NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2069512976|ref|XP_042305558|]
View 

probable ATP-dependent RNA helicase DDX46 isoform X3 [Sceloporus undulatus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
360-581 6.05e-167

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: 488.43  E-value: 6.05e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  360 TVKGKGCPKPIKTWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPL 439
Cdd:cd17953      1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  440 EEGEGPIAVIMTPTRELALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGRVTNL 519
Cdd:cd17953     81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069512976  520 RRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 581
Cdd:cd17953    161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
377-792 1.45e-157

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 472.32  E-value: 1.45e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  377 GISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPleegEGPIAVIMTPTREL 456
Cdd:COG0513      8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  457 ALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVtNLRRVTYVVLDEADRMFDM 536
Cdd:COG0513     84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGAL-DLSGVETLVLDEADRMLDM 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  537 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQNVIVIEEENKFLKLLELLGHfQ 616
Cdd:COG0513    161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRD-E 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  617 EKGSVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCP 696
Cdd:COG0513    240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  697 NHYEDYVHRAGRTGRAGNKGYAYTFITEDQVRYAGDIIKALELSGTPVP-PELEKLWTDFKDQQKAEGKTIKKSS--GFS 773
Cdd:COG0513    320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEElPGFEPVEEKRLERLKPKIKEKLKGKkaGRG 399
                          410
                   ....*....|....*....
gi 2069512976  774 GKGFKFDETEEALANERKK 792
Cdd:COG0513    400 GRPGPKGERKARRGKRRRR 418
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
936-1038 2.65e-61

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


:

Pssm-ID: 411901  Cd Length: 103  Bit Score: 203.70  E-value: 2.65e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  936 SFKRYEEELEINDFPQTARWKVTSKEALHRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1015
Cdd:cd22473      1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                           90       100
                   ....*....|....*....|...
gi 2069512976 1016 LIKEELIRLQNSYQPTNKGRYKV 1038
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) ...
360-581 6.05e-167

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: 488.43  E-value: 6.05e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  360 TVKGKGCPKPIKTWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPL 439
Cdd:cd17953      1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  440 EEGEGPIAVIMTPTRELALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGRVTNL 519
Cdd:cd17953     81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069512976  520 RRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 581
Cdd:cd17953    161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
PTZ00110 PTZ00110
helicase; Provisional
317-751 5.30e-161

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 486.20  E-value: 5.30e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  317 LEPVDHGKIEYETYRKNFYVEVPELAKMTQEEVNAYRLEMEGITVKGKGCPKPIKTWVQCGISMKILNSLKKHGYEKPTP 396
Cdd:PTZ00110    76 LQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  397 IQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGVRVV 476
Cdd:PTZ00110   156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  477 CVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANngrVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTV 556
Cdd:PTZ00110   236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESN---VTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTL 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  557 MFSATFPRAMEALARRILS-KPIEVQVGGRSV-VCSDVEQNVIVIEEENKFLKLLELLGH-FQEKGSVIIFVDKQEHADG 633
Cdd:PTZ00110   313 MWSATWPKEVQSLARDLCKeEPVHVNVGSLDLtACHNIKQEVFVVEEHEKRGKLKMLLQRiMRDGDKILIFVETKKGADF 392
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  634 LLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAG 713
Cdd:PTZ00110   393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2069512976  714 NKGYAYTFITEDQVRYAGDIIKALELSGTPVPPELEKL 751
Cdd:PTZ00110   473 AKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKL 510
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
377-792 1.45e-157

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 472.32  E-value: 1.45e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  377 GISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPleegEGPIAVIMTPTREL 456
Cdd:COG0513      8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  457 ALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVtNLRRVTYVVLDEADRMFDM 536
Cdd:COG0513     84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGAL-DLSGVETLVLDEADRMLDM 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  537 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQNVIVIEEENKFLKLLELLGHfQ 616
Cdd:COG0513    161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRD-E 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  617 EKGSVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCP 696
Cdd:COG0513    240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  697 NHYEDYVHRAGRTGRAGNKGYAYTFITEDQVRYAGDIIKALELSGTPVP-PELEKLWTDFKDQQKAEGKTIKKSS--GFS 773
Cdd:COG0513    320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEElPGFEPVEEKRLERLKPKIKEKLKGKkaGRG 399
                          410
                   ....*....|....*....
gi 2069512976  774 GKGFKFDETEEALANERKK 792
Cdd:COG0513    400 GRPGPKGERKARRGKRRRR 418
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
382-792 2.91e-72

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 250.64  E-value: 2.91e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPL--EEGEGPIAVIMTPTRELALQ 459
Cdd:PRK04537    20 LLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadRKPEDPRALILAPTRELAIQ 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  460 ITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANngRVTNLRRVTYVVLDEADRMFDMGFE 539
Cdd:PRK04537   100 IHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQH--KVVSLHACEICVLDEADRMFDLGFI 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  540 PQVMRIVDNV--RPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQNVIVIEEENKFLKLLELLGHfQE 617
Cdd:PRK04537   178 KDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLGLLSR-SE 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  618 KGSVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPN 697
Cdd:PRK04537   257 GARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPF 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  698 HYEDYVHRAGRTGRAGNKGYAYTFITEdqvRYAGDI--IKALELSGTPVPPELEKLWTDFK--DQQKAEGKTIKKSSGFS 773
Cdd:PRK04537   337 DAEDYVHRIGRTARLGEEGDAISFACE---RYAMSLpdIEAYIEQKIPVEPVTAELLTPLPrpPRVPVEGEEADDEAGDS 413
                          410
                   ....*....|....*....
gi 2069512976  774 gKGFKFDETEEALANERKK 792
Cdd:PRK04537   414 -VGTIFREAREQRAAEEQR 431
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
395-569 4.81e-63

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 210.95  E-value: 4.81e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  395 TPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPleegeGPIAVIMTPTRELALQITKECKKFSKTLGVR 474
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN-----GPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  475 VVCVYGGTGISEQIAELKrGAEVIVCTPGRMIDMLAANNgrvtNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQ 554
Cdd:pfam00270   76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK----LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQ 150
                          170
                   ....*....|....*
gi 2069512976  555 TVMFSATFPRAMEAL 569
Cdd:pfam00270  151 ILLLSATLPRNLEDL 165
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
936-1038 2.65e-61

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


Pssm-ID: 411901  Cd Length: 103  Bit Score: 203.70  E-value: 2.65e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  936 SFKRYEEELEINDFPQTARWKVTSKEALHRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1015
Cdd:cd22473      1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                           90       100
                   ....*....|....*....|...
gi 2069512976 1016 LIKEELIRLQNSYQPTNKGRYKV 1038
Cdd:cd22473     81 LIKEELLRLQASYQPINKGRYKV 103
DEXDc smart00487
DEAD-like helicases superfamily;
386-594 7.59e-56

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 191.94  E-value: 7.59e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976   386 LKKHGYEKPTPIQAQAIPAIMSG-RDLIGIAKTGSGKTIAFLLPMFRHIMdqrpleEGEGPIAVIMTPTRELALQITKEC 464
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976   465 KKFSKTLGVRVVCVYGGTGISEQIAELKRG-AEVIVCTPGRMIDMLAANNgrvTNLRRVTYVVLDEADRMFDMGFEPQVM 543
Cdd:smart00487   75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDK---LSLSNVDLVILDEAHRLLDGGFGDQLE 151
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2069512976   544 RIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRsvVCSDVEQ 594
Cdd:smart00487  152 KLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT--PLEPIEQ 200
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
592-722 7.79e-55

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: 186.56  E-value: 7.79e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  592 VEQNVIVIEEENKFLKLLELLGHFQEKGSVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKL 671
Cdd:cd18787      1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2069512976  672 LVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAGNKGYAYTFI 722
Cdd:cd18787     81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
603-713 2.88e-30

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: 115.39  E-value: 2.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  603 NKFLKLLELLgHFQEKGSVIIFVDKQEHAD-GLLKDlmRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARG 681
Cdd:pfam00271    1 EKLEALLELL-KKERGGKVLIFSQTKKTLEaELLLE--KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2069512976  682 LDVKHLTLVINYSCPNHYEDYVHRAGRTGRAG 713
Cdd:pfam00271   78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
634-713 1.48e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 98.05  E-value: 1.48e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976   634 LLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAG 713
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
381-720 1.17e-20

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: 97.98  E-value: 1.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  381 KILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrpleEGEGPIAVIMTPTRELAL-Q 459
Cdd:COG1205     44 ELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL------EDPGATALYLYPTKALARdQ 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  460 ItKECKKFSKTLGVRV-VCVY-GGTGISEQiAELKRGAEVIVCTPgrmiDML----AANNGR-VTNLRRVTYVVLDEA-- 530
Cdd:COG1205    118 L-RRLRELAEALGLGVrVATYdGDTPPEER-RWIREHPDIVLTNP----DMLhyglLPHHTRwARFFRNLRYVVIDEAht 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  531 -------------DRMfdmgfepqvMRIVDNVRPDRQTVMFSATFPRAmEALARRILSKPIEVqV-------GGRSVV-- 588
Cdd:COG1205    192 yrgvfgshvanvlRRL---------RRICRHYGSDPQFILASATIGNP-AEHAERLTGRPVTV-VdedgsprGERTFVlw 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  589 -CSDVEQNVivieEENKFLKLLELLGHFQEKG-SVIIFVD------------KQEHADGLLKDLMRAsYpclslHGGIDQ 654
Cdd:COG1205    261 nPPLVDDGI----RRSALAEAARLLADLVREGlRTLVFTRsrrgaellaryaRRALREPDLADRVAA-Y-----RAGYLP 330
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069512976  655 YDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAGNKGYAYT 720
Cdd:COG1205    331 EERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
 
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) ...
360-581 6.05e-167

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: 488.43  E-value: 6.05e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  360 TVKGKGCPKPIKTWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPL 439
Cdd:cd17953      1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  440 EEGEGPIAVIMTPTRELALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGRVTNL 519
Cdd:cd17953     81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069512976  520 RRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 581
Cdd:cd17953    161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
PTZ00110 PTZ00110
helicase; Provisional
317-751 5.30e-161

