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Conserved domains on  [gi|940389175|ref|WP_054983733|]
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MULTISPECIES: ATP-dependent RNA helicase DbpA [Pseudoalteromonas]

Protein Classification

ATP-dependent RNA helicase( domain architecture ID 11485501)

ATP-dependent RNA helicase DbpA is a DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-461 0e+00

ATP-dependent RNA helicase DbpA; Provisional


:

Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 831.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   1 MTSTAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCP 80
Cdd:PRK11776   1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  81 TRELAEQVAVEMRKLARGIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQML 160
Cdd:PRK11776  81 TRELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 161 DMGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQEKSTIKQYFYKMDNNkQRYSTLKLLLLK 240
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPD-ERLPALQRLLLH 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 241 FTPQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYHL 320
Cdd:PRK11776 240 HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 321 AHDPQTHVHRVGRTGRAGKKGIACSIYGEAEQFKVAQIGDHYERDFLPEPMPAFSLLEKPPYKPEMVTLMIDSGKKQKVR 400
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTLCIDGGKKDKLR 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940389175 401 AGDILGALTGKDGVAGRQVGKINVLDNVAFVAVERNASKPALRKLTEGNIKGRKIRARRLT 461
Cdd:PRK11776 400 PGDILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLLK 460
 
Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-461 0e+00

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 831.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   1 MTSTAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCP 80
Cdd:PRK11776   1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  81 TRELAEQVAVEMRKLARGIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQML 160
Cdd:PRK11776  81 TRELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 161 DMGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQEKSTIKQYFYKMDNNkQRYSTLKLLLLK 240
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPD-ERLPALQRLLLH 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 241 FTPQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYHL 320
Cdd:PRK11776 240 HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 321 AHDPQTHVHRVGRTGRAGKKGIACSIYGEAEQFKVAQIGDHYERDFLPEPMPAFSLLEKPPYKPEMVTLMIDSGKKQKVR 400
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTLCIDGGKKDKLR 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940389175 401 AGDILGALTGKDGVAGRQVGKINVLDNVAFVAVERNASKPALRKLTEGNIKGRKIRARRLT 461
Cdd:PRK11776 400 PGDILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLLK 460
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
3-386 0e+00

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 513.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   3 STAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKR-FRIQSLVLCPT 81
Cdd:COG0513    1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  82 RELAEQVAVEMRKLARGiHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLD 161
Cdd:COG0513   81 RELALQVAEELRKLAKY-LGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 162 MGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQEK-STIKQYFYKMDNnKQRYSTLKLLLLK 240
Cdd:COG0513  160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATaETIEQRYYLVDK-RDKLELLRRLLRD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 241 FTPQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYHL 320
Cdd:COG0513  239 EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDL 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940389175 321 AHDPQTHVHRVGRTGRAGKKGIACSIYGEAEQFKVAQIGDHYERDFLPEPMPAFSLLEKPPYKPEM 386
Cdd:COG0513  319 PEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLK 384
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
15-207 1.55e-95

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: 286.26  E-value: 1.55e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLN----VKRFRIQSLVLCPTRELAEQVAV 90
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLpepkKKGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  91 EMRKLARGiHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLDA 170
Cdd:cd00268   81 VARKLGKG-TGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 940389175 171 IIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIK 207
Cdd:cd00268  160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
28-195 1.06e-60

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 195.54  E-value: 1.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   28 TPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRELAEQVAVEMRKLARGIhNIKILTL 107
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  108 CGGVSIGPQIGSLeHGAHIIVGTPGRVDDHIRKgTLRLDDVETLVLDEADQMLDMGFQDTLDAIIECIPQNRQTLLFSAT 187
Cdd:pfam00270  80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*...
gi 940389175  188 FPRAIEAI 195
Cdd:pfam00270 158 LPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
19-220 9.05e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 173.45  E-value: 9.05e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175    19 LSTLGYSQMTPVQAQSLPPVLEG-KDIIAQAKTGSGKTAAFSLGVLAKLNvKRFRIQSLVLCPTRELAEQVAVEMRKLAr 97
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLG- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175    98 GIHNIKILTLCGGVSIGPQIGSLEHG-AHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLDAIIECIP 176
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 940389175   177 QNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQEKsTIKQY 220
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLE-PIEQF 201
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
43-380 7.00e-08

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 54.38  E-value: 7.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   43 DIIAQAKTGSGKTAAfSLGVLAKLNVKRFRIQSLVLCPTRELAEQVAVEMRKLArGIHNIKILTLCGGVSIGPQIGSLE- 121
Cdd:TIGR01587   1 LLVIEAPTGYGKTEA-ALLWALHSIKSQKADRVIIALPTRATINAMYRRAKELF-GSELVGLHHSSSFSRIKEMGDSEEf 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  122 --------HGAHIIVGTPGRVD--DHIRK---GTLRLDDVET-------LVLDEADQMLD--MGFqdtLDAIIECIPQNR 179
Cdd:TIGR01587  79 ehlfplyiHSNDKLFLDPITVCtiDQVLKsvfGEFGHYEFTLasianslLIFDEVHFYDEytLAL---ILAVLEVLKDND 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  180 QT-LLFSATFPRAIEAIAKRVL--KNPEMIKVEEEQEKStiKQYFYKMDNNKQRYSTLKLLLLKFTPQ--SCVVFCNTkV 254
Cdd:TIGR01587 156 VPiLLMSATLPKFLKEYAEKIGyvEFNEPLDLKEERRFE--NHRFILIESDKVGEISSLERLLEFIKKggSIAIIVNT-V 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  255 ETQQVCDDLASE---GFSAVALHGDLEQRDRER----TLIHFANKSAS-ILVATDVAARGLDIdDMDMVINYHLAHDPQT 326
Cdd:TIGR01587 233 DRAQEFYQQLKEkapEEEIILYHSRFTEKDRAKkeaeLLREMKKSNEKfVIVATQVIEASLDI-SADVMITELAPIDSLI 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 940389175  327 hvHRVGRTGRAGKKgiacsiygEAEQFKVAQIGDHYERDFLPEPmpaFSLLEKP 380
Cdd:TIGR01587 312 --QRLGRLHRYGRK--------IGENFEVYIITIAPEGKLFPYP---YELVERT 352
 
Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-461 0e+00

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 831.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   1 MTSTAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCP 80
Cdd:PRK11776   1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  81 TRELAEQVAVEMRKLARGIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQML 160
Cdd:PRK11776  81 TRELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 161 DMGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQEKSTIKQYFYKMDNNkQRYSTLKLLLLK 240
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPD-ERLPALQRLLLH 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 241 FTPQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYHL 320
Cdd:PRK11776 240 HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 321 AHDPQTHVHRVGRTGRAGKKGIACSIYGEAEQFKVAQIGDHYERDFLPEPMPAFSLLEKPPYKPEMVTLMIDSGKKQKVR 400
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTLCIDGGKKDKLR 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940389175 401 AGDILGALTGKDGVAGRQVGKINVLDNVAFVAVERNASKPALRKLTEGNIKGRKIRARRLT 461
Cdd:PRK11776 400 PGDILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLLK 460
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
3-386 0e+00

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 513.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   3 STAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKR-FRIQSLVLCPT 81
Cdd:COG0513    1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  82 RELAEQVAVEMRKLARGiHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLD 161
Cdd:COG0513   81 RELALQVAEELRKLAKY-LGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 162 MGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQEK-STIKQYFYKMDNnKQRYSTLKLLLLK 240
Cdd:COG0513  160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATaETIEQRYYLVDK-RDKLELLRRLLRD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 241 FTPQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYHL 320
Cdd:COG0513  239 EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDL 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940389175 321 AHDPQTHVHRVGRTGRAGKKGIACSIYGEAEQFKVAQIGDHYERDFLPEPMPAFSLLEKPPYKPEM 386
Cdd:COG0513  319 PEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLK 384
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
15-207 1.55e-95

