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Conserved domains on  [gi|39104531|dbj|BAC98030|]
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mKIAA0801 protein, partial [Mus musculus]

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) ...
378-594 5.93e-136

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: 408.30  E-value: 5.93e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  378 TVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSL 457
Cdd:cd17953    1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  458 EEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGK---- 533
Cdd:cd17953   81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRvtnl 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39104531  534 SRVFYylfsllFVLDmifvEAD-----------LRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 594
Cdd:cd17953  161 RRVTY------VVLD----EADrmfdmgfepqiMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
395-805 3.10e-130

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 401.45  E-value: 3.10e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  395 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSleegEGPIAVIMTPTREL 474
Cdd:COG0513    8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  475 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGKsrvfyylFSL----LFVLDmi 550
Cdd:COG0513   84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGA-------LDLsgveTLVLD-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  551 fvEADL-----------RIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFL 619
Cdd:COG0513  153 --EADRmldmgfiedieRILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  620 KLLELLGHYqESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKH 699
Cdd:COG0513  231 LLRRLLRDE-DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDD 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  700 LILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKAL--ELSGTAVPPDLEKLWSDFKDQQ-KAEG 776
Cdd:COG0513  310 VSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIgqKIEEEELPGFEPVEEKRLERLKpKIKE 389
                        410       420
                 ....*....|....*....|....*....
gi 39104531  777 KIIKKSSGFSGKGFKFDETEQALANERKK 805
Cdd:COG0513  390 KLKGKKAGRGGRPGPKGERKARRGKRRRR 418
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
941-1043 8.03e-62

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: 205.24  E-value: 8.03e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  941 SFKRYEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1020
Cdd:cd22473    1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                         90       100
                 ....*....|....*....|...
gi 39104531 1021 LIKEELIRLQNSYQPTNKGRYKV 1043
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) ...
378-594 5.93e-136

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: 408.30  E-value: 5.93e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  378 TVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSL 457
Cdd:cd17953    1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  458 EEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGK---- 533
Cdd:cd17953   81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRvtnl 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39104531  534 SRVFYylfsllFVLDmifvEAD-----------LRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 594
Cdd:cd17953  161 RRVTY------VVLD----EADrmfdmgfepqiMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
PTZ00110 PTZ00110
helicase; Provisional
335-764 7.33e-132

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 410.32  E-value: 7.33e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   335 LEPVDHGKIEYEPFRKNFYVEVPELAKMSQEEVNVFRLEMEGITVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTP 414
Cdd:PTZ00110   76 LQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   415 IQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVV 494
Cdd:PTZ00110  156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   495 CVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAAN-SGKSRVFYY-LFSLLFVLDMIFvEADLR-IVDNVRPDRQTVMF 571
Cdd:PTZ00110  236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNvTNLRRVTYLvLDEADRMLDMGF-EPQIRkIVSQIRPDRQTLMW 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   572 SATFPRAMEALARRILS-KPIEVQVGGRSV-VCSDVEQQVIVIEEEKKFLKLLELLGHYQESGS-VIIFVDKQEHADGLL 648
Cdd:PTZ00110  315 SATWPKEVQSLARDLCKeEPVHVNVGSLDLtACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGDkILIFVETKKGADFLT 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   649 KDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNK 728
Cdd:PTZ00110  395 KELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAK 474
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 39104531   729 GYAYTFITEDQARYAGDIIKALELSGTAVPPDLEKL 764
Cdd:PTZ00110  475 GASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKL 510
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
395-805 3.10e-130

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 401.45  E-value: 3.10e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  395 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSleegEGPIAVIMTPTREL 474
Cdd:COG0513    8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  475 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGKsrvfyylFSL----LFVLDmi 550
Cdd:COG0513   84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGA-------LDLsgveTLVLD-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  551 fvEADL-----------RIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFL 619
Cdd:COG0513  153 --EADRmldmgfiedieRILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  620 KLLELLGHYqESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKH 699
Cdd:COG0513  231 LLRRLLRDE-DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDD 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  700 LILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKAL--ELSGTAVPPDLEKLWSDFKDQQ-KAEG 776
Cdd:COG0513  310 VSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIgqKIEEEELPGFEPVEEKRLERLKpKIKE 389
                        410       420
                 ....*....|....*....|....*....
gi 39104531  777 KIIKKSSGFSGKGFKFDETEQALANERKK 805
Cdd:COG0513  390 KLKGKKAGRGGRPGPKGERKARRGKRRRR 418
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
310-761 2.50e-65

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 229.67  E-value: 2.50e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   310 EYSSEEEEVDL-----QTALTGYQTKQRKllePVDHGKIEYEPFR-KNFYVEVPEL-AKMSQEEVNVFRLEMEgITVKGK 382
Cdd:PLN00206   39 EYICDETDDDIcslecKQALLRRVAKSRV---AVGAPKPKRLPATdECFYVRDPGStSGLSSSQAELLRRKLE-IHVKGE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   383 GCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRS--LEEG 460
Cdd:PLN00206  115 AVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSghPSEQ 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   461 EGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGK-SRVFyy 539
Cdd:PLN00206  195 RNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIElDNVS-- 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   540 lfslLFVLDMI-------FVEADLRIVDNVrPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVI 612
Cdd:PLN00206  273 ----VLVLDEVdcmlergFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWV 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   613 EEEKKFLKL---LELLGHYQEsgSVIIFVDKQEHADgLLKDLMRAS--YPCMSLHGGIDQYDRDSIINDFKNGTCKLLVA 687
Cdd:PLN00206  348 ETKQKKQKLfdiLKSKQHFKP--PAVVFVSSRLGAD-LLANAITVVtgLKALSIHGEKSMKERREVMKSFLVGEVPVIVA 424
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39104531   688 TSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKALELSGTAVPPDL 761
Cdd:PLN00206  425 TGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPREL 498
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
941-1043 8.03e-62

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: 205.24  E-value: 8.03e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  941 SFKRYEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1020
Cdd:cd22473    1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                         90       100
                 ....*....|....*....|...
gi 39104531 1021 LIKEELIRLQNSYQPTNKGRYKV 1043
Cdd:cd22473   81 LIKEELLRLQASYQPINKGRYKV 103
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
413-582 2.10e-49

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: 172.43  E-value: 2.10e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531    413 TPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdqrsLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLR 492
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL-----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531    493 VVCVYGGTGISEQIAELKrGAEIIVCTPGRMIDMLAANSGKSRVfyylfsLLFVLDmifvEADL-----------RIVDN 561
Cdd:pfam00270   76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKLLKNL------KLLVLD----EAHRlldmgfgpdleEILRR 144
                          170       180
                   ....*....|....*....|.
gi 39104531    562 VRPDRQTVMFSATFPRAMEAL 582
Cdd:pfam00270  145 LPKKRQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
605-735 1.31e-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: 1.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  605 VEQQVIVIEEEKKFLKLLELLGHYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKL 684
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 39104531  685 LVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFI 735
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
404-607 4.04e-44

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 158.81  E-value: 4.04e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531     404 LKKHGYEKPTPIQTQAIPAIMSG-RDLIGIAKTGSGKTIAFLLPMFRHIMdqrsleEGEGPIAVIMTPTRELALQITKEC 482
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531     483 KKFSKTLGLRVVCVYGGTGISEQIAELKRG-AEIIVCTPGRMIDMLAANSGKSRVFYYLfsllfVLDmifvEAD------ 555
Cdd:smart00487   75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLV-----ILD----EAHrlldgg 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 39104531     556 -----LRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRsvVCSDVEQ 607
Cdd:smart00487  146 fgdqlEKLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT--PLEPIEQ 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
629-726 1.12e-27

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: 1.12e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531    629 QESGSVIIFVDKQEHAD-GLLKDlmRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYS 707
Cdd:pfam00271   13 ERGGKVLIFSQTKKTLEaELLLE--KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYD 90
                           90
                   ....*....|....*....
gi 39104531    708 CPNHYEDYVHRAGRTGRAG 726
Cdd:pfam00271   91 LPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
647-726 1.84e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.97  E-value: 1.84e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531     647 LLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAG 726
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
398-732 4.23e-14

