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Conserved domains on  [gi|20806137|ref|NP_620798|]
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probable ATP-dependent RNA helicase DDX46 isoform 1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
361-582 2.48e-166

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: 486.88  E-value: 2.48e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  361 TVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSL 440
Cdd:cd17953    1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  441 EEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNL 520
Cdd:cd17953   81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20806137  521 RRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 582
Cdd:cd17953  161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
378-793 3.97e-149

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 450.37  E-value: 3.97e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  378 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSleegEGPIAVIMTPTREL 457
Cdd:COG0513    8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  458 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYVVLDEADRMFDM 537
Cdd:COG0513   84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGAL-DLSGVETLVLDEADRMLDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  538 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLKLLELLGHYq 617
Cdd:COG0513  161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDE- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  618 ESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCP 697
Cdd:COG0513  240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  698 NHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKAL--ELSGTAVPPDLEKLWSDFKDQQ-KAEGKIIKKSSGFS 774
Cdd:COG0513  320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIgqKIEEEELPGFEPVEEKRLERLKpKIKEKLKGKKAGRG 399
                        410
                 ....*....|....*....
gi 20806137  775 GKGFKFDETEQALANERKK 793
Cdd:COG0513  400 GRPGPKGERKARRGKRRRR 418
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
929-1031 1.31e-61

type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar proteins; DDX46, also called PRP5 homolog, is an ATP-dependent RNA helicase that plays an essential role in splicing, either prior to, or during splicing A complex formation. It inhibits antiviral innate responses by entrapping selected antiviral transcripts in the nucleus. It is also involved in the development of several tumors. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


:

Pssm-ID: 411901  Cd Length: 103  Bit Score: 204.47  E-value: 1.31e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  929 SFKRYEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1008
Cdd:cd22473    1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                         90       100
                 ....*....|....*....|...
gi 20806137 1009 LIKEELIRLQNSYQPTNKGRYKV 1031
Cdd:cd22473   81 LIKEELLRLQASYQPINKGRYKV 103
 
Name Accession Description Interval E-value
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
361-582 2.48e-166

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: 486.88  E-value: 2.48e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  361 TVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSL 440
Cdd:cd17953    1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  441 EEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNL 520
Cdd:cd17953   81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20806137  521 RRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 582
Cdd:cd17953  161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
PTZ00110 PTZ00110
helicase; Provisional
318-752 1.86e-154

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 468.87  E-value: 1.86e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   318 LEPVDHGKIEYEPFRKNFYVEVPELAKMSQEEVNVFRLEMEGITVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTP 397
Cdd:PTZ00110   76 LQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   398 IQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVV 477
Cdd:PTZ00110  156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   478 CVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANsgrVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTV 557
Cdd:PTZ00110  236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESN---VTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTL 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   558 MFSATFPRAMEALARRILS-KPIEVQVGGRSV-VCSDVEQQVIVIEEEKKFLKLLELLGHYQESGS-VIIFVDKQEHADG 634
Cdd:PTZ00110  313 MWSATWPKEVQSLARDLCKeEPVHVNVGSLDLtACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGDkILIFVETKKGADF 392
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   635 LLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAG 714
Cdd:PTZ00110  393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 20806137   715 NKGYAYTFITEDQARYAGDIIKALELSGTAVPPDLEKL 752
Cdd:PTZ00110  473 AKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKL 510
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
378-793 3.97e-149

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 450.37  E-value: 3.97e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  378 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSleegEGPIAVIMTPTREL 457
Cdd:COG0513    8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  458 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYVVLDEADRMFDM 537
Cdd:COG0513   84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGAL-DLSGVETLVLDEADRMLDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  538 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLKLLELLGHYq 617
Cdd:COG0513  161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDE- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  618 ESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCP 697
Cdd:COG0513  240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  698 NHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKAL--ELSGTAVPPDLEKLWSDFKDQQ-KAEGKIIKKSSGFS 774
Cdd:COG0513  320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIgqKIEEEELPGFEPVEEKRLERLKpKIKEKLKGKKAGRG 399
                        410
                 ....*....|....*....
gi 20806137  775 GKGFKFDETEQALANERKK 793
Cdd:COG0513  400 GRPGPKGERKARRGKRRRR 418
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
293-749 1.89e-75

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 258.18  E-value: 1.89e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   293 EYSSEEEEVDL-----QTALTGYQTKQRKllePVDHGKIEYEPFR-KNFYVEVPEL-AKMSQEEVNVFRLEMEgITVKGK 365
Cdd:PLN00206   39 EYICDETDDDIcslecKQALLRRVAKSRV---AVGAPKPKRLPATdECFYVRDPGStSGLSSSQAELLRRKLE-IHVKGE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   366 GCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRS--LEEG 443
Cdd:PLN00206  115 AVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSghPSEQ 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   444 EGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRV 523
Cdd:PLN00206  195 RNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHD---IELDNV 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   524 TYVVLDEADRMFDMGFEPQVMRIVDNVrPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEE 603
Cdd:PLN00206  272 SVLVLDEVDCMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETK 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   604 KKFLKL---LELLGHYQEsgSVIIFVDKQEHADgLLKDLMRAS--YPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSV 678
Cdd:PLN00206  351 QKKQKLfdiLKSKQHFKP--PAVVFVSSRLGAD-LLANAITVVtgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGV 427
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20806137   679 AARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKALELSGTAVPPDL 749
Cdd:PLN00206  428 LGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPREL 498
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
396-570 1.78e-63

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: 212.10  E-value: 1.78e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137    396 TPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdqrsLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLR 475
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL-----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137    476 VVCVYGGTGISEQIAELKrGAEIIVCTPGRMIDMLAansgRVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQ 555
Cdd:pfam00270   76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQ----ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQ 150
                          170
                   ....*....|....*
gi 20806137    556 TVMFSATFPRAMEAL 570
Cdd:pfam00270  151 ILLLSATLPRNLEDL 165
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
929-1031 1.31e-61

type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar proteins; DDX46, also called PRP5 homolog, is an ATP-dependent RNA helicase that plays an essential role in splicing, either prior to, or during splicing A complex formation. It inhibits antiviral innate responses by entrapping selected antiviral transcripts in the nucleus. It is also involved in the development of several tumors. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411901  Cd Length: 103  Bit Score: 204.47  E-value: 1.31e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  929 SFKRYEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1008
Cdd:cd22473    1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                         90       100
                 ....*....|....*....|...
gi 20806137 1009 LIKEELIRLQNSYQPTNKGRYKV 1031
Cdd:cd22473   81 LIKEELLRLQASYQPINKGRYKV 103
DEXDc smart00487
DEAD-like helicases superfamily;
387-595 9.16e-57

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 194.63  E-value: 9.16e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137     387 LKKHGYEKPTPIQTQAIPAIMSG-RDLIGIAKTGSGKTIAFLLPMFRHIMdqrsleEGEGPIAVIMTPTRELALQITKEC 465
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137     466 KKFSKTLGLRVVCVYGGTGISEQIAELKRG-AEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFDMGFEPQVM 544
Cdd:smart00487   75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDK---LSLSNVDLVILDEAHRLLDGGFGDQLE 151
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 20806137     545 RIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRsvVCSDVEQ 595
Cdd:smart00487  152 KLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT--PLEPIEQ 200
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
593-723 1.26e-47

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: 165.76  E-value: 1.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  593 VEQQVIVIEEEKKFLKLLELLGHYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKL 672
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 20806137  673 LVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFI 723
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
617-714 9.59e-28

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: 108.07  E-value: 9.59e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137    617 QESGSVIIFVDKQEHAD-GLLKDlmRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYS 695
Cdd:pfam00271   13 ERGGKVLIFSQTKKTLEaELLLE--KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYD 90
                           90
                   ....*....|....*....
gi 20806137    696 CPNHYEDYVHRAGRTGRAG 714
Cdd:pfam00271   91 LPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
635-714 1.99e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.97  E-value: 1.99e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137     635 LLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAG 714
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
381-720 1.23e-17

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 87.64  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  381 MKILNSLKKHGYEKPTPIQTQAIPA-IMSGRDLIGIAKTGSGKT-IAFLLpMFRHIMdqrsleegEGPIAVIMTPTRELA 458
Cdd:COG1204    9 EKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTlIAELA-ILKALL--------NGGKALYIVPLRALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  459 LQITKECKKFSKTLGLRVVCVYGgtGISEQIAELKRgAEIIVCTPGRMIDMLAANSGrvtNLRRVTYVVLDEA------D 532
Cdd:COG1204   80 SEKYREFKRDFEELGIKVGVSTG--DYDSDDEWLGR-YDILVATPEKLDSLLRNGPS---WLRDVDLVVVDEAhliddeS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  533 RmfdmGFEPQVmrIVDNVR---PDRQTVMFSATFPRAmEALARRIlskpievqvgGRSVVCSD---VEQQVIVIEEEKKF 606
Cdd:COG1204  154 R----GPTLEV--LLARLRrlnPEAQIVALSATIGNA-EEIAEWL----------DAELVKSDwrpVPLNEGVLYDGVLR 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  607 LKLLELLGHYQ----------ESGSVIIFV---------------------------DKQEHADGLL--KDLMRASYP-- 645
Cdd:COG1204  217 FDDGSRRSKDPtlalaldlleEGGQVLVFVssrrdaeslakkladelkrrltpeereELEELAEELLevSEETHTNEKla 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  646 -CMSL-----HGGIDQYDRDSIINDFKNGTCKLLVATSVAARG--LDVKHLILVVNYSCPNHY---EDYVHRAGRTGRAG 714
Cdd:COG1204  297 dCLEKgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGvnLPARRVIIRDTKRGGMVPipvLEFKQMAGRAGRPG 376

                 ....*...
gi 20806137  715 --NKGYAY 720
Cdd:COG1204  377 ydPYGEAI 384
 
Name Accession Description Interval E-value
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
361-582 2.48e-166