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: 286.26  E-value: 1.55e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLN----VKRFRIQSLVLCPTRELAEQVAV 90
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLpepkKKGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  91 EMRKLARGiHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLDA 170
Cdd:cd00268   81 VARKLGKG-TGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 940389175 171 IIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIK 207
Cdd:cd00268  160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
4-346 2.42e-91

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 283.76  E-value: 2.42e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   4 TAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLN--VKRF----RIqsLV 77
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdfPRRKsgppRI--LI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  78 LCPTRELAEQVAVEMRKLARGIHnIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEAD 157
Cdd:PRK11192  79 LTPTRELAMQVADQARELAKHTH-LDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEAD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 158 QMLDMGFQDTLDAI-IECipQNR-QTLLFSATFP-RAIEAIAKRVLKNPEMIKVE-EEQEKSTIKQYFYKMDNNKQRYST 233
Cdd:PRK11192 158 RMLDMGFAQDIETIaAET--RWRkQTLLFSATLEgDAVQDFAERLLNDPVEVEAEpSRRERKKIHQWYYRADDLEHKTAL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 234 LKLLLLKFTPQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMD 313
Cdd:PRK11192 236 LCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
                        330       340       350
                 ....*....|....*....|....*....|...
gi 940389175 314 MVINYHLAHDPQTHVHRVGRTGRAGKKGIACSI 346
Cdd:PRK11192 316 HVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
2-343 1.66e-89

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 285.20  E-value: 1.66e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   2 TSTAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPT 81
Cdd:PRK11634   4 FETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  82 RELAEQVAVEMRKLARGIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLD 161
Cdd:PRK11634  84 RELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 162 MGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEE-QEKSTIKQYFYKMDN-NKQRYSTLKLLLL 239
Cdd:PRK11634 164 MGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSvTTRPDISQSYWTVWGmRKNEALVRFLEAE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 240 KFtpQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYH 319
Cdd:PRK11634 244 DF--DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYD 321
                        330       340
                 ....*....|....*....|....
gi 940389175 320 LAHDPQTHVHRVGRTGRAGKKGIA 343
Cdd:PRK11634 322 IPMDSESYVHRIGRTGRAGRAGRA 345
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
5-346 3.52e-82

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 260.90  E-value: 3.52e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   5 AFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVK------RFRIQSLVL 78
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphakgRRPVRALIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  79 CPTRELAEQVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQ 158
Cdd:PRK10590  82 TPTRELAAQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 159 MLDMGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQEKS-TIKQYFYKMDNNKQRySTLKLL 237
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASeQVTQHVHFVDKKRKR-ELLSQM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 238 LLKFTPQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVIN 317
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
                        330       340
                 ....*....|....*....|....*....
gi 940389175 318 YHLAHDPQTHVHRVGRTGRAGKKGIACSI 346
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSL 348
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
4-383 4.72e-79

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 253.68  E-value: 4.72e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   4 TAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKL-----NVKRFR--IQSL 76
Cdd:PRK01297  87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtppPKERYMgePRAL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  77 VLCPTRELAEQVAVEMRKLARgIHNIKILTLCGGVSIGPQIGSLE-HGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDE 155
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTK-YTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 156 ADQMLDMGFQDTLDAIIECIP--QNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQEKS-TIKQYFY---KMDNNKQ 229
Cdd:PRK01297 246 ADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASdTVEQHVYavaGSDKYKL 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 230 RYSTLKLLLLkftpQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDI 309
Cdd:PRK01297 326 LYNLVTQNPW----ERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940389175 310 DDMDMVINYHLAHDPQTHVHRVGRTGRAGKKGIACSIYGEAEQFKVAQIGDHYERDFLPEpMPAFSLLEKPPYK 383
Cdd:PRK01297 402 DGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCE-MPPAELLKPVPRK 474
PTZ00424 PTZ00424
helicase 45; Provisional
5-373 6.58e-77

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 245.51  E-value: 6.58e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   5 AFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTREL 84
Cdd:PTZ00424  29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTREL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  85 AEQVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGF 164
Cdd:PTZ00424 109 AQQIQKVVLALGDYL-KVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGF 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 165 QDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKV-EEEQEKSTIKQYFYKMDNNKQRYSTLKLLLLKFTP 243
Cdd:PTZ00424 188 KGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVkKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTI 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 244 QSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYHLAHD 323
Cdd:PTZ00424 268 TQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPAS 347
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 940389175 324 PQTHVHRVGRTGRAGKKGIACSIYGEAEQFKVAQIGDHYERDFlpEPMPA 373
Cdd:PTZ00424 348 PENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQI--EEMPM 395
PTZ00110 PTZ00110
helicase; Provisional
4-357 4.61e-76

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 247.76  E-value: 4.61e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   4 TAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVK-RFRIQS----LVL 78
Cdd:PTZ00110 130 VSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQpLLRYGDgpivLVL 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  79 CPTRELAEQVAVEMRKLARgIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQ 158
Cdd:PTZ00110 210 APTRELAEQIREQCNKFGA-SSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADR 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 159 MLDMGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKN-PEMIKVEEEQEKS--TIKQYFYKMDNNKQRYSTLK 235
Cdd:PTZ00110 289 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAchNIKQEVFVVEEHEKRGKLKM 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 236 LLLLKFTPQSCV-VFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDM 314
Cdd:PTZ00110 369 LLQRIMRDGDKIlIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKY 448
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 940389175 315 VINYHLAHDPQTHVHRVGRTGRAGKKGIACSIYgEAEQFKVAQ 357
Cdd:PTZ00110 449 VINFDFPNQIEDYVHRIGRTGRAGAKGASYTFL-TPDKYRLAR 490
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
1-345 2.24e-74

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 239.87  E-value: 2.24e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   1 MTSTAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKL-----NVKRFRIQ- 74
Cdd:PRK04837   5 LTEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpaPEDRKVNQp 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  75 -SLVLCPTRELAEQVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVL 153
Cdd:PRK04837  85 rALIMAPTRELAVQIHADAEPLAQAT-GLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 154 DEADQMLDMGFqdtldaiIECI---------PQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQEKST-IKQ-YFY 222
Cdd:PRK04837 164 DEADRMFDLGF-------IKDIrwlfrrmppANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHrIKEeLFY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 223 KMDNNKQRystlklllLKFT------PQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASI 296
Cdd:PRK04837 237 PSNEEKMR--------LLQTlieeewPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDI 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 940389175 297 LVATDVAARGLDIDDMDMVINYHLAHDPQTHVHRVGRTGRAGKKGIACS 345
Cdd:PRK04837 309 LVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSIS 357
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
11-206 1.38e-65

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: 209.75  E-value: 1.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  11 LPAGLVDNLSTLGYSQMTPVQAQSLPPVLE-GKDIIAQAKTGSGKTAAFSLGVLAKL-----NVKRFRIQSLVLCPTREL 84
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  85 AEQVAVEMRKLARGIHNIKILTLCGGVSIGPQIGSLEH-GAHIIVGTPGRVDDHIRKGTLR--LDDVETLVLDEADQMLD 161
Cdd:cd17964   81 ALQIAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 940389175 162 MGFQDTLDAIIECIPQN----RQTLLFSATFPRAIEAIAKRVL-KNPEMI 206
Cdd:cd17964  161 MGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTLkKDYKFI 210
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
1-384 8.76e-65

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 218.67  E-value: 8.76e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   1 MTSTAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKL-------NVKRFRI 73
Cdd:PRK04537   6 LTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  74 QSLVLCPTRELAEQVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRK-GTLRLDDVETLV 152
Cdd:PRK04537  86 RALILAPTRELAIQIHKDAVKFGADL-GLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 153 LDEADQMLDMGFQDTLDAIIECIPQ--NRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQEKST-IKQYFYkMDNNKQ 229
Cdd:PRK04537 165 LDEADRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAArVRQRIY-FPADEE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 230 RYSTLKLLLLKFTPQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDI 309
Cdd:PRK04537 244 KQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHI 323
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940389175 310 DDMDMVINYHLAHDPQTHVHRVGRTGRAGKKGIACSIYGEAEQFKVAQIGDHYERDFLPEPMPAFSL--LEKPPYKP 384
Cdd:PRK04537 324 DGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVTAELLtpLPRPPRVP 400
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
6-202 3.66e-63

