Cdd:cd17938   74 EQTYNCIENFKKYLdnPKLRVALLIGGVKAREQLKRLESGV-DIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQ 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148231835 204 lDMRRDVQEIFRLTPHEK------QCMMFSATL-SKEIRPVCRKFMQDPMEV 248
Cdd:cd17938  153 -GNLETINRIYNRIPKITsdgkrlQVIVCSATLhSFEVKKLADKIMHFPTWV 203
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 46-248 7.52e-40

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: 141.45  E-value: 7.52e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELA 125
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 126 FQISKEYERFSKYMpTVKVAVFFGGLSIkkdEDTIRK--SCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEQ 203
Cdd:cd18045   81 VQIQKVLLALGDYM-NVQCHACIGGTSV---GDDIRKldYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNK 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 148231835 204 lDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd18045  157 -GFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 51-244 1.70e-39

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: 141.09  E-value: 1.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  51 LKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI--------EAVEGQV--SVLVMCH 120
Cdd:cd17967    7 LRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvGRGRRKAypSALILAP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 121 TRELAFQISKEYERFSKYMPtVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRILALV-RSKIlNLKNVKHFVLDECDK 199
Cdd:cd17967   87 TRELAIQIYEEARKFSYRSG-VRSVVVYGGADVVHQQLQLLRGC-DILVATPGRLVDFIeRGRI-SLSSIKFLVLDEADR 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148231835 200 MLEQ---LDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQD 244
Cdd:cd17967  164 MLDMgfePQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKN 211
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 51-245 1.36e-38

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: 138.10  E-value: 1.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  51 LKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI------EAVEGQVSVLVMCHTREL 124
Cdd:cd17961    1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 125 AFQISKEYERFSKYM-PTVKVAVFFGGLSIkKDEDTIRKSCPHIVVGTPGRILALVRSK-ILNLKNVKHFVLDECDKML- 201
Cdd:cd17961   81 AQQVSKVLEQLTAYCrKDVRVVNLSASSSD-SVQRALLAEKPDIVVSTPARLLSHLESGsLLLLSTLKYLVIDEADLVLs 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 148231835 202 ---EQldmrrDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDP 245
Cdd:cd17961  160 ygyEE-----DLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 55-250 2.08e-38

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: 137.34  E-value: 2.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEA--VEGQVSVLVMCHTRELAFQISKEY 132
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKprKKKGLRALILAPTRELASQIYREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 133 ERFSKYMPtVKVAVFFGGLSIKKDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEQLdMRRDVQE 212
Cdd:cd17957   81 LKLSKGTG-LRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPG-FREQTDE 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 148231835 213 IFR-LTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFV 250
Cdd:cd17957  159 ILAaCTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 44-245 3.92e-37

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: 134.35  E-value: 3.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  44 SGFRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSV--LVMCHT 121
Cdd:cd17959    1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGAraLILSPT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 122 RELAFQISKEYERFSKYMpTVKVAVFFGGLSIkKDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKML 201
Cdd:cd17959   81 RELALQTLKVTKELGKFT-DLRTALLVGGDSL-EEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148231835 202 EqLDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDP 245
Cdd:cd17959  159 E-MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEP 201
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 55-248 4.07e-35

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: 128.69  E-value: 4.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATL------QQIEAVEGQVsVLVMCHTRELAFQI 128
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvhimdqRELEKGEGPI-AVIVAPTRELAQQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 129 SKEYERFSKYMpTVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEqLDMRR 208
Cdd:cd17952   80 YLEAKKFGKAY-NLRVVAVYGGGSKWEQAKALQEGA-EIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFD-MGFEY 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 148231835 209 DVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd17952  157 QVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 55-232 2.23e-34

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: 127.74  E-value: 2.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAIL-GMDILCQAKSGMGKTAVF-------VLATLQQIEAVEGQ--VSVLVMCHTREL 124
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFgipilerLLSQKSSNGVGGKQkpLRALILTPTREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 125 AFQISKEYERFSKYmPTVKVAVFFGGLSIKKDEDTIRKsCPHIVVGTPGRILALVRSK---ILNLKNVKHFVLDECDKML 201
Cdd:cd17946   81 AVQVKDHLKAIAKY-TNIKIASIVGGLAVQKQERLLKK-RPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRML 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148231835 202 EQLDMrRDVQEIFRLTP-------HEKQCMMFSATLSK 232
Cdd:cd17946  159 EKGHF-AELEKILELLNkdragkkRKRQTFVFSATLTL 195
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 55-248 6.99e-34