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: 486.88  E-value: 2.48e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  361 TVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSL 440
Cdd:cd17953    1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  441 EEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNL 520
Cdd:cd17953   81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20806137  521 RRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 582
Cdd:cd17953  161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
PTZ00110 PTZ00110
helicase; Provisional
318-752 1.86e-154

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 468.87  E-value: 1.86e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   318 LEPVDHGKIEYEPFRKNFYVEVPELAKMSQEEVNVFRLEMEGITVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTP 397
Cdd:PTZ00110   76 LQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   398 IQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVV 477
Cdd:PTZ00110  156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   478 CVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANsgrVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTV 557
Cdd:PTZ00110  236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESN---VTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTL 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   558 MFSATFPRAMEALARRILS-KPIEVQVGGRSV-VCSDVEQQVIVIEEEKKFLKLLELLGHYQESGS-VIIFVDKQEHADG 634
Cdd:PTZ00110  313 MWSATWPKEVQSLARDLCKeEPVHVNVGSLDLtACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGDkILIFVETKKGADF 392
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   635 LLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAG 714
Cdd:PTZ00110  393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 20806137   715 NKGYAYTFITEDQARYAGDIIKALELSGTAVPPDLEKL 752
Cdd:PTZ00110  473 AKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKL 510
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
378-793 3.97e-149

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 450.37  E-value: 3.97e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  378 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSleegEGPIAVIMTPTREL 457
Cdd:COG0513    8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  458 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYVVLDEADRMFDM 537
Cdd:COG0513   84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGAL-DLSGVETLVLDEADRMLDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  538 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLKLLELLGHYq 617
Cdd:COG0513  161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDE- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  618 ESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCP 697
Cdd:COG0513  240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  698 NHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKAL--ELSGTAVPPDLEKLWSDFKDQQ-KAEGKIIKKSSGFS 774
Cdd:COG0513  320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIgqKIEEEELPGFEPVEEKRLERLKpKIKEKLKGKKAGRG 399
                        410
                 ....*....|....*....
gi 20806137  775 GKGFKFDETEQALANERKK 793
Cdd:COG0513  400 GRPGPKGERKARRGKRRRR 418
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
383-581 2.68e-101

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: 316.28  E-value: 2.68e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQIT 462
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  463 KECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFDMGFEPQ 542
Cdd:cd17952   81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKA---TNLQRVTYLVLDEADRMFDMGFEYQ 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 20806137  543 VMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 581
Cdd:cd17952  158 VRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
383-582 6.44e-97

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: 304.36  E-value: 6.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImDQRSLEEGEGPIAVIMTPTRELALQIT 462
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKL-LPEPKKKGRGPQALVLAPTRELAMQIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  463 KECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYVVLDEADRMFDMGFEPQ 542
Cdd:cd00268   80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLI--ERGKL-DLSNVKYLVLDEADRMLDMGFEED 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 20806137  543 VMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 582
Cdd:cd00268  157 VEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
383-582 4.67e-95

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: 299.67  E-value: 4.67e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQIT 462
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  463 KECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFDMGFEPQ 542
Cdd:cd17966   81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGK---TNLRRVTYLVLDEADRMLDMGFEPQ 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 20806137  543 VMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 582
Cdd:cd17966  158 IRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
384-734 2.74e-90

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 296.71  E-value: 2.74e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   384 LNSLkkhGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImDQRSLeegeGPIAVIMTPTRELALQITK 463
Cdd:PRK11776   19 LNEL---GYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-DVKRF----RVQALVLCPTRELADQVAK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   464 ECKKFSKTL-GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFDMGFEPQ 542
Cdd:PRK11776   91 EIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGT---LDLDALNTLVLDEADRMLDMGFQDA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   543 VMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVcSDVEQQVIVIEEEKKFLKLLELLGHYQESgSV 622
Cdd:PRK11776  168 IDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSPDERLPALQRLLLHHQPE-SC 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   623 IIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYED 702
Cdd:PRK11776  246 VVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEV 325
                         330       340       350
                  ....*....|....*....|....*....|..
gi 20806137   703 YVHRAGRTGRAGNKGYAYTFITEDQARYAGDI 734
Cdd:PRK11776  326 HVHRIGRTGRAGSKGLALSLVAPEEMQRANAI 357
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
327-584 1.31e-85

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: 277.28  E-value: 1.31e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  327 EYEPFRKNFYVEVPELAKMSQEEVNVFRLEMEgITVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAI 406
Cdd:cd18050   18 ELPKFEKNFYVEHPEVARMTQYDVEELRRKKE-ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  407 MSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGIS 486
Cdd:cd18050   97 LSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKG 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  487 EQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRA 566
Cdd:cd18050  177 PQIRDLERGVEICIATPGRLIDFLEAGK---TNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKE 253
                        250
                 ....*....|....*...
gi 20806137  567 MEALARRILSKPIEVQVG 584
Cdd:cd18050  254 VRQLAEDFLRDYVQINIG 271
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
378-748 4.82e-82

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 273.99  E-value: 4.82e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   378 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPI-AVIMTPTRE 456
Cdd:PRK10590    7 GLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   457 LALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFD 536
Cdd:PRK10590   87 LAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNA---VKLDQVEILVLDEADRMLD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   537 MGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLKLLEL--LG 614
Cdd:PRK10590  164 MGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMigKG 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   615 HYQEsgsVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNY 694
Cdd:PRK10590  244 NWQQ---VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 20806137   695 SCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKAL--ELSGTAVP---PD 748
Cdd:PRK10590  321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLkkEIPRIAIPgyePD 379
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
383-584 1.72e-81

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: 263.96  E-value: 1.72e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEG-----PIAVIMTPTREL 457
Cdd:cd17967   11 LLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPSALILAPTREL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  458 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYVVLDEADRMFDM 537
Cdd:cd17967   91 AIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI--ERGRI-SLSSIKFLVLDEADRMLDM 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 20806137  538 GFEPQVMRIVD----NVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVG 584
Cdd:cd17967  168 GFEPQIRKIVEhpdmPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
348-585 2.64e-79

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: 258.40  E-value: 2.64e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  348 EEVNVFRLEMEgITVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFL 427
Cdd:cd18049    1 QEVEQYRRSKE-ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  428 LPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMI 507
Cdd:cd18049   80 LPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20806137  508 DMLAANSgrvTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGG 585
Cdd:cd18049  160 DFLEAGK---TNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
346-575 2.97e-76

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: 251.43  E-value: 2.97e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  346 SQEEVNVFRLEMEGIT----------VKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGI 415
Cdd:cd18052    7 PEDEDEIFATIQTGINfdkydeipveVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMAC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  416 AKTGSGKTIAFLLPMFRHIMDQR----SLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAE 491
Cdd:cd18052   87 AQTGSGKTAAFLLPVLTGMMKEGltasSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  492 LKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNV----RPDRQTVMFSATFPRAM 567
Cdd:cd18052  167 IEKGCHILVATPGRLLDFI--GRGKI-SLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEI 243

                 ....*...
gi 20806137  568 EALARRIL 575
Cdd:cd18052  244 QRLAAEFL 251
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
383-581 4.80e-76

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: 248.15  E-value: 4.80e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSL-EEGEGPIAVIMTPTRELALQI 461
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  462 TKECKKFSKTlGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANsgrVTNLRRVTYVVLDEADRMFDMGFEP 541
Cdd:cd17958   81 EAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNN---VINLKSITYLVLDEADRMLDMGFEP 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 20806137  542 QVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 581
Cdd:cd17958  157 QIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
383-581 8.79e-76

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: 248.39  E-value: 8.79e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEE---GEGPIAVIMTPTRELAL 459
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEetkDDGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  460 QITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaanSGRVTNLRRVTYVVLDEADRMFDMGF 539
Cdd:cd17945   81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCL---ERRLLVLNQCTYVVLDEADRMIDMGF 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20806137  540 EPQVMRI-----VDNVRPD---------------RQTVMFSATFPRAMEALARRILSKPIEV 581
Cdd:cd17945  158 EPQVTKIldampVSNKKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
293-749 1.89e-75

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 258.18  E-value: 1.89e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   293 EYSSEEEEVDL-----QTALTGYQTKQRKllePVDHGKIEYEPFR-KNFYVEVPEL-AKMSQEEVNVFRLEMEgITVKGK 365
Cdd:PLN00206   39 EYICDETDDDIcslecKQALLRRVAKSRV---AVGAPKPKRLPATdECFYVRDPGStSGLSSSQAELLRRKLE-IHVKGE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   366 GCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRS--LEEG 443
Cdd:PLN00206  115 AVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSghPSEQ 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   444 EGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRV 523
Cdd:PLN00206  195 RNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHD---IELDNV 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   524 TYVVLDEADRMFDMGFEPQVMRIVDNVrPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEE 603
Cdd:PLN00206  272 SVLVLDEVDCMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETK 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   604 KKFLKL---LELLGHYQEsgSVIIFVDKQEHADgLLKDLMRAS--YPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSV 678
Cdd:PLN00206  351 QKKQKLfdiLKSKQHFKP--PAVVFVSSRLGAD-LLANAITVVtgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGV 427
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20806137   679 AARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKALELSGTAVPPDL 749
Cdd:PLN00206  428 LGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPREL 498
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
373-741 7.03e-72

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 251.31  E-value: 7.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   373 SWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrslEEGEGPIAVIMT 452
Cdd:PRK11634    7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD-----PELKAPQILVLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   453 PTRELALQITKECKKFSKTL-GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRRVtyvVLDEA 531
Cdd:PRK11634   82 PTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGL---VLDEA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   532 DRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLKLLE 611
Cdd:PRK11634  159 DEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   612 LLgHYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILV 691
Cdd:PRK11634  239 FL-EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 20806137   692 VNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKALELS 741
Cdd:PRK11634  318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLT 367
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
358-584 9.27e-71