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 486.20  E-value: 5.30e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  317 LEPVDHGKIEYETYRKNFYVEVPELAKMTQEEVNAYRLEMEGITVKGKGCPKPIKTWVQCGISMKILNSLKKHGYEKPTP 396
Cdd:PTZ00110    76 LQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  397 IQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGVRVV 476
Cdd:PTZ00110   156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  477 CVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANngrVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTV 556
Cdd:PTZ00110   236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESN---VTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTL 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  557 MFSATFPRAMEALARRILS-KPIEVQVGGRSV-VCSDVEQNVIVIEEENKFLKLLELLGH-FQEKGSVIIFVDKQEHADG 633
Cdd:PTZ00110   313 MWSATWPKEVQSLARDLCKeEPVHVNVGSLDLtACHNIKQEVFVVEEHEKRGKLKMLLQRiMRDGDKILIFVETKKGADF 392
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  634 LLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAG 713
Cdd:PTZ00110   393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2069512976  714 NKGYAYTFITEDQVRYAGDIIKALELSGTPVPPELEKL 751
Cdd:PTZ00110   473 AKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKL 510
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
377-792 1.45e-157

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 472.32  E-value: 1.45e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  377 GISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPleegEGPIAVIMTPTREL 456
Cdd:COG0513      8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  457 ALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVtNLRRVTYVVLDEADRMFDM 536
Cdd:COG0513     84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGAL-DLSGVETLVLDEADRMLDM 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  537 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQNVIVIEEENKFLKLLELLGHfQ 616
Cdd:COG0513    161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRD-E 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  617 EKGSVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCP 696
Cdd:COG0513    240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  697 NHYEDYVHRAGRTGRAGNKGYAYTFITEDQVRYAGDIIKALELSGTPVP-PELEKLWTDFKDQQKAEGKTIKKSS--GFS 773
Cdd:COG0513    320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEElPGFEPVEEKRLERLKPKIKEKLKGKkaGRG 399
                          410
                   ....*....|....*....
gi 2069512976  774 GKGFKFDETEEALANERKK 792
Cdd:COG0513    400 GRPGPKGERKARRGKRRRR 418
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
382-580 3.54e-101

DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 315.89  E-value: 3.54e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGEGPIAVIMTPTRELALQIT 461
Cdd:cd17952      1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  462 KECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAAnngRVTNLRRVTYVVLDEADRMFDMGFEPQ 541
Cdd:cd17952     81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKK---KATNLQRVTYLVLDEADRMFDMGFEYQ 157
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2069512976  542 VMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 580
Cdd:cd17952    158 VRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
382-581 2.38e-97

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 305.52  E-value: 2.38e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImDQRPLEEGEGPIAVIMTPTRELALQIT 461
Cdd:cd00268      1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKL-LPEPKKKGRGPQALVLAPTRELAMQIA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  462 KECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVtNLRRVTYVVLDEADRMFDMGFEPQ 541
Cdd:cd00268     80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLI--ERGKL-DLSNVKYLVLDEADRMLDMGFEED 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2069512976  542 VMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 581
Cdd:cd00268    157 VEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
382-581 2.07e-96

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: 303.14  E-value: 2.07e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGEGPIAVIMTPTRELALQIT 461
Cdd:cd17966      1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  462 KECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNgrvTNLRRVTYVVLDEADRMFDMGFEPQ 541
Cdd:cd17966     81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGK---TNLRRVTYLVLDEADRMLDMGFEPQ 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2069512976  542 VMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 581
Cdd:cd17966    158 IRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
383-754 8.83e-95

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 308.65  E-value: 8.83e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  383 LNSLkkhGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPleegeGPIAVIMTPTRELALQITK 462
Cdd:PRK11776    19 LNEL---GYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRF-----RVQALVLCPTRELADQVAK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  463 ECKKFSKTL-GVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAanNGRVtNLRRVTYVVLDEADRMFDMGFEPQ 541
Cdd:PRK11776    91 EIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLR--KGTL-DLDALNTLVLDEADRMLDMGFQDA 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  542 VMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVcSDVEQNVIVIEEENKFLKLLELLGHFQEKgSV 621
Cdd:PRK11776   168 IDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSPDERLPALQRLLLHHQPE-SC 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  622 IIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPNHYED 701
Cdd:PRK11776   246 VVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEV 325
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069512976  702 YVHRAGRTGRAGNKGYAYTFITEDQVRYAGDIIKALE-------------LSGTPVPPELEKLWTD 754
Cdd:PRK11776   326 HVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGrklnweplpslspLSGVPLLPEMVTLCID 391
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
377-738 3.22e-86

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 285.55  E-value: 3.22e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  377 GISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGEGPI-AVIMTPTRE 455
Cdd:PRK10590     7 GLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  456 LALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANngrVTNLRRVTYVVLDEADRMFD 535
Cdd:PRK10590    87 LAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQN---AVKLDQVEILVLDEADRMLD 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  536 MGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQNVIVIEEENKflklLELLGHF 615
Cdd:PRK10590   164 MGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRK----RELLSQM 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  616 QEKGS---VIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVIN 692
Cdd:PRK10590   240 IGKGNwqqVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2069512976  693 YSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQVRYAGDIIKALE 738
Cdd:PRK10590   320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK 365
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
326-583 6.73e-86

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: 278.05  E-value: 6.73e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  326 EYETYRKNFYVEVPELAKMTQEEVNAYRLEMEgITVKGKGCPKPIKTWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAI 405
Cdd:cd18050     18 ELPKFEKNFYVEHPEVARMTQYDVEELRRKKE-ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  406 MSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGVRVVCVYGGTGIS 485
Cdd:cd18050     97 LSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKG 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  486 EQIAELKRGAEVIVCTPGRMIDMLAANNgrvTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRA 565
Cdd:cd18050    177 PQIRDLERGVEICIATPGRLIDFLEAGK---TNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKE 253
                          250
                   ....*....|....*...
gi 2069512976  566 MEALARRILSKPIEVQVG 583
Cdd:cd18050    254 VRQLAEDFLRDYVQINIG 271
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
334-748 2.06e-83

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 280.14  E-value: 2.06e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  334 FYVEVPEL-AKMTQEEVNAYRLEMEgITVKGKGCPKPIKTWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLI 412
Cdd:PLN00206    84 FYVRDPGStSGLSSSQAELLRRKLE-IHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLL 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  413 GIAKTGSGKTIAFLLPMFRHIMDQRP--LEEGEGPIAVIMTPTRELALQITKECKKFSKTLGVRVVCVYGGTGISEQIAE 490
Cdd:PLN00206   163 VSADTGSGKTASFLVPIISRCCTIRSghPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYR 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  491 LKRGAEVIVCTPGRMIDMLAANNgrvTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVrPDRQTVMFSATFPRAMEALA 570
Cdd:PLN00206   243 IQQGVELIVGTPGRLIDLLSKHD---IELDNVSVLVLDEVDCMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFA 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  571 RRILSKPIEVQVGGRSVVCSDVEQNVIVIEEENKFLKLLELL---GHFQEkgSVIIFVDKQEHADgLLKDLMRAS--YPC 645
Cdd:PLN00206   319 SSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILkskQHFKP--PAVVFVSSRLGAD-LLANAITVVtgLKA 395
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  646 LSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITED 725
Cdd:PLN00206   396 LSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE 475
                          410       420
                   ....*....|....*....|...
gi 2069512976  726 QVRYAGDIIKALELSGTPVPPEL 748
Cdd:PLN00206   476 DRNLFPELVALLKSSGAAIPREL 498
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
382-583 6.75e-82

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: 265.12  E-value: 6.75e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGEG-----PIAVIMTPTREL 456
Cdd:cd17967     11 LLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPSALILAPTREL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  457 ALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVtNLRRVTYVVLDEADRMFDM 536
Cdd:cd17967     91 AIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI--ERGRI-SLSSIKFLVLDEADRMLDM 167
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2069512976  537 GFEPQVMRIVD----NVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVG 583
Cdd:cd17967    168 GFEPQIRKIVEhpdmPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
347-584 9.74e-80

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: 259.94  E-value: 9.74e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  347 EEVNAYRLEMEgITVKGKGCPKPIKTWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFL 426
Cdd:cd18049      1 QEVEQYRRSKE-ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  427 LPMFRHIMDQRPLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMI 506
Cdd:cd18049     80 LPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLI 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069512976  507 DMLAANNgrvTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGG 584
Cdd:cd18049    160 DFLEAGK---TNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
382-580 8.82e-76

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 248.39  E-value: 8.82e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEE---GEGPIAVIMTPTRELAL 458
Cdd:cd17945      1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEetkDDGPYALILAPTRELAQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  459 QITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaanNGRVTNLRRVTYVVLDEADRMFDMGF 538
Cdd:cd17945     81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCL---ERRLLVLNQCTYVVLDEADRMIDMGF 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069512976  539 EPQVMRI-----VDNVRPD---------------RQTVMFSATFPRAMEALARRILSKPIEV 580
Cdd:cd17945    158 EPQVTKIldampVSNKKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
382-580 1.59e-75

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: 246.99  E-value: 1.59e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQ-RPLEEGEGPIAVIMTPTRELALQI 460
Cdd:cd17958      1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQpIPREQRNGPGVLVLTPTRELALQI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  461 TKECKKFSKTlGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANngrVTNLRRVTYVVLDEADRMFDMGFEP 540
Cdd:cd17958     81 EAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNN---VINLKSITYLVLDEADRMLDMGFEP 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2069512976  541 QVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 580
Cdd:cd17958    157 QIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
372-749 4.05e-75