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: 203.87  E-value: 3.66e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   6 FSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKL------NVKRFRI----QS 75
Cdd:cd17967    2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppSVGRGRRkaypSA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  76 LVLCPTRELAEQVAVEMRKLARGIHnIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDE 155
Cdd:cd17967   82 LILAPTRELAIQIYEEARKFSYRSG-VRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940389175 156 ADQMLDMGFQDTLDAIIEC----IPQNRQTLLFSATFPRAIEAIAKRVLKN 202
Cdd:cd17967  161 ADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKN 211
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
15-203 2.72e-61

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: 198.25  E-value: 2.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKL---NVKRFRIQSLVLCPTRELAEQVAVE 91
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  92 MRKLARgIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKG-TLRLDDVETLVLDEADQMLDMGFQDTLDA 170
Cdd:cd17947   81 LQQLAQ-FTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKE 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 940389175 171 IIECIPQNRQTLLFSATFPRAIEAIAKRVLKNP 203
Cdd:cd17947  160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
28-195 1.06e-60

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 195.54  E-value: 1.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   28 TPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRELAEQVAVEMRKLARGIhNIKILTL 107
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  108 CGGVSIGPQIGSLeHGAHIIVGTPGRVDDHIRKgTLRLDDVETLVLDEADQMLDMGFQDTLDAIIECIPQNRQTLLFSAT 187
Cdd:pfam00270  80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*...
gi 940389175  188 FPRAIEAI 195
Cdd:pfam00270 158 LPRNLEDL 165
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
6-209 2.76e-60

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: 195.61  E-value: 2.76e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   6 FSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRELA 85
Cdd:cd17954    2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  86 EQVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIR--KGtLRLDDVETLVLDEADQMLDMG 163
Cdd:cd17954   82 QQISEQFEALGSSI-GLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEntKG-FSLKSLKFLVMDEADRLLNMD 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 940389175 164 FQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPemIKVE 209
Cdd:cd17954  160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP--VKIE 203
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
6-207 3.06e-60

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 195.60  E-value: 3.06e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   6 FSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLN--VKRFRIQSLVLCPTRE 83
Cdd:cd17959    3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKahSPTVGARALILSPTRE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  84 LAEQVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMG 163
Cdd:cd17959   83 LALQTLKVTKELGKFT-DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 940389175 164 FQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIK 207
Cdd:cd17959  162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
6-343 7.87e-59

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 201.55  E-value: 7.87e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   6 FSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKlnVKRFRIQ---------SL 76
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISR--CCTIRSGhpseqrnplAM 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  77 VLCPTRELAEQVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEA 156
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGL-PFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEV 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 157 DQMLDMGFQDTLDAIIECIPQNrQTLLFSATFPRAIEAIAKRVLKNPEMIKV-EEEQEKSTIKQYFYKMD--NNKQRYST 233
Cdd:PLN00206 280 DCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIgNPNRPNKAVKQLAIWVEtkQKKQKLFD 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 234 LKLLLLKFTPQScVVFCNTKVETqqvcdDLASE------GFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGL 307
Cdd:PLN00206 359 ILKSKQHFKPPA-VVFVSSRLGA-----DLLANaitvvtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGV 432
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 940389175 308 DIDDMDMVINYHLAHDPQTHVHRVGRTGRAGKKGIA 343
Cdd:PLN00206 433 DLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTA 468
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
6-203 1.22e-57

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


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 188.97  E-value: 1.22e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   6 FSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRELA 85
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  86 EQVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIR---KGTLRLDDVETLVLDEADQMLDM 162
Cdd:cd17955   81 YQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 940389175 163 GFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNP 203
Cdd:cd17955  160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
6-206 1.38e-57

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: 188.66  E-value: 1.38e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   6 FSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRELA 85
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  86 EQVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQ 165
Cdd:cd17940   81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 940389175 166 DTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMI 206
Cdd:cd17940  160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
4-201 3.73e-56

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: 187.10  E-value: 3.73e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   4 TAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRI---------Q 74
Cdd:cd18052   43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTAssfsevqepQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  75 SLVLCPTRELAEQVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLD 154
Cdd:cd18052  123 ALIVAPTRELANQIFLEARKFSYGT-CIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILD 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940389175 155 EADQMLDMGFQDTLDAIIEC--IP--QNRQTLLFSATFPRAIEAIAKRVLK 201
Cdd:cd18052  202 EADRMLDMGFGPEIRKLVSEpgMPskEDRQTLMFSATFPEEIQRLAAEFLK 252
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
15-207 1.44e-55

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: 183.55  E-value: 1.44e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKL-----NVKRFRIQSLVLCPTRELAEQV- 88
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIy 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  89 AVEMRKLARGIHNIKILTLCGGVSIGPQIGSL-EHGAHIIVGTPGRVDDHIRKGTLRLD--DVETLVLDEADQMLDMGFQ 165
Cdd:cd17960   81 EVLQSFLEHHLPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLGFE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 940389175 166 DTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIK 207
Cdd:cd17960  161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
15-206 3.64e-55

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: 182.90  E-value: 3.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKL-------NVKRFRI-QSLVLCPTRELAE 86
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsrlppldEETKDDGpYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  87 QVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQD 166
Cdd:cd17945   81 QIEEETQKFAKPL-GIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 167 TLDAIIECIP--------------------QNRQTLLFSATFPRAIEAIAKRVLKNPEMI 206
Cdd:cd17945  160 QVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
15-206 1.34e-54

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: 180.82  E-value: 1.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRELAEQVAVEMRK 94
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  95 LARGIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLDAIIEC 174
Cdd:cd17962   81 LMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 940389175 175 IPQNRQTLLFSATFPRAIEAIAKRVLKNPEMI 206
Cdd:cd17962  161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
4-203 2.39e-54

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: 181.04  E-value: 2.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   4 TAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQS-----LVL 78
Cdd:cd17953   12 QKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGegpigLIM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  79 CPTRELAEQVAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLR---LDDVETLVLDE 155
Cdd:cd17953   92 APTRELALQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRvtnLRRVTYVVLDE 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 940389175 156 ADQMLDMGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNP 203
Cdd:cd17953  171 ADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
15-208 1.57e-53

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: 178.17  E-value: 1.57e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNV--KRFRIQSLVLCPTRELAEQVAVEM 92
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKprKKKGLRALILAPTRELASQIYREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  93 RKLARGIhNIKILTLCGG----VSIGPQIGSlehGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTL 168
Cdd:cd17957   81 LKLSKGT-GLRIVLLSKSleakAKDGPKSIT---KYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 940389175 169 DAIIE-CIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKV 208
Cdd:cd17957  157 DEILAaCTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
23-209 5.03e-53

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


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 176.71  E-value: 5.03e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  23 GYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFR----IQSLVLCPTRELAEQVAVEMRKLARG 98
Cdd:cd17941    9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTpedgLGALIISPTRELAMQIFEVLRKVGKY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  99 iHNIKILTLCGGVSIGPQIGSLeHGAHIIVGTPGRVDDHIRKG-TLRLDDVETLVLDEADQMLDMGFQDTLDAIIECIPQ 177
Cdd:cd17941   89 -HSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDAIVENLPK 166
                        170       180       190
                 ....*....|....*....|....*....|..
gi 940389175 178 NRQTLLFSATFPRAIEAIAKRVLKNPEMIKVE 209
Cdd:cd17941  167 SRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
15-203 2.32e-52

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: 174.86  E-value: 2.32e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQS-----LVLCPTRELAEQVA 89
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGdgpivLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  90 VEMRKLARGiHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLD 169
Cdd:cd17966   81 QEANKFGGS-SRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 940389175 170 AIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNP 203
Cdd:cd17966  160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDY 193
DEXDc smart00487
DEAD-like helicases superfamily;
19-220 9.05e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 173.45  E-value: 9.05e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175    19 LSTLGYSQMTPVQAQSLPPVLEG-KDIIAQAKTGSGKTAAFSLGVLAKLNvKRFRIQSLVLCPTRELAEQVAVEMRKLAr 97
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLG- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175    98 GIHNIKILTLCGGVSIGPQIGSLEHG-AHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLDAIIECIP 176
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 940389175   177 QNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQEKsTIKQY 220
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLE-PIEQF 201
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
15-203 1.87e-51