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 76.47  E-value: 4.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  398 MKILNSLKKHGYEKPTPIQTQAIPA-IMSGRDLIGIAKTGSGKT-IAFLLpMFRHIMdqrsleegEGPIAVIMTPTRELA 475
Cdd:COG1204    9 EKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTlIAELA-ILKALL--------NGGKALYIVPLRALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  476 LQITKECKKFSKTLGLRVVCVYGgtGISEQIAELKRgAEIIVCTPGRMIDMLAANSgksrvfyylfSLLFVLDMIFV-EA 554
Cdd:COG1204   80 SEKYREFKRDFEELGIKVGVSTG--DYDSDDEWLGR-YDILVATPEKLDSLLRNGP----------SWLRDVDLVVVdEA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  555 DLrIVDNVR---------------PDRQTVMFSATFPRAmEALARRIlskpievqvgGRSVVCSD---VEQQVIVIEEEK 616
Cdd:COG1204  147 HL-IDDESRgptlevllarlrrlnPEAQIVALSATIGNA-EEIAEWL----------DAELVKSDwrpVPLNEGVLYDGV 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  617 KFLKLLELLGHYQ----------ESGSVIIFV---------------------------DKQEHADGLL--KDLMRASYP 657
Cdd:COG1204  215 LRFDDGSRRSKDPtlalaldlleEGGQVLVFVssrrdaeslakkladelkrrltpeereELEELAEELLevSEETHTNEK 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  658 ---CMSL-----HGGIDQYDRDSIINDFKNGTCKLLVATSVAARG--LDVKHLILVVNYSCPNHY---EDYVHRAGRTGR 724
Cdd:COG1204  295 ladCLEKgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGvnLPARRVIIRDTKRGGMVPipvLEFKQMAGRAGR 374
                        410
                 ....*....|
gi 39104531  725 AG--NKGYAY 732
Cdd:COG1204  375 PGydPYGEAI 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) ...
378-594 5.93e-136

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: 408.30  E-value: 5.93e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  378 TVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSL 457
Cdd:cd17953    1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  458 EEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGK---- 533
Cdd:cd17953   81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRvtnl 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39104531  534 SRVFYylfsllFVLDmifvEAD-----------LRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 594
Cdd:cd17953  161 RRVTY------VVLD----EADrmfdmgfepqiMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
PTZ00110 PTZ00110
helicase; Provisional
335-764 7.33e-132

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 410.32  E-value: 7.33e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   335 LEPVDHGKIEYEPFRKNFYVEVPELAKMSQEEVNVFRLEMEGITVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTP 414
Cdd:PTZ00110   76 LQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   415 IQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVV 494
Cdd:PTZ00110  156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   495 CVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAAN-SGKSRVFYY-LFSLLFVLDMIFvEADLR-IVDNVRPDRQTVMF 571
Cdd:PTZ00110  236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNvTNLRRVTYLvLDEADRMLDMGF-EPQIRkIVSQIRPDRQTLMW 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   572 SATFPRAMEALARRILS-KPIEVQVGGRSV-VCSDVEQQVIVIEEEKKFLKLLELLGHYQESGS-VIIFVDKQEHADGLL 648
Cdd:PTZ00110  315 SATWPKEVQSLARDLCKeEPVHVNVGSLDLtACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGDkILIFVETKKGADFLT 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   649 KDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNK 728
Cdd:PTZ00110  395 KELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAK 474
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 39104531   729 GYAYTFITEDQARYAGDIIKALELSGTAVPPDLEKL 764
Cdd:PTZ00110  475 GASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKL 510
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
395-805 3.10e-130

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 401.45  E-value: 3.10e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  395 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSleegEGPIAVIMTPTREL 474
Cdd:COG0513    8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  475 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGKsrvfyylFSL----LFVLDmi 550
Cdd:COG0513   84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGA-------LDLsgveTLVLD-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  551 fvEADL-----------RIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFL 619
Cdd:COG0513  153 --EADRmldmgfiedieRILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  620 KLLELLGHYqESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKH 699
Cdd:COG0513  231 LLRRLLRDE-DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDD 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  700 LILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKAL--ELSGTAVPPDLEKLWSDFKDQQ-KAEG 776
Cdd:COG0513  310 VSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIgqKIEEEELPGFEPVEEKRLERLKpKIKE 389
                        410       420
                 ....*....|....*....|....*....
gi 39104531  777 KIIKKSSGFSGKGFKFDETEQALANERKK 805
Cdd:COG0513  390 KLKGKKAGRGGRPGPKGERKARRGKRRRR 418
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
400-593 3.92e-80

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: 259.27  E-value: 3.92e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQIT 479
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  480 KECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGK-SRVFYYLF---SLLFvlDMIFvEAD 555
Cdd:cd17952   81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNlQRVTYLVLdeaDRMF--DMGF-EYQ 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 39104531  556 LR-IVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd17952  158 VRsIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
400-594 8.11e-77

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: 250.44  E-value: 8.11e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImDQRSLEEGEGPIAVIMTPTRELALQIT 479
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKL-LPEPKKKGRGPQALVLAPTRELAMQIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  480 KECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGKsrvfyylFSL----LFVLDmifvEAD 555
Cdd:cd00268   80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLI--ERGK-------LDLsnvkYLVLD----EAD 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 39104531  556 L-----------RIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 594
Cdd:cd00268  147 RmldmgfeedveKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
401-746 4.27e-76

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 258.19  E-value: 4.27e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   401 LNSLkkhGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImDQRSLeegeGPIAVIMTPTRELALQITK 480
Cdd:PRK11776   19 LNEL---GYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-DVKRF----RVQALVLCPTRELADQVAK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   481 ECKKFSKTL-GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGKsrvfyyLFSL-LFVLD-------MIF 551
Cdd:PRK11776   91 EIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLD------LDALnTLVLDeadrmldMGF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   552 VEADLRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVcSDVEQQVIVIEEEKKFLKLLELLGHYQES 631
Cdd:PRK11776  165 QDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSPDERLPALQRLLLHHQPE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   632 gSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNH 711
Cdd:PRK11776  244 -SCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARD 322
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 39104531   712 YEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDI 746
Cdd:PRK11776  323 PEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAI 357
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
400-594 8.39e-73

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: 239.19  E-value: 8.39e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQIT 479
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  480 KECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGK---SRVFYylfsLLF-----VLDMIF 551
Cdd:cd17966   81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFL--DQGKtnlRRVTY----LVLdeadrMLDMGF 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 39104531  552 vEADLR-IVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 594
Cdd:cd17966  155 -EPQIRkIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
395-760 1.26e-71

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 245.49  E-value: 1.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   395 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPI-AVIMTPTRE 473
Cdd:PRK10590    7 GLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   474 LALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGK-SRV-FYYLFSLLFVLDMIF 551
Cdd:PRK10590   87 LAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKlDQVeILVLDEADRMLDMGF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   552 VEADLRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLKLLEL--LGHYQ 629
Cdd:PRK10590  167 IHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMigKGNWQ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   630 EsgsVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCP 709
Cdd:PRK10590  247 Q---VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELP 323
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 39104531   710 NHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKAL--ELSGTAVP---PD 760
Cdd:PRK10590  324 NVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLkkEIPRIAIPgyePD 379
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
344-596 3.22e-68

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: 229.51  E-value: 3.22e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  344 EYEPFRKNFYVEVPELAKMSQEEVNVFRLEMEgITVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAI 423
Cdd:cd18050   18 ELPKFEKNFYVEHPEVARMTQYDVEELRRKKE-ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  424 MSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGIS 503
Cdd:cd18050   97 LSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKG 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  504 EQIAELKRGAEIIVCTPGRMIDMLAANSGKSRVFYYLF--SLLFVLDMIFVEADLRIVDNVRPDRQTVMFSATFPRAMEA 581
Cdd:cd18050  177 PQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVldEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQ 256
                        250
                 ....*....|....*
gi 39104531  582 LARRILSKPIEVQVG 596
Cdd:cd18050  257 LAEDFLRDYVQINIG 271
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
310-761 2.50e-65

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 229.67  E-value: 2.50e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   310 EYSSEEEEVDL-----QTALTGYQTKQRKllePVDHGKIEYEPFR-KNFYVEVPEL-AKMSQEEVNVFRLEMEgITVKGK 382
Cdd:PLN00206   39 EYICDETDDDIcslecKQALLRRVAKSRV---AVGAPKPKRLPATdECFYVRDPGStSGLSSSQAELLRRKLE-IHVKGE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   383 GCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRS--LEEG 460
Cdd:PLN00206  115 AVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSghPSEQ 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   461 EGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGK-SRVFyy 539
Cdd:PLN00206  195 RNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIElDNVS-- 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   540 lfslLFVLDMI-------FVEADLRIVDNVrPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVI 612
Cdd:PLN00206  273 ----VLVLDEVdcmlergFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWV 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   613 EEEKKFLKL---LELLGHYQEsgSVIIFVDKQEHADgLLKDLMRAS--YPCMSLHGGIDQYDRDSIINDFKNGTCKLLVA 687
Cdd:PLN00206  348 ETKQKKQKLfdiLKSKQHFKP--PAVVFVSSRLGAD-LLANAITVVtgLKALSIHGEKSMKERREVMKSFLVGEVPVIVA 424
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39104531   688 TSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKALELSGTAVPPDL 761
Cdd:PLN00206  425 TGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPREL 498
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
390-753 5.12e-63