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: 235.70  E-value: 9.27e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  358 EGITVK--GKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIM 435
Cdd:cd18051    5 EDIPVEatGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  436 DQ---RSLEEGEG--------PIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPG 504
Cdd:cd18051   85 EQgpgESLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  505 RMIDMLaaNSGRVtNLRRVTYVVLDEADRMFDMGFEPQVMRIV--DNVRP--DRQTVMFSATFPRAMEALARRILSKPIE 580
Cdd:cd18051  165 RLVDML--ERGKI-GLDYCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPtgERQTLMFSATFPKEIQMLARDFLDNYIF 241

                 ....
gi 20806137  581 VQVG 584
Cdd:cd18051  242 LAVG 245
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
384-737 6.80e-69

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 237.15  E-value: 6.80e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   384 LNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEgPIAVIMTPTRELALQITK 463
Cdd:PRK11192   13 LEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGP-PRILILTPTRELAMQVAD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   464 ECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFDMGFEPQV 543
Cdd:PRK11192   92 QARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEN---FDCRAVETLILDEADRMLDMGFAQDI 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   544 MRIVDNVRPDRQTVMFSATFP-RAMEALARRILSKPIEVQVGG----RSVV------CSDVEQQVIVIEEEKKFlkllel 612
Cdd:PRK11192  169 ETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPsrreRKKIhqwyyrADDLEHKTALLCHLLKQ------ 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   613 lghyQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVV 692
Cdd:PRK11192  243 ----PEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 20806137   693 NYSCPNHYEDYVHRAGRTGRAGNKGYAYTFI-TEDQ------ARYAGDIIKA 737
Cdd:PRK11192  319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVeAHDHlllgkiERYIEEPLKA 370
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
382-728 3.05e-66

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 229.47  E-value: 3.05e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   382 KILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGE--GPIAVIMTPTRELAL 459
Cdd:PRK04837   18 QVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKvnQPRALIMAPTRELAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   460 QITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANsgrVTNLRRVTYVVLDEADRMFDMGF 539
Cdd:PRK04837   98 QIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQN---HINLGAIQVVVLDEADRMFDLGF 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   540 epqvmriVDNVR------PD---RQTVMFSATFPRAMEALARRILSKPIEVQVggrsvvcsDVEQQVivieeekkflkll 610
Cdd:PRK04837  175 -------IKDIRwlfrrmPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVEV--------EPEQKT------------- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   611 ellGH-YQESgsviIFVDKQEHADGLLKDLMRASYP------------CMSLH--------------GGIDQYDRDSIIN 663
Cdd:PRK04837  227 ---GHrIKEE----LFYPSNEEKMRLLQTLIEEEWPdraiifantkhrCEEIWghlaadghrvglltGDVAQKKRLRILE 299
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20806137   664 DFKNGTCKLLVATSVAARGL---DVKHlilVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQA 728
Cdd:PRK04837  300 EFTRGDLDILVATDVAARGLhipAVTH---VFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYA 364
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
383-731 3.74e-66

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 233.69  E-value: 3.74e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSL--EEGEGPIAVIMTPTRELALQ 460
Cdd:PRK04537   20 LLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadRKPEDPRALILAPTRELAIQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   461 ITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANsgRVTNLRRVTYVVLDEADRMFDMGFE 540
Cdd:PRK04537  100 IHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQH--KVVSLHACEICVLDEADRMFDLGFI 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   541 PQVMRIVDNV--RPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQvIVIEEEKKFLKLLELLGHYQE 618
Cdd:PRK04537  178 KDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQR-IYFPADEEKQTLLLGLLSRSE 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   619 SGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPN 698
Cdd:PRK04537  257 GARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPF 336
                         330       340       350
                  ....*....|....*....|....*....|...
gi 20806137   699 HYEDYVHRAGRTGRAGNKGYAYTFITEdqaRYA 731
Cdd:PRK04537  337 DAEDYVHRIGRTARLGEEGDAISFACE---RYA 366
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
391-738 4.05e-65

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 227.87  E-value: 4.05e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   391 GYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEE---GEgPIAVIMTPTRELALQITKECKK 467
Cdd:PRK01297  106 GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymGE-PRALIIAPTRELVVQIAKDAAA 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   468 FSKTLGLRVVCVYGGTGISEQIAELK-RGAEIIVCTPGRMIDMlaaNSGRVTNLRRVTYVVLDEADRMFDMGFEPQVMRI 546
Cdd:PRK01297  185 LTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDF---NQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQI 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   547 VDNVRP--DRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLKLLELLGHyQESGSVII 624
Cdd:PRK01297  262 IRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLVTQ-NPWERVMV 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   625 FVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYV 704
Cdd:PRK01297  341 FANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYV 420
                         330       340       350
                  ....*....|....*....|....*....|....
gi 20806137   705 HRAGRTGRAGNKGYAYTFITEDQARYAGDIIKAL 738
Cdd:PRK01297  421 HRIGRTGRAGASGVSISFAGEDDAFQLPEIEELL 454
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
378-582 1.56e-64

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: 216.79  E-value: 1.56e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  378 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdqRSLEEGEGPIAVIMTPTREL 457
Cdd:cd17959    7 GLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL---KAHSPTVGARALILSPTREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  458 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFDM 537
Cdd:cd17959   84 ALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMN---LKLSSVEYVVFDEADRLFEM 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 20806137  538 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 582
Cdd:cd17959  161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
396-570 1.78e-63

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: 212.10  E-value: 1.78e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137    396 TPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdqrsLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLR 475
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL-----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137    476 VVCVYGGTGISEQIAELKrGAEIIVCTPGRMIDMLAansgRVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQ 555
Cdd:pfam00270   76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQ----ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQ 150
                          170
                   ....*....|....*
gi 20806137    556 TVMFSATFPRAMEAL 570
Cdd:pfam00270  151 ILLLSATLPRNLEDL 165
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
383-581 1.18e-62

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: 211.43  E-value: 1.18e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQR---SLEEGEGPIAVIMTPTRELAL 459
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEkklPFIKGEGPYGLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  460 QITKECKKFSKTL------GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAAnsgRVTNLRRVTYVVLDEADR 533
Cdd:cd17951   81 QTHEVIEYYCKALqeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNK---KKINLDICRYLCLDEADR 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 20806137  534 MFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 581
Cdd:cd17951  158 MIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
929-1031 1.31e-61

type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar proteins; DDX46, also called PRP5 homolog, is an ATP-dependent RNA helicase that plays an essential role in splicing, either prior to, or during splicing A complex formation. It inhibits antiviral innate responses by entrapping selected antiviral transcripts in the nucleus. It is also involved in the development of several tumors. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411901  Cd Length: 103  Bit Score: 204.47  E-value: 1.31e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  929 SFKRYEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1008
Cdd:cd22473    1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                         90       100
                 ....*....|....*....|...
gi 20806137 1009 LIKEELIRLQNSYQPTNKGRYKV 1031
Cdd:cd22473   81 LIKEELLRLQASYQPINKGRYKV 103
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
383-584 3.14e-61

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: 207.06  E-value: 3.14e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRsleEGEGPIAVIMTPTRELALQIT 462
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPR---KKKGLRALILAPTRELASQIY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  463 KECKKFSKTLGLRVVCVYGGT-GISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFDMGFEP 541
Cdd:cd17957   78 RELLKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGP---IDLSSVEYLVLDEADKLFEPGFRE 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 20806137  542 QVMRIVDNVR-PDRQTVMFSATFPRAMEALARRILSKPIEVQVG 584
Cdd:cd17957  155 QTDEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
379-577 2.24e-59

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: 202.43  E-value: 2.24e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  379 ISMKILNSLKKHGYEKPTPIQTQAIPAIMS-GRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTREL 457
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  458 ALQITKECKKFSKTL-GLRVVCVYGGTGISEQIAELKR-GAEIIVCTPGRMIDMLAANSGRVTnLRRVTYVVLDEADRMF 535
Cdd:cd17964   81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVAKA-FTDLDYLVLDEADRLL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 20806137  536 DMGFEPQVMRIVDNVRP----DRQTVMFSATFPRAMEALARRILSK 577
Cdd:cd17964  160 DMGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLKK 205
PTZ00424 PTZ00424
helicase 45; Provisional
382-726 9.35e-58

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 204.68  E-value: 9.35e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   382 KILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHI-MDQRSLEegegpiAVIMTPTRELALQ 460
Cdd:PTZ00424   38 DLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIdYDLNACQ------ALILAPTRELAQQ 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   461 ITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRrvtYVVLDEADRMFDMGFE 540
Cdd:PTZ00424  112 IQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLK---LFILDEADEMLSRGFK 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   541 PQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLKLLELLGHYQESG 620
Cdd:PTZ00424  189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTIT 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   621 SVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHY 700
Cdd:PTZ00424  269 QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP 348
                         330       340
                  ....*....|....*....|....*.
gi 20806137   701 EDYVHRAGRTGRAGNKGYAYTFITED 726
Cdd:PTZ00424  349 ENYIHRIGRSGRFGRKGVAINFVTPD 374
DEXDc smart00487
DEAD-like helicases superfamily;
387-595 9.16e-57

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 194.63  E-value: 9.16e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137     387 LKKHGYEKPTPIQTQAIPAIMSG-RDLIGIAKTGSGKTIAFLLPMFRHIMdqrsleEGEGPIAVIMTPTRELALQITKEC 465
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137     466 KKFSKTLGLRVVCVYGGTGISEQIAELKRG-AEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFDMGFEPQVM 544
Cdd:smart00487   75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDK---LSLSNVDLVILDEAHRLLDGGFGDQLE 151
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 20806137     545 RIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRsvVCSDVEQ 595
Cdd:smart00487  152 KLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT--PLEPIEQ 200
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
378-582 1.10e-56