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: 172.60  E-value: 1.87e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQ-----SLVLCPTRELAEQVA 89
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKgegpiAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  90 VEMRKLARgIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLD 169
Cdd:cd17952   81 LEAKKFGK-AYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 940389175 170 AIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNP 203
Cdd:cd17952  160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDP 193
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
23-206 5.67e-51

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: 171.35  E-value: 5.67e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  23 GYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRELAEQVAVEMRKLarGIH-N 101
Cdd:cd17939   16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKAL--GDYmG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 102 IKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLDAIIECIPQNRQT 181
Cdd:cd17939   94 VKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPETQV 173
                        170       180
                 ....*....|....*....|....*
gi 940389175 182 LLFSATFPRAIEAIAKRVLKNPEMI 206
Cdd:cd17939  174 VLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
15-207 6.80e-51

DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 171.61  E-value: 6.80e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLST-LGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQ------SLVLCPTRELAEQ 87
Cdd:cd17949    1 LVSHLKSkMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  88 VAVEMRKLARGIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGT-LRLDDVETLVLDEADQMLDMGFQD 166
Cdd:cd17949   81 IYEVLEKLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940389175 167 TLDAIIECI-------------PQNRQTLLFSATFPRAIEAIAKRVLKNPEMIK 207
Cdd:cd17949  161 DITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
22-208 7.74e-51

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: 171.23  E-value: 7.74e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  22 LGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKL------NVKRFRIQSLVLCPTRELAEQVAVEMRKL 95
Cdd:cd17961   12 LGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQVSKVLEQL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  96 ARGIHN-IKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRL-DDVETLVLDEADQMLDMGFQDTLDAIIE 173
Cdd:cd17961   92 TAYCRKdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSYGYEEDLKSLLS 171
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 940389175 174 CIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKV 208
Cdd:cd17961  172 YLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
217-347 4.35e-50

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: 166.53  E-value: 4.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 217 IKQYFYKMDNNKQRYSTLKLLLLKFTPQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASI 296
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940389175 297 LVATDVAARGLDIDDMDMVINYHLAHDPQTHVHRVGRTGRAGKKGIACSIY 347
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
4-202 6.19e-49

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: 167.91  E-value: 6.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   4 TAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKL----------------- 66
Cdd:cd18051   21 ETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgeslpsesgyyg 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  67 NVKRFRIqSLVLCPTRELAEQVAVEMRKLARGIHnIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLD 146
Cdd:cd18051  101 RRKQYPL-ALVLAPTRELASQIYDEARKFAYRSR-VRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLD 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 147 DVETLVLDEADQMLDMGFQDTLDAIIE--CIPQ--NRQTLLFSATFPRAIEAIAKRVLKN 202
Cdd:cd18051  179 YCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPtgERQTLMFSATFPKEIQMLARDFLDN 238
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
15-207 1.04e-46

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: 160.12  E-value: 1.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRELAEQVAVEMRK 94
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  95 LARGIHNIKILTLCGGVSIGPQIGSLEhGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLDAIIEC 174
Cdd:cd17943   81 IGKKLEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 940389175 175 IPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIK 207
Cdd:cd17943  160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
6-206 8.64e-46

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: 157.99  E-value: 8.64e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   6 FSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRELA 85
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  86 EQVAVEMrkLARGIH-NIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGF 164
Cdd:cd18046   81 QQIQKVV--MALGDYmGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 940389175 165 QDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMI 206
Cdd:cd18046  159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
19-205 1.53e-45

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: 157.14  E-value: 1.53e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  19 LSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQS----LVLCPTRELAEQVAVEMRK 94
Cdd:cd17942    5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNgtgvIIISPTRELALQIYGVAKE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  95 LARgIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIR-KGTLRLDDVETLVLDEADQMLDMGFQDTLDAIIE 173
Cdd:cd17942   85 LLK-YHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIK 163
                        170       180       190
                 ....*....|....*....|....*....|..
gi 940389175 174 CIPQNRQTLLFSATFPRAIEAIAKRVLKNPEM 205
Cdd:cd17942  164 LLPKRRQTMLFSATQTRKVEDLARISLKKKPL 195
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
11-207 2.17e-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: 156.58  E-value: 2.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  11 LPAGLVDNLSTLGYSQMTPVQAQSLPPVLEG--KDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRELAEQV 88
Cdd:cd17963    1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  89 AVEMRKLARgIHNIKI-LTLCGG-VSIGPQIgslehGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDM-GFQ 165
Cdd:cd17963   81 GEVVEKMGK-FTGVKVaLAVPGNdVPRGKKI-----TAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHG 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 940389175 166 DTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIK 207
Cdd:cd17963  155 DQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
6-206 2.46e-45

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: 156.86  E-value: 2.46e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   6 FSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRELA 85
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  86 EQVAVEMrkLARGIH-NIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGF 164
Cdd:cd18045   81 VQIQKVL--LALGDYmNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 940389175 165 QDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMI 206
Cdd:cd18045  159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
16-201 4.82e-45

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


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 155.78  E-value: 4.82e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  16 VDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLN-----VKRFRI-QSLVLCPTRELAEQVA 89
Cdd:cd17944    2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQedqqpRKRGRApKVLVLAPTRELANQVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  90 VEMRKLARgihNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLD 169
Cdd:cd17944   82 KDFKDITR---KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVE 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 940389175 170 AIIECI-----PQNRQTLLFSATFPRAIEAIAKRVLK 201
Cdd:cd17944  159 EILSVSykkdsEDNPQTLLFSATCPDWVYNVAKKYMK 195
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
3-208 8.22e-45

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: 155.58  E-value: 8.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   3 STAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTR 82
Cdd:cd17950    1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  83 ELAEQVAVEMRKLARGIHNIKILTLCGGVSIGPQIGSLEHGA-HIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQML- 160
Cdd:cd17950   81 ELAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLe 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 940389175 161 DMGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKV 208
Cdd:cd17950  161 QLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
15-203 9.35e-44

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: 152.49  E-value: 9.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVL--AKLNVKRFRIQ------SLVLCPTRELAE 86
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfALEQEKKLPFIkgegpyGLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  87 Q---VAVEMRKL--ARGIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLD 161
Cdd:cd17951   81 QtheVIEYYCKAlqEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 940389175 162 MGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNP 203
Cdd:cd17951  161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKP 202
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
6-202 2.01e-43

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: 152.86  E-value: 2.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   6 FSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQS-----LVLCP 80
Cdd:cd18049   26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpicLVLAP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  81 TRELAEQV---AVEMRKLARgihnIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEAD 157
Cdd:cd18049  106 TRELAQQVqqvAAEYGRACR----LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 940389175 158 QMLDMGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKN 202
Cdd:cd18049  182 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
6-203 7.89e-43

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: 150.16  E-value: 7.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   6 FSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKlnvkrfrIQSLVLCPTRELA 85
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  86 EQVAVEMRKLARGIHNIKI--LTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMG 163
Cdd:cd17938   74 EQTYNCIENFKKYLDNPKLrvALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 940389175 164 FQDTLDAIIECIPQ------NRQTLLFSATFPR-AIEAIAKRVLKNP 203
Cdd:cd17938  154 NLETINRIYNRIPKitsdgkRLQVIVCSATLHSfEVKKLADKIMHFP 200
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
19-230 5.35e-42