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 226.27  E-value: 5.12e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   390 SWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrslEEGEGPIAVIMT 469
Cdd:PRK11634    7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD-----PELKAPQILVLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   470 PTRELALQITKECKKFSKTL-GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaansgkSRVFYYLFSLL-FVL 547
Cdd:PRK11634   82 PTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHL------KRGTLDLSKLSgLVL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   548 D-------MIFVEADLRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLK 620
Cdd:PRK11634  156 DeademlrMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   621 LLELLgHYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHL 700
Cdd:PRK11634  236 LVRFL-EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERI 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 39104531   701 ILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKALELS 753
Cdd:PRK11634  315 SLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLT 367
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
400-596 8.18e-63

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 212.35  E-value: 8.18e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEG-----PIAVIMTPTREL 474
Cdd:cd17967   11 LLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPSALILAPTREL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  475 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGK---SRVFYylfsllFVLDmif 551
Cdd:cd17967   91 AIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI--ERGRislSSIKF------LVLD--- 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  552 vEAD--L---------RIVD----NVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVG 596
Cdd:cd17967  160 -EADrmLdmgfepqirKIVEhpdmPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
941-1043 8.03e-62

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: 205.24  E-value: 8.03e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  941 SFKRYEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1020
Cdd:cd22473    1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                         90       100
                 ....*....|....*....|...
gi 39104531 1021 LIKEELIRLQNSYQPTNKGRYKV 1043
Cdd:cd22473   81 LIKEELLRLQASYQPINKGRYKV 103
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
365-597 7.62e-61

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: 207.55  E-value: 7.62e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  365 EEVNVFRLEMEgITVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFL 444
Cdd:cd18049    1 QEVEQYRRSKE-ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  445 LPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMI 524
Cdd:cd18049   80 LPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39104531  525 DMLAANSGKSRVFYYLF--SLLFVLDMIFVEADLRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGG 597
Cdd:cd18049  160 DFLEAGKTNLRRCTYLVldEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
363-587 4.75e-60

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: 206.36  E-value: 4.75e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  363 SQEEVNVFRLEMEGIT----------VKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGI 432
Cdd:cd18052    7 PEDEDEIFATIQTGINfdkydeipveVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMAC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  433 AKTGSGKTIAFLLPMFRHIMDQR----SLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAE 508
Cdd:cd18052   87 AQTGSGKTAAFLLPVLTGMMKEGltasSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  509 LKRGAEIIVCTPGRMIDMLaansGKSRVfyYLFSLLFV--------LDMIFVEADLRIVDNV----RPDRQTVMFSATFP 576
Cdd:cd18052  167 IEKGCHILVATPGRLLDFI----GRGKI--SLSKLKYLildeadrmLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFP 240
                        250
                 ....*....|.
gi 39104531  577 RAMEALARRIL 587
Cdd:cd18052  241 EEIQRLAAEFL 251
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
400-593 5.22e-58

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: 198.07  E-value: 5.22e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSL-EEGEGPIAVIMTPTRELALQI 478
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  479 TKECKKFSKTlGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGKSRVFYYLF--SLLFVLDMIFVEADL 556
Cdd:cd17958   81 EAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVldEADRMLDMGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 39104531  557 RIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd17958  160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
400-593 4.68e-57

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: 196.39  E-value: 4.68e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEE---GEGPIAVIMTPTRELAL 476
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEetkDDGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  477 QITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaansgKSRVF-----YYLfsllfVLDmif 551
Cdd:cd17945   81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCL-----ERRLLvlnqcTYV-----VLD--- 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39104531  552 vEADLRI----------------VDNVRPD---------------RQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd17945  148 -EADRMIdmgfepqvtkildampVSNKKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
401-749 1.18e-56

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 202.48  E-value: 1.18e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   401 LNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEgPIAVIMTPTRELALQITK 480
Cdd:PRK11192   13 LEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGP-PRILILTPTRELAMQVAD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   481 ECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGKSRVfyyLFSLLF-----VLDMIFVEAD 555
Cdd:PRK11192   92 QARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRA---VETLILdeadrMLDMGFAQDI 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   556 LRIVDNVRPDRQTVMFSATFP-RAMEALARRILSKPIEVQVGG----RSVV------CSDVEQQVIVIEEEKKFlkllel 624
Cdd:PRK11192  169 ETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPsrreRKKIhqwyyrADDLEHKTALLCHLLKQ------ 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   625 lghyQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVV 704
Cdd:PRK11192  243 ----PEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 39104531   705 NYSCPNHYEDYVHRAGRTGRAGNKGYAYTFI-TEDQ------ARYAGDIIKA 749
Cdd:PRK11192  319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVeAHDHlllgkiERYIEEPLKA 370
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
400-743 4.68e-56

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 204.80  E-value: 4.68e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSL--EEGEGPIAVIMTPTRELALQ 477
Cdd:PRK04537   20 LLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadRKPEDPRALILAPTRELAIQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   478 ITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGKS-------------RvfyyLFSLL 544
Cdd:PRK04537  100 IHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSlhaceicvldeadR----MFDLG 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   545 FVLDMIFVeadLRIVDNvRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQvIVIEEEKKFLKLLEL 624
Cdd:PRK04537  176 FIKDIRFL---LRRMPE-RGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQR-IYFPADEEKQTLLLG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   625 LGHYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVV 704
Cdd:PRK04537  251 LLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVY 330
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 39104531   705 NYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEdqaRYA 743
Cdd:PRK04537  331 NYDLPFDAEDYVHRIGRTARLGEEGDAISFACE---RYA 366
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
399-740 1.06e-54

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 196.73  E-value: 1.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   399 KILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGE--GPIAVIMTPTRELAL 476
Cdd:PRK04837   18 QVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKvnQPRALIMAPTRELAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   477 QITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaansgKSRVFYYLFSLLFVLDmifvEA-- 554
Cdd:PRK04837   98 QIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYA-----KQNHINLGAIQVVVLD----EAdr 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   555 --DLRIVDNVR------PD---RQTVMFSATFPRAMEALARRILSKPIEVQVggrsvvcsDVEQQVivieeekkflklle 623
Cdd:PRK04837  169 mfDLGFIKDIRwlfrrmPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVEV--------EPEQKT-------------- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   624 llGH-YQESgsviIFVDKQEHADGLLKDLMRASYP------------CMSLH--------------GGIDQYDRDSIIND 676
Cdd:PRK04837  227 --GHrIKEE----LFYPSNEEKMRLLQTLIEEEWPdraiifantkhrCEEIWghlaadghrvglltGDVAQKKRLRILEE 300
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39104531   677 FKNGTCKLLVATSVAARGL---DVKHlilVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQA 740
Cdd:PRK04837  301 FTRGDLDILVATDVAARGLhipAVTH---VFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYA 364
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
375-596 4.24e-54

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: 189.10  E-value: 4.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  375 EGITVK--GKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIM 452
Cdd:cd18051    5 EDIPVEatGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  453 DQ---RSLEEGEG--------PIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPG 521
Cdd:cd18051   85 EQgpgESLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  522 RMIDMLaaNSGKSRVFYYLFSLL----FVLDMIFVEADLRIV--DNVRP--DRQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd18051  165 RLVDML--ERGKIGLDYCKYLVLdeadRMLDMGFEPQIRRIVeqDTMPPtgERQTLMFSATFPKEIQMLARDFLDNYIFL 242

                 ...
gi 39104531  594 QVG 596
Cdd:cd18051  243 AVG 245
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
408-750 1.31e-52

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 192.05  E-value: 1.31e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   408 GYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEE---GEgPIAVIMTPTRELALQITKECKK 484
Cdd:PRK01297  106 GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymGE-PRALIIAPTRELVVQIAKDAAA 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   485 FSKTLGLRVVCVYGGTGISEQIAELK-RGAEIIVCTPGRMIDMlaanSGKSRVFYYLFSLLFV------LDMIFVEADLR 557
Cdd:PRK01297  185 LTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDF----NQRGEVHLDMVEVMVLdeadrmLDMGFIPQVRQ 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   558 IVDNVRP--DRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLKLLELLGHyQESGSVI 635
Cdd:PRK01297  261 IIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLVTQ-NPWERVM 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   636 IFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDY 715
Cdd:PRK01297  340 VFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDY 419
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 39104531   716 VHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKAL 750
Cdd:PRK01297  420 VHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELL 454
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
395-594 7.11e-51

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: 178.27  E-value: 7.11e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  395 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdqRSLEEGEGPIAVIMTPTREL 474
Cdd:cd17959    7 GLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL---KAHSPTVGARALILSPTREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  475 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMID-MLAANSGKSRVFYYLF---SLLFvlDMI 550
Cdd:cd17959   84 ALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHlLVEMNLKLSSVEYVVFdeaDRLF--EMG 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 39104531  551 FVEADLRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 594
Cdd:cd17959  162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
400-593 1.85e-49