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: 194.37  E-value: 1.10e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  378 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFrhimdQRSLEEGEGPIAVIMTPTREL 457
Cdd:cd17955    5 GLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-----QRLSEDPYGIFALVLTPTREL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  458 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRRVTYVVLDEADRMFDM 537
Cdd:cd17955   80 AYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTKVLSRVKFLVLDEADRLLTG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 20806137  538 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 582
Cdd:cd17955  160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
373-582 2.19e-56

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: 193.69  E-value: 2.19e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  373 SWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRsleegEGPIAVIMT 452
Cdd:cd17954    1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENP-----QRFFALVLA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  453 PTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGrvTNLRRVTYVVLDEAD 532
Cdd:cd17954   76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKG--FSLKSLKFLVMDEAD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 20806137  533 RMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 582
Cdd:cd17954  154 RLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
383-581 1.28e-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: 188.14  E-value: 1.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMfrhIMdqRSLEEGEGPIAVIMTPTRELALQIT 462
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPV---II--RCLTEHRNPSALILTPTRELAVQIE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  463 KECKKFSKTL-GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFDMGFEP 541
Cdd:cd17962   76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSS---VELDNIKIVVVDEADTMLKMGFQQ 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 20806137  542 QVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 581
Cdd:cd17962  153 QVLDILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
383-582 1.38e-53

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: 185.54  E-value: 1.38e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPmfrhIMDQRSLEEGEGPI--AVIMTPTRELALQ 460
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLP----ILERLLYRPKKKAAtrVLVLVPTRELAMQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  461 ITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaANSGRVTnLRRVTYVVLDEADRMFDMGFE 540
Cdd:cd17947   77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHL-RNSPSFD-LDSIEILVLDEADRMLEEGFA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 20806137  541 PQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 582
Cdd:cd17947  155 DELKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
391-581 4.92e-52

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: 181.34  E-value: 4.92e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  391 GYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHI-MDQRSLEegegpiAVIMTPTRELALQITKECKKFS 469
Cdd:cd17940   18 GFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdPKKDVIQ------ALILVPTRELALQTSQVCKELG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  470 KTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaanSGRVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDN 549
Cdd:cd17940   92 KHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLA---KKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNF 168
                        170       180       190
                 ....*....|....*....|....*....|..
gi 20806137  550 VRPDRQTVMFSATFPRAMEALARRILSKPIEV 581
Cdd:cd17940  169 LPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
383-581 6.28e-51

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: 178.15  E-value: 6.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQIT 462
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  463 KECKKFSKTLG--LRVVCVYGGTGISEQIAELKR-GAEIIVCTPGRMIDMLAANSGRVtNLRRVTYVVLDEADRMFDMGF 539
Cdd:cd17960   81 EVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKV-KVKSLEVLVLDEADRLLDLGF 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 20806137  540 EPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 581
Cdd:cd17960  160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
383-563 1.04e-50

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: 178.59  E-value: 1.04e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIP-AIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRS----LEEGEGPIAVIMTPTREL 457
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSsngvGGKQKPLRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  458 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRRVTYVVLDEADRMFDM 537
Cdd:cd17946   81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSLRFLVLDEADRMLEK 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 20806137  538 G-FEP--QVMRIVDNVRP----DRQTVMFSATF 563
Cdd:cd17946  161 GhFAEleKILELLNKDRAgkkrKRQTFVFSATL 193
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
383-583 5.80e-49

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: 172.47  E-value: 5.80e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQR-SLEEGEGpiAVIMTPTRELALQI 461
Cdd:cd17941    1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwTPEDGLG--ALIISPTRELAMQI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  462 TKECKKFSKTLGLRVVCVYGGTGISEqiaELKRGAE--IIVCTPGRMIDMLAANSGRVTNLRRVtyVVLDEADRMFDMGF 539
Cdd:cd17941   79 FEVLRKVGKYHSFSAGLIIGGKDVKE---EKERINRmnILVCTPGRLLQHMDETPGFDTSNLQM--LVLDEADRILDMGF 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 20806137  540 EPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQV 583
Cdd:cd17941  154 KETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
593-723 1.26e-47

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: 165.76  E-value: 1.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  593 VEQQVIVIEEEKKFLKLLELLGHYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKL 672
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 20806137  673 LVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFI 723
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
388-579 4.91e-47

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: 167.38  E-value: 4.91e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  388 KKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIM-DQRSLEEGEGPIAVIMTPTRELALQITKECK 466
Cdd:cd17949    7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPRVDRSDGTLALVLVPTRELALQIYEVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  467 KF-SKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDML-AANSGRVTNLRrvtYVVLDEADRMFDMGFEPQVM 544
Cdd:cd17949   87 KLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLR---WLVLDEADRLLDMGFEKDIT 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 20806137  545 RIVDNVR-------------PDRQTVMFSATFPRAMEALARRILSKPI 579
Cdd:cd17949  164 KILELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPV 211
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
383-581 1.54e-44

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


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 159.83  E-value: 1.54e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEgEGPIAVIMTPTRELALQI- 461
Cdd:cd17942    1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPR-NGTGVIIISPTRELALQIy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  462 --TKE-CKKFSKTLGlrvvCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVT-NLRrvtYVVLDEADRMFDM 537
Cdd:cd17942   80 gvAKElLKYHSQTFG----IVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYkNLQ---CLIIDEADRILEI 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 20806137  538 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRIL-SKPIEV 581
Cdd:cd17942  153 GFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLkKKPLYV 197
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
378-581 4.50e-44

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: 158.26  E-value: 4.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  378 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHI-MDQRSLEegegpiAVIMTPTRE 456
Cdd:cd17939    3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQ------ALVLAPTRE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  457 LALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRrvtYVVLDEADRMFD 536
Cdd:cd17939   77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIK---MFVLDEADEMLS 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 20806137  537 MGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 581
Cdd:cd17939  154 RGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
383-579 2.05e-40

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: 148.12  E-value: 2.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGE-GPIAVIMTPTRELALQI 461
Cdd:cd17961    5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqGTRALILVPTRELAQQV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  462 TKECKKFSKTLG--LRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVTNLRRVTYVVLDEADRMFDMGF 539
Cdd:cd17961   85 SKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHL--ESGSLLLLSTLKYLVIDEADLVLSYGY 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 20806137  540 EPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPI 579
Cdd:cd17961  163 EEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
383-582 8.65e-40

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 145.87  E-value: 8.65e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFrhimdQRSLEEGEGPIAVIMTPTRELALQIT 462
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-----ESLDLERRHPQVLILAPTREIAVQIH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  463 KECKKFSKTL-GLRVVCVYGGTGISEQIAELKRgAEIIVCTPGRMIDMLAANSGRVTNLRrvtYVVLDEADRMFDMGFEP 541
Cdd:cd17943   76 DVFKKIGKKLeGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVR---LFVLDEADKLMEGSFQK 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 20806137  542 QVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 582
Cdd:cd17943  152 DVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
391-581 1.42e-39

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: 145.41  E-value: 1.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  391 GYEKPTPIQTQAIPAIMSG--RDLIGIAKTGSGKTIAFLLPMFRHImDQRSLEegegPIAVIMTPTRELALQITKECKKF 468
Cdd:cd17963   13 GFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKS----PQALCLAPTRELARQIGEVVEKM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  469 SKTLGLRVVC------VYGGTGISEQIaelkrgaeiIVCTPGRMIDMLAAnsgRVTNLRRVTYVVLDEADRMFDM-GFEP 541
Cdd:cd17963   88 GKFTGVKVALavpgndVPRGKKITAQI---------VIGTPGTVLDWLKK---RQLDLKKIKILVLDEADVMLDTqGHGD 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 20806137  542 QVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 581
Cdd:cd17963  156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
383-581 1.88e-38

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: 143.28  E-value: 1.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGE--GPIAVIMTPTRELALQ 460
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfnAPRGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  461 ITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRmidMLAANSGRVTNLRRVTYVVLDEADRMFDMGFE 540
Cdd:cd17948   81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGA---LSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 20806137  541 PQVMRIV-------------DNVRPDRQTVMFSATFPRAMealaRRILSKPIEV 581
Cdd:cd17948  158 EKLSHFLrrfplasrrsentDGLDPGTQLVLVSATMPSGV----GEVLSKVIDV 207
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
387-580 3.49e-38

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: 141.52  E-value: 3.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  387 LKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIM-DQRSLEEGEGPIAVIMTPTRELALQITKEC 465
Cdd:cd17944    5 LQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQVTKDF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  466 KKFSKTLglRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYVVLDEADRMFDMGFEPQVMR 545
Cdd:cd17944   85 KDITRKL--SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHL--QNGRL-DLTKLKHVVLDEVDQMLDMGFAEQVEE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 20806137  546 IVD-----NVRPDRQTVMFSATFPRAMEALARRILSKPIE 580
Cdd:cd17944  160 ILSvsykkDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYE 199
KH-I_AtRH42_like cd22475
type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana DEAD-box ATP-dependent ...
931-1031 1.75e-37

type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana DEAD-box ATP-dependent RNA helicase RH42 and similar proteins; RH42, also called DEAD-box RNA helicase RCF1, or REGULATOR OF CBF GENE EXPRESSION 1, is a helicase required for pre-mRNA splicing, cold-responsive gene regulation and cold tolerance. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411903  Cd Length: 102  Bit Score: 135.98  E-value: 1.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  931 KRYEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITRlI 1010
Cdd:cd22475    3 EHFEEELEINDFPQHARWKVTHKDTLGQISELTGAAITTRGQYYPPGRIPGPGERKLYLLIEGPSEASVKEAKAEIKR-I 81
                         90       100
                 ....*....|....*....|.
gi 20806137 1011 KEELIRLQNSYQPTNKGRYKV 1031
Cdd:cd22475   82 LEEATEKASRPGGQQPGRYSV 102
KH-I_DDX46_like cd22387
type I K homology (KH) RNA-binding domain found in the family of DEAD box protein 46 (DDX46); ...
929-1010 1.54e-36

type I K homology (KH) RNA-binding domain found in the family of DEAD box protein 46 (DDX46); The DDX46 family includes DEAD box protein 46 (DDX46), fungal pre-mRNA-processing ATP-dependent RNA helicase PRP5, Arabidopsis thaliana DEAD-box ATP-dependent RNA helicase RH42 and similar proteins. DDX46, also called PRP5 homolog, is an ATP-dependent RNA helicase that plays an essential role in splicing, either prior to, or during splicing A complex formation. It inhibits antiviral innate responses by entrapping selected antiviral transcripts in the nucleus. It is also involved in the development of several tumors. PRP5 is an ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. It catalyzes an ATP-dependent conformational change of U2 snRNP. PRP5 interacts with the U2 snRNP and HSH155. RH42, also called DEAD-box RNA helicase RCF1, or REGULATOR OF CBF GENE EXPRESSION 1, is a helicase required for pre-mRNA splicing, cold-responsive gene regulation and cold tolerance. Members in this family contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411815  Cd Length: 82  Bit Score: 132.40  E-value: 1.54e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  929 SFKRYEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1008
Cdd:cd22387    1 NNGNFVEEFEINDYPQIARLKVTSKEVLNSIMEETGATITIKGQYYPPGKKPKPGERKLYLLIEGATEESVQSARNEIKR 80