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: 148.93  E-value: 5.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  19 LSTLGYSQMTPVQAQSLPP-VLEGKDIIAQAKTGSGKTAAFSLGVLAK-LNVKRFRI--------QSLVLCPTRELAEQV 88
Cdd:cd17946    5 LADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERlLSQKSSNGvggkqkplRALILTPTRELAVQV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  89 AVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKG---TLRLDDVETLVLDEADQMLDMGFQ 165
Cdd:cd17946   85 KDHLKAIAKYT-NIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEKGHF 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940389175 166 DTLDAIIECIP-------QNRQTLLFSATFpraieaiaKRVLKNPEMIKVEEEQEKSTIKQyfyKMDNNKQR 230
Cdd:cd17946  164 AELEKILELLNkdragkkRKRQTFVFSATL--------TLDHQLPLKLNSKKKKKKKEKKQ---KLELLIEK 224
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
15-206 5.21e-41

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: 144.91  E-value: 5.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNV------KRFRIQSLVLCPTRELAEQV 88
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLqpipreQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  89 AVEMRKLArgIHNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTL 168
Cdd:cd17958   81 EAECSKYS--YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 940389175 169 DAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMI 206
Cdd:cd17958  159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
4-208 3.11e-40

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: 145.54  E-value: 3.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   4 TAFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQS-----LVL 78
Cdd:cd18050   62 FAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLVL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  79 CPTRELAEQV---AVEMRKLARgihnIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDE 155
Cdd:cd18050  142 APTRELAQQVqqvADDYGKSSR----LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDE 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 940389175 156 ADQMLDMGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKV 208
Cdd:cd18050  218 ADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
15-206 4.47e-35

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: 130.44  E-value: 4.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEG---------KDIIAQAKTGSGKTAAFSLGVLAKLnVKRF--RIQSLVLCPTRE 83
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQAL-SKRVvpRLRALIVVPTKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  84 LAEQVAVEMRKLARGIHnIKILTLCGGVSIGPQIGSLEHGAH--------IIVGTPGRVDDHIRKGT-LRLDDVETLVLD 154
Cdd:cd17956   80 LVQQVYKVFESLCKGTG-LKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPgFTLKHLRFLVID 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940389175 155 EADQMLDMGFQDTLDAIIECI--------------------PQNRQTLLFSATFPRAIEAIAKRVLKNPEMI 206
Cdd:cd17956  159 EADRLLNQSFQDWLETVMKALgrptapdlgsfgdanllersVRPLQKLLFSATLTRDPEKLSSLKLHRPRLF 230
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
5-212 3.58e-32

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: 122.44  E-value: 3.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   5 AFSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEG--KDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTR 82
Cdd:cd18048   19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  83 ELAEQVAVEMRKLARGIHNIKILTLCGGVSIGPqiGSlEHGAHIIVGTPGRVDDHIRKgtLRLDDVETL---VLDEADQM 159
Cdd:cd18048   99 ELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGK--GT-DIEAQIVIGTPGTVLDWCFK--LRLIDVTNIsvfVLDEADVM 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940389175 160 LDM-GFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIKVEEEQ 212
Cdd:cd18048  174 INVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEE 227
RRM_EcDbpA_like cd12501
RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; ...
388-460 5.08e-31

RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of dbpA. E. coli dbpA is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity for RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions. As a non-processive ATP-dependent helicase, DbpA destabilizes and unwinds short <9bp (base pairs) RNA duplexes as well as long duplex RNA stretches. It disrupts RNA helices exclusively in a 3'- 5' direction and requires a single-stranded loading site 3' of the substrate helix. dbpA contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain binds specifically to hairpin 92.


Pssm-ID: 409924 [Multi-domain]  Cd Length: 73  Bit Score: 113.87  E-value: 5.08e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940389175 388 TLMIDSGKKQKVRAGDILGALTGKDGVAGRQVGKINVLDNVAFVAVERNASKPALRKLTEGNIKGRKIRARRL 460
Cdd:cd12501    1 TIQIDGGKKQKLRPGDILGALTGDNGIDGEDIGKINITDFVSYVAVKRSVAKDALKKLREGKIKGRKFRVRLL 73
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
15-199 1.58e-28

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: 112.46  E-value: 1.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  15 LVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSL----GVLAKLNVKRFRIQS---LVLCPTRELAEQ 87
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLpiiqRLLRYKLLAEGPFNAprgLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  88 VAVEMRKLARGIhNIKILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDT 167
Cdd:cd17948   81 IGSVAQSLTEGL-GLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 940389175 168 LDAIIECIP-------------QNRQTLLFSATFPRAIEAIAKRV 199
Cdd:cd17948  160 LSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSKV 204
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
246-338 1.98e-25

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: 99.98  E-value: 1.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  246 CVVFCNTK--VETQQVCDdlaSEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYHLAHD 323
Cdd:pfam00271  18 VLIFSQTKktLEAELLLE---KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWN 94
                          90
                  ....*....|....*
gi 940389175  324 PQTHVHRVGRTGRAG 338
Cdd:pfam00271  95 PASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
257-338 1.91e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.73  E-value: 1.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   257 QQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYHLAHDPQTHVHRVGRTGR 336
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 940389175   337 AG 338
Cdd:smart00490  81 AG 82
DbpA pfam03880
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ...
388-459 2.15e-22

DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of DEAD helicase proteins. It is sufficient to confer specificity for hairpin 92 of 23S rRNA, which is part of the ribosomal A-site. However, several members of this family lack specificity for 23S rRNA. These can proteins can generally be distinguished by a basic region that extends beyond this domain [Karl Kossen, unpublished data].


Pssm-ID: 461082 [Multi-domain]  Cd Length: 72  Bit Score: 90.51  E-value: 2.15e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940389175  388 TLMIDSGKKQKVRAGDILGALTGKDGVAGRQVGKINVLDNVAFVAVERNASKPALRKLTEGNIKGRKIRARR 459
Cdd:pfam03880   1 RLFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKGRKVRVEP 72
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
6-207 6.51e-22

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: 93.25  E-value: 6.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   6 FSSLALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEG--KDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIQSLVLCPTRE 83
Cdd:cd18047    3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  84 LAEQVAVEMRKLARGIHNIKILTLCGGvsigpqiGSLEHGA----HIIVGTPGRVDDHIRKgtLRLDD---VETLVLDEA 156
Cdd:cd18047   83 LALQTGKVIEQMGKFYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSK--LKFIDpkkIKVFVLDEA 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 940389175 157 DQML-DMGFQDTLDAIIECIPQNRQTLLFSATFPRAIEAIAKRVLKNPEMIK 207
Cdd:cd18047  154 DVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
41-187 1.36e-20

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 87.84  E-value: 1.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  41 GKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIqsLVLCPTRELAEQVAVEMRKLARgiHNIKILTLCGGVSIGPQIGSL 120
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKV--LVLVPTKALALQTAERLRELFG--PGIRVAVLVGGSSAEEREKNK 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 121 EHGAHIIVGTPGRVDDHI-RKGTLRLDDVETLVLDEADQMLDMGFQDTLDAIIEC--IPQNRQTLLFSAT 187
Cdd:cd00046   77 LGDADIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
40-347 1.84e-18

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 87.77  E-value: 1.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  40 EGKDIIAQAKTGSGKTAaFSLGVLAKLNVKRfRIqsLVLCPTRELAEQVAVEMRKLARGIHNIKiltlcggvsigpqiGS 119
Cdd:COG1061   99 GGGRGLVVAPTGTGKTV-LALALAAELLRGK-RV--LVLVPRRELLEQWAEELRRFLGDPLAGG--------------GK 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 120 LEHGAHIIVGTPGRVDDHIRKGTLRlDDVETLVLDEADQMLDMGFQDTLDAIiecipQNRQTLLFSATFPR--------- 190
Cdd:COG1061  161 KDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRRILEAF-----PAAYRLGLTATPFRsdgreillf 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 191 ----------AIEAIAKRVLKNPEMIKV-----EEEQEKSTIKQ-YFYKMDNNKQRYSTLKLLLLKFTPQS--CVVFCNT 252
Cdd:COG1061  235 lfdgivyeysLKEAIEDGYLAPPEYYGIrvdltDERAEYDALSErLREALAADAERKDKILRELLREHPDDrkTLVFCSS 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 253 KVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVInyHLAH--DPQTHVHR 330
Cdd:COG1061  315 VDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI--LLRPtgSPREFIQR 392
                        330
                 ....*....|....*..
gi 940389175 331 VGRTGRAGKKGIACSIY 347
Cdd:COG1061  393 LGRGLRPAPGKEDALVY 409
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
48-193 4.99e-13