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 260.55  E-value: 4.05e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  372 TWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrplEEGEGPIAVIMT 451
Cdd:PRK11634     7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD-----PELKAPQILVLA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  452 PTRELALQITKECKKFSKTL-GVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGRVTNLRRVtyvVLDEA 530
Cdd:PRK11634    82 PTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGL---VLDEA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  531 DRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQNVIVIEEENKFLKLLE 610
Cdd:PRK11634   159 DEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  611 LLgHFQEKGSVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLV 690
Cdd:PRK11634   239 FL-EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2069512976  691 INYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQVRYAGDIIKALELSgtpvPPELE 749
Cdd:PRK11634   318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLT----IPEVE 372
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
361-574 6.85e-75

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: 247.57  E-value: 6.85e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  361 VKGKGCPKPIKTWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQR--- 437
Cdd:cd18052     33 VTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGlta 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  438 -PLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRV 516
Cdd:cd18052    113 sSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFI--GRGKI 190
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069512976  517 tNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNV----RPDRQTVMFSATFPRAMEALARRIL 574
Cdd:cd18052    191 -SLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFL 251
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
383-768 4.77e-74

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 251.40  E-value: 4.77e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  383 LNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDqRPLEEGEGPIAVIMTPTRELALQITK 462
Cdd:PRK11192    13 LEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLD-FPRRKSGPPRILILTPTRELAMQVAD 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  463 ECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNgrvTNLRRVTYVVLDEADRMFDMGFEPQV 542
Cdd:PRK11192    92 QARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEN---FDCRAVETLILDEADRMLDMGFAQDI 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  543 MRIVDNVRPDRQTVMFSATFP-RAMEALARRILSKPIEVQVGGrsvvcSDVEQNVI------VIEEENKFLKLLELLGHF 615
Cdd:PRK11192   169 ETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEP-----SRRERKKIhqwyyrADDLEHKTALLCHLLKQP 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  616 QEKGSvIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSC 695
Cdd:PRK11192   244 EVTRS-IVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDM 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  696 PNHYEDYVHRAGRTGRAGNKGYAYTFI-TEDQV------RYAGDIIKALELSG----TPVPPELEKLWTDFKDQQKAEGK 764
Cdd:PRK11192   323 PRSADTYLHRIGRTGRAGRKGTAISLVeAHDHLllgkieRYIEEPLKARVIDElrpkTKAPSEKKTGKPSKKVLAKRAEK 402

                   ....
gi 2069512976  765 TIKK 768
Cdd:PRK11192   403 KEKE 406
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
382-792 2.91e-72

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 250.64  E-value: 2.91e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPL--EEGEGPIAVIMTPTRELALQ 459
Cdd:PRK04537    20 LLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadRKPEDPRALILAPTRELAIQ 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  460 ITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANngRVTNLRRVTYVVLDEADRMFDMGFE 539
Cdd:PRK04537   100 IHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQH--KVVSLHACEICVLDEADRMFDLGFI 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  540 PQVMRIVDNV--RPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQNVIVIEEENKFLKLLELLGHfQE 617
Cdd:PRK04537   178 KDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLGLLSR-SE 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  618 KGSVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPN 697
Cdd:PRK04537   257 GARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPF 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  698 HYEDYVHRAGRTGRAGNKGYAYTFITEdqvRYAGDI--IKALELSGTPVPPELEKLWTDFK--DQQKAEGKTIKKSSGFS 773
Cdd:PRK04537   337 DAEDYVHRIGRTARLGEEGDAISFACE---RYAMSLpdIEAYIEQKIPVEPVTAELLTPLPrpPRVPVEGEEADDEAGDS 413
                          410
                   ....*....|....*....
gi 2069512976  774 gKGFKFDETEEALANERKK 792
Cdd:PRK04537   414 -VGTIFREAREQRAAEEQR 431
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
357-583 3.42e-72

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: 239.56  E-value: 3.42e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  357 EGITVK--GKGCPKPIKTWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIM 434
Cdd:cd18051      5 EDIPVEatGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  435 DQRPLE---EGEG--------PIAVIMTPTRELALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPG 503
Cdd:cd18051     85 EQGPGEslpSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  504 RMIDMLaaNNGRVtNLRRVTYVVLDEADRMFDMGFEPQVMRIV--DNVRP--DRQTVMFSATFPRAMEALARRILSKPIE 579
Cdd:cd18051    165 RLVDML--ERGKI-GLDYCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPtgERQTLMFSATFPKEIQMLARDFLDNYIF 241

                   ....
gi 2069512976  580 VQVG 583
Cdd:cd18051    242 LAVG 245
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
390-750 1.84e-70

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 242.90  E-value: 1.84e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  390 GYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEE---GEgPIAVIMTPTRELALQITKECKK 466
Cdd:PRK01297   106 GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymGE-PRALIIAPTRELVVQIAKDAAA 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  467 FSKTLGVRVVCVYGGTGISEQIAELK-RGAEVIVCTPGRMIDMlaaNNGRVTNLRRVTYVVLDEADRMFDMGFEPQVMRI 545
Cdd:PRK01297   185 LTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDF---NQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQI 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  546 VDNVRP--DRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQNVIVIEEENKFlKLLELLGHFQEKGSVII 623
Cdd:PRK01297   262 IRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKY-KLLYNLVTQNPWERVMV 340
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  624 FVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPNHYEDYV 703
Cdd:PRK01297   341 FANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYV 420
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2069512976  704 HRAGRTGRAGNKGYAYTFITEDQVRYAGDIIKAL--ELSGTPVPPELEK 750
Cdd:PRK01297   421 HRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLgrKISCEMPPAELLK 469
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
381-730 6.63e-68

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 234.10  E-value: 6.63e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  381 KILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdQRPLEEGE---GPIAVIMTPTRELA 457
Cdd:PRK04837    18 QVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLL-SHPAPEDRkvnQPRALIMAPTRELA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  458 LQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANngrVTNLRRVTYVVLDEADRMFDMG 537
Cdd:PRK04837    97 VQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQN---HINLGAIQVVVLDEADRMFDLG 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  538 FepqvmriVDNVR------PD---RQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQNVIVIEEENKFLKL 608
Cdd:PRK04837   174 F-------IKDIRwlfrrmPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLL 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  609 LELLGH-FQEKgsVIIFVDKQeH----------ADGLLKDLmrasypclsLHGGIDQYDRDSIINDFKSGVCKLLVATSV 677
Cdd:PRK04837   247 QTLIEEeWPDR--AIIFANTK-HrceeiwghlaADGHRVGL---------LTGDVAQKKRLRILEEFTRGDLDILVATDV 314
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2069512976  678 AARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDqvrYA 730
Cdd:PRK04837   315 AARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE---YA 364
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
377-581 2.44e-64

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


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 216.02  E-value: 2.44e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  377 GISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLeegEGPIAVIMTPTREL 456
Cdd:cd17959      7 GLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPT---VGARALILSPTREL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  457 ALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNgrvTNLRRVTYVVLDEADRMFDM 536
Cdd:cd17959     84 ALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMN---LKLSSVEYVVFDEADRLFEM 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2069512976  537 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 581
Cdd:cd17959    161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
382-580 1.51e-63

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: 214.13  E-value: 1.51e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQR---PLEEGEGPIAVIMTPTRELAL 458
Cdd:cd17951      1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEkklPFIKGEGPYGLIVCPSRELAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  459 QITKECKKFSKTL------GVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaanNGRVTNLRRVTYVVLDEADR 532
Cdd:cd17951     81 QTHEVIEYYCKALqeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML---NKKKINLDICRYLCLDEADR 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2069512976  533 MFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 580
Cdd:cd17951    158 MIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
395-569 4.81e-63

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 210.95  E-value: 4.81e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  395 TPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPleegeGPIAVIMTPTRELALQITKECKKFSKTLGVR 474
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN-----GPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  475 VVCVYGGTGISEQIAELKrGAEVIVCTPGRMIDMLAANNgrvtNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQ 554
Cdd:pfam00270   76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK----LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQ 150
                          170
                   ....*....|....*
gi 2069512976  555 TVMFSATFPRAMEAL 569
Cdd:pfam00270  151 ILLLSATLPRNLEDL 165
PTZ00424 PTZ00424
helicase 45; Provisional
381-733 3.22e-62

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 217.39  E-value: 3.22e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  381 KILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHI-MDQRPLEegegpiAVIMTPTRELALQ 459
Cdd:PTZ00424    38 DLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIdYDLNACQ------ALILAPTRELAQQ 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  460 ITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGRVTNLRrvtYVVLDEADRMFDMGFE 539
Cdd:PTZ00424   112 IQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLK---LFILDEADEMLSRGFK 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  540 PQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQNVIVIE-EENKFLKLLELLGHFQEK 618
Cdd:PTZ00424   189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEkEEWKFDTLCDLYETLTIT 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  619 GSvIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPNH 698
Cdd:PTZ00424   269 QA-IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPAS 347
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2069512976  699 YEDYVHRAGRTGRAGNKGYAYTFITEDQVRYAGDI 733
Cdd:PTZ00424   348 PENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
936-1038 2.65e-61

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


Pssm-ID: 411901  Cd Length: 103  Bit Score: 203.70  E-value: 2.65e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  936 SFKRYEEELEINDFPQTARWKVTSKEALHRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1015
Cdd:cd22473      1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                           90       100
                   ....*....|....*....|...
gi 2069512976 1016 LIKEELIRLQNSYQPTNKGRYKV 1038
Cdd:cd22473     81 LIKEELLRLQASYQPINKGRYKV 103
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
382-583 3.62e-60

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: 203.97  E-value: 3.62e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRpleEGEGPIAVIMTPTRELALQIT 461
Cdd:cd17957      1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPR---KKKGLRALILAPTRELASQIY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  462 KECKKFSKTLGVRVVCVYGGT-GISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVTnLRRVTYVVLDEADRMFDMGFEP 540
Cdd:cd17957     78 RELLKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLL--KQGPID-LSSVEYLVLDEADKLFEPGFRE 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2069512976  541 QVMRIVDNVR-PDRQTVMFSATFPRAMEALARRILSKPIEVQVG 583
Cdd:cd17957    155 QTDEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
378-576 2.23e-59