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: 126.28  E-value: 6.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVS--------VLVMCHTRELAF 126
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEetkddgpyALILAPTRELAQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 127 QISKEYERFSKYMPtVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKM------ 200
Cdd:cd17945   81 QIEEETQKFAKPLG-IRVVSIVGGHSIEEQAFSLRNGC-EILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMidmgfe 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148231835 201 ------LEQLD---MRRDVQEIFRLTPHEK----QCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd17945  159 pqvtkiLDAMPvsnKKPDTEEAEKLAASGKhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 33-242 8.23e-34

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: 127.39  E-value: 8.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  33 EVKGSYVSIHSSGFRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI--EAVE 110
Cdd:cd18052   32 EVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkEGLT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 111 GQVS-------VLVMCHTRELAFQISKEYERFSkYMPTVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRILALV-RSK 182
Cdd:cd18052  112 ASSFsevqepqALIVAPTRELANQIFLEARKFS-YGTCIRPVVVYGGVSVGHQIRQIEKGC-HILVATPGRLLDFIgRGK 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148231835 183 IlNLKNVKHFVLDECDKMLE---QLDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFM 242
Cdd:cd18052  190 I-SLSKLKYLILDEADRMLDmgfGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL 251
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 51-248 1.39e-33

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: 125.57  E-value: 1.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  51 LKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI------EAVEGQVSvLVMCHTREL 124
Cdd:cd17953   19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIkdqrpvKPGEGPIG-LIMAPTREL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 125 AFQISKEYERFSKYMpTVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGR---ILALVRSKILNLKNVKHFVLDECDKML 201
Cdd:cd17953   98 ALQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKRGA-EIVVCTPGRmidILTANNGRVTNLRRVTYVVLDEADRMF 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 148231835 202 EqLDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd17953  176 D-MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 55-248 1.38e-32

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: 121.89  E-value: 1.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRELAFQISKEYER 134
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 135 FSKYMPTVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLeQLDMRRDVQEIF 214
Cdd:cd17962   81 LMKGLPPMKTALLVGGLPLPPQLYRLQQGV-KVIIATPGRLLDILKQSSVELDNIKIVVVDEADTML-KMGFQQQVLDIL 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 148231835 215 RLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd17962  159 ENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 55-248 1.38e-31

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: 119.22  E-value: 1.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI-----EAVEGQVSVLVMCHTRELAFQIS 129
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 130 KEYERF-SKYMPTVKVAVFFGGLSIKKDEDTIRKSCPHIVVGTPGRILALVRSK--ILNLKNVKHFVLDECDKMLEqLDM 206
Cdd:cd17960   81 EVLQSFlEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKadKVKVKSLEVLVLDEADRLLD-LGF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148231835 207 RRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd17960  160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 55-248 1.75e-31

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: 119.37  E-value: 1.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQieAVEGQVSV----------LVMCHTREL 124
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMF--ALEQEKKLpfikgegpygLIVCPSREL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 125 AFQISKEYERFSKY-----MPTVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRILALVRSKILNLKNVKHFVLDECDK 199
Cdd:cd17951   79 ARQTHEVIEYYCKAlqeggYPQLRCLLCIGGMSVKEQLEVIRKGV-HIVVATPGRLMDMLNKKKINLDICRYLCLDEADR 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 148231835 200 MLEqLDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd17951  158 MID-MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 55-248 3.93e-30

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: 115.16  E-value: 3.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAV------EGQVsVLVMCHTRELAFQI 128
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQpplergDGPI-VLVLAPTRELAQQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 129 SKEYERFSKyMPTVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMleqLDM-- 206
Cdd:cd17966   80 QQEANKFGG-SSRLRNTCVYGGAPKGPQIRDLRRGV-EICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRM---LDMgf 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 148231835 207 ----RRDVQEIfrlTPhEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd17966  155 epqiRKIVDQI---RP-DRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 33-244 4.56e-30