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 68.56  E-value: 4.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  48 AKTGSGKTAAFSLGVLAKLN-----------------VKRFRIQSLVLCPTRELAEQVAVEMRKLARGIH-NIKILTLCG 109
Cdd:cd17965   68 AETGSGKTLAYLAPLLDYLKrqeqepfeeaeeeyesaKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKlGIKTFSSGF 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 110 GVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLDAIIECIPQNRQTLLFSATFP 189
Cdd:cd17965  148 GPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227

                 ....
gi 940389175 190 RAIE 193
Cdd:cd17965  228 KEFD 231
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
27-193 6.24e-13

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: 66.90  E-value: 6.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  27 MTPVQAQSLPPV-LEGKDIIAQAKTGSGKTAAFSLGVLAKLNVKRFRIqsLVLCPTRELAEQVAVEMRKLARGIH-NIKI 104
Cdd:cd17921    2 LNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKA--VYIAPTRALVNQKEADLRERFGPLGkNVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 105 LTlcGGVSIGPQigsLEHGAHIIVGTPGRVDDHIRKG-TLRLDDVETLVLDEAdQMLDMGFQ-DTLDAIIECIPQ---NR 179
Cdd:cd17921   80 LT--GDPSVNKL---LLAEADILVATPEKLDLLLRNGgERLIQDVRLVVVDEA-HLIGDGERgVVLELLLSRLLRinkNA 153
                        170
                 ....*....|....
gi 940389175 180 QTLLFSATFPRAIE 193
Cdd:cd17921  154 RFVGLSATLPNAED 167
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
11-161 3.25e-12

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 68.38  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  11 LPAGLVDNLSTLGYSQMTPVQAQSLPP-VLEGKDIIAQAKTGSGKTAafsLGVLAKLNVKRFRIQSLVLCPTRELAEQVA 89
Cdd:COG1204    7 PLEKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTL---IAELAILKALLNGGKALYIVPLRALASEKY 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940389175  90 VEMRKLARGIhNIKIltlcgGVSIGP-QIGSLEHG-AHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEAdQMLD 161
Cdd:COG1204   84 REFKRDFEEL-GIKV-----GVSTGDyDSDDEWLGrYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLID 150
RRM_DbpA cd12252
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; ...
388-456 4.11e-11

RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; This subfamily corresponds to the C-terminal RRM homology domain of dbpA proteins implicated in ribosome biogenesis. They bind with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92), which is part of the ribosomal A-site. The majority of dbpA proteins contain two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding. Several members of this family lack specificity for 23S rRNA. These proteins can generally be distinguished by a basic region that extends beyond the C-terminal domain.


Pssm-ID: 409698 [Multi-domain]  Cd Length: 71  Bit Score: 58.33  E-value: 4.11e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940389175 388 TLMIDSGKKQKVRAGDILGALTGKDGVAGRQVGKINVLDNVAFVAVERNASKPALRKLTEGNIKGRKIR 456
Cdd:cd12252    1 RLFINVGRKDGIDPRDLLGAICRAGGISRDDIGAIRIFDNFSFVEVPEAEAERVIEALNGKKIKGKKLR 69
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
244-347 1.31e-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: 59.14  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 244 QSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATdvAARGLDIDDMD--MVINYHLA 321
Cdd:cd18794   31 GSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT--VAFGMGIDKPDvrFVIHYSLP 108
                         90       100
                 ....*....|....*....|....*.
gi 940389175 322 HDPQTHVHRVGRTGRAGKKGIACSIY 347
Cdd:cd18794  109 KSMESYYQESGRAGRDGLPSECILFY 134
RRM_BsYxiN_like cd12500
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and ...
389-459 2.42e-09

RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of YxiN. B. subtilis YxiN is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions in an ATP-dependent manner. YxiN contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.


Pssm-ID: 409923 [Multi-domain]  Cd Length: 73  Bit Score: 53.62  E-value: 2.42e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940389175 389 LMIDSGKKQKVRAGDILGALTGKDGVAGRQVGKINVLDNVAFVAVERNASKPALRKLTEGNIKGRKIRARR 459
Cdd:cd12500    2 LYFNGGKKKKIRAVDIVGAISNIDGVTGDDIGIITVQDNCSYVDILNGKGDHVLKVMKNTTIKGKQVKVNK 72
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
43-340 4.91e-09

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: 57.82  E-value: 4.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  43 DIIAQAKTGSGKTAAfSLGVLAKLNVKRFRIQSLVLCPTRELAEQVAVEMRKLARGIHNIKILTLCGGVSIGPQIGSLE- 121
Cdd:cd09639    1 LLVIEAPTGYGKTEA-ALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSSRIKEMGDSEEFEh 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 122 ------HGAHIIVGTPGRVD--DHIRK---GTLRLDDVET-------LVLDEADQMLD--MGFqdtLDAIIECIPQNRQT 181
Cdd:cd09639   80 lfplyiHSNDTLFLDPITVCtiDQVLKsvfGEFGHYEFTLasianslLIFDEVHFYDEytLAL---ILAVLEVLKDNDVP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 182 -LLFSATFPRAIeaiaKRVLKNPEMIKVEEEQEKSTIKQYFY-----KMDNNKQRYSTLKLLLLKFTPQscVVFCNTkVE 255
Cdd:cd09639  157 iLLMSATLPKFL----KEYAEKIGYVEENEPLDLKPNERAPFikiesDKVGEISSLERLLEFIKKGGSV--AIIVNT-VD 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 256 TQQVCDDLASE---GFSAVALHGDLEQRDRERT----LIHFANKSASILVATDVAARGLDIdDMDMVINYHLAHDPQThv 328
Cdd:cd09639  230 RAQEFYQQLKEkgpEEEIMLIHSRFTEKDRAKKeaelLLEFKKSEKFVIVATQVIEASLDI-SVDVMITELAPIDSLI-- 306
                        330
                 ....*....|..
gi 940389175 329 HRVGRTGRAGKK 340
Cdd:cd09639  307 QRLGRLHRYGEK 318
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
29-197 2.44e-08

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: 53.49  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  29 PVQAQSLPP-VLEGKDIIAQAKTGSGKTAafsLGVLAKLNVKRFRIQSLVLCPTRELAEQVAVEMRKLARGihnikiltl 107
Cdd:cd18028    4 PPQAEAVRAgLLKGENLLISIPTASGKTL---IAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKLEEI--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 108 cgGVSIGPQIGSLE------HGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQMLDMGFQDTLDAII---ECIPQN 178
Cdd:cd18028   72 --GLKVGISTGDYDeddewlGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVarlRRLNPN 149
                        170
                 ....*....|....*....
gi 940389175 179 RQTLLFSATFPRAiEAIAK 197
Cdd:cd18028  150 TQIIGLSATIGNP-DELAE 167
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
43-380 7.00e-08