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: 174.06  E-value: 1.85e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQR---SLEEGEGPIAVIMTPTRELAL 476
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEkklPFIKGEGPYGLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  477 QITKECKKFSKTL------GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGKSRVFYYLfsLL----FV 546
Cdd:cd17951   81 QTHEVIEYYCKALqeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYL--CLdeadRM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 39104531  547 LDMIFvEADLR-IVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd17951  159 IDMGF-EEDIRtIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
413-582 2.10e-49

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: 172.43  E-value: 2.10e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531    413 TPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdqrsLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLR 492
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL-----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531    493 VVCVYGGTGISEQIAELKrGAEIIVCTPGRMIDMLAANSGKSRVfyylfsLLFVLDmifvEADL-----------RIVDN 561
Cdd:pfam00270   76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKLLKNL------KLLVLD----EAHRlldmgfgpdleEILRR 144
                          170       180
                   ....*....|....*....|.
gi 39104531    562 VRPDRQTVMFSATFPRAMEAL 582
Cdd:pfam00270  145 LPKKRQILLLSATLPRNLEDL 165
PTZ00424 PTZ00424
helicase 45; Provisional
399-738 2.16e-49

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 180.79  E-value: 2.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   399 KILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHI-MDQRSLEegegpiAVIMTPTRELALQ 477
Cdd:PTZ00424   38 DLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIdYDLNACQ------ALILAPTRELAQQ 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   478 ITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGKSRVFYYLfslLFVLDmifvEAD-- 555
Cdd:PTZ00424  112 IQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI--DKRHLRVDDLK---LFILD----EADem 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   556 ------LRIVDNVR---PDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLKLLELLG 626
Cdd:PTZ00424  183 lsrgfkGQIYDVFKklpPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLY 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   627 HYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNY 706
Cdd:PTZ00424  263 ETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINY 342
                         330       340       350
                  ....*....|....*....|....*....|..
gi 39104531   707 SCPNHYEDYVHRAGRTGRAGNKGYAYTFITED 738
Cdd:PTZ00424  343 DLPASPENYIHRIGRSGRFGRKGVAINFVTPD 374
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
400-596 1.34e-48

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: 171.23  E-value: 1.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRsleEGEGPIAVIMTPTRELALQIT 479
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPR---KKKGLRALILAPTRELASQIY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  480 KECKKFSKTLGLRVVCVYGGT-GISEQIAELKRGAEIIVCTPGRMIDMLAANSgksrvfyylFSLLFVLDMIFVEAD--- 555
Cdd:cd17957   78 RELLKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGP---------IDLSSVEYLVLDEADklf 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 39104531  556 -----------LRIVDNvrPDRQTVMFSATFPRAMEALARRILSKPIEVQVG 596
Cdd:cd17957  149 epgfreqtdeiLAACTN--PNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
605-735 1.31e-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: 1.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  605 VEQQVIVIEEEKKFLKLLELLGHYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKL 684
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 39104531  685 LVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFI 735
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
396-589 8.90e-47

DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 166.60  E-value: 8.90e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  396 ISMKILNSLKKHGYEKPTPIQTQAIPAIMS-GRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTREL 474
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  475 ALQITKECKKFSKTL-GLRVVCVYGGTGISEQIAELKR-GAEIIVCTPGRMIDMLaANSGKSRVFYYLFSLLF-----VL 547
Cdd:cd17964   81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHL-ENPGVAKAFTDLDYLVLdeadrLL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 39104531  548 DMIFVEADLRIVDNVRP----DRQTVMFSATFPRAMEALARRILSK 589
Cdd:cd17964  160 DMGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLKK 205
DEXDc smart00487
DEAD-like helicases superfamily;
404-607 4.04e-44

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 158.81  E-value: 4.04e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531     404 LKKHGYEKPTPIQTQAIPAIMSG-RDLIGIAKTGSGKTIAFLLPMFRHIMdqrsleEGEGPIAVIMTPTRELALQITKEC 482
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531     483 KKFSKTLGLRVVCVYGGTGISEQIAELKRG-AEIIVCTPGRMIDMLAANSGKSRVFYYLfsllfVLDmifvEAD------ 555
Cdd:smart00487   75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLV-----ILD----EAHrlldgg 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 39104531     556 -----LRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRsvVCSDVEQ 607
Cdd:smart00487  146 fgdqlEKLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT--PLEPIEQ 200
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
395-594 4.88e-44

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: 158.54  E-value: 4.88e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  395 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFrhimdQRSLEEGEGPIAVIMTPTREL 474
Cdd:cd17955    5 GLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-----QRLSEDPYGIFALVLTPTREL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  475 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGKSRVFYylFSLL--FVLDmifv 552
Cdd:cd17955   80 AYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHL--RSSDDTTKV--LSRVkfLVLD---- 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 39104531  553 EAD----------LR-IVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 594
Cdd:cd17955  152 EADrlltgsfeddLAtILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
400-593 5.48e-43

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: 155.01  E-value: 5.48e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMfrhIMdqRSLEEGEGPIAVIMTPTRELALQIT 479
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPV---II--RCLTEHRNPSALILTPTRELAVQIE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  480 KECKKFSKTL-GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGKsrvfyyLFSL-LFVLD-------MI 550
Cdd:cd17962   76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVE------LDNIkIVVVDeadtmlkMG 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 39104531  551 FVEADLRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd17962  150 FQQQVLDILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
390-594 6.58e-43

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: 155.17  E-value: 6.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  390 SWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRsleegEGPIAVIMT 469
Cdd:cd17954    1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENP-----QRFFALVLA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  470 PTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGKSrvfyyLFSLLF---- 545
Cdd:cd17954   76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFS-----LKSLKFlvmd 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 39104531  546 ----VLDMIFVEADLRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 594
Cdd:cd17954  151 eadrLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
408-593 7.62e-43

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: 154.76  E-value: 7.62e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  408 GYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHI-MDQRSLEegegpiAVIMTPTRELALQITKECKKFS 486
Cdd:cd17940   18 GFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdPKKDVIQ------ALILVPTRELALQTSQVCKELG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  487 KTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGKSRVFYYlfsllFVLDmifvEAD----------- 555
Cdd:cd17940   92 KHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKT-----LVLD----EADkllsqdfqpii 162
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 39104531  556 LRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd17940  163 EKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
400-575 1.10e-41

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: 152.78  E-value: 1.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIP-AIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRS----LEEGEGPIAVIMTPTREL 474
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSsngvGGKQKPLRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  475 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDML-AANSGKSRvfyyLFSLLF-VLDmifv 552
Cdd:cd17946   81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIqEGNEHLAN----LKSLRFlVLD---- 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 39104531  553 EAD--------------LRIVDNVRP----DRQTVMFSATF 575
Cdd:cd17946  153 EADrmlekghfaelekiLELLNKDRAgkkrKRQTFVFSATL 193
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
400-594 3.48e-41

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: 150.10  E-value: 3.48e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPmfrhIMDQRSLEEGEGPI--AVIMTPTRELALQ 477
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLP----ILERLLYRPKKKAAtrVLVLVPTRELAMQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  478 ITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaANSgKSrvfyylFSL----LFVLD----- 548
Cdd:cd17947   77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHL-RNS-PS------FDLdsieILVLDeadrm 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 39104531  549 --MIFVEADLRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 594
Cdd:cd17947  149 leEGFADELKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
400-593 6.31e-38

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: 140.79  E-value: 6.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQIT 479
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  480 KECKKFSKTLG--LRVVCVYGGTGISEQIAELKR-GAEIIVCTPGRMIDMLAANSGKSRVfyYLFSLLfVLDmifvEAD- 555
Cdd:cd17960   81 EVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKV--KSLEVL-VLD----EADr 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 39104531  556 ----------LRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd17960  154 lldlgfeadlNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
KH-I_AtRH42_like cd22475
type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana DEAD-box ATP-dependent ...
943-1043 1.33e-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: 1.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  943 KRYEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITRlI 1022
Cdd:cd22475    3 EHFEEELEINDFPQHARWKVTHKDTLGQISELTGAAITTRGQYYPPGRIPGPGERKLYLLIEGPSEASVKEAKAEIKR-I 81
                         90       100
                 ....*....|....*....|.
gi 39104531 1023 KEELIRLQNSYQPTNKGRYKV 1043
Cdd:cd22475   82 LEEATEKASRPGGQQPGRYSV 102
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
400-595 2.25e-37