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


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 202.43  E-value: 2.23e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  378 ISMKILNSLKKHGYEKPTPIQAQAIPAIMS-GRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGEGPIAVIMTPTREL 456
Cdd:cd17964      1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  457 ALQITKECKKFSKTL-GVRVVCVYGGTGISEQIAELKR-GAEVIVCTPGRMIDMLAANNGRVTnLRRVTYVVLDEADRMF 534
Cdd:cd17964     81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVAKA-FTDLDYLVLDEADRLL 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2069512976  535 DMGFEPQVMRIVDNVRP----DRQTVMFSATFPRAMEALARRILSK 576
Cdd:cd17964    160 DMGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLKK 205
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
372-581 5.45e-58

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: 198.31  E-value: 5.45e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  372 TWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPleegeGPIAVIMT 451
Cdd:cd17954      1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ-----RFFALVLA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  452 PTRELALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGrvTNLRRVTYVVLDEAD 531
Cdd:cd17954     76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKG--FSLKSLKFLVMDEAD 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2069512976  532 RMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 581
Cdd:cd17954    154 RLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
377-581 9.06e-57

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


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 194.75  E-value: 9.06e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  377 GISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFrhimdQRPLEEGEGPIAVIMTPTREL 456
Cdd:cd17955      5 GLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-----QRLSEDPYGIFALVLTPTREL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  457 ALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGRVTNLRRVTYVVLDEADRMFDM 536
Cdd:cd17955     80 AYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTKVLSRVKFLVLDEADRLLTG 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2069512976  537 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 581
Cdd:cd17955    160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
DEXDc smart00487
DEAD-like helicases superfamily;
386-594 7.59e-56

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 191.94  E-value: 7.59e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976   386 LKKHGYEKPTPIQAQAIPAIMSG-RDLIGIAKTGSGKTIAFLLPMFRHIMdqrpleEGEGPIAVIMTPTRELALQITKEC 464
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976   465 KKFSKTLGVRVVCVYGGTGISEQIAELKRG-AEVIVCTPGRMIDMLAANNgrvTNLRRVTYVVLDEADRMFDMGFEPQVM 543
Cdd:smart00487   75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDK---LSLSNVDLVILDEAHRLLDGGFGDQLE 151
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2069512976   544 RIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRsvVCSDVEQ 594
Cdd:smart00487  152 KLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT--PLEPIEQ 200
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
592-722 7.79e-55

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: 186.56  E-value: 7.79e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  592 VEQNVIVIEEENKFLKLLELLGHFQEKGSVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKL 671
Cdd:cd18787      1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2069512976  672 LVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAGNKGYAYTFI 722
Cdd:cd18787     81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
382-581 1.02e-54

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: 188.62  E-value: 1.02e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdQRPLEEGeGPIAVIMTPTRELALQIT 461
Cdd:cd17947      1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLL-YRPKKKA-ATRVLVLVPTRELAMQCF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  462 KECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVTNLRRVTYVVLDEADRMFDMGFEPQ 541
Cdd:cd17947     79 SVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHL--RNSPSFDLDSIEILVLDEADRMLEEGFADE 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2069512976  542 VMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 581
Cdd:cd17947    157 LKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
382-580 5.67e-54

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 186.60  E-value: 5.67e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMfrhIMdqRPLEEGEGPIAVIMTPTRELALQIT 461
Cdd:cd17962      1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPV---II--RCLTEHRNPSALILTPTRELAVQIE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  462 KECKKFSKTL-GVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaanNGRVTNLRRVTYVVLDEADRMFDMGFEP 540
Cdd:cd17962     76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL---KQSSVELDNIKIVVVDEADTMLKMGFQQ 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2069512976  541 QVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 580
Cdd:cd17962    153 QVLDILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
390-580 1.87e-51

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: 179.42  E-value: 1.87e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  390 GYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEgegpiAVIMTPTRELALQITKECKKFSK 469
Cdd:cd17940     18 GFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQ-----ALILVPTRELALQTSQVCKELGK 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  470 TLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaanNGRVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNV 549
Cdd:cd17940     93 HMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLA---KKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNFL 169
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2069512976  550 RPDRQTVMFSATFPRAMEALARRILSKPIEV 580
Cdd:cd17940    170 PKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
382-562 5.19e-51

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: 179.74  E-value: 5.19e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIP-AIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQR----PLEEGEGPIAVIMTPTREL 456
Cdd:cd17946      1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKssngVGGKQKPLRALILTPTREL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  457 ALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGRVTNLRRVTYVVLDEADRMFDM 536
Cdd:cd17946     81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSLRFLVLDEADRMLEK 160
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2069512976  537 G-FEP--QVMRIVDNVRP----DRQTVMFSATF 562
Cdd:cd17946    161 GhFAEleKILELLNKDRAgkkrKRQTFVFSATL 193
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
382-580 5.66e-51

DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 178.15  E-value: 5.66e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGEGPIAVIMTPTRELALQIT 461
Cdd:cd17960      1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  462 KECKKFSKTLG--VRVVCVYGGTGISEQIAELKR-GAEVIVCTPGRMIDMLAANNGRVtNLRRVTYVVLDEADRMFDMGF 538
Cdd:cd17960     81 EVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKV-KVKSLEVLVLDEADRLLDLGF 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2069512976  539 EPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 580
Cdd:cd17960    160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
382-582 1.00e-47

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


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 168.62  E-value: 1.00e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRpLEEGEGPIAVIMTPTRELALQIT 461
Cdd:cd17941      1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRER-WTPEDGLGALIISPTRELAMQIF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  462 KECKK------FSKTLgvrvvcVYGGTGISEqiaELKRGAE--VIVCTPGRMIDMLAANNGRVTNLRRVtyVVLDEADRM 533
Cdd:cd17941     80 EVLRKvgkyhsFSAGL------IIGGKDVKE---EKERINRmnILVCTPGRLLQHMDETPGFDTSNLQM--LVLDEADRI 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2069512976  534 FDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQV 582
Cdd:cd17941    149 LDMGFKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
387-578 4.72e-46

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: 164.68  E-value: 4.72e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  387 KKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRP-LEEGEGPIAVIMTPTRELALQITKECK 465
Cdd:cd17949      7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPrVDRSDGTLALVLVPTRELALQIYEVLE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  466 KF-SKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDML-AANNGRVTNLRrvtYVVLDEADRMFDMGFEPQVM 543
Cdd:cd17949     87 KLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLR---WLVLDEADRLLDMGFEKDIT 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2069512976  544 RIVDNVR-------------PDRQTVMFSATFPRAMEALARRILSKPI 578
Cdd:cd17949    164 KILELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPV 211
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
382-580 1.37e-44

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


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 159.83  E-value: 1.37e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRpLEEGEGPIAVIMTPTRELALQI- 460
Cdd:cd17942      1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLK-FKPRNGTGVIIISPTRELALQIy 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  461 --TKE-CKKFSKTLGvrvvCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGRVT-NLRrvtYVVLDEADRMFDM 536
Cdd:cd17942     80 gvAKElLKYHSQTFG----IVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYkNLQ---CLIIDEADRILEI 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2069512976  537 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRIL-SKPIEV 580
Cdd:cd17942    153 GFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLkKKPLYV 197
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
377-580 1.74e-43

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: 156.72  E-value: 1.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  377 GISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHI-MDQRPLEegegpiAVIMTPTRE 455
Cdd:cd17939      3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQ------ALVLAPTRE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  456 LALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGRVTNLRrvtYVVLDEADRMFD 535
Cdd:cd17939     77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIK---MFVLDEADEMLS 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2069512976  536 MGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 580
Cdd:cd17939    154 RGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
382-581 1.52e-40

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


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 148.18  E-value: 1.52e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFrhimdQRPLEEGEGPIAVIMTPTRELALQIT 461
Cdd:cd17943      1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-----ESLDLERRHPQVLILAPTREIAVQIH 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  462 KECKKFSKTLGVRVVCVY-GGTGISEQIAELKRgAEVIVCTPGRMIDMLaanNGRVTNLRRVTYVVLDEADRMFDMGFEP 540
Cdd:cd17943     76 DVFKKIGKKLEGLKCEVFiGGTPVKEDKKKLKG-CHIAVGTPGRIKQLI---ELGALNVSHVRLFVLDEADKLMEGSFQK 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2069512976  541 QVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQ 581
Cdd:cd17943    152 DVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
390-580 3.28e-40

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: 147.34  E-value: 3.28e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  390 GYEKPTPIQAQAIPAIMSG--RDLIGIAKTGSGKTIAFLLPMFRHImDQRPLEegegPIAVIMTPTRELALQITKECKKF 467
Cdd:cd17963     13 GFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKS----PQALCLAPTRELARQIGEVVEKM 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  468 SKTLGVRVVC------VYGGTGISEQIaelkrgaevIVCTPGRMIDMLAAnngRVTNLRRVTYVVLDEADRMFDM-GFEP 540
Cdd:cd17963     88 GKFTGVKVALavpgndVPRGKKITAQI---------VIGTPGTVLDWLKK---RQLDLKKIKILVLDEADVMLDTqGHGD 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2069512976  541 QVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 580
Cdd:cd17963    156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
382-578 5.06e-40

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


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 146.96  E-value: 5.06e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGE-GPIAVIMTPTRELALQI 460
Cdd:cd17961      5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqGTRALILVPTRELAQQV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  461 TKECKKFSKTLG--VRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAAnnGRVTNLRRVTYVVLDEADRMFDMGF 538
Cdd:cd17961     85 SKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLES--GSLLLLSTLKYLVIDEADLVLSYGY 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2069512976  539 EPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPI 578
Cdd:cd17961    163 EEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
386-579 1.83e-39

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: 145.38  E-value: 1.83e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  386 LKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIM-DQRPLEEGEGPIAVIMTPTRELALQITKEC 464
Cdd:cd17944      5 LQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQVTKDF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  465 KKFSKTLgvRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVtNLRRVTYVVLDEADRMFDMGFEPQVMR 544
Cdd:cd17944     85 KDITRKL--SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHL--QNGRL-DLTKLKHVVLDEVDQMLDMGFAEQVEE 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2069512976  545 IVD-----NVRPDRQTVMFSATFPRAMEALARRILSKPIE 579
Cdd:cd17944    160 ILSvsykkDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYE 199
KH-I_AtRH42_like cd22475
type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana DEAD-box ATP-dependent ...
938-1038 1.75e-37