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 54.38  E-value: 7.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   43 DIIAQAKTGSGKTAAfSLGVLAKLNVKRFRIQSLVLCPTRELAEQVAVEMRKLArGIHNIKILTLCGGVSIGPQIGSLE- 121
Cdd:TIGR01587   1 LLVIEAPTGYGKTEA-ALLWALHSIKSQKADRVIIALPTRATINAMYRRAKELF-GSELVGLHHSSSFSRIKEMGDSEEf 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  122 --------HGAHIIVGTPGRVD--DHIRK---GTLRLDDVET-------LVLDEADQMLD--MGFqdtLDAIIECIPQNR 179
Cdd:TIGR01587  79 ehlfplyiHSNDKLFLDPITVCtiDQVLKsvfGEFGHYEFTLasianslLIFDEVHFYDEytLAL---ILAVLEVLKDND 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  180 QT-LLFSATFPRAIEAIAKRVL--KNPEMIKVEEEQEKStiKQYFYKMDNNKQRYSTLKLLLLKFTPQ--SCVVFCNTkV 254
Cdd:TIGR01587 156 VPiLLMSATLPKFLKEYAEKIGyvEFNEPLDLKEERRFE--NHRFILIESDKVGEISSLERLLEFIKKggSIAIIVNT-V 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  255 ETQQVCDDLASE---GFSAVALHGDLEQRDRER----TLIHFANKSAS-ILVATDVAARGLDIdDMDMVINYHLAHDPQT 326
Cdd:TIGR01587 233 DRAQEFYQQLKEkapEEEIILYHSRFTEKDRAKkeaeLLREMKKSNEKfVIVATQVIEASLDI-SADVMITELAPIDSLI 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 940389175  327 hvHRVGRTGRAGKKgiacsiygEAEQFKVAQIGDHYERDFLPEPmpaFSLLEKP 380
Cdd:TIGR01587 312 --QRLGRLHRYGRK--------IGENFEVYIITIAPEGKLFPYP---YELVERT 352
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
243-350 1.99e-07

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 53.22  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 243 PQSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATdvAARGLDID--DMDMVINYHL 320
Cdd:COG0514  230 GGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT--IAFGMGIDkpDVRFVIHYDL 307
                         90       100       110
                 ....*....|....*....|....*....|
gi 940389175 321 AHDPQTHVHRVGRTGRAGKKGIACSIYGEA 350
Cdd:COG0514  308 PKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
261-340 5.79e-07

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 52.04  E-value: 5.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 261 DDLASEGFSAVALHGD--------LEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYHLAHDPQTHVHRVG 332
Cdd:COG1111  371 EFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKG 450

                 ....*...
gi 940389175 333 RTGRAGKK 340
Cdd:COG1111  451 RTGRKREG 458
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
277-336 8.67e-07

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: 48.12  E-value: 8.67e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 277 LEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYHLAHDPQTHVHRVGRTGR 336
Cdd:cd18801   74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
246-332 3.34e-06

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 46.32  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 246 CVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSAS--ILVATDVAARGLDIDDMDMVINYHLAHD 323
Cdd:cd18793   30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPWWN 109
                         90
                 ....*....|....*
gi 940389175 324 PQTH------VHRVG 332
Cdd:cd18793  110 PAVEeqaidrAHRIG 124
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
39-156 5.54e-06

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: 46.74  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  39 LEGKDIIAqAKTGSGKTAAFSLGVLAKLNVKRFRIqsLVLCPTRELAEQVAVEMRKLARGihNIKILTLCGGVSIGPQiG 118
Cdd:cd18035   15 LNGNTLIV-LPTGLGKTIIAILVAADRLTKKGGKV--LILAPSRPLVEQHAENLKRVLNI--PDKITSLTGEVKPEER-A 88
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 940389175 119 SLEHGAHIIVGTPGRVDDHIRKGTLRLDDVETLVLDEA 156
Cdd:cd18035   89 ERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
42-156 6.61e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 46.88  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  42 KDIIAQAKTGSGKT-------AAFSLGVLAKLNVKRFriqSLVLCPTRELAEQVAVEMRklargIH-NIKILTLCGGVSI 113
Cdd:cd18034   17 RNTIVVLPTGSGKTliavmliKEMGELNRKEKNPKKR---AVFLVPTVPLVAQQAEAIR-----SHtDLKVGEYSGEMGV 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 940389175 114 GPQIGSLEHGA----HIIVGTPGRVDDHIRKGTLRLDDVETLVLDEA 156
Cdd:cd18034   89 DKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
10-99 7.69e-06

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 48.29  E-value: 7.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  10 ALPAGLVDNLSTLGYSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLnVKRFRIQSLVLCPTRELA-EQV 88
Cdd:COG1205   40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALArDQL 118
                         90
                 ....*....|.
gi 940389175  89 AvEMRKLARGI 99
Cdd:COG1205  119 R-RLRELAEAL 128
PRK02362 PRK02362
ATP-dependent DNA helicase;
7-155 9.24e-06

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 48.03  E-value: 9.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   7 SSLALPAGLVDNLSTLGYSQMTPVQAQSLPP-VLEGKDIIAQAKTGSGKTaafslgVLAKLNVKRfRIQ----SLVLCPT 81
Cdd:PRK02362   4 AELPLPEGVIEFYEAEGIEELYPPQAEAVEAgLLDGKNLLAAIPTASGKT------LIAELAMLK-AIArggkALYIVPL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  82 RELAEQVAVEMRKLARGihnikiltlcgGVSIGPQIGSLEHGAH------IIVGTPGRVDDHIRKGTLRLDDVETLVLDE 155
Cdd:PRK02362  77 RALASEKFEEFERFEEL-----------GVRVGISTGDYDSRDEwlgdndIIVATSEKVDSLLRNGAPWLDDITCVVVDE 145
RRM_EcCsdA_like cd12499
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and ...
391-460 9.42e-06

RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of E. coli CsdA, also termed ATP-dependent RNA helicase deaD, or translation factor W2, a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. CsdA may be involved in translation initiation, gene regulation after cold-shock, mRNA decay and biogenesis of the large or small ribosomal subunit. It contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.


Pssm-ID: 409922 [Multi-domain]  Cd Length: 73  Bit Score: 43.33  E-value: 9.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 391 IDSGKKQKVRAGDILGALTGKDGVAGRQVGKINVLDNVAFVAVERNASKPALRKLTEGNIKGRKIRARRL 460
Cdd:cd12499    4 IEVGRKDGVKPGNIVGAIANEAGIDSRFIGRIKIFDDHSTVELPKGMPKDVLQHLKKVRVCGQPLNIKLL 73
PRK13766 PRK13766
Hef nuclease; Provisional
247-339 1.17e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 47.95  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 247 VVFCNTKVETQQVCDDLASEGFSAVALHGD--------LEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINY 318
Cdd:PRK13766 369 IVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFY 448
                         90       100
                 ....*....|....*....|....*....
gi 940389175 319 hlahDP--------QthvhRVGRTGRAGK 339
Cdd:PRK13766 449 ----EPvpseirsiQ----RKGRTGRQEE 469
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
31-156 1.84e-05

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 45.27  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  31 QAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGVLAKLnVKRFRIQSLVLCPTRELAEQVAVEMRKLARGIH-NIKILTLCG 109
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAQDQLRSLRELLEQLGlGIRVATYDG 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 940389175 110 GVSIGPQIGSLEHGAHIIVGTPgrvdDHIRKGTLRLDD--------VETLVLDEA 156
Cdd:cd17923   84 DTPREERRAIIRNPPRILLTNP----DMLHYALLPHHDrwarflrnLRYVVLDEA 134
ResIII pfam04851
Type III restriction enzyme, res subunit;
26-190 2.02e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 44.59  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   26 QMTPVQAQSLPPVLEG-----KDIIAQAKTGSGKT---AAFSLGVLAKLNVKRFriqsLVLCPTRELAEQVAVEMRKLAR 97
Cdd:pfam04851   3 ELRPYQIEAIENLLESikngqKRGLIVMATGSGKTltaAKLIARLFKKGPIKKV----LFLVPRKDLLEQALEEFKKFLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175   98 GIHNIkiltlcGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTLRLD----DVetLVLDEADQMLDMGFQdtldAIIE 173
Cdd:pfam04851  79 NYVEI------GEIISGDKKDESVDDNKIVVTTIQSLYKALELASLELLpdffDV--IIIDEAHRSGASSYR----NILE 146
                         170
                  ....*....|....*..
gi 940389175  174 CIPQNRQtLLFSATFPR 190
Cdd:pfam04851 147 YFKPAFL-LGLTATPER 162
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
292-341 7.58e-05

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 41.15  E-value: 7.58e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 940389175 292 KSASILVATDVAARGLDIDDMDMVINYHLAHDPQTHVHRVGRTGRAGKKG 341
Cdd:cd18785   21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
50-188 1.07e-04