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: 138.96  E-value: 2.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQR-SLEEGEGpiAVIMTPTRELALQI 478
Cdd:cd17941    1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwTPEDGLG--ALIISPTRELAMQI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  479 TKECKKFSKTLGLRVVCVYGGTGISEqiaELKRGAE--IIVCTPGRMIDMLAANSGksrvFYY--LFSLLF-----VLDM 549
Cdd:cd17941   79 FEVLRKVGKYHSFSAGLIIGGKDVKE---EKERINRmnILVCTPGRLLQHMDETPG----FDTsnLQMLVLdeadrILDM 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 39104531  550 IFVEADLRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQV 595
Cdd:cd17941  152 GFKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
KH-I_DDX46_like cd22387
type I K homology (KH) RNA-binding domain found in the family of DEAD box protein 46 (DDX46); ...
941-1022 1.42e-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: 1.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  941 SFKRYEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1020
Cdd:cd22387    1 NNGNFVEEFEINDYPQIARLKVTSKEVLNSIMEETGATITIKGQYYPPGKKPKPGERKLYLLIEGATEESVQSARNEIKR 80

                 ..
gi 39104531 1021 LI 1022
Cdd:cd22387   81 VL 82
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
400-593 2.26e-36

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: 136.34  E-value: 2.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEgEGPIAVIMTPTRELALQI- 478
Cdd:cd17942    1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPR-NGTGVIIISPTRELALQIy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  479 --TKE-CKKFSKTLGlrvvCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGksrvFYYLFSLLFVLDmifvEAD 555
Cdd:cd17942   80 gvAKElLKYHSQTFG----IVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKG----FLYKNLQCLIID----EAD 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 39104531  556 lRIVD-----------NVRP-DRQTVMFSATFPRAMEALARRIL-SKPIEV 593
Cdd:cd17942  148 -RILEigfeeemrqiiKLLPkRRQTMLFSATQTRKVEDLARISLkKKPLYV 197
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
400-594 3.26e-34

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: 129.69  E-value: 3.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFrhimdQRSLEEGEGPIAVIMTPTRELALQIT 479
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-----ESLDLERRHPQVLILAPTREIAVQIH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  480 KECKKFSKTL-GLRVVCVYGGTGISEQIAELKRgAEIIVCTPGR---MIDMLAANSGKSRvfyylfslLFVLDmifvEAD 555
Cdd:cd17943   76 DVFKKIGKKLeGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRikqLIELGALNVSHVR--------LFVLD----EAD 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 39104531  556 LRIVDNVRPD-----------RQTVMFSATFPRAMEALARRILSKPIEVQ 594
Cdd:cd17943  143 KLMEGSFQKDvnwifsslpknKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
408-593 5.36e-33

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: 126.54  E-value: 5.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  408 GYEKPTPIQTQAIPAIMSG--RDLIGIAKTGSGKTIAFLLPMFRHImDQRSLEegegPIAVIMTPTRELALQITKECKKF 485
Cdd:cd17963   13 GFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKS----PQALCLAPTRELARQIGEVVEKM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  486 SKTLGLRVVC------VYGGTGISEQIaelkrgaeiIVCTPGRMIDMLaansgKSRVFYYLFSLLFVLDmifvEAD---- 555
Cdd:cd17963   88 GKFTGVKVALavpgndVPRGKKITAQI---------VIGTPGTVLDWL-----KKRQLDLKKIKILVLD----EADvmld 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 39104531  556 --------LRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd17963  150 tqghgdqsIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
395-593 1.03e-32

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: 125.90  E-value: 1.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  395 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHI-MDQRSLEegegpiAVIMTPTRE 473
Cdd:cd17939    3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQ------ALVLAPTRE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  474 LALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaansgKSRVFYYLFSLLFVLDmifvE 553
Cdd:cd17939   77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDML-----QRRSLRTDKIKMFVLD----E 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 39104531  554 AD-----------LRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd17939  148 ADemlsrgfkdqiYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
400-591 1.85e-32

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: 125.39  E-value: 1.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGE-GPIAVIMTPTRELALQI 478
Cdd:cd17961    5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqGTRALILVPTRELAQQV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  479 TKECKKFSKTLG--LRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSG--KSRVFYylfsllFVLDmifvEA 554
Cdd:cd17961   85 SKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLllLSTLKY------LVID----EA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 39104531  555 DL-----------RIVDNVRPDRQTVMFSATFPRAMEALARRILSKPI 591
Cdd:cd17961  155 DLvlsygyeedlkSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
405-591 1.55e-31

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: 123.08  E-value: 1.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  405 KKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIM-DQRSLEEGEGPIAVIMTPTRELALQITKECK 483
Cdd:cd17949    7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPRVDRSDGTLALVLVPTRELALQIYEVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  484 KF-SKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGKSRVFYYLFSLLF-----VLDMIFvEADLR 557
Cdd:cd17949   87 KLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHL--KNTQSFDVSNLRWLVLdeadrLLDMGF-EKDIT 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 39104531  558 -IVDNVR-------------PDRQTVMFSATFPRAMEALARRILSKPI 591
Cdd:cd17949  164 kILELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPV 211
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
400-593 1.22e-30

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: 120.93  E-value: 1.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGE--GPIAVIMTPTRELALQ 477
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfnAPRGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  478 ITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaansgKSRvFYYLFSLLF-VLDmifvEAD- 555
Cdd:cd17948   81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLL-----TSR-IYSLEQLRHlVLD----EADt 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39104531  556 -----------------------LRIVDNVRPDRQTVMFSATFPRAMealaRRILSKPIEV 593
Cdd:cd17948  151 llddsfneklshflrrfplasrrSENTDGLDPGTQLVLVSATMPSGV----GEVLSKVIDV 207
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
400-595 1.60e-30

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: 119.76  E-value: 1.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdqrslEEGEGPIAVI-MTPTRELALQI 478
Cdd:cd17950   13 LLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL------EPVDGQVSVLvICHTRELAFQI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  479 TKECKKFSKTL-GLRVVCVYGGTGISEQIAELK-RGAEIIVCTPGRMIDMLAANSGK-SRVFYylfsllFVLD----MIf 551
Cdd:cd17950   87 SNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKlSHVKH------FVLDecdkML- 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 39104531  552 VEADLR-----IVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQV 595
Cdd:cd17950  160 EQLDMRrdvqeIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
408-574 2.73e-28

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: 113.18  E-value: 2.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  408 GYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrsleegegpiAVIMTPTRELALQITKECKKFSK 487
Cdd:cd17938   18 DWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------ALILEPSRELAEQTYNCIENFKK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  488 TL---GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGK---SRVfyylfsLLFVLDmifvEAD------ 555
Cdd:cd17938   86 YLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLI--KTGKldlSSV------RFFVLD----EADrllsqg 153
                        170       180       190
                 ....*....|....*....|....*....|
gi 39104531  556 -----LRIVD-----NVRPDR-QTVMFSAT 574
Cdd:cd17938  154 nletiNRIYNripkiTSDGKRlQVIVCSAT 183
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
629-726 1.12e-27

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: 1.12e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531    629 QESGSVIIFVDKQEHAD-GLLKDlmRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYS 707
Cdd:pfam00271   13 ERGGKVLIFSQTKKTLEaELLLE--KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYD 90
                           90
                   ....*....|....*....
gi 39104531    708 CPNHYEDYVHRAGRTGRAG 726
Cdd:pfam00271   91 LPWNPASYIQRIGRAGRAG 109
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
404-592 8.45e-27

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: 108.78  E-value: 8.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  404 LKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIM-DQRSLEEGEGPIAVIMTPTRELALQITKEC 482
Cdd:cd17944    5 LQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQVTKDF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  483 KKFSKTlgLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGK---SRVFYYLFSLL-FVLDMIF---VEAD 555
Cdd:cd17944   85 KDITRK--LSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHL--QNGRldlTKLKHVVLDEVdQMLDMGFaeqVEEI 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 39104531  556 LRIVDNVRPDR--QTVMFSATFPRAMEALARRILSKPIE 592
Cdd:cd17944  161 LSVSYKKDSEDnpQTLLFSATCPDWVYNVAKKYMKSQYE 199
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
407-593 5.01e-26

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: 106.76  E-value: 5.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  407 HGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdQRSLEEgegPIAVIMTPTRELALQITKECKKFS 486
Cdd:cd18046   17 YGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI--DTSLKA---TQALVLAPTRELAQQIQKVVMALG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  487 KTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGKSRVFYYlfsLLFVLD----MI---FVEADLRIV 559
Cdd:cd18046   92 DYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI--NRRYLRTDYI---KMFVLDeadeMLsrgFKDQIYDIF 166
                        170       180       190
                 ....*....|....*....|....*....|....
gi 39104531  560 DNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd18046  167 QKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
400-555 9.50e-24

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: 100.78  E-value: 9.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  400 ILNSLKKHGYEKPTPIQTQAIPAIMSG---------RDLIGIAKTGSGKTIAFLLPMFRHIMDQ--RSLEegegpiAVIM 468
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRvvPRLR------ALIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  469 TPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRG--------AEIIVCTPGRMIDMLAANSGksrvfyyl 540
Cdd:cd17956   75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPG-------- 146
                        170
                 ....*....|....*
gi 39104531  541 FSLLFVLDMIFVEAD 555
Cdd:cd17956  147 FTLKHLRFLVIDEAD 161
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
395-593 1.52e-23