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: 116.68  E-value: 4.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  33 EVKGSYVSIHSSGFRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI------ 106
Cdd:cd18051   10 EATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 107 EAVEGQVS----------VLVMCHTRELAFQISKEYERFSkYMPTVKVAVFFGGLSIKKDEDTIRKSCpHIVVGTPGRIL 176
Cdd:cd18051   90 ESLPSESGyygrrkqyplALVLAPTRELASQIYDEARKFA-YRSRVRPCVVYGGADIGQQMRDLERGC-HLLVATPGRLV 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148231835 177 ALV-RSKIlNLKNVKHFVLDECDKMleqLDM------RRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQD 244
Cdd:cd18051  168 DMLeRGKI-GLDYCKYLVLDEADRM---LDMgfepqiRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 56-250 1.12e-29

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: 113.92  E-value: 1.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  56 LRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQ-----QIEAVEGqVSVLVMCHTRELAFQISK 130
Cdd:cd17941    2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEklyreRWTPEDG-LGALIISPTRELAMQIFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 131 EYERFSKYMpTVKVAVFFGGLSIKKDEDtiRKSCPHIVVGTPGRILA-LVRSKILNLKNVKHFVLDECDKMLEqLDMRRD 209
Cdd:cd17941   81 VLRKVGKYH-SFSAGLIIGGKDVKEEKE--RINRMNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILD-MGFKET 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 148231835 210 VQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFV 250
Cdd:cd17941  157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 272-381 5.06e-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: 109.22  E-value: 5.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  272 EKNRKLFDLLDVLEFNQVVIFVKSVQRCMAlAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMD 351
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 148231835  352 IERVNIVFNYDMPEDSDTYLHRVARAGRFG 381
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 27-245 1.42e-28

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: 112.04  E-value: 1.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  27 VPIARKEVKGSYVSIHSsgFRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILG--MDILCQAKSGMGKTAVFVLATLQ 104
Cdd:cd18048    3 VEVLQRDPTSPLFSVKS--FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 105 QIEAVEGQVSVLVMCHTRELAFQISKEYERFSKYMPTVKVAVFFGGLSIKKDEDTIRKscphIVVGTPGRILA-LVRSKI 183
Cdd:cd18048   81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQ----IVIGTPGTVLDwCFKLRL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148231835 184 LNLKNVKHFVLDECDKMLEQLDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDP 245
Cdd:cd18048  157 IDVTNISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 63-246 6.33e-27

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: 106.90  E-value: 6.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  63 GFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVS------VLVMCHTRELAFQISKEYERFS 136
Cdd:cd17949   10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKLL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 137 KYMPTVKVAVFFGGLSIKKDEDTIRKSCPhIVVGTPGRILALVRS-KILNLKNVKHFVLDECDKMLEQ------------ 203
Cdd:cd17949   90 KPFHWIVPGYLIGGEKRKSEKARLRKGVN-ILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMgfekditkilel 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148231835 204 LDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPM 246
Cdd:cd17949  169 LDDKRSKAGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPV 211
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 46-245 6.88e-27

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: 106.73  E-value: 6.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  46 FRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILG--MDILCQAKSGMGKTAVFVLATLQQIEAVEGQVSVLVMCHTRE 123
Cdd:cd18047    3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 124 LAFQISKEYERFSKYMPTVKVAVFFGGlsiKKDEDTIRKScPHIVVGTPGRILA-LVRSKILNLKNVKHFVLDECDKMLE 202
Cdd:cd18047   83 LALQTGKVIEQMGKFYPELKLAYAVRG---NKLERGQKIS-EQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148231835 203 QLDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDP 245
Cdd:cd18047  159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 56-239 1.66e-26