                 ..
gi 20806137 1009 LI 1010
Cdd:cd22387   81 VL 82
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
383-583 2.92e-36

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 136.32  E-value: 2.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdqrslEEGEGPIAVI-MTPTRELALQI 461
Cdd:cd17950   13 LLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL------EPVDGQVSVLvICHTRELAFQI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  462 TKECKKFSKTL-GLRVVCVYGGTGISEQIAELKRGA-EIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMF-DMG 538
Cdd:cd17950   87 SNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKK---LKLSHVKHFVLDECDKMLeQLD 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 20806137  539 FEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQV 583
Cdd:cd17950  164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
391-562 1.17e-35

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: 134.37  E-value: 1.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  391 GYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrsleegegpiAVIMTPTRELALQITKECKKFSK 470
Cdd:cd17938   18 DWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------ALILEPSRELAEQTYNCIENFKK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  471 TL---GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYVVLDEADRMFDMGFEPQVMRIV 547
Cdd:cd17938   86 YLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLI--KTGKL-DLSSVRFFVLDEADRLLSQGNLETINRIY 162
                        170       180
                 ....*....|....*....|.
gi 20806137  548 D-----NVRPDR-QTVMFSAT 562
Cdd:cd17938  163 NripkiTSDGKRlQVIVCSAT 183
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
390-581 6.87e-34

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


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 129.10  E-value: 6.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  390 HGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdQRSLEEgegPIAVIMTPTRELALQITKECKKFS 469
Cdd:cd18046   17 YGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI--DTSLKA---TQALVLAPTRELAQQIQKVVMALG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  470 KTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRrvtYVVLDEADRMFDMGFEPQVMRIVDN 549
Cdd:cd18046   92 DYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIK---MFVLDEADEMLSRGFKDQIYDIFQK 168
                        170       180       190
                 ....*....|....*....|....*....|..
gi 20806137  550 VRPDRQTVMFSATFPRAMEALARRILSKPIEV 581
Cdd:cd18046  169 LPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
378-581 1.55e-33

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: 128.35  E-value: 1.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  378 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdQRSLEEgegPIAVIMTPTREL 457
Cdd:cd18045    5 GLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL--DIQVRE---TQALILSPTREL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  458 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRrvtYVVLDEADRMFDM 537
Cdd:cd18045   80 AVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIK---MLVLDEADEMLNK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 20806137  538 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 581
Cdd:cd18045  157 GFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
383-578 1.55e-31

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: 123.51  E-value: 1.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  383 ILNSLKKHGYEKPTPIQTQAIPAIMSG---------RDLIGIAKTGSGKTIAFLLPMFRHIMDQ--RSLEegegpiAVIM 451
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRvvPRLR------ALIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  452 TPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRG--------AEIIVCTPGRMIDMLAANSGrvTNLRRV 523
Cdd:cd17956   75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPG--FTLKHL 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20806137  524 TYVVLDEADRMFDMGFE---PQVMRIVDNVRPDR-----------------QTVMFSATFPRAMEALARRILSKP 578
Cdd:cd17956  153 RFLVIDEADRLLNQSFQdwlETVMKALGRPTAPDlgsfgdanllersvrplQKLLFSATLTRDPEKLSSLKLHRP 227
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
617-714 9.59e-28

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: 108.07  E-value: 9.59e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137    617 QESGSVIIFVDKQEHAD-GLLKDlmRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYS 695
Cdd:pfam00271   13 ERGGKVLIFSQTKKTLEaELLLE--KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYD 90
                           90
                   ....*....|....*....
gi 20806137    696 CPNHYEDYVHRAGRTGRAG 714
Cdd:pfam00271   91 LPWNPASYIQRIGRAGRAG 109
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
386-573 4.26e-25

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: 105.54  E-value: 4.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  386 SLKKHGYEKPTPIQTQAIPAI----MSGRDLIGI------------AKTGSGKTIAFLLPMFRHI--MDQRSLEEGEG-- 445
Cdd:cd17965   22 SNKTDEEIKPSPIQTLAIKKLlktlMRKVTKQTSneepklevfllaAETGSGKTLAYLAPLLDYLkrQEQEPFEEAEEey 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  446 --------PIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGIS-EQIAEL-KRGAEIIVCTPGRmIDMLAANSG 515
Cdd:cd17965  102 esakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSyQRLQLAfKGRIDILVTTPGK-LASLAKSRP 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 20806137  516 RVtnLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARR 573
Cdd:cd17965  181 KI--LSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRK 236
HELICc smart00490
helicase superfamily c-terminal domain;
635-714 1.99e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.97  E-value: 1.99e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137     635 LLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAG 714
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
KH-I_PRP5_like cd22474
type I K homology (KH) RNA-binding domain found in fungal pre-mRNA-processing ATP-dependent ...
937-1012 5.69e-22

type I K homology (KH) RNA-binding domain found in fungal pre-mRNA-processing ATP-dependent RNA helicase PRP5 and similar proteins; PRP5 is an ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. It catalyzes an ATP-dependent conformational change of U2 snRNP. PRP5 interacts with the U2 snRNP and HSH155. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411902  Cd Length: 89  Bit Score: 91.23  E-value: 5.69e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20806137  937 LEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKE--GERKIYLAIESANELAVQKAKAEITRLIKE 1012
Cdd:cd22474    9 VEINDLPQKARWEATNNTSLSKIIEETGCSITNKGNFYPPGKEPQPnnDEPKLYLLIEGTTEKAVRLAIELLRRKLVE 86
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
371-578 3.32e-21

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: 93.55  E-value: 3.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  371 IKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSG--RDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLeegegPIA 448
Cdd:cd18048   17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY-----PQC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  449 VIMTPTRELALQITKECKKFSK-TLGLRVVCVYGGT--GISEQIAelkrgAEIIVCTPGRMIDMlaANSGRVTNLRRVTY 525
Cdd:cd18048   92 LCLSPTFELALQTGKVVEEMGKfCVGIQVIYAIRGNrpGKGTDIE-----AQIVIGTPGTVLDW--CFKLRLIDVTNISV 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 20806137  526 VVLDEADRMFDM-GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKP 578
Cdd:cd18048  165 FVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
381-720 1.23e-17

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 87.64  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  381 MKILNSLKKHGYEKPTPIQTQAIPA-IMSGRDLIGIAKTGSGKT-IAFLLpMFRHIMdqrsleegEGPIAVIMTPTRELA 458
Cdd:COG1204    9 EKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTlIAELA-ILKALL--------NGGKALYIVPLRALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  459 LQITKECKKFSKTLGLRVVCVYGgtGISEQIAELKRgAEIIVCTPGRMIDMLAANSGrvtNLRRVTYVVLDEA------D 532
Cdd:COG1204   80 SEKYREFKRDFEELGIKVGVSTG--DYDSDDEWLGR-YDILVATPEKLDSLLRNGPS---WLRDVDLVVVDEAhliddeS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  533 RmfdmGFEPQVmrIVDNVR---PDRQTVMFSATFPRAmEALARRIlskpievqvgGRSVVCSD---VEQQVIVIEEEKKF 606
Cdd:COG1204  154 R----GPTLEV--LLARLRrlnPEAQIVALSATIGNA-EEIAEWL----------DAELVKSDwrpVPLNEGVLYDGVLR 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  607 LKLLELLGHYQ----------ESGSVIIFV---------------------------DKQEHADGLL--KDLMRASYP-- 645
Cdd:COG1204  217 FDDGSRRSKDPtlalaldlleEGGQVLVFVssrrdaeslakkladelkrrltpeereELEELAEELLevSEETHTNEKla 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  646 -CMSL-----HGGIDQYDRDSIINDFKNGTCKLLVATSVAARG--LDVKHLILVVNYSCPNHY---EDYVHRAGRTGRAG 714
Cdd:COG1204  297 dCLEKgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGvnLPARRVIIRDTKRGGMVPipvLEFKQMAGRAGRPG 376