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: 99.46  E-value: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  395 GISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdQRSLEEgegPIAVIMTPTREL 474
Cdd:cd18045    5 GLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL--DIQVRE---TQALILSPTREL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  475 ALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGKSRVFYYLfsllfVLD----MI 550
Cdd:cd18045   80 AVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKML-----VLDeadeML 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 39104531  551 FVEADLRIVDNVR---PDRQTVMFSATFPRAMEALARRILSKPIEV 593
Cdd:cd18045  155 NKGFKEQIYDVYRylpPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
HELICc smart00490
helicase superfamily c-terminal domain;
647-726 1.84e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.97  E-value: 1.84e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531     647 LLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAG 726
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 ...
949-1024 5.12e-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: 5.12e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39104531  949 LEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKE--GERKIYLAIESANELAVQKAKAEITRLIKE 1024
Cdd:cd22474    9 VEINDLPQKARWEATNNTSLSKIIEETGCSITNKGNFYPPGKEPQPnnDEPKLYLLIEGTTEKAVRLAIELLRRKLVE 86
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
403-585 5.35e-15

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: 75.88  E-value: 5.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  403 SLKKHGYEKPTPIQTQAIPAI----MSGRDLIGI------------AKTGSGKTIAFLLPMFRHI--MDQRSLEEGEG-- 462
Cdd:cd17965   22 SNKTDEEIKPSPIQTLAIKKLlktlMRKVTKQTSneepklevfllaAETGSGKTLAYLAPLLDYLkrQEQEPFEEAEEey 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  463 --------PIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGIS-EQIAEL-KRGAEIIVCTPGRmIDMLAANSG 532
Cdd:cd17965  102 esakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSyQRLQLAfKGRIDILVTTPGK-LASLAKSRP 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 39104531  533 K--SRVFYYLF----SLlfvLDMIFVEADLRIVDNVRPDRQTVMFSATFPRAMEALARR 585
Cdd:cd17965  181 KilSRVTHLVVdeadTL---FDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRK 236
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
388-590 5.46e-15

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


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 75.44  E-value: 5.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  388 IKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSG--RDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLeegegPIA 465
Cdd:cd18048   17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY-----PQC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  466 VIMTPTRELALQITKECKKFSK-TLGLRVVCVYGGT--GISEQIAelkrgAEIIVCTPGRMIDMLAansgKSRVFYYLFS 542
Cdd:cd18048   92 LCLSPTFELALQTGKVVEEMGKfCVGIQVIYAIRGNrpGKGTDIE-----AQIVIGTPGTVLDWCF----KLRLIDVTNI 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 39104531  543 LLFVLD----MIFVEA----DLRIVDNVRPDRQTVMFSATFPRAMEALARRILSKP 590
Cdd:cd18048  163 SVFVLDeadvMINVQGhsdhSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
398-732 4.23e-14

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 76.47  E-value: 4.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  398 MKILNSLKKHGYEKPTPIQTQAIPA-IMSGRDLIGIAKTGSGKT-IAFLLpMFRHIMdqrsleegEGPIAVIMTPTRELA 475
Cdd:COG1204    9 EKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTlIAELA-ILKALL--------NGGKALYIVPLRALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  476 LQITKECKKFSKTLGLRVVCVYGgtGISEQIAELKRgAEIIVCTPGRMIDMLAANSgksrvfyylfSLLFVLDMIFV-EA 554
Cdd:COG1204   80 SEKYREFKRDFEELGIKVGVSTG--DYDSDDEWLGR-YDILVATPEKLDSLLRNGP----------SWLRDVDLVVVdEA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  555 DLrIVDNVR---------------PDRQTVMFSATFPRAmEALARRIlskpievqvgGRSVVCSD---VEQQVIVIEEEK 616
Cdd:COG1204  147 HL-IDDESRgptlevllarlrrlnPEAQIVALSATIGNA-EEIAEWL----------DAELVKSDwrpVPLNEGVLYDGV 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  617 KFLKLLELLGHYQ----------ESGSVIIFV---------------------------DKQEHADGLL--KDLMRASYP 657
Cdd:COG1204  215 LRFDDGSRRSKDPtlalaldlleEGGQVLVFVssrrdaeslakkladelkrrltpeereELEELAEELLevSEETHTNEK 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  658 ---CMSL-----HGGIDQYDRDSIINDFKNGTCKLLVATSVAARG--LDVKHLILVVNYSCPNHY---EDYVHRAGRTGR 724
Cdd:COG1204  295 ladCLEKgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGvnLPARRVIIRDTKRGGMVPipvLEFKQMAGRAGR 374
                        410
                 ....*....|
gi 39104531  725 AG--NKGYAY 732
Cdd:COG1204  375 PGydPYGEAI 384
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
411-882 1.81e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 74.29  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  411 KPTPIQTQAIPAIMS-----GRDLIGIAKTGSGKTIAFLLPMFRHIMDQRsleegegpiAVIMTPTRELALQITKECKKF 485
Cdd:COG1061   80 ELRPYQQEALEALLAalergGGRGLVVAPTGTGKTVLALALAAELLRGKR---------VLVLVPRRELLEQWAEELRRF 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  486 sktlgLRVVCVYGGtgiseqiaELKRGAEIIVCTpgrmIDMLAANSgKSRVFYYLFSLLfVLDmifvEADL-------RI 558
Cdd:COG1061  151 -----LGDPLAGGG--------KKDSDAPITVAT----YQSLARRA-HLDELGDRFGLV-IID----EAHHagapsyrRI 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  559 VDNVRPDRqTVMFSATFPR-------------------AMEALARRILSKP--IEVQVGGRS-----VVCSDVEQQVIVI 612
Cdd:COG1061  208 LEAFPAAY-RLGLTATPFRsdgreillflfdgivyeysLKEAIEDGYLAPPeyYGIRVDLTDeraeyDALSERLREALAA 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  613 EEEKKFLKLLELLGHYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAA 692
Cdd:COG1061  287 DAERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLN 366
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  693 RGLDV---KHLILVVNYSCPNHyedYVHRAGRTGR-AGNKGYA--YTFITEdqaryagdiikalelsgtavppDLEKLWS 766
Cdd:COG1061  367 EGVDVprlDVAILLRPTGSPRE---FIQRLGRGLRpAPGKEDAlvYDFVGN----------------------DVPVLEE 421
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  767 DFKDQQKAEGKIIKKSSGFSGKGFKFDETEQALANERKKLQKAALGLQDSDDEDAAVDIDEQIESMFNSKKRVKDMAAPG 846
Cdd:COG1061  422 LAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKA 501
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 39104531  847 TSSVPAPTAGNAEKLEIAKRLALRINAQKNLGIESQ 882
Cdd:COG1061  502 EGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLE 537
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
426-589 1.43e-12

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: 66.27  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  426 GRDLIGIAKTGSGKTIAFLLPMFRHIMDQrsleegeGPIAVIMTPTRELALQITKECKKFSKtLGLRVVCVYGGTGISEQ 505
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLKK-------GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEER 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  506 IAELKRGAEIIVCTPGRMIDMLAANsgkSRVFYYLFSLLFVlDmifvEADlRIVDNvrpDRQTVMFSATFPRAMEALARR 585
Cdd:cd00046   73 EKNKLGDADIIIATPDMLLNLLLRE---DRLFLKDLKLIIV-D----EAH-ALLID---SRGALILDLAVRKAGLKNAQV 140

                 ....
gi 39104531  586 ILSK 589
Cdd:cd00046  141 ILLS 144
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
399-733 2.12e-12

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 71.41  E-value: 2.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  399 KILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrsleEGEGPIAVIMTPTRELAL-Q 477
Cdd:COG1205   44 ELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL------EDPGATALYLYPTKALARdQ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  478 ItKECKKFSKTLGLRV-VCVY-GGTGISEQiAELKRGAEIIVCTPgrmiDMLaaNSG---KSRVFYYLFSLL--FVLDmi 550
Cdd:COG1205  118 L-RRLRELAEALGLGVrVATYdGDTPPEER-RWIREHPDIVLTNP----DML--HYGllpHHTRWARFFRNLryVVID-- 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  551 fvEAD-----------------LRIVDNVRPDRQTVMFSATFPRAmEALARRILSKPIEVqV-------GGRsvvcsdve 606
Cdd:COG1205  188 --EAHtyrgvfgshvanvlrrlRRICRHYGSDPQFILASATIGNP-AEHAERLTGRPVTV-VdedgsprGER-------- 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  607 qqVIVIEEEKKFLKLLELLGHYQ---------ESG-SVIIFVD------------KQEHADGLLKDLMRAsYpcmslHGG 664
Cdd:COG1205  256 --TFVLWNPPLVDDGIRRSALAEaarlladlvREGlRTLVFTRsrrgaellaryaRRALREPDLADRVAA-Y-----RAG 327
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39104531  665 IDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYT 733
Cdd:COG1205  328 YLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
413-527 3.53e-11