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: 105.52  E-value: 1.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  56 LRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEAVEGQ----VSVLVMCHTRELAFQISKE 131
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKprngTGVIIISPTRELALQIYGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 132 YERFSKYMpTVKVAVFFGGLSIKKDEDTIRKSCPhIVVGTPGRIL-ALVRSKILNLKNVKHFVLDECDKMLEQlDMRRDV 210
Cdd:cd17942   82 AKELLKYH-SQTFGIVIGGANRKAEAEKLGKGVN-ILVATPGRLLdHLQNTKGFLYKNLQCLIIDEADRILEI-GFEEEM 158

                        170       180
                 ....*....|....*....|....*....
gi 148231835 211 QEIFRLTPHEKQCMMFSATLSKEIRPVCR 239
Cdd:cd17942  159 RQIIKLLPKRRQTMLFSATQTRKVEDLAR 187
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 55-249 2.42e-26

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: 104.85  E-value: 2.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQIEA------VEGQVSVLVMCHTRELAFQI 128
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLqpipreQRNGPGVLVLTPTRELALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 129 SKEYERFSkYMPTVKVAVFFGGLSIKKDEDTIRKscPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMleqLDMRR 208
Cdd:cd17958   81 EAECSKYS-YKGLKSVCVYGGGNRNEQIEDLSKG--VDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRM---LDMGF 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148231835 209 DVQ--EIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVF 249
Cdd:cd17958  155 EPQirKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
HELICc smart00490
helicase superfamily c-terminal domain;
302-381 2.74e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 93.05  E-value: 2.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835   302 LAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFG 381
Cdd:smart00490   3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 81-247 3.33e-23

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: 96.46  E-value: 3.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  81 GMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVS------VLVMCHTRELAFQISKEYERFSKYMptvKVAVFFGGLSIK 154
Cdd:cd17944   27 GKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKrgrapkVLVLAPTRELANQVTKDFKDITRKL---SVACFYGGTPYQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 155 KDEDTIRKSCpHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEqLDMRRDVQEIFRLT----PHEK-QCMMFSAT 229
Cdd:cd17944  104 QQIFAIRNGI-DILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLD-MGFAEQVEEILSVSykkdSEDNpQTLLFSAT 181

                        170
                 ....*....|....*...
gi 148231835 230 LSKEIRPVCRKFMQDPME 247
Cdd:cd17944  182 CPDWVYNVAKKYMKSQYE 199
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 63-202 6.80e-21

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: 90.89  E-value: 6.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  63 GFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI----EAVEGQVS---VLVMCHTRELAFQISKEYERF 135
Cdd:cd17948    9 GITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykLLAEGPFNaprGLVITPSRELAEQIGSVAQSL 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148231835 136 SKYMPtVKVAVFFGGlSIKKDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLE 202
Cdd:cd17948   89 TEGLG-LKVKVITGG-RTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLD 153
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 34-248 9.56e-19

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: 85.83  E-value: 9.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  34 VKGSYVSIHSSGFRDFLLKPELLRSIVDCGFEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI------E 107
Cdd:cd18050   52 IRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHInhqpylE 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 108 AVEGQVsVLVMCHTRELAFQISKEYERFSKYMPTVKVAVFFGGLSIKKDEDTIRKScpHIVVGTPGRILALVRSKILNLK 187
Cdd:cd18050  132 RGDGPI-CLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGV--EICIATPGRLIDFLEAGKTNLR 208

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148231835 188 NVKHFVLDECDKMLEqLDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd18050  209 RCTYLVLDEADRMLD-MGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 64-248 2.17e-18

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: 83.91  E-value: 2.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  64 FEHPSEVQHECIPQAILGMDILCQAKSGMGKTAVFVLATLQQI------EAVEGQVsVLVMCHTRELAFQISK---EYER 134
Cdd:cd18049   44 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHInhqpflERGDGPI-CLVLAPTRELAQQVQQvaaEYGR 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 135 FSKymptVKVAVFFGGL----SIKKDEDTIRkscphIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEqLDMRRDV 210
Cdd:cd18049  123 ACR----LKSTCIYGGApkgpQIRDLERGVE-----ICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLD-MGFEPQI 192

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148231835 211 QEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEV 248
Cdd:cd18049  193 RKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 55-232 5.12e-18