                 ....*...
gi 20806137  715 --NKGYAY 720
Cdd:COG1204  377 ydPYGEAI 384
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
394-870 2.68e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 86.62  E-value: 2.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  394 KPTPIQTQAIPAIMS-----GRDLIGIAKTGSGKTIAFLLPMFRHIMDQRsleegegpiAVIMTPTRELALQITKECKKF 468
Cdd:COG1061   80 ELRPYQQEALEALLAalergGGRGLVVAPTGTGKTVLALALAAELLRGKR---------VLVLVPRRELLEQWAEELRRF 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  469 sktlgLRVVCVYGGtgiseqiaELKRGAEIIVCTpgrmIDMLAANSGRVTNLRRVTYVVLDEADRMFDMGFEpqvmRIVD 548
Cdd:COG1061  151 -----LGDPLAGGG--------KKDSDAPITVAT----YQSLARRAHLDELGDRFGLVIIDEAHHAGAPSYR----RILE 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  549 NVRPDRqTVMFSATFPR-------------------AMEALARRILSKP--IEVQVGGRS-----VVCSDVEQQVIVIEE 602
Cdd:COG1061  210 AFPAAY-RLGLTATPFRsdgreillflfdgivyeysLKEAIEDGYLAPPeyYGIRVDLTDeraeyDALSERLREALAADA 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  603 EKKFLKLLELLGHYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARG 682
Cdd:COG1061  289 ERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEG 368
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  683 LDV---KHLILVVNYSCPNHyedYVHRAGRTGR-AGNKGYA--YTFITEdqaryagdiikalelsgtavppDLEKLWSDF 756
Cdd:COG1061  369 VDVprlDVAILLRPTGSPRE---FIQRLGRGLRpAPGKEDAlvYDFVGN----------------------DVPVLEELA 423
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  757 KDQQKAEGKIIKKSSGFSGKGFKFDETEQALANERKKLQKAALGLQDSDDEDAAVDIDEQIESMFNSKKRVKDMAAPGTS 836
Cdd:COG1061  424 KDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEG 503
                        490       500       510
                 ....*....|....*....|....*....|....
gi 20806137  837 SAPAPTAGNAEKLEIAKRLALRINAQKNLGIESQ 870
Cdd:COG1061  504 KAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLE 537
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
409-562 5.01e-17

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 78.98  E-value: 5.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  409 GRDLIGIAKTGSGKTIAFLLPMFRHIMDQrsleegeGPIAVIMTPTRELALQITKECKKFSKtLGLRVVCVYGGTGISEQ 488
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLKK-------GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEER 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20806137  489 IAELKRGAEIIVCTPGRMIDMLAANSGRVtnLRRVTYVVLDEADRMFDMGFEPQVMRIVDN--VRPDRQTVMFSAT 562
Cdd:cd00046   73 EKNKLGDADIIIATPDMLLNLLLREDRLF--LKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
382-721 8.60e-17

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: 85.66  E-value: 8.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  382 KILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrsleEGEGPIAVIMTPTRELAL-Q 460
Cdd:COG1205   44 ELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL------EDPGATALYLYPTKALARdQ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  461 ItKECKKFSKTLGLRV-VCVY-GGTGISEQiAELKRGAEIIVCTPgrmiDM-----LAANSGRVTNLRRVTYVVLDEA-- 531
Cdd:COG1205  118 L-RRLRELAEALGLGVrVATYdGDTPPEER-RWIREHPDIVLTNP----DMlhyglLPHHTRWARFFRNLRYVVIDEAht 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  532 -------------DRMfdmgfepqvMRIVDNVRPDRQTVMFSATFPRAmEALARRILSKPIEVqV-------GGRsvvcs 591
Cdd:COG1205  192 yrgvfgshvanvlRRL---------RRICRHYGSDPQFILASATIGNP-AEHAERLTGRPVTV-VdedgsprGER----- 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  592 dveqqVIVIEEEKKFLKLLELLGHYQ---------ESG-SVIIFVD------------KQEHADGLLKDLMRAsYpcmsl 649
Cdd:COG1205  256 -----TFVLWNPPLVDDGIRRSALAEaarlladlvREGlRTLVFTRsrrgaellaryaRRALREPDLADRVAA-Y----- 324
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20806137  650 HGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYT 721
Cdd:COG1205  325 RAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
396-574 1.02e-16

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: 79.23  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  396 TPIQTQAIPAIM-SGRDLIGIAKTGSGKTIAFLLPMFRHIMDQrsleegeGPIAVIMTPTRELALQITKECKKFSKTLGL 474
Cdd:cd17921    3 NPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATS-------GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  475 RVVCVYGGTGISeqiAELKRGAEIIVCTPGRMIDMLaaNSGRVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVR--- 551
Cdd:cd17921   76 NVGLLTGDPSVN---KLLLAEADILVATPEKLDLLL--RNGGERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrin 150
                        170       180
                 ....*....|....*....|...
gi 20806137  552 PDRQTVMFSATFPRAMEaLARRI 574
Cdd:cd17921  151 KNARFVGLSATLPNAED-LAEWL 172
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
372-578 2.17e-15

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: 75.91  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  372 KSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSG--RDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEgegpiAV 449
Cdd:cd18047    1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ-----CL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  450 IMTPTRELALQITKECKKFSKTLGlRVVCVYGGTGiseqiAELKRGA----EIIVCTPGRMIDMLAanSGRVTNLRRVTY 525
Cdd:cd18047   76 CLSPTYELALQTGKVIEQMGKFYP-ELKLAYAVRG-----NKLERGQkiseQIVIGTPGTVLDWCS--KLKFIDPKKIKV 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 20806137  526 VVLDEADRMF-DMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKP 578
Cdd:cd18047  148 FVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
399-574 6.97e-13

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: 68.00  E-value: 6.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  399 QTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRsleegeGPIAVIMTPTRELALQITKECKKFSKTLGLRVVC 478
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELLEQLGLGIRV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  479 -VYGG-TGISEQIAELKRGAEIIVCTPgrmiDMLAA-----NSGRVTNLRRVTYVVLDEAdRMFDMGFEPQV-------M 544
Cdd:cd17923   79 aTYDGdTPREERRAIIRNPPRILLTNP----DMLHYallphHDRWARFLRNLRYVVLDEA-HTYRGVFGSHValllrrlR 153
                        170       180       190
                 ....*....|....*....|....*....|
gi 20806137  545 RIVDNVRPDRQTVMFSATFpRAMEALARRI 574
Cdd:cd17923  154 RLCRRYGADPQFILTSATI-GNPAEHARTL 182
KH-I_KHDC4_rpt1 cd22385
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
933-1010 2.25e-10

first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411813  Cd Length: 84  Bit Score: 57.99  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  933 YEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPG--KEPKEGERKIYLAIESANELAVQKAKAEITRLI 1010
Cdd:cd22385    5 YVAEIEINDLPNTCRNLLTKGSTQEEIQKESGAAVSTRGRYMPPEekATFNPGERPLYLHVQAPTKEAVDRAVNKINEII 84
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
398-572 6.38e-09

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: 56.98  E-value: 6.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  398 IQTQAIPAIM-SGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEgPIAVIMTPTRELALQITKECK-KFSKtLGLR 475
Cdd:cd18023    5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDWKeKFGP-LGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  476 VVCVYGGTGI--SEQIaelkRGAEIIVCTPGRMIDMLAANSGRVTNLRRVTYVVLDE---------------ADRMFDMG 538
Cdd:cd18023   83 CAELTGDTEMddTFEI----QDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDEvhiikenrgatlevvVSRMKTLS 158
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 20806137  539 FEPQVMR-IVDNVRpdrqTVMFSATFPRAmEALAR 572
Cdd:cd18023  159 SSSELRGsTVRPMR----FVAVSATIPNI-EDLAE 188
KH-I_RIK_like_rpt1 cd22471
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and ...
936-1010 8.95e-09

first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and similar proteins; RIK, also called rough sheath 2-interacting KH domain protein, or RS2-interacting KH domain protein, is a RNA binding protein that acts together with RS2/AS1 in the recruitment of HIRA. RIK contains two type I K homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411899  Cd Length: 91  Bit Score: 53.63  E-value: 8.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  936 ELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANEL---------AVQKAKAEI 1006
Cdd:cd22471    8 EIVINDAPPSVRHHLTKRSTQDEIQSKTGVVVVTRGRYYPPGTPPPDNEKPLYLHITAGAQLppddaerqkAVDAAAADI 87

                 ....
gi 20806137 1007 TRLI 1010
Cdd:cd22471   88 QAML 91
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
394-533 9.37e-09

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: 56.67  E-value: 9.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  394 KPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEgpiAVIMTPTRELALQITKECKKFSKTLG 473
Cdd:cd17927    2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGK---VVFLANKVPLVEQQKEVFRKHFERPG 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  474 LRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVTNLRRVTYVVLDEADR 533
Cdd:cd17927   79 YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDL--KSGTIVSLSDFSLLVFDECHN 136
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
409-530 9.66e-09

DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 55.67  E-value: 9.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  409 GRDLIGIAKTGSGKTIAFLLPMFRHIMDqrsleEGEGPIAVI-MTPTRELALQITKECKKFSK--TLGLRVVCVYGGTGI 485
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLAD-----EPEKGVQVLyISPLKALINDQERRLEEPLDeiDLEIPVAVRHGDTSQ 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 20806137  486 SEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTnLRRVTYVVLDE 530
Cdd:cd17922   76 SEKAKQLKNPPGILITTPESLELLLVNKKLREL-FAGLRYVVVDE 119
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
387-575 1.28e-08

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 56.00  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  387 LKKH-GYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFrhimdqrsLEEGegpIAVIMTPTreLAL---QIT 462
Cdd:cd17920    4 LKEVfGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL--------LLDG---VTLVVSPL--ISLmqdQVD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  463 KeCkkfsKTLGLRVVCVYGGTGISEQ---IAELKRG-AEIIVCTP-----GRMIDMLAansgRVTNLRRVTYVVLDEA-- 531
Cdd:cd17920   71 R-L----QQLGIRAAALNSTLSPEEKrevLLRIKNGqYKLLYVTPerllsPDFLELLQ----RLPERKRLALIVVDEAhc 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 20806137  532 ------DrmfdmgFEPQVMRI--VDNVRPDRQTVMFSATFPRAMEALARRIL 575
Cdd:cd17920  142 vsqwghD------FRPDYLRLgrLRRALPGVPILALTATATPEVREDILKRL 187
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
615-719 2.05e-08