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 42.29  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  50 TGSGKTAafslgVLAKLNVKRFRIQSLVLCPTRELAEQVAvemrklargihnIKILTLCGGVSIGpQIGSLEH----GAH 125
Cdd:cd17926   27 TGSGKTL-----TALALIAYLKELRTLIVVPTDALLDQWK------------ERFEDFLGDSSIG-LIGGGKKkdfdDAN 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940389175 126 IIVGTPGRVDDHIRKGTLRLDDVETLVLDEADQmldmGFQDTLDAIIECIPQNRQtLLFSATF 188
Cdd:cd17926   89 VVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEILKELNAKYR-LGLTATP 146
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
30-155 1.56e-04

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 42.73  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  30 VQAQSLPPVLEG-KDIIAQAKTGSGKTAAFSLGVL---------AKLNVKRFRIqslvlCPTRELAEQVAVEMR-KLarG 98
Cdd:cd18023    5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILrllkernplPWGNRKVVYI-----APIKALCSEKYDDWKeKF--G 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940389175  99 IHNIKILTLCGGVSIGPqIGSLEHgAHIIVGTPGRVDDHIRK----GTLrLDDVETLVLDE 155
Cdd:cd18023   78 PLGLSCAELTGDTEMDD-TFEIQD-ADIILTTPEKWDSMTRRwrdnGNL-VQLVALVLIDE 135
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
29-155 1.86e-04

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


Pssm-ID: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 42.46  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  29 PVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLgvLAKLNVKRFRIQS-----LVLCPTRELAEQVA-VEMRKLARGihnI 102
Cdd:cd18036    5 NYQLELVLPALRGKNTIICAPTGSGKTRVAVY--ICRHHLEKRRSAGekgrvVVLVNKVPLVEQQLeKFFKYFRKG---Y 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 940389175 103 KILTLCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGT----LRLDDVETLVLDE 155
Cdd:cd18036   80 KVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGReeerVYLSDFSLLIFDE 136
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
31-156 2.13e-04

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 42.42  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  31 QAQSLPPVLEGKDIIAQAKTGSGKTaaFSLGVLAKLNVKRFRI----QSLVLCPTRELAEQVAVEMRKLArGIHNIKILT 106
Cdd:cd17927    7 QLELAQPALKGKNTIICLPTGSGKT--FVAVLICEHHLKKFPAgrkgKVVFLANKVPLVEQQKEVFRKHF-ERPGYKVTG 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940389175 107 LCGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRKGTL-RLDDVETLVLDEA 156
Cdd:cd17927   84 LSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDEC 134
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
273-343 3.64e-04

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 40.79  E-value: 3.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940389175 273 LHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVI-----NYHLAhdpQTHVHRvGRTGRAGKKGIA 343
Cdd:cd18810   57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGLA---QLYQLR-GRVGRSKERAYA 128
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
28-130 3.72e-04

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 41.25  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  28 TPVQAQSLPPVL------EGKDIIAQAKTGSGKTAAFslGVLAKLNVKRFRiQSLVLCPTRELAEQVAVEMRKLargIHN 101
Cdd:cd17918   17 TKDQAQAIKDIEkdlhspEPMDRLLSGDVGSGKTLVA--LGAALLAYKNGK-QVAILVPTEILAHQHYEEARKF---LPF 90
                         90       100       110
                 ....*....|....*....|....*....|.
gi 940389175 102 IKILTLCGGV--SIGPQIGslehgahIIVGT 130
Cdd:cd17918   91 INVELVTGGTkaQILSGIS-------LLVGT 114
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
38-130 3.97e-04

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


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 41.16  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  38 VLEGKDIIAQAKTGSGKTaafSLGVLAKLNVKRFRIQSLVLCPTRELAEQVAVEMRKLARGIH-NIKILTLCGGVSIGPQ 116
Cdd:cd17924   29 LLRGKSFAIIAPTGVGKT---TFGLATSLYLASKGKRSYLIFPTKSLVKQAYERLSKYAEKAGvEVKILVYHSRLKKKEK 105
                         90
                 ....*....|....*...
gi 940389175 117 IGSLEH----GAHIIVGT 130
Cdd:cd17924  106 EELLEKiekgDFDILVTT 123
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
24-66 8.95e-04

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 42.01  E-value: 8.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 940389175  24 YSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKT-AAFsLGVLAKL 66
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDEL 64
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
244-338 2.13e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 40.47  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 244 QSCVVFCNTKVETQQVCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMDMVINYHLAHD 323
Cdd:PRK11057 237 KSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRN 316
                         90
                 ....*....|....*
gi 940389175 324 PQTHVHRVGRTGRAG 338
Cdd:PRK11057 317 IESYYQETGRAGRDG 331
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
246-318 2.87e-03

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 40.21  E-value: 2.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940389175 246 CVVFCnTKVETQQ-VCDDLASEGFSAVALHGDLEQRDRERTLIHFANKSAS--ILVATDVAARGLDIDDMDMVINY 318
Cdd:COG0553  552 VLVFS-QFTDTLDlLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHY 626
DEXHc_SKIV2L cd18027
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ...
26-193 2.91e-03

DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350785 [Multi-domain]  Cd Length: 179  Bit Score: 38.78  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  26 QMTPVQAQSLPPVLEGKDIIAQAKTGSGKTAAFSLGV-LAKLNVKRfriqSLVLCPTRELAEQvavEMRKLARGIHNIKI 104
Cdd:cd18027    8 ELDVFQKQAILHLEAGDSVFVAAHTSAGKTVVAEYAIaLAQKHMTR----TIYTSPIKALSNQ---KFRDFKNTFGDVGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 105 LTlcGGVSIGPQIGSLEHGAHIIVGTPGRVDDHIRkgtlrldDVETLVLDEADQMLDMGFQDTLDAIIECIPQNRQTLLF 184
Cdd:cd18027   81 IT--GDVQLNPEASCLIMTTEILRSMLYNGSDVIR-------DLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSIILL 151

                 ....*....
gi 940389175 185 SATFPRAIE 193
Cdd:cd18027  152 SATVPNTVE 160
PRK13767 PRK13767
ATP-dependent helicase; Provisional
24-66 2.99e-03

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 40.25  E-value: 2.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 940389175  24 YSQMTPVQAQSLPPVLEGKDIIAQAKTGSGKT-AAFsLGVLAKL 66
Cdd:PRK13767  30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF-LAIIDEL 72
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
273-343 3.00e-03

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 38.40  E-value: 3.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940389175 273 LHGDLEQRDRERTLIHFANKSASILVATDVAARGLDIDDMD-MVIN----YHLAhdpQTHVHRvGRTGRAGKKGIA 343
Cdd:cd18792   66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANtMIIEdadrFGLS---QLHQLR-GRVGRGKHQSYC 137
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
245-337 4.45e-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: 37.57  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175 245 SCVVFCNTKV----------ETQQVCDDLASE-----GFSAVALHGDLEQRDRERTLIHFANKSASILVATDVAARGLDI 309
Cdd:cd18802   27 RGIIFVERRAtavvlsrllkEHPSTLAFIRCGfligrGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDV 106
                         90       100
                 ....*....|....*....|....*...
gi 940389175 310 DDMDMVINYHLahdPQTHVHRVGRTGRA 337
Cdd:cd18802  107 PACNLVIRFDL---PKTLRSYIQSRGRA 131
PRK13766 PRK13766
Hef nuclease; Provisional
50-156 6.55e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 39.09  E-value: 6.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940389175  50 TGSGKTAaFSLGVLA-KLNVKRFRIqsLVLCPTRELAEQVAVEMRKLARgIHNIKILTLCGGVSigP-QIGSLEHGAHII 127
Cdd:PRK13766  38 TGLGKTA-IALLVIAeRLHKKGGKV--LILAPTKPLVEQHAEFFRKFLN-IPEEKIVVFTGEVS--PeKRAELWEKAKVI 111
                         90       100
                 ....*....|....*....|....*....
gi 940389175 128 VGTPGRVDDHIRKGTLRLDDVETLVLDEA 156
Cdd:PRK13766 112 VATPQVIENDLIAGRISLEDVSLLIFDEA 140
 
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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