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: 82.68  E-value: 5.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  55 LLRSIVDCGFEHPSEVQHECIPQAI---------LGMDILCQAKSGMGKTAVFVLATLQQI-EAVEGQVSVLVMCHTREL 124
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLpsskstppyRPGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 125 AFQISKEYERFSKYMPtVKVAVFFGGLSIKKDEDTIRK-------SCPHIVVGTPGRILA-LVRSKILNLKNVKHFVLDE 196
Cdd:cd17956   81 VQQVYKVFESLCKGTG-LKVVSLSGQKSFKKEQKLLLVdtsgrylSRVDILVATPGRLVDhLNSTPGFTLKHLRFLVIDE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148231835 197 CDKMLEQ--------LDMR---------RDVQEIFRLTPHEKQC--MMFSATLSK 232
Cdd:cd17956  160 ADRLLNQsfqdwletVMKAlgrptapdlGSFGDANLLERSVRPLqkLLFSATLTR 214
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 81-229 7.18e-14

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: 68.58  E-value: 7.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  81 GMDILCQAKSGMGKTAVFVLATLQQIEAVEGQVsvLVMCHTRELAFQISKEYERFSKymPTVKVAVFFGGLSIKKDEDTI 160
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKV--LVLVPTKALALQTAERLRELFG--PGIRVAVLVGGSSAEEREKNK 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148231835 161 RKScPHIVVGTPGRIL-ALVRSKILNLKNVKHFVLDECDKMLEQLD-MRRDVQEIFRLTPHEKQCMMFSAT 229
Cdd:cd00046   77 LGD-ADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRgALILDLAVRKAGLKNAQVILLSAT 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
85-427 8.90e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 73.14  E-value: 8.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  85 LCQAKSGMGKTAVFVLAtlqqIEAVEGQVSVLVMCHTRELAFQISKEYERFskymptvkvavffggLSIKKDEDTIRKSC 164
Cdd:COG1061  104 LVVAPTGTGKTVLALAL----AAELLRGKRVLVLVPRRELLEQWAEELRRF---------------LGDPLAGGGKKDSD 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 165 PHIVVGTPGRILALVRSKILNlKNVKHFVLDEC--------DKMLEQLDMRrdvqeiFRL----TP-----HEKQCMMF- 226
Cdd:COG1061  165 APITVATYQSLARRAHLDELG-DRFGLVIIDEAhhagapsyRRILEAFPAA------YRLgltaTPfrsdgREILLFLFd 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 227 ----SATLSKEIR-PVCRKFMQDPMEVFVDDETKLTLHGLQQYYVKL--KDSEKNRKLFDLLD-VLEFNQVVIFVKSVQR 298
Cdd:COG1061  238 givyEYSLKEAIEdGYLAPPEYYGIRVDLTDERAEYDALSERLREALaaDAERKDKILRELLReHPDDRKTLVFCSSVDH 317

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 299 CMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFnYDMPEDSDTYLH----RV 374
Cdd:COG1061  318 AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTGSPREFIqrlgRG 396

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148231835 375 ARAGRFGTKGLAITFVSDEED--AKILNDVQDRF--EVNVGELPDEIDISTYIEQSR 427
Cdd:COG1061  397 LRPAPGKEDALVYDFVGNDVPvlEELAKDLRDLAgyRVEFLDEEESEELALLIAVKP 453
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
266-399 5.17e-11

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 64.39  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 266 VKLKDSEKNRKLFDLLDVLEFNQVVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILVATNL 345
Cdd:COG0514  210 VPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIA 289

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148231835 346 FGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSdEEDAKIL 399
Cdd:COG0514  290 FGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYG-PEDVAIQ 342
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 264-389 4.29e-10

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: 57.60  E-value: 4.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 264 YYVKLKDSEKNRKLFDLLDVLEFNQ--VVIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQRRILV 341
Cdd:cd18794    6 YSVRPKDKKDEKLDLLKRIKVEHLGgsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIV 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 148231835 342 ATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITF 389
Cdd:cd18794   86 ATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 339-390 3.76e-07

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: 47.31  E-value: 3.76e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148231835 339 ILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTK-GLAITFV 390
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDeGEVILFV 77
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 88-244 1.88e-06