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: 54.13  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  615 HYQESGSV--IIFVdKQEHADGLLKDLM------RASYPCMSL--HGGIDQYDRD--------SIINDFKNGTCKLLVAT 676
Cdd:cd18802   19 YFPKTPDFrgIIFV-ERRATAVVLSRLLkehpstLAFIRCGFLigRGNSSQRKRSlmtqrkqkETLDKFRDGELNLLIAT 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 20806137  677 SVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRtGRAGNKGYA 719
Cdd:cd18802   98 SVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNSKYI 139
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
394-530 2.92e-08

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: 55.17  E-value: 2.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  394 KPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSleEGEGPIAVIMTPTRELALQ-ITKECKKFSKtl 472
Cdd:cd18036    2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRS--AGEKGRVVVLVNKVPLVEQqLEKFFKYFRK-- 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20806137  473 GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVTNLRRV---TYVVLDE 530
Cdd:cd18036   78 GYKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNL--LSGREEERVYLsdfSLLIFDE 136
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
671-724 5.88e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 50.78  E-value: 5.88e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 20806137  671 KLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFIT 724
Cdd:cd18785   24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
397-568 7.89e-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: 53.11  E-value: 7.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  397 PIQTQAIPA-IMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrsleegEGPIAVIMTPTRELALQITKECKKFSKtLGLR 475
Cdd:cd18028    4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLL--------EGGKALYLVPLRALASEKYEEFKKLEE-IGLK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  476 VVCvygGTGISEQIAELKRGAEIIVCTPGRmIDMLAANsgRVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVR---P 552
Cdd:cd18028   75 VGI---STGDYDEDDEWLGDYDIIVATYEK-FDSLLRH--SPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnP 148
                        170
                 ....*....|....*.
gi 20806137  553 DRQTVMFSATFPRAME 568
Cdd:cd18028  149 NTQIIGLSATIGNPDE 164
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
615-722 8.33e-08

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


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 52.21  E-value: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  615 HYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNY 694
Cdd:cd18794   26 VEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHY 105
                         90       100
                 ....*....|....*....|....*...
gi 20806137  695 SCPNHYEDYVHRAGRTGRAGNKGYAYTF 722
Cdd:cd18794  106 SLPKSMESYYQESGRAGRDGLPSECILF 133
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
622-815 3.56e-07

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 54.35  E-value: 3.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  622 VIIFVDKQEHADGLLKDLMRASYPCMSLHG--------GIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVN 693
Cdd:COG1111  356 IIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIF 435
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  694 yscpnhYED------YVHRAGRTGRaGNKGYAYTFITE---DQARY---------AGDIIKAL-----ELSGTAVPPDLE 750
Cdd:COG1111  436 ------YEPvpseirSIQRKGRTGR-KREGRVVVLIAKgtrDEAYYwssrrkekkMKSILKKLkklldKQEKEKLKESAQ 508
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20806137  751 KLWSDFKDQQKAEGKIIKKSSGFSGKGFKFDETEQALANERKKLQKAALGLQDSDDEDAAVDIDE 815
Cdd:COG1111  509 ATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVIVSTLAESLELRELGEKVDDE 573
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
391-564 2.10e-06

N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 49.68  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  391 GYEKPTPIQTQAIP-AIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSlEEGEGPIA----VIMTPTRELALQITKEC 465
Cdd:cd18019   14 GFKSLNRIQSKLFPaAFETDENLLLCAPTGAGKTNVALLTILREIGKHRN-PDGTINLDafkiVYIAPMKALVQEMVGNF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  466 KKFSKTLGLRVVCVYGGTGIS-EQIAElkrgAEIIVCTPGRMiDMLAANSGRVTNLRRVTYVVLDEADRMFD-MG--FEP 541
Cdd:cd18019   93 SKRLAPYGITVAELTGDQQLTkEQISE----TQIIVTTPEKW-DIITRKSGDRTYTQLVRLIIIDEIHLLHDdRGpvLES 167
                        170       180
                 ....*....|....*....|....*.
gi 20806137  542 QVMRIVDNVRPDRQTVM---FSATFP 564
Cdd:cd18019  168 IVARTIRQIEQTQEYVRlvgLSATLP 193
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
397-685 3.54e-06

CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 50.85  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  397 PIQTQAIPAIMSGRDLIG-----IAKTGSGKTIAFLLPMFRHimdqrsLEEGEGPIAVIMTPTRELALQITKECKKFskt 471
Cdd:COG1203  130 PLQNEALELALEAAEEEPglfilTAPTGGGKTEAALLFALRL------AAKHGGRRIIYALPFTSIINQTYDRLRDL--- 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  472 LGLRVVCVYGGTGISEQIAE------------LKRG--AEIIVCTPGRMIDMLAANSG----RVTNLRRvTYVVLDEADr 533
Cdd:COG1203  201 FGEDVLLHHSLADLDLLEEEeeyesearwlklLKELwdAPVVVTTIDQLFESLFSNRKgqerRLHNLAN-SVIILDEVQ- 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  534 MFDMGFEPQVMRIVDNVRPDRQTVMF-SATFPRAMEALARR----ILSKPIEVQVGGRSVVCSDVEqqvIVIEEEKKFLK 608
Cdd:COG1203  279 AYPPYMLALLLRLLEWLKNLGGSVILmTATLPPLLREELLEayelIPDEPEELPEYFRAFVRKRVE---LKEGPLSDEEL 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  609 LLELLGHYQESGSVIIFVDKQEHADGL---LKDLMrASYPCMSLHGGIDQYDR----DSIINDFKNGTCKLLVATSVAAR 681
Cdd:COG1203  356 AELILEALHKGKSVLVIVNTVKDAQELyeaLKEKL-PDEEVYLLHSRFCPADRseieKEIKERLERGKPCILVSTQVVEA 434

                 ....
gi 20806137  682 GLDV 685
Cdd:COG1203  435 GVDI 438
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
397-531 4.05e-06

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 48.41  E-value: 4.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  397 PIQTQAIPAIMSGRD--LIGiAKTGSGKTIAFLLPMFRHimdqrsLEEGEGPIAVIMTPTRELALQITKE-CKKFSKTLG 473
Cdd:cd18021    6 PIQTQVFNSLYNTDDnvFVG-APTGSGKTVCAELALLRH------WRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLG 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  474 LRVVCVYGgtgisEQIAELK--RGAEIIVCTPGRMiDMLAANSGRVTNLRRVTYVVLDEA 531
Cdd:cd18021   79 KKVVKLTG-----ETSTDLKllAKSDVILATPEQW-DVLSRRWKQRKNVQSVELFIADEL 132
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
392-530 4.34e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 50.87  E-value: 4.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  392 YEKPTPIQTQAIPAIMSGRD-LIgIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVI----------------MTPT 454
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGEStLL-IAPTGSGKTLAAFLPALDELARRPRPGELPDGLRVLyisplkalandiernlRAPL 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20806137  455 RELALQITKECKKFskTLGLRVvcvyGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRvTNLRRVTYVVLDE 530
Cdd:COG1201  101 EEIGEAAGLPLPEI--RVGVRT----GDTPASERQRQRRRPPHILITTPESLALLLTSPDAR-ELLRGVRTVIVDE 169
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
410-531 4.91e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 48.42  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  410 RDLIGIAKTGSGKT-IAFLLpMFRHIMDQRSLEEGeGPIAVIMTPTRELALQitkECKKFSKTLGLRVVCVYGGTGISEQ 488
Cdd:cd18034   17 RNTIVVLPTGSGKTlIAVML-IKEMGELNRKEKNP-KKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEMGVDKW 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 20806137  489 IA----ELKRGAEIIVCTPGRMIDMLaaNSGRVTnLRRVTYVVLDEA 531
Cdd:cd18034   92 TKerwkEELEKYDVLVMTAQILLDAL--RHGFLS-LSDINLLIFDEC 135
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
397-530 5.09e-05

C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350780 [Multi-domain]  Cd Length: 189  Bit Score: 45.06  E-value: 5.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  397 PIQTQAIPAIMSGRD--LIGiAKTGSGKTIAFLLPMFrhimdqRSLEEGEGPIAVIMTPTRELALQITKECKK-FSKTLG 473
Cdd:cd18022    4 PIQTQVFHTLYHTDNnvLLG-APTGSGKTIAAELAMF------RAFNKYPGSKVVYIAPLKALVRERVDDWKKrFEEKLG 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 20806137  474 LRVVCVYGGTgiSEQIAELkRGAEIIVCTPGRMiDMLAANSGRVTNLRRVTYVVLDE 530
Cdd:cd18022   77 KKVVELTGDV--TPDMKAL-ADADIIITTPEKW-DGISRSWQTREYVQQVSLIIIDE 129
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
382-722 5.83e-05

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 47.06  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  382 KILNSLKKH-GYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLP--MFrhimdqrsleegEGPiAVIMTPTreLA 458
Cdd:COG0514    4 DALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLL------------PGL-TLVVSPL--IA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  459 L---QItkeckKFSKTLGLRVVCVYGGTGISEQ---IAELKRGA-EIIVCTP-----GRMIDMLAAnsgrvtnlRRVTYV 526
Cdd:COG0514   69 LmkdQV-----DALRAAGIRAAFLNSSLSAEERrevLRALRAGElKLLYVAPerllnPRFLELLRR--------LKISLF 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  527 VLDEA--------DrmfdmgFEPQVMRIVDNVR--PDRQTVMFSATF-PRAMEALARRI-LSKPiEVQVGG--------- 585
Cdd:COG0514  136 AIDEAhcisqwghD------FRPDYRRLGELRErlPNVPVLALTATAtPRVRADIAEQLgLEDP-RVFVGSfdrpnlrle 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  586 -RSVVCSDVEQQVIvieeekkflklLELLGHYQESGsvIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIIND 664
Cdd:COG0514  209 vVPKPPDDKLAQLL-----------DFLKEHPGGSG--IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDR 275
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20806137  665 FKNGTCKLLVATSvaARGL-----DVKhliLVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTF 722
Cdd:COG0514  276 FLRDEVDVIVATI--AFGMgidkpDVR---FVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
397-552 7.72e-05