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: 63.05  E-value: 3.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  413 TPIQTQAIPAIM-SGRDLIGIAKTGSGKTIAFLLPMFRHIMDQrsleegeGPIAVIMTPTRELALQITKECKKFSKTLGL 491
Cdd:cd17921    3 NPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATS-------GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 39104531  492 RVVCVYGGTGISeqiAELKRGAEIIVCTPGRMIDML 527
Cdd:cd17921   76 NVGLLTGDPSVN---KLLLAEADILVATPEKLDLLL 108
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
389-590 9.00e-11

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: 62.43  E-value: 9.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  389 KSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSG--RDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEgegpiAV 466
Cdd:cd18047    1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ-----CL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  467 IMTPTRELALQITKECKKFSKTLGlRVVCVYGGTGiseqiAELKRGA----EIIVCTPGRMID----MLAANSGKSRVFY 538
Cdd:cd18047   76 CLSPTYELALQTGKVIEQMGKFYP-ELKLAYAVRG-----NKLERGQkiseQIVIGTPGTVLDwcskLKFIDPKKIKVFV 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 39104531  539 YLFSLLFVLDMIFVEADLRIVDNVRPDRQTVMFSATFPRAMEALARRILSKP 590
Cdd:cd18047  150 LDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
KH-I_KHDC4_rpt1 cd22385
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
945-1022 1.83e-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: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  945 YEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPG--KEPKEGERKIYLAIESANELAVQKAKAEITRLI 1022
Cdd:cd22385    5 YVAEIEINDLPNTCRNLLTKGSTQEEIQKESGAAVSTRGRYMPPEekATFNPGERPLYLHVQAPTKEAVDRAVNKINEII 84
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
411-553 2.61e-09

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: 58.26  E-value: 2.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  411 KPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSleEGEGPIAVIMTPTRELALQ-ITKECKKFSKtl 489
Cdd:cd18036    2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRS--AGEKGRVVVLVNKVPLVEQqLEKFFKYFRK-- 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39104531  490 GLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGKSRVFYYLFSLlfvldMIFVE 553
Cdd:cd18036   78 GYKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEERVYLSDFSL-----LIFDE 136
KH-I_RIK_like_rpt1 cd22471
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and ...
939-1022 6.19e-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: 54.01  E-value: 6.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  939 SESFKRyeeELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANEL--------- 1009
Cdd:cd22471    2 ESSIAR---EIVINDAPPSVRHHLTKRSTQDEIQSKTGVVVVTRGRYYPPGTPPPDNEKPLYLHITAGAQLppddaerqk 78
                         90
                 ....*....|...
gi 39104531 1010 AVQKAKAEITRLI 1022
Cdd:cd22471   79 AVDAAAADIQAML 91
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
416-527 7.40e-09

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: 56.44  E-value: 7.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  416 QTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRsleegeGPIAVIMTPTRELALQITKECKKFSKTLGLRVVC 495
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELLEQLGLGIRV 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 39104531  496 -VYGG-TGISEQIAELKRGAEIIVCTPgrmiDML 527
Cdd:cd17923   79 aTYDGdTPREERRAIIRNPPRILLTNP----DML 108
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
627-731 2.06e-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: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  627 HYQESGSV--IIFVdKQEHADGLLKDLM------RASYPCMSL--HGGIDQYDRD--------SIINDFKNGTCKLLVAT 688
Cdd:cd18802   19 YFPKTPDFrgIIFV-ERRATAVVLSRLLkehpstLAFIRCGFLigRGNSSQRKRSlmtqrkqkETLDKFRDGELNLLIAT 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 39104531  689 SVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRtGRAGNKGYA 731
Cdd:cd18802   98 SVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNSKYI 139
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
683-736 5.95e-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: 5.95e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 39104531  683 KLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFIT 736
Cdd:cd18785   24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
627-734 8.04e-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: 8.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  627 HYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNY 706
Cdd:cd18794   26 VEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHY 105
                         90       100
                 ....*....|....*....|....*...
gi 39104531  707 SCPNHYEDYVHRAGRTGRAGNKGYAYTF 734
Cdd:cd18794  106 SLPKSMESYYQESGRAGRDGLPSECILF 133
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
415-520 9.38e-08

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: 53.51  E-value: 9.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  415 IQTQAIPAIM-SGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEgPIAVIMTPTRELALQITKECK-KFSKtLGLR 492
Cdd:cd18023    5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDWKeKFGP-LGLS 82
                         90       100       110
                 ....*....|....*....|....*....|
gi 39104531  493 VVCVYGGTGI--SEQIaelkRGAEIIVCTP 520
Cdd:cd18023   83 CAELTGDTEMddTFEI----QDADIILTTP 108
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
634-827 3.24e-07

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 54.35  E-value: 3.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  634 VIIFVDKQEHADGLLKDLMRASYPCMSLHG--------GIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVN 705
Cdd:COG1111  356 IIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIF 435
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  706 yscpnhYED------YVHRAGRTGRaGNKGYAYTFITE---DQARY---------AGDIIKAL-----ELSGTAVPPDLE 762
Cdd:COG1111  436 ------YEPvpseirSIQRKGRTGR-KREGRVVVLIAKgtrDEAYYwssrrkekkMKSILKKLkklldKQEKEKLKESAQ 508
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39104531  763 KLWSDFKDQQKAEGKIIKKSSGFSGKGFKFDETEQALANERKKLQKAALGLQDSDDEDAAVDIDE 827
Cdd:COG1111  509 ATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVIVSTLAESLELRELGEKVDDE 573
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
426-520 6.29e-06

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: 47.58  E-value: 6.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  426 GRDLIGIAKTGSGKTIAFLLPMFRHIMDqrsleEGEGPIAVI-MTPTRELALQITKECKKFSK--TLGLRVVCVYGGTGI 502
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLAD-----EPEKGVQVLyISPLKALINDQERRLEEPLDeiDLEIPVAVRHGDTSQ 75
                         90
                 ....*....|....*...
gi 39104531  503 SEQIAELKRGAEIIVCTP 520
Cdd:cd17922   76 SEKAKQLKNPPGILITTP 93
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
404-446 7.14e-06

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: 47.91  E-value: 7.14e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 39104531  404 LKKH-GYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLP 446
Cdd:cd17920    4 LKEVfGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLP 47
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
414-520 1.01e-05

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: 47.25  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  414 PIQTQAIPAIMSGRD--LIGiAKTGSGKTIAFLLPMFRHimdqrsLEEGEGPIAVIMTPTRELALQITKE-CKKFSKTLG 490
Cdd:cd18021    6 PIQTQVFNSLYNTDDnvFVG-APTGSGKTVCAELALLRH------WRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLG 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 39104531  491 LRVVCVYGgtgisEQIAELK--RGAEIIVCTP 520
Cdd:cd18021   79 KKVVKLTG-----ETSTDLKllAKSDVILATP 105
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
427-527 2.05e-05

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 46.49  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  427 RDLIGIAKTGSGKT-IAFLLpMFRHIMDQRSLEEGeGPIAVIMTPTRELALQitkECKKFSKTLGLRVVCVYGGTGISEQ 505
Cdd:cd18034   17 RNTIVVLPTGSGKTlIAVML-IKEMGELNRKEKNP-KKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEMGVDKW 91
                         90       100
                 ....*....|....*....|....*.
gi 39104531  506 IA----ELKRGAEIIVCTPGRMIDML 527
Cdd:cd18034   92 TKerwkEELEKYDVLVMTAQILLDAL 117
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
409-444 2.56e-05

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 48.56  E-value: 2.56e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 39104531  409 YEKPTPIQTQAIPAIMSGRD-LIgIAKTGSGKTIA-FL 444
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGEStLL-IAPTGSGKTLAaFL 58
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
411-520 2.81e-05

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: 46.27  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  411 KPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEgpiAVIMTPTRELALQITKECKKFSKTLG 490
Cdd:cd17927    2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGK---VVFLANKVPLVEQQKEVFRKHFERPG 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 39104531  491 LRVVCVYGGTGISEQIAELKRGAEIIVCTP 520
Cdd:cd17927   79 YKVTGLSGDTSENVSVEQIVESSDVIIVTP 108
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
408-576 1.02e-04