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: 48.91  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  88 AKSGMGKTAVFVLATLQQI------------EAVE-----GQVSVLVMCHTRELAFQISKEYERFSKYmptvkvaVFFGG 150
Cdd:cd17965   68 AETGSGKTLAYLAPLLDYLkrqeqepfeeaeEEYEsakdtGRPRSVILVPTHELVEQVYSVLKKLSHT-------VKLGI 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 151 LSIKKDEDTIR-------KSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECDKMLEQlDMRRDVQEIFRLTPHEKQC 223
Cdd:cd17965  141 KTFSSGFGPSYqrlqlafKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDR-SFLQDTTSIIKRAPKLKHL 219

                        170       180
                 ....*....|....*....|.
gi 148231835 224 MMFSATLSKEIRPVCRKFMQD 244
Cdd:cd17965  220 ILCSATIPKEFDKTLRKLFPD 240
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
91-197 1.36e-05

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 47.42  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  91 GMGKTAVFVLATLQQIEAVEGQvsVLVMCHTRELAFQISKEYERFSKyMPTVKVAVFFGGLSIKKDEDTIRKScpHIVVG 170
Cdd:COG1111   27 GLGKTAVALLVIAERLHKKGGK--VLFLAPTKPLVEQHAEFFKEALN-IPEDEIVVFTGEVSPEKRKELWEKA--RIIVA 101

                         90       100
                 ....*....|....*....|....*..
gi 148231835 171 TPGRILALVRSKILNLKNVKHFVLDEC 197
Cdd:COG1111  102 TPQVIENDLIAGRIDLDDVSLLIFDEA 128
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 67-200 2.15e-05

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 44.71  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  67 PSEVQHECIpQAILG-------MDILCQAKSGMGKTAVFVLATLQqieAVEGQVSVLVMCHTRELAFQIskeYERFSKYM 139
Cdd:cd17918   16 LTKDQAQAI-KDIEKdlhspepMDRLLSGDVGSGKTLVALGAALL---AYKNGKQVAILVPTEILAHQH---YEEARKFL 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148231835 140 PTVKVAVFFGGlsiKKDEDtirKSCPHIVVGTPGRILALVRSKILNLknvkhFVLDECDKM 200
Cdd:cd17918   89 PFINVELVTGG---TKAQI---LSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHRF 138
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 88-196 2.79e-05

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: 44.56  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  88 AKSGMGKTAVFVLATLQQIEAVEGqvSVLVMCHTRELAFQISKE-YERFSKYMptVKVAVFFGGLSIKKDEDtirkSCPH 166
Cdd:cd17921   24 APTSSGKTLIAELAILRALATSGG--KAVYIAPTRALVNQKEADlRERFGPLG--KNVGLLTGDPSVNKLLL----AEAD 95

                         90       100       110
                 ....*....|....*....|....*....|.
gi 148231835 167 IVVGTPGRILALVR-SKILNLKNVKHFVLDE 196
Cdd:cd17921   96 ILVATPEKLDLLLRnGGERLIQDVRLVVVDE 126
PRK13766 PRK13766
Hef nuclease; Provisional
 85-197 4.79e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 45.63  E-value: 4.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  85 LCQAKSGMGKTAVFVLATLQQIEAVEGQvsVLVMCHTRELAFQiskEYERFSKYM--PTVKVAVFFGGLSIKKDEDTIRK 162
Cdd:PRK13766  33 LVVLPTGLGKTAIALLVIAERLHKKGGK--VLILAPTKPLVEQ---HAEFFRKFLniPEEKIVVFTGEVSPEKRAELWEK 107

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 148231835 163 ScpHIVVGTPGRILALVRSKILNLKNVKHFVLDEC 197
Cdd:PRK13766 108 A--KVIVATPQVIENDLIAGRISLEDVSLLIFDEA 140
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
53-308 9.29e-05