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


Pssm-ID: 411903  Cd Length: 102  Bit Score: 135.98  E-value: 1.75e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  938 KRYEEELEINDFPQTARWKVTSKEALHRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITRlI 1017
Cdd:cd22475      3 EHFEEELEINDFPQHARWKVTHKDTLGQISELTGAAITTRGQYYPPGRIPGPGERKLYLLIEGPSEASVKEAKAEIKR-I 81
                           90       100
                   ....*....|....*....|.
gi 2069512976 1018 KEELIRLQNSYQPTNKGRYKV 1038
Cdd:cd22475     82 LEEATEKASRPGGQQPGRYSV 102
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
382-580 1.78e-37

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: 140.58  E-value: 1.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGE--GPIAVIMTPTRELALQ 459
Cdd:cd17948      1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfnAPRGLVITPSRELAEQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  460 ITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRmidMLAANNGRVTNLRRVTYVVLDEADRMFDMGFE 539
Cdd:cd17948     81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGA---LSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2069512976  540 PQVMRIV-------------DNVRPDRQTVMFSATFPRAMealaRRILSKPIEV 580
Cdd:cd17948    158 EKLSHFLrrfplasrrsentDGLDPGTQLVLVSATMPSGV----GEVLSKVIDV 207
KH-I_DDX46_like cd22387
type I K homology (KH) RNA-binding domain found in the family of DEAD box protein 46 (DDX46); ...
936-1017 1.25e-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: 132.79  E-value: 1.25e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  936 SFKRYEEELEINDFPQTARWKVTSKEALHRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITR 1015
Cdd:cd22387      1 NNGNFVEEFEINDYPQIARLKVTSKEVLNSIMEETGATITIKGQYYPPGKKPKPGERKLYLLIEGATEESVQSARNEIKR 80

                   ..
gi 2069512976 1016 LI 1017
Cdd:cd22387     81 VL 82
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
382-582 2.62e-36

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


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 136.32  E-value: 2.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdqrplEEGEGPIAVI-MTPTRELALQI 460
Cdd:cd17950     13 LLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL------EPVDGQVSVLvICHTRELAFQI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  461 TKECKKFSKTL-GVRVVCVYGGTGISEQIAELKRGA-EVIVCTPGRMIDMlaANNGRVtNLRRVTYVVLDEADRMF-DMG 537
Cdd:cd17950     87 SNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILAL--VREKKL-KLSHVKHFVLDECDKMLeQLD 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2069512976  538 FEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQV 582
Cdd:cd17950    164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
390-561 2.53e-35

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


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 133.60  E-value: 2.53e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  390 GYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrpleegegpiAVIMTPTRELALQITKECKKFSK 469
Cdd:cd17938     18 DWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------ALILEPSRELAEQTYNCIENFKK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  470 TL---GVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVtNLRRVTYVVLDEADRMFDMGFEPQVMRIV 546
Cdd:cd17938     86 YLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLI--KTGKL-DLSSVRFFVLDEADRLLSQGNLETINRIY 162
                          170       180
                   ....*....|....*....|.
gi 2069512976  547 D-----NVRPDR-QTVMFSAT 561
Cdd:cd17938    163 NripkiTSDGKRlQVIVCSAT 183
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
389-580 4.23e-34

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


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 129.87  E-value: 4.23e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  389 HGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFrhimdQRPLEEGEGPIAVIMTPTRELALQITKECKKFS 468
Cdd:cd18046     17 YGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISIL-----QQIDTSLKATQALVLAPTRELAQQIQKVVMALG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  469 KTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaanNGRVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDN 548
Cdd:cd18046     92 DYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI---NRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQK 168
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2069512976  549 VRPDRQTVMFSATFPRAMEALARRILSKPIEV 580
Cdd:cd18046    169 LPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
377-580 4.18e-33

DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 126.81  E-value: 4.18e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  377 GISMKILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImdQRPLEEgegPIAVIMTPTREL 456
Cdd:cd18045      5 GLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL--DIQVRE---TQALILSPTREL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  457 ALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGRVTNLRrvtYVVLDEADRMFDM 536
Cdd:cd18045     80 AVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIK---MLVLDEADEMLNK 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2069512976  537 GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEV 580
Cdd:cd18045    157 GFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
603-713 2.88e-30

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: 115.39  E-value: 2.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  603 NKFLKLLELLgHFQEKGSVIIFVDKQEHAD-GLLKDlmRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARG 681
Cdd:pfam00271    1 EKLEALLELL-KKERGGKVLIFSQTKKTLEaELLLE--KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2069512976  682 LDVKHLTLVINYSCPNHYEDYVHRAGRTGRAG 713
Cdd:pfam00271   78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
382-577 6.11e-30

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: 118.89  E-value: 6.11e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  382 ILNSLKKHGYEKPTPIQAQAIPAIMSG---------RDLIGIAKTGSGKTIAFLLPMFRhIMDQRPleegeGPI--AVIM 450
Cdd:cd17956      1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQ-ALSKRV-----VPRlrALIV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  451 TPTRELALQITKECKKFSKTLGVRVVCVYGGTGISEQIAELKRG--------AEVIVCTPGRMIDMLAANNGrvTNLRRV 522
Cdd:cd17956     75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPG--FTLKHL 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069512976  523 TYVVLDEADRMFDMGFE---PQVMRIVDNVRPDR-----------------QTVMFSATFPRAMEALARRILSKP 577
Cdd:cd17956    153 RFLVIDEADRLLNQSFQdwlETVMKALGRPTAPDlgsfgdanllersvrplQKLLFSATLTRDPEKLSSLKLHRP 227
HELICc smart00490
helicase superfamily c-terminal domain;
634-713 1.48e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 98.05  E-value: 1.48e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976   634 LLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAG 713
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
385-572 2.26e-24

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: 103.23  E-value: 2.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  385 SLKKHGYEKPTPIQAQAIPAI----MSGRDLIGI------------AKTGSGKTIAFLLPMFRHI--MDQRPLEEGEG-- 444
Cdd:cd17965     22 SNKTDEEIKPSPIQTLAIKKLlktlMRKVTKQTSneepklevfllaAETGSGKTLAYLAPLLDYLkrQEQEPFEEAEEey 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  445 --------PIAVIMTPTRELALQITKECKKFSKTLGVRVVCVYGGTGIS-EQIAEL-KRGAEVIVCTPGRmIDMLAANNG 514
Cdd:cd17965    102 esakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSyQRLQLAfKGRIDILVTTPGK-LASLAKSRP 180
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2069512976  515 RVtnLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARR 572
Cdd:cd17965    181 KI--LSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRK 236
KH-I_PRP5_like cd22474
type I K homology (KH) RNA-binding domain found in fungal pre-mRNA-processing ATP-dependent ...
944-1019 1.25e-21

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: 90.08  E-value: 1.25e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069512976  944 LEINDFPQTARWKVTSKEALHRISEYSEAAITIRGTYFPPGKEPKE--GERKIYLAIESANELAVQKAKAEITRLIKE 1019
Cdd:cd22474      9 VEINDLPQKARWEATNNTSLSKIIEETGCSITNKGNFYPPGKEPQPnnDEPKLYLLIEGTTEKAVRLAIELLRRKLVE 86
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
370-577 6.52e-21

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


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 92.78  E-value: 6.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  370 IKTWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAIMSG--RDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLeegegPIA 447
Cdd:cd18048     17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY-----PQC 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  448 VIMTPTRELALQITKECKKFSK-TLGVRVVCVYGGT--GISEQIAelkrgAEVIVCTPGRMIDMlaANNGRVTNLRRVTY 524
Cdd:cd18048     92 LCLSPTFELALQTGKVVEEMGKfCVGIQVIYAIRGNrpGKGTDIE-----AQIVIGTPGTVLDW--CFKLRLIDVTNISV 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2069512976  525 VVLDEADRMFDM-GFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKP 577
Cdd:cd18048    165 FVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
381-720 1.17e-20

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: 97.98  E-value: 1.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  381 KILNSLKKHGYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrpleEGEGPIAVIMTPTRELAL-Q 459
Cdd:COG1205     44 ELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL------EDPGATALYLYPTKALARdQ 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  460 ItKECKKFSKTLGVRV-VCVY-GGTGISEQiAELKRGAEVIVCTPgrmiDML----AANNGR-VTNLRRVTYVVLDEA-- 530
Cdd:COG1205    118 L-RRLRELAEALGLGVrVATYdGDTPPEER-RWIREHPDIVLTNP----DMLhyglLPHHTRwARFFRNLRYVVIDEAht 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  531 -------------DRMfdmgfepqvMRIVDNVRPDRQTVMFSATFPRAmEALARRILSKPIEVqV-------GGRSVV-- 588
Cdd:COG1205    192 yrgvfgshvanvlRRL---------RRICRHYGSDPQFILASATIGNP-AEHAERLTGRPVTV-VdedgsprGERTFVlw 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  589 -CSDVEQNVivieEENKFLKLLELLGHFQEKG-SVIIFVD------------KQEHADGLLKDLMRAsYpclslHGGIDQ 654
Cdd:COG1205    261 nPPLVDDGI----RRSALAEAARLLADLVREGlRTLVFTRsrrgaellaryaRRALREPDLADRVAA-Y-----RAGYLP 330
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069512976  655 YDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAGNKGYAYT 720
Cdd:COG1205    331 EERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
393-827 2.04e-19