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: 44.67  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  408 GYEKPTPIQTQAIP-AIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSlEEGEGPIA----VIMTPTRELALQITKEC 482
Cdd:cd18019   14 GFKSLNRIQSKLFPaAFETDENLLLCAPTGAGKTNVALLTILREIGKHRN-PDGTINLDafkiVYIAPMKALVQEMVGNF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  483 KKFSKTLGLRVVCVYGGTGIS-EQIAElkrgAEIIVCTPGRMiDMLAANSGkSRVFYYLFSLLfVLDMIFVEADLR---- 557
Cdd:cd18019   93 SKRLAPYGITVAELTGDQQLTkEQISE----TQIIVTTPEKW-DIITRKSG-DRTYTQLVRLI-IIDEIHLLHDDRgpvl 165
                        170       180
                 ....*....|....*....|....*...
gi 39104531  558 ---IVDNVRPDRQT------VMFSATFP 576
Cdd:cd18019  166 esiVARTIRQIEQTqeyvrlVGLSATLP 193
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
411-583 1.03e-04

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 44.33  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  411 KPTPIQTQAIPAIMSG------RDLIGIAKTGSGKTIAFLLPMFRHIMDQRSleegegpiAVIMTPTRELALQITKECKK 484
Cdd:cd17918   15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYKNGKQ--------VAILVPTEILAHQHYEEARK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  485 FSKTlgLRVVCVYGGTgiSEQIAElkrGAEIIVCTpgrmidmlaansgksrvfyylfSLLFVLDMIFVEADLRIVD---- 560
Cdd:cd17918   87 FLPF--INVELVTGGT--KAQILS---GISLLVGT----------------------HALLHLDVKFKNLDLVIVDeqhr 137
                        170       180       190
                 ....*....|....*....|....*....|...
gi 39104531  561 ---------NVRPDRQTVMFSAT-FPRAMeALA 583
Cdd:cd17918  138 fgvaqrealYNLGATHFLEATATpIPRTL-ALA 169
PRK13766 PRK13766
Hef nuclease; Provisional
673-738 2.08e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 45.25  E-value: 2.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39104531   673 IINDFKNGTCKLLVATSVAARGLDVKHLILVVnyscpnHYED------YVHRAGRTGRaGNKGYAYTFITED 738
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) ...
634-696 2.40e-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: 2.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39104531  634 VIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKN--GTCKLLVATSVAARGLD 696
Cdd:cd18793   30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGVGLN 94
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
414-520 3.49e-04

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: 42.75  E-value: 3.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  414 PIQTQAIPAIMSGRD--LIGiAKTGSGKTIAFLLPMFrhimdqRSLEEGEGPIAVIMTPTRELALQITKECKK-FSKTLG 490
Cdd:cd18022    4 PIQTQVFHTLYHTDNnvLLG-APTGSGKTIAAELAMF------RAFNKYPGSKVVYIAPLKALVRERVDDWKKrFEEKLG 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 39104531  491 LRVVCVYGGTgiSEQIAELkRGAEIIVCTP 520
Cdd:cd18022   77 KKVVELTGDV--TPDMKAL-ADADIIITTP 103
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
414-493 4.27e-04

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 42.32  E-value: 4.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  414 PIQTQAIPA-IMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrsleegEGPIAVIMTPTRELALQITKECKKFSKtLGLR 492
Cdd:cd18028    4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLL--------EGGKALYLVPLRALASEKYEEFKKLEE-IGLK 74

                 .
gi 39104531  493 V 493
Cdd:cd18028   75 V 75
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
664-732 4.39e-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: 4.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39104531  664 GIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRaGNKGYAY 732
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 ...
659-731 6.28e-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: 6.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39104531  659 MSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYA 731
Cdd:cd18797   70 ASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLV 142
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
414-697 6.65e-04

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: 43.53  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  414 PIQTQAIPAIMSGRDLIG-----IAKTGSGKTIAFLLPMFRHimdqrsLEEGEGPIAVIMTPTRELALQITKECKKFskt 488
Cdd:COG1203  130 PLQNEALELALEAAEEEPglfilTAPTGGGKTEAALLFALRL------AAKHGGRRIIYALPFTSIINQTYDRLRDL--- 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  489 LGLRVVCVYGGTGISEQIAE------------LKRG--AEIIVCTPGRMID-MLAANSGKSRVFYYLFSLLFVLDmifvE 553
Cdd:COG1203  201 FGEDVLLHHSLADLDLLEEEeeyesearwlklLKELwdAPVVVTTIDQLFEsLFSNRKGQERRLHNLANSVIILD----E 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  554 AD----------LRIVDNVRPDRQTVMF-SATFPRAMEALARR----ILSKPIEVQVGGRSVVCSDVEqqvIVIEEEKKF 618
Cdd:COG1203  277 VQayppymlallLRLLEWLKNLGGSVILmTATLPPLLREELLEayelIPDEPEELPEYFRAFVRKRVE---LKEGPLSDE 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  619 LKLLELLGHYQESGSVIIFVDKQEHADGL---LKDLMrASYPCMSLHGGIDQYDR----DSIINDFKNGTCKLLVATSVA 691
Cdd:COG1203  354 ELAELILEALHKGKSVLVIVNTVKDAQELyeaLKEKL-PDEEVYLLHSRFCPADRseieKEIKERLERGKPCILVSTQVV 432

                 ....*.
gi 39104531  692 ARGLDV 697
Cdd:COG1203  433 EAGVDI 438
PRK00254 PRK00254
ski2-like helicase; Provisional
396-519 1.26e-03

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 42.88  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531   396 ISMKILNSLKKHGYEKPTPIQTQAIPA-IMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDqrsleegEGPIAVIMTPTREL 474
Cdd:PRK00254    8 VDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR-------EGGKAVYLVPLKAL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 39104531   475 ALQITKECKKFSKtLGLRVVCVyggTGISEQIAELKRGAEIIVCT 519
Cdd:PRK00254   81 AEEKYREFKDWEK-LGLRVAMT---TGDYDSTDEWLGKYDIIIAT 121
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
648-697 1.65e-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: 40.41  E-value: 1.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 39104531  648 LKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDV 697
Cdd:cd18811   54 LKERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDV 103
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
633-704 1.76e-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: 1.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39104531  633 SVIIFVDKQEHADGLLKDLMRASYPCMSLHGG-IDQYDRDSIINDFKNGTCKLLVATSVA--ARGLDVKHLILVV 704
Cdd:cd18799    8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDySDRERGDEALILLFFGELKPPILVTVDllTTGVDIPEVDNVV 82
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
410-446 2.54e-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: 2.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 39104531  410 EKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLP 446
Cdd:cd18015   17 EKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLP 53
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
662-727 2.69e-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: 2.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39104531  662 HGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGN 727
Cdd:cd18796   75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
399-734 2.85e-03

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 41.28  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  399 KILNSLKKH-GYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLP--MFrhimdqrsleegEGPiAVIMTPTreLA 475
Cdd:COG0514    4 DALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLL------------PGL-TLVVSPL--IA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  476 L---QItkeckKFSKTLGLRVVCVYGGTGISEQ---IAELKRGA-EIIVCTP-----GRMIDMLAansgKSRVfyylfSL 543
Cdd:COG0514   69 LmkdQV-----DALRAAGIRAAFLNSSLSAEERrevLRALRAGElKLLYVAPerllnPRFLELLR----RLKI-----SL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  544 lFVLDmifvEA--------D-----LRIVDNVR--PDRQTVMFSATF-PRAMEALARRI-LSKPiEVQVGG--------- 597
Cdd:COG0514  135 -FAID----EAhcisqwghDfrpdyRRLGELRErlPNVPVLALTATAtPRVRADIAEQLgLEDP-RVFVGSfdrpnlrle 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  598 -RSVVCSDVEQQVIvieeekkflklLELLGHYQESGsvIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIIND 676
Cdd:COG0514  209 vVPKPPDDKLAQLL-----------DFLKEHPGGSG--IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDR 275
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39104531  677 FKNGTCKLLVATSvaARGL-----DVKhliLVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTF 734
Cdd:COG0514  276 FLRDEVDVIVATI--AFGMgidkpDVR---FVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
661-751 3.71e-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: 39.25  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  661 LHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVkhlilvvnyscPNHYEDYVHRA------------GRTGRAGNK 728
Cdd:cd18810   57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDI-----------PNANTIIIERAdkfglaqlyqlrGRVGRSKER 125
                         90       100
                 ....*....|....*....|...
gi 39104531  729 GYAYtFITEDQARYAGDIIKALE 751
Cdd:cd18810  126 AYAY-FLYPDQKKLTEDALKRLE 147
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
661-739 8.20e-03

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 38.40  E-value: 8.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39104531  661 LHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVkhlilvvnyscPNHYEDYVHRA------------GRTGRAGNK 728
Cdd:cd18792   66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDV-----------PNANTMIIEDAdrfglsqlhqlrGRVGRGKHQ 134
                         90
                 ....*....|.
gi 39104531  729 GYAYtFITEDQ 739
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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