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 44.50  E-value: 9.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  53 PELLRSIvdcGFEHPSEVQHECIPQAIL-GMDILCQAKSGMGKTAVFVLATLQqieAVEGQVSVLVMCHTRELAFQISKE 131
Cdd:COG1204   12 IEFLKER---GIEELYPPQAEALEAGLLeGKNLVVSAPTASGKTLIAELAILK---ALLNGGKALYIVPLRALASEKYRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 132 YER-FSKYMptVKVAVFFGGLsikkDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDECdKMLEqlDMRR-- 208
Cdd:COG1204   86 FKRdFEELG--IKVGVSTGDY----DSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLID--DESRgp 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 209 ---DVQEIFRLTPHEKQCMMFSATLS--KEI-------------RPVCRK--FMQDPMEVFVDDETKltlhglqqyyvkl 268
Cdd:COG1204  157 tleVLLARLRRLNPEAQIVALSATIGnaEEIaewldaelvksdwRPVPLNegVLYDGVLRFDDGSRR------------- 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 148231835 269 kdsEKNRKLFDLLDVLEFN-QVVIFVKSVQRCMALAQLLIE 308
Cdd:COG1204  224 ---SKDPTLALALDLLEEGgQVLVFVSSRRDAESLAKKLAD 261
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 290-389 9.79e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 44.70  E-value: 9.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 290 VIFVKSVQRCMALAQLLIEQNFPAIAIHRNMSQEERlSRYQQfkDFQR---RILVATNLFGRGMDIERVNIVFNYDMPED 366
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVR-ADVQE--AFQRddlQIVVATVAFGMGINKPNVRFVVHFDIPRN 316

                         90       100
                 ....*....|....*....|...
gi 148231835 367 SDTYLHRVARAGRFGTKGLAITF 389
Cdd:PRK11057 317 IESYYQETGRAGRDGLPAEAMLF 339
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 91-197 1.10e-04

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 43.02  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  91 GMGKTAVFVLATLQQIEAVEGQVS----VLVMCHTRELAFQISKEYERFSKYmptvKVAVFFGGLSIKKDEDTIRKSCP- 165
Cdd:cd18034   26 GSGKTLIAVMLIKEMGELNRKEKNpkkrAVFLVPTVPLVAQQAEAIRSHTDL----KVGEYSGEMGVDKWTKERWKEELe 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 148231835 166 --HIVVGTPGRILALVRSKILNLKNVKHFVLDEC 197
Cdd:cd18034  102 kyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 235-390 6.34e-04

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA 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: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 40.23  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 235 RPVcrkfmqdPMEVFVDDETKLTLHGLQQyyVKLKDSEKNRKLFDLLDVLEFNQVVIFVKSVQRCMALAQLLIeqnfpAI 314
Cdd:cd18795    1 RPV-------PLEEYVLGFNGLGIKLRVD--VMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA-----GI 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 315 AIHR-NMSQEERLSRYQQFKDFQRRILVAT-------NLFGRGMDIERVNIVFNYDMPE-DSDTYLHRVARAGR--FGTK 383
Cdd:cd18795   67 AFHHaGLTREDRELVEELFREGLIKVLVATstlaagvNLPARTVIIKGTQRYDGKGYRElSPLEYLQMIGRAGRpgFDTR 146


                 ....*..
gi 148231835 384 GLAITFV 390
Cdd:cd18795  147 GEAIIMT 153
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 69-196 1.87e-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: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  69 EVQHECIPQAIL-GMDILCQAKSGMGKTAVFVLATLQqiEAVEGQVSVLVMcHTRELAFQiskEYERFSK-YMPTVKVAV 146
Cdd:cd18028    4 PPQAEAVRAGLLkGENLLISIPTASGKTLIAEMAMVN--TLLEGGKALYLV-PLRALASE---KYEEFKKlEEIGLKVGI 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 148231835 147 FFGglsiKKDEDTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDE 196
Cdd:cd18028   78 STG----DYDEDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
 224-383 1.99e-03

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 40.11  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 224 MMFSATLSKEIRpvcrKFMQDpMEVFVDDETkLTLHGLQQYYVKLKDSEKNRKLFDLLDVLEF----NQVVIFVKSVQRC 299
Cdd:cd09639  158 LLMSATLPKFLK----EYAEK-IGYVEENEP-LDLKPNERAPFIKIESDKVGEISSLERLLEFikkgGSVAIIVNTVDRA 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 300 MALAQLLIEQN--FPAIAIHRNMSQEERLSRYQQ----FKDFQRRILVATNLFGRGMDIErVNIVFNYDMPEDSdtYLHR 373
Cdd:cd09639  232 QEFYQQLKEKGpeEEIMLIHSRFTEKDRAKKEAEllleFKKSEKFVIVATQVIEASLDIS-VDVMITELAPIDS--LIQR 308