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 93.55  E-value: 2.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  393 KPTPIQAQAIPAIMS-----GRDLIGIAKTGSGKTIAFLLPMFRHIMDQRpleegegpiAVIMTPTRELALQITKECKKF 467
Cdd:COG1061     80 ELRPYQQEALEALLAalergGGRGLVVAPTGTGKTVLALALAAELLRGKR---------VLVLVPRRELLEQWAEELRRF 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  468 sktlgVRVVCVYGGtgiseqiaELKRGAEVIVCTpgrmIDMLAANNGRVTNLRRVTYVVLDEADRMFDMGFEpqvmRIVD 547
Cdd:COG1061    151 -----LGDPLAGGG--------KKDSDAPITVAT----YQSLARRAHLDELGDRFGLVIIDEAHHAGAPSYR----RILE 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  548 NVRPDRqTVMFSATFPR-------------------AMEALARRILSKP--IEVQVGGRS-----VVCSDVEQNVIVIEE 601
Cdd:COG1061    210 AFPAAY-RLGLTATPFRsdgreillflfdgivyeysLKEAIEDGYLAPPeyYGIRVDLTDeraeyDALSERLREALAADA 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  602 ENKFLKLLELLGHFQEKGSVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARG 681
Cdd:COG1061    289 ERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEG 368
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  682 LDVKHLTLVINYScPNHYE-DYVHRAGRTGR-AGNKGYA--YTFITEDqvryagdiikalelsgtpvPPELEKLwtdFKD 757
Cdd:COG1061    369 VDVPRLDVAILLR-PTGSPrEFIQRLGRGLRpAPGKEDAlvYDFVGND-------------------VPVLEEL---AKD 425
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  758 QQKAEGKTIKKSSGFSGKGFKFDETEEALANERKKLQKAALGLQDSDDEDTAVDIDEQIESMFNSKKRVK 827
Cdd:COG1061    426 LRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALEL 495
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
380-719 2.59e-18

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 89.57  E-value: 2.59e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  380 MKILNSLKKHGYEKPTPIQAQAIPA-IMSGRDLIGIAKTGSGKT-IAFLLpMFRHIMdqrpleegEGPIAVIMTPTRELA 457
Cdd:COG1204      9 EKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTlIAELA-ILKALL--------NGGKALYIVPLRALA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  458 LQITKECKKFSKTLGVRVVCVYGgtGISEQIAELKRgAEVIVCTPGRMiDMLAANNGRVtnLRRVTYVVLDEA------D 531
Cdd:COG1204     80 SEKYREFKRDFEELGIKVGVSTG--DYDSDDEWLGR-YDILVATPEKL-DSLLRNGPSW--LRDVDLVVVDEAhliddeS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  532 RmfdmGFEPQVmrIVDNVR---PDRQTVMFSATFPRAmEALARRIlskpievqvgGRSVVCSD---VEQNVIVI------ 599
Cdd:COG1204    154 R----GPTLEV--LLARLRrlnPEAQIVALSATIGNA-EEIAEWL----------DAELVKSDwrpVPLNEGVLydgvlr 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  600 ------EEENKFLKLleLLGHFQEKGSVIIFV---------------------------DKQEHADGLL--KDLMRASYP 644
Cdd:COG1204    217 fddgsrRSKDPTLAL--ALDLLEEGGQVLVFVssrrdaeslakkladelkrrltpeereELEELAEELLevSEETHTNEK 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  645 ---CLSL-----HGGIDQYDRDSIINDFKSGVCKLLVATSVAARG--LDVKhlTLVI-NYSCPNHYE----DYVHRAGRT 709
Cdd:COG1204    295 ladCLEKgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGvnLPAR--RVIIrDTKRGGMVPipvlEFKQMAGRA 372
                          410
                   ....*....|..
gi 2069512976  710 GRAG--NKGYAY 719
Cdd:COG1204    373 GRPGydPYGEAI 384
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
395-573 7.29e-17

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 79.61  E-value: 7.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  395 TPIQAQAIPAIM-SGRDLIGIAKTGSGKTIAFLLPMFRHIMDQrpleegeGPIAVIMTPTRELALQITKECKKFSKTLGV 473
Cdd:cd17921      3 NPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATS-------GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  474 RVVCVYGGTGISeqiAELKRGAEVIVCTPGRMIDMLaaNNGRVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVR--- 550
Cdd:cd17921     76 NVGLLTGDPSVN---KLLLAEADILVATPEKLDLLL--RNGGERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrin 150
                          170       180
                   ....*....|....*....|...
gi 2069512976  551 PDRQTVMFSATFPRAMEaLARRI 573
Cdd:cd17921    151 KNARFVGLSATLPNAED-LAEWL 172
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
408-561 8.67e-17

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 78.21  E-value: 8.67e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  408 GRDLIGIAKTGSGKTIAFLLPMFRHIMDQrpleegeGPIAVIMTPTRELALQITKECKKFSKtLGVRVVCVYGGTGISEQ 487
Cdd:cd00046      1 GENVLITAPTGSGKTLAALLAALLLLLKK-------GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEER 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069512976  488 IAELKRGAEVIVCTPGrMIDMLAANNGRVTnLRRVTYVVLDEADRMFDMGFEPQVMRIVDN--VRPDRQTVMFSAT 561
Cdd:cd00046     73 EKNKLGDADIIIATPD-MLLNLLLREDRLF-LKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
371-577 1.27e-15

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 76.68  E-value: 1.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  371 KTWVQCGISMKILNSLKKHGYEKPTPIQAQAIPAIMSG--RDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEgegpiAV 448
Cdd:cd18047      1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ-----CL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  449 IMTPTRELALQITKECKKFSKtLGVRVVCVYGGTGiseqiAELKRGA----EVIVCTPGRMIDMLAanNGRVTNLRRVTY 524
Cdd:cd18047     76 CLSPTYELALQTGKVIEQMGK-FYPELKLAYAVRG-----NKLERGQkiseQIVIGTPGTVLDWCS--KLKFIDPKKIKV 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2069512976  525 VVLDEADRMF-DMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKP 577
Cdd:cd18047    148 FVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
398-573 1.10e-12

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


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 67.61  E-value: 1.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  398 QAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRpleegeGPIAVIMTPTRELALQITKECKKF--SKTLGVRV 475
Cdd:cd17923      5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELleQLGLGIRV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  476 VCVYGGTGISEQIAELKRGAEVIVCTPgrmiDMLAA-----NNGRVTNLRRVTYVVLDEAdRMFDMGFEPQV-------M 543
Cdd:cd17923     79 ATYDGDTPREERRAIIRNPPRILLTNP----DMLHYallphHDRWARFLRNLRYVVLDEA-HTYRGVFGSHValllrrlR 153
                          170       180       190
                   ....*....|....*....|....*....|
gi 2069512976  544 RIVDNVRPDRQTVMFSATFpRAMEALARRI 573
Cdd:cd17923    154 RLCRRYGADPQFILTSATI-GNPAEHARTL 182
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
604-718 1.12e-10

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: 60.68  E-value: 1.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  604 KFLKLLELLGHFQEKG---SVIIFVdKQEHADGLLKDLM------RASYPCLSL--HGGIDQYDRD--------SIINDF 664
Cdd:cd18802      8 KLQKLIEILREYFPKTpdfRGIIFV-ERRATAVVLSRLLkehpstLAFIRCGFLigRGNSSQRKRSlmtqrkqkETLDKF 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2069512976  665 KSGVCKLLVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRtGRAGNKGYA 718
Cdd:cd18802     87 RDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNSKYI 139
KH-I_KHDC4_rpt1 cd22385
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
940-1017 6.89e-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: 56.45  E-value: 6.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  940 YEEELEINDFPQTARWKVTSKEALHRISEYSEAAITIRGTYFPPG--KEPKEGERKIYLAIESANELAVQKAKAEITRLI 1017
Cdd:cd22385      5 YVAEIEINDLPNTCRNLLTKGSTQEEIQKESGAAVSTRGRYMPPEekATFNPGERPLYLHVQAPTKEAVDRAVNKINEII 84
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
386-574 1.92e-09

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: 58.31  E-value: 1.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  386 LKKH-GYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFrhimdqrpLEEGegpIAVIMTPTreLAL---QIT 461
Cdd:cd17920      4 LKEVfGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL--------LLDG---VTLVVSPL--ISLmqdQVD 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  462 KeCkkfsKTLGVRVVCVYGGTGISEQ---IAELKRG-AEVIVCTP-----GRMIDMLAanngRVTNLRRVTYVVLDEA-- 530
Cdd:cd17920     71 R-L----QQLGIRAAALNSTLSPEEKrevLLRIKNGqYKLLYVTPerllsPDFLELLQ----RLPERKRLALIVVDEAhc 141
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2069512976  531 ------DrmfdmgFEPQVMRI--VDNVRPDRQTVMFSATFPRAMEALARRIL 574
Cdd:cd17920    142 vsqwghD------FRPDYLRLgrLRRALPGVPILALTATATPEVREDILKRL 187
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
381-721 2.21e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 60.92  E-value: 2.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  381 KILNSLKKH-GYEKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLP--MFrhimdqrpleegEGPiAVIMTPTreLA 457
Cdd:COG0514      4 DALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLL------------PGL-TLVVSPL--IA 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  458 L---QItkeckKFSKTLGVRVVCVYGGTGISEQ---IAELKRGA-EVIVCTP-----GRMIDMLAAnngrvtnlRRVTYV 525
Cdd:COG0514     69 LmkdQV-----DALRAAGIRAAFLNSSLSAEERrevLRALRAGElKLLYVAPerllnPRFLELLRR--------LKISLF 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  526 VLDEA--------DrmfdmgFEPQVMRIVDNVR--PDRQTVMFSATF-PRAMEALARRI-LSKPiEVQVGG--Rsvvcsd 591
Cdd:COG0514    136 AIDEAhcisqwghD------FRPDYRRLGELRErlPNVPVLALTATAtPRVRADIAEQLgLEDP-RVFVGSfdR------ 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  592 veQN----VIVIEEENKFLKLLELLGHfQEKGSVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSG 667
Cdd:COG0514    203 --PNlrleVVPKPPDDKLAQLLDFLKE-HPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRD 279
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2069512976  668 VCKLLVATSvaARGL-----DVKhltLVINYSCPNHYEDYVHRAGRTGRAGNKGYAYTF 721
Cdd:COG0514    280 EVDVIVATI--AFGMgidkpDVR---FVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
604-831 6.23e-09