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


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 44.94  E-value: 7.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  397 PIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFrhIMDQRSleegeGPIAVIMTPTreLAL---QITKeckkfsktL- 472
Cdd:cd18018   15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL--LLRRRG-----PGLTLVVSPL--IALmkdQVDA--------Lp 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  473 -GLRVVCVYGGTGISEQIAELK--RGAE--IIVCTPGRmidmLAANSGR--VTNLRRVTYVVLDEADRMFDMG--FEPQV 543
Cdd:cd18018   78 rAIKAAALNSSLTREERRRILEklRAGEvkILYVSPER----LVNESFRelLRQTPPISLLVVDEAHCISEWShnFRPDY 153

                 ....*....
gi 20806137  544 MRIVDNVRP 552
Cdd:cd18018  154 LRLCRVLRE 162
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
394-571 9.81e-05

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 44.33  E-value: 9.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  394 KPTPIQTQAIPAIMSG------RDLIGIAKTGSGKTIAFLLPMFRHIMDQRSleegegpiAVIMTPTRELALQITKECKK 467
Cdd:cd17918   15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYKNGKQ--------VAILVPTEILAHQHYEEARK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  468 FSKTlgLRVVCVYGGTgiSEQIAElkrGAEIIVCTPGrmidMLAANSgrvtNLRRVTYVVLDEADRmfdMGFEpQVMRIV 547
Cdd:cd17918   87 FLPF--INVELVTGGT--KAQILS---GISLLVGTHA----LLHLDV----KFKNLDLVIVDEQHR---FGVA-QREALY 147
                        170       180
                 ....*....|....*....|....*
gi 20806137  548 DNVRPDrqTVMFSAT-FPRAMeALA 571
Cdd:cd17918  148 NLGATH--FLEATATpIPRTL-ALA 169
PRK00254 PRK00254
ski2-like helicase; Provisional
379-530 2.15e-04

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 45.19  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   379 ISMKILNSLKKHGYEKPTPIQTQAIPA-IMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDqrsleegEGPIAVIMTPTREL 457
Cdd:PRK00254    8 VDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR-------EGGKAVYLVPLKAL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20806137   458 ALQITKECKKFSKtLGLRVVCVyggTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVtnlRRVTYVVLDE 530
Cdd:PRK00254   81 AEEKYREFKDWEK-LGLRVAMT---TGDYDSTDEWLGKYDIIIATAEKFDSLLRHGSSWI---KDVKLVVADE 146
PRK13766 PRK13766
Hef nuclease; Provisional
661-726 2.15e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 45.25  E-value: 2.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20806137   661 IINDFKNGTCKLLVATSVAARGLDVKHLILVVnyscpnHYED------YVHRAGRTGRaGNKGYAYTFITED 726
Cdd:PRK13766  415 ILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI------FYEPvpseirSIQRKGRTGR-QEEGRVVVLIAKG 479
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
622-684 2.35e-04

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: 42.08  E-value: 2.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20806137  622 VIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKN--GTCKLLVATSVAARGLD 684
Cdd:cd18793   30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGVGLN 94
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
652-720 4.59e-04

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: 41.57  E-value: 4.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20806137  652 GIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRaGNKGYAY 720
Cdd:cd18801   73 GMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
647-719 6.32e-04

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 41.09  E-value: 6.32e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20806137  647 MSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYA 719
Cdd:cd18797   70 ASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLV 142
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
419-531 1.29e-03

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 42.90  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  419 GSGKTIAFLLpmfrhIMDQRSLEEGEGPIAVImTPTReLALQITKECKKFskTLGLRVVCVYGGTGISEQIAELKRgAEI 498
Cdd:COG0553  270 GLGKTIQALA-----LLLELKERGLARPVLIV-APTS-LVGNWQRELAKF--APGLRVLVLDGTRERAKGANPFED-ADL 339
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 20806137  499 IVCTPG---RMIDMLAAnsgrvtnlRRVTYVVLDEA 531
Cdd:COG0553  340 VITSYGllrRDIELLAA--------VDWDLVILDEA 367
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
394-530 1.67e-03

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 40.96  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  394 KPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdqRSLEEGEGPIAVIMTPTRELALQITKECKKFSKTLG 473
Cdd:cd18073    2 KPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHL---KKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHG 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 20806137  474 LRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVTNLRRVTYVVLDE 530
Cdd:cd18073   79 YRVTGISGATAENVPVEQIIENNDIIILTPQILVNNL--KKGTIPSLSIFTLMIFDE 133
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
621-692 1.74e-03

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 39.08  E-value: 1.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20806137  621 SVIIFVDKQEHADGLLKDLMRASYPCMSLHGG-IDQYDRDSIINDFKNGTCKLLVATSVA--ARGLDVKHLILVV 692
Cdd:cd18799    8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDySDRERGDEALILLFFGELKPPILVTVDllTTGVDIPEVDNVV 82
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
636-685 1.78e-03

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 40.02  E-value: 1.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 20806137  636 LKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDV 685
Cdd:cd18811   54 LKERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDV 103
PRK01172 PRK01172
ATP-dependent DNA helicase;
399-723 2.40e-03

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 41.79  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   399 QTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdQRSLEegegpiAVIMTPTRELALQITKECKKFsKTLGLRVVC 478
Cdd:PRK01172   27 QRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETF--LAGLK------SIYIVPLRSLAMEKYEELSRL-RSLGMRVKI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   479 VYGGTGISEQIaeLKRgAEIIVCTPGRMIDMLAANSgrvTNLRRVTYVVLDEADRMFDMGFEPQ---VMRIVDNVRPDRQ 555
Cdd:PRK01172   98 SIGDYDDPPDF--IKR-YDVVILTSEKADSLIHHDP---YIINDVGLIVADEIHIIGDEDRGPTletVLSSARYVNPDAR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   556 TVMFSATFPRAMEAL----ARRILS--KPIEVQVG----GRSVVCSDVEQQVIVIEEEKKFLkllellghyQESGSVIIF 625
Cdd:PRK01172  172 ILALSATVSNANELAqwlnASLIKSnfRPVPLKLGilyrKRLILDGYERSQVDINSLIKETV---------NDGGQVLVF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137   626 VDKQEHADGLLKDLMRASYPCMSL-------------------------HGGIDQYDRDSIINDFKNGTCKLLVATSVAA 680
Cdd:PRK01172  243 VSSRKNAEDYAEMLIQHFPEFNDFkvssennnvyddslnemlphgvafhHAGLSNEQRRFIEEMFRNRYIKVIVATPTLA 322
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 20806137   681 RGLDVKHLILVV--------NYSCPNHYEDYVHRAGRTGRAGNKGYAYTFI 723
Cdd:PRK01172  323 AGVNLPARLVIVrditrygnGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYI 373
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
393-429 2.50e-03

DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350773 [Multi-domain]  Cd Length: 209  Bit Score: 40.43  E-value: 2.50e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 20806137  393 EKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLP 429
Cdd:cd18015   17 EKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLP 53
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
650-715 2.63e-03

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 39.55  E-value: 2.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20806137  650 HGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGN 715
Cdd:cd18796   75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
649-739 3.99e-03

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: 38.86  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  649 LHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVkhlilvvnyscPNHYEDYVHRA------------GRTGRAGNK 716
Cdd:cd18810   57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDI-----------PNANTIIIERAdkfglaqlyqlrGRVGRSKER 125
                         90       100
                 ....*....|....*....|...
gi 20806137  717 GYAYtFITEDQARYAGDIIKALE 739
Cdd:cd18810  126 AYAY-FLYPDQKKLTEDALKRLE 147
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
381-531 4.19e-03

DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.


Pssm-ID: 350774 [Multi-domain]  Cd Length: 208  Bit Score: 39.81  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  381 MKILNslKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMfrhimdqrSLEEGegpIAVIMTPTRELalq 460
Cdd:cd18016    6 MKIFH--KKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPA--------CVSPG---VTVVISPLRSL--- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  461 ITKECKKFsKTLGLRVVCVYGGTGISEQIA---ELKRGAEII---------VCTPGRMIDMLaansgrvTNLRRVTYV-- 526
Cdd:cd18016   70 IVDQVQKL-TSLDIPATYLTGDKTDAEATKiylQLSKKDPIIkllyvtpekISASNRLISTL-------ENLYERKLLar 141

                 ....*.
gi 20806137  527 -VLDEA 531
Cdd:cd18016  142 fVIDEA 147
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
419-534 8.71e-03

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 38.32  E-value: 8.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  419 GSGKT---IAFLLpmfrhimDQRSLEEGEGPIAVImTPtreLALQIT--KECKKFskTLGLRVVCVYGGTGISEQIAELK 493
Cdd:cd17919   29 GLGKTlqaIAFLA-------YLLKEGKERGPVLVV-CP---LSVLENweREFEKW--TPDLRVVVYHGSQRERAQIRAKE 95
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 20806137  494 RGAE--IIVCTPgrmiDMLAANSGRVTNLRRvTYVVLDEADRM 534
Cdd:cd17919   96 KLDKfdVVLTTY----ETLRRDKASLRKFRW-DLVVVDEAHRL 133
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
649-727 8.90e-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: 38.02  E-value: 8.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806137  649 LHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVkhlilvvnyscPNHYEDYVHRA------------GRTGRAGNK 716
Cdd:cd18792   66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDV-----------PNANTMIIEDAdrfglsqlhqlrGRVGRGKHQ 134
                         90
                 ....*....|.
gi 20806137  717 GYAYtFITEDQ 727
Cdd:cd18792  135 SYCY-LLYPDP 144
 
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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