                        170
                 ....*....|
gi 148231835 374 VARAGRFGTK 383
Cdd:cd09639  309 LGRLHRYGEK 318
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 85-197 2.34e-03

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 38.65  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  85 LCQAKSGMGKTAVFVLATLQQIEAVEGQvsVLVMCHTRELAFQiskEYERFSKYM-PTVKVAVFFGGLSIKKDEDTIRKS 163
Cdd:cd18035   20 LIVLPTGLGKTIIAILVAADRLTKKGGK--VLILAPSRPLVEQ---HAENLKRVLnIPDKITSLTGEVKPEERAERWDAS 94

                         90       100       110
                 ....*....|....*....|....*....|....
gi 148231835 164 cpHIVVGTPGRILALVRSKILNLKNVKHFVLDEC 197
Cdd:cd18035   95 --KIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 273-377 2.35e-03

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 38.34  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 273 KNRKLFDLLDVL--EFNQV-----VIFVKSVQRCMALAQLL--IEQNFPAIAIH-------RNMSQEERLSRYQQ---FK 333
Cdd:cd18802    5 VIPKLQKLIEILreYFPKTpdfrgIIFVERRATAVVLSRLLkeHPSTLAFIRCGfligrgnSSQRKRSLMTQRKQketLD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148231835 334 DFQR---RILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARA 377
Cdd:cd18802   85 KFRDgelNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRA 131
CMS1 pfam14617
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant ...
 143-216 2.64e-03

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


Pssm-ID: 373164  Cd Length: 250  Bit Score: 39.46  E-value: 2.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148231835  143 KVAVFFGGlSIKKDE--DTIRKSCPHIVVGTPGRILALVRSKILNLKNVKHFVLDEC---DKMLEQLDMRRDVQEIFRL 216
Cdd:pfam14617 153 KVAKLFAK-HIKLEEhiTYCKASRIGIGVGTPGRIADLLENESLSVDNLKYIILDASfrdIKNRGILDIRETRKAVIKF 230
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 273-383 3.11e-03

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: 37.84  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 273 KNRKLFDLLDVLEFNQ--VVIFVKSVQrcMA--LAQLLIEQNFPAIAIHRNMSQEERLSRYQQFKDFQ--RRILVATNLF 346
Cdd:cd18793   12 KLEALLELLEELREPGekVLIFSQFTD--TLdiLEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAG 89

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 148231835 347 GRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTK 383
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQK 126
DEXHc_RecG cd17992
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ...
 82-171 4.50e-03

DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350750 [Multi-domain]  Cd Length: 225  Bit Score: 38.28  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835  82 MDILCQAKSGMGKTAVFVLATLQqieAVEGQVSVLVMCHTRELAFQiskEYERFSKYMP--TVKVAVFFGGLSIKKDE-- 157
Cdd:cd17992   67 MNRLLQGDVGSGKTVVAALAMLA---AVENGYQVALMAPTEILAEQ---HYDSLKKLLEplGIRVALLTGSTKAKEKRei 140

                         90
                 ....*....|....*
gi 148231835 158 -DTIRKSCPHIVVGT 171
Cdd:cd17992  141 lEKIASGEIDIVIGT 155
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 291-379 5.35e-03

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 37.24  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231835 291 IFVKSVQRCMALAQLL---IEQNFPAIAI---HRNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMP 364
Cdd:cd18796   43 VFTNTRSQAERLAQRLrelCPDRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122

                         90
                 ....*....|....*
gi 148231835 365 EDSDTYLHRVARAGR 379
Cdd:cd18796  123 KSVARLLQRLGRSGH 137
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 318-379 7.41e-03

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 36.95  E-value: 7.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148231835 318 RNMSQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGR 379
Cdd:cd18801   72 KGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 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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