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 60.13  E-value: 6.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  604 KFLKLLELLGHFQEK---GSVIIFVDKQEHADGLLKDLMRASYPCLSLHG--------GIDQYDRDSIINDFKSGVCKLL 672
Cdd:COG1111    336 KLSKLREILKEQLGTnpdSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVL 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  673 VATSVAARGLDVKHLTLVINyscpnhYED------YVHRAGRTGRaGNKGYAYTFITEDQ----VRYAG--------DII 734
Cdd:COG1111    416 VATSVAEEGLDIPEVDLVIF------YEPvpseirSIQRKGRTGR-KREGRVVVLIAKGTrdeaYYWSSrrkekkmkSIL 488
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  735 KAL-----ELSGTPVPPELEKLWTDFKDQQKAEGKTIKKSSGFSGKGFKFDETEEALANERKKLQKAALGLQDSDDEDTA 809
Cdd:COG1111    489 KKLkklldKQEKEKLKESAQATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVIVSTLAESLELRELGE 568
                          250       260
                   ....*....|....*....|..
gi 2069512976  810 VDIDEQIESMFNSKKRVKDMAS 831
Cdd:COG1111    569 KVDDEVNLILEIDRVDVVDDGS 590
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
601-721 8.77e-09

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: 54.91  E-value: 8.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  601 EENKFLKLLELLGHFQEkGSVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAAR 680
Cdd:cd18794     14 KDEKLDLLKRIKVEHLG-GSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGM 92
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2069512976  681 GLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAGNKGYAYTF 721
Cdd:cd18794     93 GIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
KH-I_RIK_like_rpt1 cd22471
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and ...
943-1017 1.17e-08

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


Pssm-ID: 411899  Cd Length: 91  Bit Score: 53.24  E-value: 1.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  943 ELEINDFPQTARWKVTSKEALHRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANEL---------AVQKAKAEI 1013
Cdd:cd22471      8 EIVINDAPPSVRHHLTKRSTQDEIQSKTGVVVVTRGRYYPPGTPPPDNEKPLYLHITAGAQLppddaerqkAVDAAAADI 87

                   ....
gi 2069512976 1014 TRLI 1017
Cdd:cd22471     88 QAML 91
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
670-723 1.19e-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: 52.71  E-value: 1.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2069512976  670 KLLVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAGNKGYAYTFIT 723
Cdd:cd18785     24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
397-571 2.35e-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: 55.44  E-value: 2.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  397 IQAQAIPAIM-SGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRPLEEGEgPIAVIMTPTRELALQITKECK-KFSKtLGVR 474
Cdd:cd18023      5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDWKeKFGP-LGLS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  475 VVCVYGGTGI--SEQIaelkRGAEVIVCTPGRMIDM--LAANNGRVtnLRRVTYVVLDE---------------ADRMFD 535
Cdd:cd18023     83 CAELTGDTEMddTFEI----QDADIILTTPEKWDSMtrRWRDNGNL--VQLVALVLIDEvhiikenrgatlevvVSRMKT 156
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2069512976  536 MGFEPQVMR-IVDNVRpdrqTVMFSATFPRAmEALAR 571
Cdd:cd18023    157 LSSSSELRGsTVRPMR----FVAVSATIPNI-EDLAE 188
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
604-693 2.98e-08

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: 53.25  E-value: 2.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  604 KFLKLLELLGHFQEKGS-VIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFK--SGVCKLLVATSVAAR 680
Cdd:cd18793     12 KLEALLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGV 91
                           90
                   ....*....|...
gi 2069512976  681 GLDVKHLTLVINY 693
Cdd:cd18793     92 GLNLTAANRVILY 104
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
408-529 3.67e-08

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: 54.13  E-value: 3.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  408 GRDLIGIAKTGSGKTIAFLLPMFRHIMDqrpleEGEGPIAVI-MTPTRELALQITKECKKFSK--TLGVRVVCVYGGTGI 484
Cdd:cd17922      1 GRNVLIAAPTGSGKTEAAFLPALSSLAD-----EPEKGVQVLyISPLKALINDQERRLEEPLDeiDLEIPVAVRHGDTSQ 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2069512976  485 SEQIAELKRGAEVIVCTPGRMIDMLAANNGRVTnLRRVTYVVLDE 529
Cdd:cd17922     76 SEKAKQLKNPPGILITTPESLELLLVNKKLREL-FAGLRYVVVDE 119
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
393-529 4.98e-08

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


Pssm-ID: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 54.40  E-value: 4.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  393 KPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHImDQRPlEEGEGPIAVIMTPTRELALQ-ITKECKKFSKtl 471
Cdd:cd18036      2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHL-EKRR-SAGEKGRVVVLVNKVPLVEQqLEKFFKYFRK-- 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069512976  472 GVRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVTNLRRV---TYVVLDE 529
Cdd:cd18036     78 GYKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNL--LSGREEERVYLsdfSLLIFDE 136
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
393-532 5.28e-08

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: 54.36  E-value: 5.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  393 KPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHiMDQRPleEGEGPIAVIMTPTRELALQITKECKKFSKTLG 472
Cdd:cd17927      2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHH-LKKFP--AGRKGKVVFLANKVPLVEQQKEVFRKHFERPG 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  473 VRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVTNLRRVTYVVLDEADR 532
Cdd:cd17927     79 YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDL--KSGTIVSLSDFSLLVFDECHN 136
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
396-684 5.57e-08

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: 56.63  E-value: 5.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  396 PIQAQAIPAIMSGRDLIG-----IAKTGSGKTIAFLLPMFRHimdqrpLEEGEGPIAVIMTPTRELALQITKECKKFskt 470
Cdd:COG1203    130 PLQNEALELALEAAEEEPglfilTAPTGGGKTEAALLFALRL------AAKHGGRRIIYALPFTSIINQTYDRLRDL--- 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  471 LGVRVVCVYGGTGISEQIAE------------LKRG--AEVIVCTPGRMIDMLAANNG----RVTNLRRvTYVVLDEADr 532
Cdd:COG1203    201 FGEDVLLHHSLADLDLLEEEeeyesearwlklLKELwdAPVVVTTIDQLFESLFSNRKgqerRLHNLAN-SVIILDEVQ- 278
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  533 MFDMGFEPQVMRIVDNVRPDRQTVMF-SATFPrameALARRILSKPIEVqVGGRSVVCSDVEQN-----VIVIEEENKFL 606
Cdd:COG1203    279 AYPPYMLALLLRLLEWLKNLGGSVILmTATLP----PLLREELLEAYEL-IPDEPEELPEYFRAfvrkrVELKEGPLSDE 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  607 KLLE-LLGHFQEKGSVIIFVDKQEHADGL---LKDLMRASYPCLsLHGGIDQYDR----DSIINDFKSGVCKLLVATSVA 678
Cdd:COG1203    354 ELAElILEALHKGKSVLVIVNTVKDAQELyeaLKEKLPDEEVYL-LHSRFCPADRseieKEIKERLERGKPCILVSTQVV 432

                   ....*.
gi 2069512976  679 ARGLDV 684
Cdd:COG1203    433 EAGVDI 438
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
396-567 1.14e-07

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: 52.72  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  396 PIQAQAIPA-IMSGRDLIGIAKTGSGKTIAFLLPMFRHIMdqrpleegEGPIAVIMTPTRELALQITKECKKFSKtLGVR 474
Cdd:cd18028      4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLL--------EGGKALYLVPLRALASEKYEEFKKLEE-IGLK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  475 VVCvygGTGISEQIAELKRGAEVIVCTPGRmIDMLAANngRVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVR---P 551
Cdd:cd18028     75 VGI---STGDYDEDDEWLGDYDIIVATYEK-FDSLLRH--SPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnP 148
                          170
                   ....*....|....*.
gi 2069512976  552 DRQTVMFSATFPRAME 567
Cdd:cd18028    149 NTQIIGLSATIGNPDE 164
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
391-529 8.78e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 53.18  E-value: 8.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  391 YEKPTPIQAQAIPAIMSGRD-LIgIAKTGSGKTIAFLLPMFRHIMDQRPLEEGEGPIAVI----------------MTPT 453
Cdd:COG1201     22 FGAPTPPQREAWPAIAAGEStLL-IAPTGSGKTLAAFLPALDELARRPRPGELPDGLRVLyisplkalandiernlRAPL 100
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069512976  454 RELALQITKECKKFskTLGVRVvcvyGGTGISEQIAELKRGAEVIVCTPGRMIDMLAANNGRvTNLRRVTYVVLDE 529
Cdd:COG1201    101 EEIGEAAGLPLPEI--RVGVRT----GDTPASERQRQRRRPPHILITTPESLALLLTSPDAR-ELLRGVRTVIVDE 169
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
409-530 3.41e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 48.80  E-value: 3.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  409 RDLIGIAKTGSGKT-IAFLLpMFRHIMDQRPLEEGeGPIAVIMTPTRELALQitkECKKFSKTLGVRVVCVYGGTGISEQ 487
Cdd:cd18034     17 RNTIVVLPTGSGKTlIAVML-IKEMGELNRKEKNP-KKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEMGVDKW 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2069512976  488 IA----ELKRGAEVIVCTPGRMIDMLaaNNGRVTnLRRVTYVVLDEA 530
Cdd:cd18034     92 TKerwkEELEKYDVLVMTAQILLDAL--RHGFLS-LSDINLLIFDEC 135
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
604-725 6.91e-06

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 50.22  E-value: 6.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  604 KFLKLLELLGHFQEKG-SVIIFVDKQEHADGLLKDLMRASYPCLSLHGGIDQYDRDSIINDFKSG--VCKLLVATSVAAR 680
Cdd:COG0553    534 KLEALLELLEELLAEGeKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGE 613
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2069512976  681 GLDvkhLT---LVINYSC---PNHYE---DYVHRAGRTgragNKGYAYTFITED 725
Cdd:COG0553    614 GLN---LTaadHVIHYDLwwnPAVEEqaiDRAHRIGQT----RDVQVYKLVAEG 660
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
604-719 1.05e-05

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: 46.19  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  604 KFLKLLELL-GHFQEKGS-----VIIFVDKQEHADGLLKDLMRaSYPCLSLH-----------GGIDQYDRDSIINDFKS 666
Cdd:cd18801     10 KLEKLEEIVkEHFKKKQEgsdtrVIIFSEFRDSAEEIVNFLSK-IRPGIRATrfigqasgkssKGMSQKEQKEVIEQFRK 88
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2069512976  667 GVCKLLVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRaGNKGYAY 719
Cdd:cd18801     89 GGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
393-570 2.51e-05

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 45.87  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  393 KPTPIQAQAIPAIMSG------RDLIGIAKTGSGKTIAFLLPMFrhimdqrpLEEGEGPIAVIMTPTRELALQITKECKK 466
Cdd:cd17918     15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAAL--------LAYKNGKQVAILVPTEILAHQHYEEARK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  467 FSKTlgVRVVCVYGGTgiSEQIAElkrGAEVIVCTpgrmidmlAANNGRVTNLRRVTYVVLDEADRmfdMGFEpQVMRIV 546
Cdd:cd17918     87 FLPF--INVELVTGGT--KAQILS---GISLLVGT--------HALLHLDVKFKNLDLVIVDEQHR---FGVA-QREALY 147
                          170       180
                   ....*....|....*....|....*
gi 2069512976  547 DNVRPDrqTVMFSAT-FPRAMeALA 570
Cdd:cd17918    148 NLGATH--FLEATATpIPRTL-ALA 169
PRK13766 PRK13766
Hef nuclease; Provisional
599-725 2.52e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 48.33  E-value: 2.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  599 IEEEN-KFLKLLELL-GHFQEKGS--VIIFVDKQEHADGLLKDLMRASYPCLSLHGgidQYDRDS-----------IIND 663
Cdd:PRK13766   342 LDIEHpKLEKLREIVkEQLGKNPDsrIIVFTQYRDTAEKIVDLLEKEGIKAVRFVG---QASKDGdkgmsqkeqieILDK 418
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069512976  664 FKSGVCKLLVATSVAARGLDVKHLTLVInyscpnHYED------YVHRAGRTGRaGNKGYAYTFITED 725
Cdd:PRK13766   419 FRAGEFNVLVSTSVAEEGLDIPSVDLVI------FYEPvpseirSIQRKGRTGR-QEEGRVVVLIAKG 479
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
390-563 3.24e-05

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: 46.21  E-value: 3.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  390 GYEKPTPIQAQAIP-AIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRpLEEGEGPIA----VIMTPTRELALQITKEC 464
Cdd:cd18019     14 GFKSLNRIQSKLFPaAFETDENLLLCAPTGAGKTNVALLTILREIGKHR-NPDGTINLDafkiVYIAPMKALVQEMVGNF 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  465 KKFSKTLGVRVVCVYGGTGIS-EQIAElkrgAEVIVCTPGRMiDMLAANNGRVTNLRRVTYVVLDEADRMFD-MG--FEP 540
Cdd:cd18019     93 SKRLAPYGITVAELTGDQQLTkEQISE----TQIIVTTPEKW-DIITRKSGDRTYTQLVRLIIIDEIHLLHDdRGpvLES 167
                          170       180
                   ....*....|....*....|....*.
gi 2069512976  541 QVMRIVDNVRPDRQTVM---FSATFP 563
Cdd:cd18019    168 IVARTIRQIEQTQEYVRlvgLSATLP 193
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
396-530 5.50e-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: 45.33  E-value: 5.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  396 PIQAQAIPAIMSGRD--LIGiAKTGSGKTIAFLLPMFRHimdqrpLEEGEGPIAVIMTPTRELALQITKE-CKKFSKTLG 472
Cdd:cd18021      6 PIQTQVFNSLYNTDDnvFVG-APTGSGKTVCAELALLRH------WRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLG 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  473 VRVVCVYGgtgisEQIAELK--RGAEVIVCTPGRMiDMLAANNGRVTNLRRVTYVVLDEA 530
Cdd:cd18021     79 KKVVKLTG-----ETSTDLKllAKSDVILATPEQW-DVLSRRWKQRKNVQSVELFIADEL 132
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
610-714 1.93e-04

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: 42.64  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  610 ELLGHFQEKGSVIIFVDKQEHADGL---LKDLMRASYPCLSL---HGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLD 683
Cdd:cd18796     30 EVIFLLERHKSTLVFTNTRSQAERLaqrLRELCPDRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVVATSSLELGID 109
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2069512976  684 VKHLTLVINYSCPNHYEDYVHRAGRTGRAGN 714
Cdd:cd18796    110 IGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
635-691 5.24e-04

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: 41.56  E-value: 5.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2069512976  635 LKDLMRASYPCLSLHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVI 691
Cdd:cd18811     54 LKERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMV 110
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
396-551 7.92e-04

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


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 41.86  E-value: 7.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  396 PIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFrhIMDQRpleegEGPIAVIMTPTreLAL---QITKeckkfsktL- 471
Cdd:cd18018     15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL--LLRRR-----GPGLTLVVSPL--IALmkdQVDA--------Lp 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  472 -GVRVVCVYGGTGISEQIAELK--RGAEV--IVCTPGRMidmlaANNGRVTNLR---RVTYVVLDEADRMFDMG--FEPQ 541
Cdd:cd18018     78 rAIKAAALNSSLTREERRRILEklRAGEVkiLYVSPERL-----VNESFRELLRqtpPISLLVVDEAHCISEWShnFRPD 152
                          170
                   ....*....|
gi 2069512976  542 VMRIVDNVRP 551
Cdd:cd18018    153 YLRLCRVLRE 162
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
593-716 1.04e-03

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 40.70  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  593 EQNVIVIEEENKFLKLLELLGHFQEKGSVIIFVDKQEHADGLLKDLMRASypclsLHGGIDQYDRDSIINDFKSGVCKLL 672
Cdd:cd18789     24 KRRLLAAMNPNKLRALEELLKRHEQGDKIIVFTDNVEALYRYAKRLLKPF-----ITGETPQSEREEILQNFREGEYNTL 98
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2069512976  673 VATSVAARGLDVKHLTLVINYScpNHY---EDYVHRAGRTGRAGNKG 716
Cdd:cd18789     99 VVSKVGDEGIDLPEANVAIQIS--GHGgsrRQEAQRLGRILRPKKGG 143
PRK00254 PRK00254
ski2-like helicase; Provisional
378-480 1.12e-03

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 42.88  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  378 ISMKILNSLKKHGYEKPTPIQAQAIPA-IMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDqrpleegEGPIAVIMTPTREL 456
Cdd:PRK00254     8 VDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR-------EGGKAVYLVPLKAL 80
                           90       100
                   ....*....|....*....|....
gi 2069512976  457 ALQITKECKKFSKtLGVRVVCVYG 480
Cdd:PRK00254    81 AEEKYREFKDWEK-LGLRVAMTTG 103
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
396-529 1.16e-03

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: 41.21  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  396 PIQAQAIPAIMSGRD--LIGiAKTGSGKTIAFLLPMFRhIMDQRPleegeGPIAVIMTPTRELALQITKECKK-FSKTLG 472
Cdd:cd18022      4 PIQTQVFHTLYHTDNnvLLG-APTGSGKTIAAELAMFR-AFNKYP-----GSKVVYIAPLKALVRERVDDWKKrFEEKLG 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2069512976  473 VRVVCVYGGTgiSEQIAELkRGAEVIVCTPGRMiDMLAANNGRVTNLRRVTYVVLDE 529
Cdd:cd18022     77 KKVVELTGDV--TPDMKAL-ADADIIITTPEKW-DGISRSWQTREYVQQVSLIIIDE 129
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
650-718 1.80e-03

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: 39.93  E-value: 1.80e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069512976  650 GGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVINYSCPNHYEDYVHRAGRTGRAGNKGYA 718
Cdd:cd18797     74 AGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLV 142
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
393-529 1.93e-03

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


Pssm-ID: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 40.57  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  393 KPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLpMFRHIMDQRPlEEGEGPIAVIMTPTRELALQITKECKKFSKtLG 472
Cdd:cd18073      2 KPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLL-ICEHHLKKFP-QGQKGKVVFFATKVPVYEQQKSVFSKYFER-HG 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2069512976  473 VRVVCVYGGTGISEQIAELKRGAEVIVCTPGRMIDMLaaNNGRVTNLRRVTYVVLDE 529
Cdd:cd18073     79 YRVTGISGATAENVPVEQIIENNDIIILTPQILVNNL--KKGTIPSLSIFTLMIFDE 133
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
392-428 2.71e-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: 2.71e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2069512976  392 EKPTPIQAQAIPAIMSGRDLIGIAKTGSGKTIAFLLP 428
Cdd:cd18015     17 EKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLP 53
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
635-738 2.73e-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: 39.63  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  635 LKDLMRASYPCLS---LHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHL-TLVINYSCPNHYEDYVHRAGRTG 710
Cdd:cd18810     41 LATQLRQLVPEARiaiAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNAnTIIIERADKFGLAQLYQLRGRVG 120
                           90       100
                   ....*....|....*....|....*...
gi 2069512976  711 RAGNKGYAYtFITEDQVRYAGDIIKALE 738
Cdd:cd18810    121 RSKERAYAY-FLYPDQKKLTEDALKRLE 147
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
648-738 5.65e-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: 38.79  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069512976  648 LHGGIDQYDRDSIINDFKSGVCKLLVATSVAARGLDVKHLTLVInyscpnhyedyVHRA------------GRTGRAGNK 715
Cdd:cd18792     66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMI-----------IEDAdrfglsqlhqlrGRVGRGKHQ 134
                           90       100
                   ....*....|....*....|...
gi 2069512976  716 GYAYtFITEDQVRYAGDIIKALE 738
Cdd:cd18792    135 SYCY-LLYPDPKKLTETAKKRLR 156
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH