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Conserved domains on  [gi|15231748|ref|NP_190879|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13028937)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 98-301 2.09e-111

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: 328.00  E-value: 2.09e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  98 LSPELMKGLYVeMKFEKPSKIQAISLPMIMTPPHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTRELANQ 177
Cdd:cd17963   1 LKPELLKGLYA-MGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 178 NMEVLQKMGKFTGITAELAVPDSTRgapaaTRGAPVSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATDGFR 257
Cdd:cd17963  80 IGEVVEKMGKFTGVKVALAVPGNDV-----PRGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTQGHG 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15231748 258 DDSLKIMKDIGRvnpNFQVLLFSATFNETVKDFVARTVKDPNQL 301
Cdd:cd17963 155 DQSIRIKRMLPR---NCQILLFSATFPDSVRKFAEKIAPNANTI 195
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 313-451 6.98e-47

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 158.82  E-value: 6.98e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 313 VKQYKVVCPKEQnKIEVIKDQIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQ 392
Cdd:cd18787   1 IKQLYVVVEEEE-KKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15231748 393 VLIATDVIARGFDQQRVNLVVNYNLPTkyetgepDYEVYLHRVGRAGRFGRKGAVFNLL 451
Cdd:cd18787  80 VLVATDVAARGLDIPGVDHVINYDLPR-------DAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 98-301 2.09e-111

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: 328.00  E-value: 2.09e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  98 LSPELMKGLYVeMKFEKPSKIQAISLPMIMTPPHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTRELANQ 177
Cdd:cd17963   1 LKPELLKGLYA-MGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 178 NMEVLQKMGKFTGITAELAVPDSTRgapaaTRGAPVSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATDGFR 257
Cdd:cd17963  80 IGEVVEKMGKFTGVKVALAVPGNDV-----PRGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTQGHG 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15231748 258 DDSLKIMKDIGRvnpNFQVLLFSATFNETVKDFVARTVKDPNQL 301
Cdd:cd17963 155 DQSIRIKRMLPR---NCQILLFSATFPDSVRKFAEKIAPNANTI 195
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
92-490 5.95e-107

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 324.79  E-value: 5.95e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  92 RFEDLNLSPELMKGLyVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVDPTL-REPQALCICP 170
Cdd:COG0513   3 SFADLGLSPPLLKAL-AELGYTTPTPIQAQAIPLILA--GRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 171 TRELANQNMEVLQKMGKFTGITAELAVPdstrGAP------AATRGApvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVF 244
Cdd:COG0513  80 TRELALQVAEELRKLAKYLGLRVATVYG----GVSigrqirALKRGV----DIVVATPGRLLDLIERGALDLSGVETLVL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 245 DEADHMLatD-GFRDDSLKIMKdigRVNPNFQVLLFSATFNETVKDFVARTVKDPNQLFVKREDLALDSVKQYKVVCPKE 323
Cdd:COG0513 152 DEADRML--DmGFIEDIERILK---LLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 324 QnKIEVIKDqIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARG 403
Cdd:COG0513 227 D-KLELLRR-LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARG 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 404 FDQQRVNLVVNYNLPTkyetgepDYEVYLHRVGRAGRFGRKGAVFNLLLDDgwDKEVMEKIEKYFEANVKEIKSWNSEEE 483
Cdd:COG0513 305 IDIDDVSHVINYDLPE-------DPEDYVHRIGRTGRAGAEGTAISLVTPD--ERRLLRAIEKLIGQKIEEEELPGFEPV 375


                ....*..
gi 15231748 484 YKSALKE 490
Cdd:COG0513 376 EEKRLER 382
PTZ00424 PTZ00424
helicase 45; Provisional
 69-475 1.14e-81

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 258.99  E-value: 1.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   69 LEEPEDSNIKAVTSGDTPYTS-----ASRFEDLNLSPELMKGLYvEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSG 143
Cdd:PTZ00424   1 MATSEQKNQSEQVASTGTIESnydeiVDSFDALKLNEDLLRGIY-SYGFEKPSAIQQRGIKPILD--GYDTIGQAQSGTG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  144 KTTCFVLGMLSRVDPTLREPQALCICPTRELANQNMEVLQKMGKFTGITAELAVPDSTRGAPAATRGAPVsaHVVIGTPG 223
Cdd:PTZ00424  78 KTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGV--HMVVGTPG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  224 TLKKWMAFKRLGLNHLKILVFDEADHMLATdGFRDDSLKIMKdigRVNPNFQVLLFSATFNETVKDFVARTVKDPNQLFV 303
Cdd:PTZ00424 156 RVYDMIDKRHLRVDDLKLFILDEADEMLSR-GFKGQIYDVFK---KLPPDVQVALFSATMPNEILELTTKFMRDPKRILV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  304 KREDLALDSVKQYKVVCPKEQNKIEVIKDqIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIV 383
Cdd:PTZ00424 232 KKDELTLEGIRQFYVAVEKEEWKFDTLCD-LYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIM 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  384 KEFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPTKYETgepdyevYLHRVGRAGRFGRKGAVFNLLLDDgwDKEVMEK 463
Cdd:PTZ00424 311 REFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN-------YIHRIGRSGRFGRKGVAINFVTPD--DIEQLKE 381

                        410
                 ....*....|..
gi 15231748  464 IEKYFEANVKEI 475
Cdd:PTZ00424 382 IERHYNTQIEEM 393
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 313-451 6.98e-47

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 158.82  E-value: 6.98e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 313 VKQYKVVCPKEQnKIEVIKDQIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQ 392
Cdd:cd18787   1 IKQLYVVVEEEE-KKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15231748 393 VLIATDVIARGFDQQRVNLVVNYNLPTkyetgepDYEVYLHRVGRAGRFGRKGAVFNLL 451
Cdd:cd18787  80 VLVATDVAARGLDIPGVDHVINYDLPR-------DAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 116-290 2.04e-44

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: 153.55  E-value: 2.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   116 SKIQAISLPMIMTPphKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTRELANQNMEVLQKMGKFTGITAEL 195
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   196 AVPDSTRGapaATRGAPVSAHVVIGTPGTLKKWMAFKRLgLNHLKILVFDEADHMLaTDGFRDDSLKImkdIGRVNPNFQ 275
Cdd:pfam00270  79 LLGGDSRK---EQLEKLKGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLL-DMGFGPDLEEI---LRRLPKKRQ 150

                         170
                  ....*....|....*
gi 15231748   276 VLLFSATFNETVKDF 290
Cdd:pfam00270 151 ILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
109-316 2.29e-36

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 133.39  E-value: 2.29e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748    109 EMKFEKPSKIQAISLPMIMTPpHKHLIAQAHNGSGKTTCFVLGMLSRVDPTlREPQALCICPTRELANQNMEVLQKMGKF 188
Cdd:smart00487   3 KFGFEPLRPYQKEAIEALLSG-LRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748    189 TGITAELAVPDSTRGAPAA--TRGAPvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLAtDGFRDDSLKIMKd 266
Cdd:smart00487  81 LGLKVVGLYGGDSKREQLRklESGKT---DILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLK- 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 15231748    267 igRVNPNFQVLLFSATFNETVKDFVARTVKDPnqLFVKREDLALDSVKQY 316
Cdd:smart00487 156 --LLPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 325-442 8.65e-28

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 106.91  E-value: 8.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   325 NKIEVIKDqIMELGDIGQTIIFVKTKASAqKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGF 404
Cdd:pfam00271   1 EKLEALLE-LLKKERGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15231748   405 DQQRVNLVVNYNLPTkyetgepDYEVYLHRVGRAGRFG 442
Cdd:pfam00271  79 DLPDVDLVINYDLPW-------NPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
354-442 1.22e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 1.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748    354 QKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPtkyetgePDYEVYLH 433
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-------WSPASYIQ 73


                   ....*....
gi 15231748    434 RVGRAGRFG 442
Cdd:smart00490  74 RIGRAGRAG 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
236-440 2.84e-10

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 62.47  E-value: 2.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 236 LNHLKI--LVFDEAdHMLATDG--FRDDSLKIMKDIGRVnPNFQVLLFSATFNETVKDFVART--VKDPNQL---FVkRE 306
Cdd:COG0514 127 LRRLKIslFAIDEA-HCISQWGhdFRPDYRRLGELRERL-PNVPVLALTATATPRVRADIAEQlgLEDPRVFvgsFD-RP 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 307 DLaldsvkQYKVVCPKEQNKIEVIKDQIMELGDiGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEF 386
Cdd:COG0514 204 NL------RLEVVPKPPDDKLAQLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRF 276

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15231748 387 KECLTQVLIATdvIA--RGFDQQRVNLVVNYNLPtkyetgePDYEVYLHRVGRAGR 440
Cdd:COG0514 277 LRDEVDVIVAT--IAfgMGIDKPDVRFVIHYDLP-------KSIEAYYQEIGRAGR 323
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 236-444 2.92e-06

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 50.28  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   236 LNHLKIL---------VFDEAdHMLATDG--FRDD--SLKIMKdigRVNPNFQVLLFSATFNETVKDFVARTVKDPN--- 299
Cdd:PLN03137  570 LRHLENLnsrgllarfVIDEA-HCVSQWGhdFRPDyqGLGILK---QKFPNIPVLALTATATASVKEDVVQALGLVNcvv 645

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   300 --QLFvKREDLaldsvkQYKVVcPKEQNKIEVIKDQIME--LGDIGqtIIFVKTKASAQKVHKALAEMGYDVTSVHGNLT 375
Cdd:PLN03137  646 frQSF-NRPNL------WYSVV-PKTKKCLEDIDKFIKEnhFDECG--IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMD 715

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231748   376 ESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPTKYETgepdyevYLHRVGRAGRFGRK 444
Cdd:PLN03137  716 PAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG-------YHQECGRAGRDGQR 777
 
Name Accession Description Interval E-value
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 98-301 2.09e-111

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: 328.00  E-value: 2.09e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  98 LSPELMKGLYVeMKFEKPSKIQAISLPMIMTPPHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTRELANQ 177
Cdd:cd17963   1 LKPELLKGLYA-MGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 178 NMEVLQKMGKFTGITAELAVPDSTRgapaaTRGAPVSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATDGFR 257
Cdd:cd17963  80 IGEVVEKMGKFTGVKVALAVPGNDV-----PRGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTQGHG 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15231748 258 DDSLKIMKDIGRvnpNFQVLLFSATFNETVKDFVARTVKDPNQL 301
Cdd:cd17963 155 DQSIRIKRMLPR---NCQILLFSATFPDSVRKFAEKIAPNANTI 195
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
92-490 5.95e-107

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 324.79  E-value: 5.95e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  92 RFEDLNLSPELMKGLyVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVDPTL-REPQALCICP 170
Cdd:COG0513   3 SFADLGLSPPLLKAL-AELGYTTPTPIQAQAIPLILA--GRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 171 TRELANQNMEVLQKMGKFTGITAELAVPdstrGAP------AATRGApvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVF 244
Cdd:COG0513  80 TRELALQVAEELRKLAKYLGLRVATVYG----GVSigrqirALKRGV----DIVVATPGRLLDLIERGALDLSGVETLVL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 245 DEADHMLatD-GFRDDSLKIMKdigRVNPNFQVLLFSATFNETVKDFVARTVKDPNQLFVKREDLALDSVKQYKVVCPKE 323
Cdd:COG0513 152 DEADRML--DmGFIEDIERILK---LLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 324 QnKIEVIKDqIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARG 403
Cdd:COG0513 227 D-KLELLRR-LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARG 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 404 FDQQRVNLVVNYNLPTkyetgepDYEVYLHRVGRAGRFGRKGAVFNLLLDDgwDKEVMEKIEKYFEANVKEIKSWNSEEE 483
Cdd:COG0513 305 IDIDDVSHVINYDLPE-------DPEDYVHRIGRTGRAGAEGTAISLVTPD--ERRLLRAIEKLIGQKIEEEELPGFEPV 375


                ....*..
gi 15231748 484 YKSALKE 490
Cdd:COG0513 376 EEKRLER 382
PTZ00424 PTZ00424
helicase 45; Provisional
 69-475 1.14e-81

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 258.99  E-value: 1.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   69 LEEPEDSNIKAVTSGDTPYTS-----ASRFEDLNLSPELMKGLYvEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSG 143
Cdd:PTZ00424   1 MATSEQKNQSEQVASTGTIESnydeiVDSFDALKLNEDLLRGIY-SYGFEKPSAIQQRGIKPILD--GYDTIGQAQSGTG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  144 KTTCFVLGMLSRVDPTLREPQALCICPTRELANQNMEVLQKMGKFTGITAELAVPDSTRGAPAATRGAPVsaHVVIGTPG 223
Cdd:PTZ00424  78 KTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGV--HMVVGTPG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  224 TLKKWMAFKRLGLNHLKILVFDEADHMLATdGFRDDSLKIMKdigRVNPNFQVLLFSATFNETVKDFVARTVKDPNQLFV 303
Cdd:PTZ00424 156 RVYDMIDKRHLRVDDLKLFILDEADEMLSR-GFKGQIYDVFK---KLPPDVQVALFSATMPNEILELTTKFMRDPKRILV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  304 KREDLALDSVKQYKVVCPKEQNKIEVIKDqIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIV 383
Cdd:PTZ00424 232 KKDELTLEGIRQFYVAVEKEEWKFDTLCD-LYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIM 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  384 KEFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPTKYETgepdyevYLHRVGRAGRFGRKGAVFNLLLDDgwDKEVMEK 463
Cdd:PTZ00424 311 REFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN-------YIHRIGRSGRFGRKGVAINFVTPD--DIEQLKE 381

                        410
                 ....*....|..
gi 15231748  464 IEKYFEANVKEI 475
Cdd:PTZ00424 382 IERHYNTQIEEM 393
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 88-473 1.08e-68

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 226.99  E-value: 1.08e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   88 TSASRFEDLNLSPELMKGL----YVEMkfekpSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREP 163
Cdd:PRK11776   1 MSMTAFSTLPLPPALLANLnelgYTEM-----TPIQAQSLPAILA--GKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  164 QALCICPTRELANQNMEVLQKMGKFTGITAELAVpdsTRGAP-AATRGAPV-SAHVVIGTPGTLKKWMAFKRLGLNHLKI 241
Cdd:PRK11776  74 QALVLCPTRELADQVAKEIRRLARFIPNIKVLTL---CGGVPmGPQIDSLEhGAHIIVGTPGRILDHLRKGTLDLDALNT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  242 LVFDEADHMLatD-GFRDDslkIMKDIGRVNPNFQVLLFSATFNETVKDFVARTVKDPNQlfVKREDL-ALDSVKQ--YK 317
Cdd:PRK11776 151 LVLDEADRML--DmGFQDA---IDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVE--VKVESThDLPAIEQrfYE 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  318 VvcpKEQNKIEVikdqimeLGDIGQ------TIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLT 391
Cdd:PRK11776 224 V---SPDERLPA-------LQRLLLhhqpesCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSC 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  392 QVLIATDVIARGFDQQRVNLVVNYNLPtkyetgePDYEVYLHRVGRAGRFGRKGAVFNLLLDDgwDKEVMEKIEKYFEAN 471
Cdd:PRK11776 294 SVLVATDVAARGLDIKALEAVINYELA-------RDPEVHVHRIGRTGRAGSKGLALSLVAPE--EMQRANAIEDYLGRK 364


                 ..
gi 15231748  472 VK 473
Cdd:PRK11776 365 LN 366
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 93-481 7.92e-60

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 207.78  E-value: 7.92e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   93 FEDLNLSPELMKGLyVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTR 172
Cdd:PRK11634   8 FADLGLKAPILEAL-NDLGYEKPSPIQAECIPHLLN--GRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  173 ELANQNMEVLQKMGKFTGITAELAVPDSTRGAPA--ATRGAPvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHM 250
Cdd:PRK11634  85 ELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQlrALRQGP---QIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  251 LATdGFRDDSLKIMKDIgrvNPNFQVLLFSATFNETVKDFVARTVKDPNQLFVK-----REDLAldsvKQYKVVCPKEQN 325
Cdd:PRK11634 162 LRM-GFIEDVETIMAQI---PEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQssvttRPDIS----QSYWTVWGMRKN 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  326 KIEVikdQIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGFD 405
Cdd:PRK11634 234 EALV---RFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLD 310

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231748  406 QQRVNLVVNYNLPTkyetgepDYEVYLHRVGRAGRFGRKGAVfnLLLDDGWDKEVMEKIEKYFEANVKEIKSWNSE 481
Cdd:PRK11634 311 VERISLVVNYDIPM-------DSESYVHRIGRTGRAGRAGRA--LLFVENRERRLLRNIERTMKLTIPEVELPNAE 377
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 85-308 1.02e-57

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: 191.00  E-value: 1.02e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  85 TPYTSASRFEDLNLSPELMKGLYVeMKFEKPSKIQAISLPMIMTPPHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQ 164
Cdd:cd18048  12 SPLFSVKSFEELHLKEELLRGIYA-MGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 165 ALCICPTRELANQNMEVLQKMGKF-TGITAELAVPDSTRGapaatRGAPVSAHVVIGTPGTLKKW-MAFKRLGLNHLKIL 242
Cdd:cd18048  91 CLCLSPTFELALQTGKVVEEMGKFcVGIQVIYAIRGNRPG-----KGTDIEAQIVIGTPGTVLDWcFKLRLIDVTNISVF 165

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231748 243 VFDEADHMLATDGFRDDSLKIMKDIGRvnpNFQVLLFSATFNETVKDFVARTVKDPNQLFVKREDL 308
Cdd:cd18048 166 VLDEADVMINVQGHSDHSVRVKRSMPK---ECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEEL 228
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 93-299 3.31e-52

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: 175.68  E-value: 3.31e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  93 FEDLNLSPELMKGLYvEMKFEKPSKIQAISLPMIMTPPHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTR 172
Cdd:cd18047   3 FEELRLKPQLLQGVY-AMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 173 ELANQNMEVLQKMGKFtgiTAELAVPDSTRGApAATRGAPVSAHVVIGTPGTLKKW-MAFKRLGLNHLKILVFDEADHML 251
Cdd:cd18047  82 ELALQTGKVIEQMGKF---YPELKLAYAVRGN-KLERGQKISEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15231748 252 ATDGFRDDSLKIMKDIGRvnpNFQVLLFSATFNETVKDFVARTVKDPN 299
Cdd:cd18047 158 ATQGHQDQSIRIQRMLPR---NCQMLLFSATFEDSVWKFAQKVVPDPN 202
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 109-298 4.89e-51

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: 172.24  E-value: 4.89e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 109 EMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVDPTL----REPQALCICPTRELANQNMEVLQK 184
Cdd:cd00268   7 KLGFEKPTPIQAQAIPLILS--GRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAEVARK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 185 MGKFTGITAELAVPdstrGAP------AATRGApvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLaTDGFRD 258
Cdd:cd00268  85 LGKGTGLKVAAIYG----GAPikkqieALKKGP----DIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRML-DMGFEE 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15231748 259 DSLKIMKdigRVNPNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd00268 156 DVEKILS---ALPKDRQTLLFSATLPEEVKELAKKFLKNP 192
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 313-451 6.98e-47

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 158.82  E-value: 6.98e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 313 VKQYKVVCPKEQnKIEVIKDQIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQ 392
Cdd:cd18787   1 IKQLYVVVEEEE-KKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15231748 393 VLIATDVIARGFDQQRVNLVVNYNLPTkyetgepDYEVYLHRVGRAGRFGRKGAVFNLL 451
Cdd:cd18787  80 VLVATDVAARGLDIPGVDHVINYDLPR-------DAEDYVHRIGRTGRAGRKGTAITFV 131
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 93-474 6.32e-46

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 165.89  E-value: 6.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   93 FEDLNLSPELMKGLYvEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLRE----PQALCI 168
Cdd:PRK11192   3 FSELELDESLLEALQ-DKGYTRPTAIQAEAIPPALD--GRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRksgpPRILIL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  169 CPTRELANQNMEVLQKMGKFTGitaeLAVPDSTRGAPAATRGAPVSAH--VVIGTPGTLKKWMAFKRLGLNHLKILVFDE 246
Cdd:PRK11192  80 TPTRELAMQVADQARELAKHTH----LDIATITGGVAYMNHAEVFSENqdIVVATPGRLLQYIKEENFDCRAVETLILDE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  247 ADHMLatD-GFRDDSLKIMKDI-GRVnpnfQVLLFSATFN-ETVKDFVARTVKDPNQLFV---KREDlalDSVKQYKVVC 320
Cdd:PRK11192 156 ADRML--DmGFAQDIETIAAETrWRK----QTLLFSATLEgDAVQDFAERLLNDPVEVEAepsRRER---KKIHQWYYRA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  321 PKEQNKIEVIKdQIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVI 400
Cdd:PRK11192 227 DDLEHKTALLC-HLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVA 305

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231748  401 ARGFDQQRVNLVVNYNLPTKYETgepdyevYLHRVGRAGRFGRKGAVFNLLldDGWDKEVMEKIEKYFEANVKE 474
Cdd:PRK11192 306 ARGIDIDDVSHVINFDMPRSADT-------YLHRIGRTGRAGRKGTAISLV--EAHDHLLLGKIERYIEEPLKA 370
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 116-290 2.04e-44

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: 153.55  E-value: 2.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   116 SKIQAISLPMIMTPphKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTRELANQNMEVLQKMGKFTGITAEL 195
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   196 AVPDSTRGapaATRGAPVSAHVVIGTPGTLKKWMAFKRLgLNHLKILVFDEADHMLaTDGFRDDSLKImkdIGRVNPNFQ 275
Cdd:pfam00270  79 LLGGDSRK---EQLEKLKGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLL-DMGFGPDLEEI---LRRLPKKRQ 150

                         170
                  ....*....|....*
gi 15231748   276 VLLFSATFNETVKDF 290
Cdd:pfam00270 151 ILLLSATLPRNLEDL 165
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 84-445 6.68e-44

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 163.20  E-value: 6.68e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   84 DTPYTSASrFEDLNLSPELMKGLyVEMKFEKPSKIQAISLPMIMtpPHKHLIAQAHNGSGKTTCFVLGMLSR-------V 156
Cdd:PRK04537   3 DKPLTDLT-FSSFDLHPALLAGL-ESAGFTRCTPIQALTLPVAL--PGGDVAGQAQTGTGKTLAFLVAVMNRllsrpalA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  157 DPTLREPQALCICPTRELANQNMEVLQKMGKFTGITAELAVP--DSTRGAPAATRGApvsaHVVIGTPGTLKKWMA-FKR 233
Cdd:PRK04537  79 DRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGgvDYDKQRELLQQGV----DVIIATPGRLIDYVKqHKV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  234 LGLNHLKILVFDEADHMLatdgfrddSLKIMKDIG---RVNP---NFQVLLFSATFNETVKDFVARTVKDPNQLFVKRED 307
Cdd:PRK04537 155 VSLHACEICVLDEADRMF--------DLGFIKDIRfllRRMPergTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETET 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  308 LALDSVKQyKVVCPKEQNKIEVIKDqIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFK 387
Cdd:PRK04537 227 ITAARVRQ-RIYFPADEEKQTLLLG-LLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQ 304

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231748  388 ECLTQVLIATDVIARGFDQQRVNLVVNYNLPTkyetgepDYEVYLHRVGRAGRFGRKG 445
Cdd:PRK04537 305 KGQLEILVATDVAARGLHIDGVKYVYNYDLPF-------DAEDYVHRIGRTARLGEEG 355
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 93-475 8.49e-44

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 160.36  E-value: 8.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   93 FEDLNLSPELMKGLyVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVD-----PTLREP-QAL 166
Cdd:PRK10590   3 FDSLGLSPDILRAV-AEQGYREPTPIQQQAIPAVLE--GRDLMASAQTGTGKTAGFTLPLLQHLItrqphAKGRRPvRAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  167 CICPTRELANQNMEVLQKMGKFTGITAeLAVPDSTRGAPAAT--RGApvsAHVVIGTPGTLKKWMAFKRLGLNHLKILVF 244
Cdd:PRK10590  80 ILTPTRELAAQIGENVRDYSKYLNIRS-LVVFGGVSINPQMMklRGG---VDVLVATPGRLLDLEHQNAVKLDQVEILVL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  245 DEADHMLATdGFRDDslkIMKDIGRVNPNFQVLLFSATFNETVKDFVARTVKDPNQLFVKREDLALDSVKQYKVVCPKEQ 324
Cdd:PRK10590 156 DEADRMLDM-GFIHD---IRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  325 nKIEVIKDQIMElGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGF 404
Cdd:PRK10590 232 -KRELLSQMIGK-GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGL 309

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231748  405 DQQRVNLVVNYNLPTKYETgepdyevYLHRVGRAGRFGRKGAVFNLLLDDgwDKEVMEKIEKYFEanvKEI 475
Cdd:PRK10590 310 DIEELPHVVNYELPNVPED-------YVHRIGRTGRAAATGEALSLVCVD--EHKLLRDIEKLLK---KEI 368
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 93-298 1.66e-42

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: 149.76  E-value: 1.66e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  93 FEDLNLSPELMKGLYvEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTR 172
Cdd:cd17940   1 FEDYGLKRELLMGIF-EKGFEKPSPIQEESIPIALS--GRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 173 ELANQNMEVLQKMGKFTGITaelaVPDSTRGAPAATR----GAPVsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEAD 248
Cdd:cd17940  78 ELALQTSQVCKELGKHMGVK----VMVTTGGTSLRDDimrlYQTV--HVLVGTPGRILDLAKKGVADLSHCKTLVLDEAD 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15231748 249 HMLATDgFRDDSLKImkdIGRVNPNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17940 152 KLLSQD-FQPIIEKI---LNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 95-298 4.74e-42

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: 148.63  E-value: 4.74e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  95 DLNLSPELMKGLYvEMKFEKPSKIQ--AIsLPMIMTpphKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTR 172
Cdd:cd17939   1 DMGLSEDLLRGIY-AYGFEKPSAIQqrAI-VPIIKG---RDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 173 ELANQNMEVLQKMGKFTGITAELAV-PDSTRGAPAATRGAPvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHML 251
Cdd:cd17939  76 ELAQQIQKVVKALGDYMGVKVHACIgGTSVREDRRKLQYGP---HIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEML 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15231748 252 aTDGFRDDSLKIMKdigRVNPNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17939 153 -SRGFKDQIYDIFQ---FLPPETQVVLFSATMPHEVLEVTKKFMRDP 195
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 60-466 1.68e-40

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 151.99  E-value: 1.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   60 KEEEKPD-SILEEPEDSNIKavtsgdtPYTSASRFEDLNLSPELMKGLYvEMKFEKPSKIQAISLPMimTPPHKHLIAQA 138
Cdd:PRK01297  62 RRERKPKpASLWKLEDFVVE-------PQEGKTRFHDFNLAPELMHAIH-DLGFPYCTPIQAQVLGY--TLAGHDAIGRA 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  139 HNGSGKTTCFVLGMLSRVDPT-------LREPQALCICPTRELANQNMEVLQKMGKFTGitaeLAVPDSTRGAPAATRGA 211
Cdd:PRK01297 132 QTGTGKTAAFLISIINQLLQTpppkeryMGEPRALIIAPTRELVVQIAKDAAALTKYTG----LNVMTFVGGMDFDKQLK 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  212 PVSAH---VVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATdGFrddsLKIMKDIGRVNP---NFQVLLFSATFNE 285
Cdd:PRK01297 208 QLEARfcdILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDM-GF----IPQVRQIIRQTPrkeERQTLLFSATFTD 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  286 TVKDFVARTVKDPNQLFVKREDLALDSVKQYKVVCPKeQNKIEVIKDQIMElGDIGQTIIFVKTKASAQKVHKALAEMGY 365
Cdd:PRK01297 283 DVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAG-SDKYKLLYNLVTQ-NPWERVMVFANRKDEVRRIEERLVKDGI 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  366 DVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPTkyetgEPDYevYLHRVGRAGRFGRKG 445
Cdd:PRK01297 361 NAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPE-----DPDD--YVHRIGRTGRAGASG 433

                        410       420
                 ....*....|....*....|.
gi 15231748  446 AVFNLLLDDgwDKEVMEKIEK 466
Cdd:PRK01297 434 VSISFAGED--DAFQLPEIEE 452
PTZ00110 PTZ00110
helicase; Provisional
 112-454 3.59e-40

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 152.23  E-value: 3.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  112 FEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVD--PTLRE---PQALCICPTRELANQNMEVLQKMG 186
Cdd:PTZ00110 150 FTEPTPIQVQGWPIALS--GRDMIGIAETGSGKTLAFLLPAIVHINaqPLLRYgdgPIVLVLAPTRELAEQIREQCNKFG 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  187 KFTGITAELA---VPDSTRGApAATRGApvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATdGFRddsLKI 263
Cdd:PTZ00110 228 ASSKIRNTVAyggVPKRGQIY-ALRRGV----EILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDM-GFE---PQI 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  264 MKDIGRVNPNFQVLLFSATFNETVKDfVARTV--KDPNQLFVKREDL-ALDSVKQYkVVCPKEQNKIEVIK---DQIMEl 337
Cdd:PTZ00110 299 RKIVSQIRPDRQTLMWSATWPKEVQS-LARDLckEEPVHVNVGSLDLtACHNIKQE-VFVVEEHEKRGKLKmllQRIMR- 375

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  338 gDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNL 417
Cdd:PTZ00110 376 -DGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDF 454

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 15231748  418 PTKYETgepdyevYLHRVGRAGRFGRKGAVFNLLLDD 454
Cdd:PTZ00110 455 PNQIED-------YVHRIGRTGRAGAKGASYTFLTPD 484
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 102-302 2.49e-37

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: 135.85  E-value: 2.49e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 102 LMKGLYvEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRV---DPTLREPQALCICPTRELANQN 178
Cdd:cd17947   1 LLRALS-SLGFTKPTPIQAAAIPLALL--GKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 179 MEVLQKMGKFTGITAELAVPD-STRGAPAATRGAPvsaHVVIGTPGT----LKKWMAFkrlGLNHLKILVFDEADHMLaT 253
Cdd:cd17947  78 FSVLQQLAQFTDITFALAVGGlSLKAQEAALRARP---DIVIATPGRlidhLRNSPSF---DLDSIEILVLDEADRML-E 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15231748 254 DGFRDDSLKIMKDIGRvnpNFQVLLFSATFNETVKDFVARTVKDPNQLF 302
Cdd:cd17947 151 EGFADELKEILRLCPR---TRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 93-298 2.94e-37

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: 135.65  E-value: 2.94e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  93 FEDLNLSPELMKGLYVeMKFEKPSKIQ--AIsLPMIMTpphKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICP 170
Cdd:cd18046   1 FDDMNLKESLLRGIYA-YGFEKPSAIQqrAI-MPCIKG---YDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAP 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 171 TRELANQNMEVLQKMGKFTGITAELAV-PDSTRGAPAATRGAPvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADH 249
Cdd:cd18046  76 TRELAQQIQKVVMALGDYMGIKCHACIgGTSVRDDAQKLQAGP---HIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADE 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15231748 250 MLATdGFRDDSLKIMKdigRVNPNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd18046 153 MLSR-GFKDQIYDIFQ---KLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEXDc smart00487
DEAD-like helicases superfamily;
109-316 2.29e-36

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 133.39  E-value: 2.29e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748    109 EMKFEKPSKIQAISLPMIMTPpHKHLIAQAHNGSGKTTCFVLGMLSRVDPTlREPQALCICPTRELANQNMEVLQKMGKF 188
Cdd:smart00487   3 KFGFEPLRPYQKEAIEALLSG-LRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748    189 TGITAELAVPDSTRGAPAA--TRGAPvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLAtDGFRDDSLKIMKd 266
Cdd:smart00487  81 LGLKVVGLYGGDSKREQLRklESGKT---DILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLK- 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 15231748    267 igRVNPNFQVLLFSATFNETVKDFVARTVKDPnqLFVKREDLALDSVKQY 316
Cdd:smart00487 156 --LLPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 93-298 4.26e-36

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: 132.59  E-value: 4.26e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  93 FEDLNLSPELMKGLYVeMKFEKPSKIQ--AIsLPMIMTpphKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICP 170
Cdd:cd18045   1 FETMGLREDLLRGIYA-YGFEKPSAIQqrAI-KPIIKG---RDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSP 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 171 TRELANQNMEVLQKMGKFTGITAELAVPDSTRGAPaaTRGAPVSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHM 250
Cdd:cd18045  76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDD--IRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEM 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15231748 251 LaTDGFRDDslkiMKDIGR-VNPNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd18045 154 L-NKGFKEQ----IYDVYRyLPPATQVVLVSATLPQDILEMTNKFMTDP 197
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 87-445 6.20e-36

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 138.18  E-value: 6.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   87 YTSASRFEDLNLSPELMKGLyVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLG----MLSRVDPTLRE 162
Cdd:PRK04837   4 HLTEQKFSDFALHPQVVEAL-EKKGFHNCTPIQALALPLTLA--GRDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  163 ---PQALCICPTRELANQNMEVLQKMGKFTGITAELAVP----DSTRGAPAAtrgapvSAHVVIGTPGTLKKWMAFKRLG 235
Cdd:PRK04837  81 vnqPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGgdgyDKQLKVLES------GVDILIGTTGRLIDYAKQNHIN 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  236 LNHLKILVFDEADHMLatD-GFrddslkiMKDI-----------GRVNpnfqvLLFSATFNETVKDFVARTVKDPNQLFV 303
Cdd:PRK04837 155 LGAIQVVVLDEADRMF--DlGF-------IKDIrwlfrrmppanQRLN-----MLFSATLSYRVRELAFEHMNNPEYVEV 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  304 KREDLALDSVKQyKVVCPKEQNKIEVIKDQIME-LGDigQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKI 382
Cdd:PRK04837 221 EPEQKTGHRIKE-ELFYPSNEEKMRLLQTLIEEeWPD--RAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRI 297

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231748  383 VKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPTkyetgepDYEVYLHRVGRAGRFGRKG 445
Cdd:PRK04837 298 LEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPD-------DCEDYVHRIGRTGRAGASG 353
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 102-299 5.56e-32

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: 121.22  E-value: 5.56e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 102 LMKGLyVEMKFEKPSKIQAISLPMIMTpphKH-LIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTRELANQNME 180
Cdd:cd17943   1 VLEGL-KAAGFQRPSPIQLAAIPLGLA---GHdLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 181 VLQKMG-KFTGITAELAVPdstrgapaatrGAPVS--------AHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHML 251
Cdd:cd17943  77 VFKKIGkKLEGLKCEVFIG-----------GTPVKedkkklkgCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLM 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15231748 252 aTDGFRDDSLKIMKDIGRvnpNFQVLLFSATFNETVKDFVARTVKDPN 299
Cdd:cd17943 146 -EGSFQKDVNWIFSSLPK---NKQVIAFSATYPKNLDNLLARYMRKPV 189
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 93-298 2.36e-31

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: 119.72  E-value: 2.36e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  93 FEDLNLSPELMKGLyVEMKFEKPSKIQAISLPMIMTPphKHLIAQAHNGSGKTTCFVLGMLSRVDPtlREPQ----ALCI 168
Cdd:cd17959   3 FQSMGLSPPLLRAI-KKKGYKVPTPIQRKTIPLILDG--RDVVAMARTGSGKTAAFLIPMIEKLKA--HSPTvgarALIL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 169 CPTRELANQNMEVLQKMGKFTGITAELAV-PDSTRGAPAATRGAPvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEA 247
Cdd:cd17959  78 SPTRELALQTLKVTKELGKFTDLRTALLVgGDSLEEQFEALASNP---DIIIATPGRLLHLLVEMNLKLSSVEYVVFDEA 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15231748 248 DHMLATdGFRDDSLKIMKdigRVNPNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17959 155 DRLFEM-GFAEQLHEILS---RLPENRQTLLFSATLPKLLVEFAKAGLNEP 201
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 90-303 7.32e-31

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: 118.60  E-value: 7.32e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  90 ASRFEDLNLSPELMKGLyVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCIC 169
Cdd:cd17950   1 SSGFRDFLLKPELLRAI-VDCGFEHPSEVQHECIPQAIL--GMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVIC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 170 PTRELANQNMEVLQKMGKFtgitaelaVPDSTRGAPAAtrGAPVSA----------HVVIGTPGTLKKWMAFKRLGLNHL 239
Cdd:cd17950  78 HTRELAFQISNEYERFSKY--------MPNVKTAVFFG--GVPIKKdievlknkcpHIVVGTPGRILALVREKKLKLSHV 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231748 240 KILVFDEADHMLATDGFRDDslkiMKDIGRVNP-NFQVLLFSATFNETVKDFVARTVKDPNQLFV 303
Cdd:cd17950 148 KHFVLDECDKMLEQLDMRRD----VQEIFRATPhDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 93-290 1.67e-30

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: 117.97  E-value: 1.67e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  93 FEDLNLSPELMKGLyVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRV----------DPTLRE 162
Cdd:cd17967   2 FEEAGLRELLLENI-KRAGYTKPTPVQKYAIPIILA--GRDLMACAQTGSGKTAAFLLPIISKLledgppsvgrGRRKAY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 163 PQALCICPTRELANQNMEVLQKMGKFTGITAELAVpdstrGapaatrGAPVS---------AHVVIGTPGTLKKWMAFKR 233
Cdd:cd17967  79 PSALILAPTRELAIQIYEEARKFSYRSGVRSVVVY-----G------GADVVhqqlqllrgCDILVATPGRLVDFIERGR 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231748 234 LGLNHLKILVFDEADHMLatD-GFRDDSLKIMKDIGRVNP-NFQVLLFSATFNETV----KDF 290
Cdd:cd17967 148 ISLSSIKFLVLDEADRML--DmGFEPQIRKIVEHPDMPPKgERQTLMFSATFPREIqrlaADF 208
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 83-445 4.35e-30

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 122.97  E-value: 4.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   83 GDTPYTSASRFEDLNLSPELMKGLYVeMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRV------ 156
Cdd:PLN00206 113 GEAVPPPILSFSSCGLPPKLLLNLET-AGYEFPTPIQMQAIPAALS--GRSLLVSADTGSGKTASFLVPIISRCctirsg 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  157 -DPTLREPQALCICPTRELANQNMEVLQKMGKftGITAELAVPDSTRGAPAATRGAPVSAHVVIGTPGTLKKWMAFKRLG 235
Cdd:PLN00206 190 hPSEQRNPLAMVLTPTRELCVQVEDQAKVLGK--GLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIE 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  236 LNHLKILVFDEADHMLATdGFRDDSLKIMKDIgrvnPNFQVLLFSATFNETVKDFVARTVKDPNQLFVKREDLALDSVKQ 315
Cdd:PLN00206 268 LDNVSVLVLDEVDCMLER-GFRDQVMQIFQAL----SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQ 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  316 YKV-VCPKEQNKievikdqimELGDIGQT--------IIFVKTKASAQKVHKALAEM-GYDVTSVHGNLTESDRDKIVKE 385
Cdd:PLN00206 343 LAIwVETKQKKQ---------KLFDILKSkqhfkppaVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKS 413

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  386 FKECLTQVLIATDVIARGFDQQRVNLVVNYNLPTKYETgepdyevYLHRVGRAGRFGRKG 445
Cdd:PLN00206 414 FLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKE-------YIHQIGRASRMGEKG 466
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 98-303 4.83e-28

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: 110.75  E-value: 4.83e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  98 LSPELMKGLyVEMKFEKPSKIQAISLPMIMTPPHKhLIAQAHNGSGKTTCFVL----GMLSRVDPTLREP-QALCICPTR 172
Cdd:cd17964   1 LDPSLLKAL-TRMGFETMTPVQQKTLKPILSTGDD-VLARAKTGTGKTLAFLLpaiqSLLNTKPAGRRSGvSALIISPTR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 173 ELANQNMEVLQKM-GKFTGITAELAVPDSTRGAPAA--TRGAPvsaHVVIGTPGTLK----KWMAFKRLGlnHLKILVFD 245
Cdd:cd17964  79 ELALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNrlRRGRP---DILVATPGRLIdhleNPGVAKAFT--DLDYLVLD 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15231748 246 EADHMLaTDGFRDDSLKIMKDI-GRVNPNFQVLLFSATFNETVKDFvARTVKDPNQLFV 303
Cdd:cd17964 154 EADRLL-DMGFRPDLEQILRHLpEKNADPRQTLLFSATVPDEVQQI-ARLTLKKDYKFI 210
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 93-298 6.68e-28

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: 110.48  E-value: 6.68e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  93 FEDLNLSPELMKGLYvEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVdptLREPQ---ALCIC 169
Cdd:cd17954   2 FKELGVCEELCEACE-KLGWKKPTKIQEEAIPVALQ--GRDIIGLAETGSGKTAAFALPILQAL---LENPQrffALVLA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 170 PTRELANQNMEVLQKMGKFTGITAELAVP--DSTRGAPAATRgapvSAHVVIGTPGTLKKWMA-FKRLGLNHLKILVFDE 246
Cdd:cd17954  76 PTRELAQQISEQFEALGSSIGLKSAVLVGgmDMMAQAIALAK----KPHVIVATPGRLVDHLEnTKGFSLKSLKFLVMDE 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15231748 247 ADHMLATDgFRDDSLKIMKDIGRvnpNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17954 152 ADRLLNMD-FEPEIDKILKVIPR---ERTTYLFSATMTTKVAKLQRASLKNP 199
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 325-442 8.65e-28

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 106.91  E-value: 8.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   325 NKIEVIKDqIMELGDIGQTIIFVKTKASAqKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGF 404
Cdd:pfam00271   1 EKLEALLE-LLKKERGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15231748   405 DQQRVNLVVNYNLPTkyetgepDYEVYLHRVGRAGRFG 442
Cdd:pfam00271  79 DLPDVDLVINYDLPW-------NPASYIQRIGRAGRAG 109
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 93-298 8.84e-28

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: 110.01  E-value: 8.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  93 FEDLNLSPELMKGLYvEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSR--VDPTlrEPQALCICP 170
Cdd:cd17955   1 FEDLGLSSWLVKQCA-SLGIKEPTPIQKLCIPEILA--GRDVIGGAKTGSGKTAAFALPILQRlsEDPY--GIFALVLTP 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 171 TRELANQNMEVLQKMGKFTGITAELAV--PDSTRGApAATRGAPvsaHVVIGTPGTLKKWM---AFKRLGLNHLKILVFD 245
Cdd:cd17955  76 TRELAYQIAEQFRALGAPLGLRCCVIVggMDMVKQA-LELSKRP---HIVVATPGRLADHLrssDDTTKVLSRVKFLVLD 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15231748 246 EADHMLaTDGFRDDSLKImkdIGRVNPNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17955 152 EADRLL-TGSFEDDLATI---LSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 76-303 9.34e-28

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: 111.60  E-value: 9.34e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  76 NIKAVTSGDTPYTSASRFEDLNLSPELMKGLYvEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSR 155
Cdd:cd18052  28 EIPVEVTGRNPPPAILTFEEANLCETLLKNIR-KAGYEKPTPVQKYAIPIILA--GRDLMACAQTGSGKTAAFLLPVLTG 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 156 -----VDPT----LREPQALCICPTRELANQNMEVLQKMGKFTGITAEL-----AVPDSTRgapAATRGapvsAHVVIGT 221
Cdd:cd18052 105 mmkegLTASsfseVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVvyggvSVGHQIR---QIEKG----CHILVAT 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 222 PGTLKKWMAFKRLGLNHLKILVFDEADHMLatD-GFRDDSLKIMKDIGRvnP---NFQVLLFSATFNETVKDFVARTVKd 297
Cdd:cd18052 178 PGRLLDFIGRGKISLSKLKYLILDEADRML--DmGFGPEIRKLVSEPGM--PskeDRQTLMFSATFPEEIQRLAAEFLK- 252


                ....*.
gi 15231748 298 PNQLFV 303
Cdd:cd18052 253 EDYLFL 258
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
141-438 1.72e-26

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 112.81  E-value: 1.72e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 141 GSGKTT--CFVLGMLSRVDPTLrepqalCICPTRELANQNMEVLQKmgkftgitaelavpdSTRGAPAATRGAPVSAHVV 218
Cdd:COG1061 110 GTGKTVlaLALAAELLRGKRVL------VLVPRRELLEQWAEELRR---------------FLGDPLAGGGKKDSDAPIT 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 219 IGTPGTLKKWMAFKRLGlNHLKILVFDEAdHMLATDGFRddslKIMKdigRVNPNFqVLLFSAT---------------- 282
Cdd:COG1061 169 VATYQSLARRAHLDELG-DRFGLVIIDEA-HHAGAPSYR----RILE---AFPAAY-RLGLTATpfrsdgreillflfdg 238

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 283 --FNETVKDFVA-------RTVKDPNQLFVKREDLALDSVKQYKVVCPKEQNKIEVIKDQIMELGDIGQTIIFVKTKASA 353
Cdd:COG1061 239 ivYEYSLKEAIEdgylappEYYGIRVDLTDERAEYDALSERLREALAADAERKDKILRELLREHPDDRKTLVFCSSVDHA 318

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 354 QKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVnYNLPTKYETgepdyeVYLH 433
Cdd:COG1061 319 EALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTGSPR------EFIQ 391


                ....*
gi 15231748 434 RVGRA 438
Cdd:COG1061 392 RLGRG 396
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 109-298 1.37e-25

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: 103.82  E-value: 1.37e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 109 EMKFEKPSKIQAISLPMIMtppHKH-LIAQAHNGSGKTTCFVLGMLSRVDPTLRE--PQALCICPTRELANQNMEVLQKM 185
Cdd:cd17957   7 ESGYREPTPIQMQAIPILL---HGRdLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYRELLKL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 186 GKFTGITAELaVPDSTRGAPAATRGAPVSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATdGFRDDSLKIMK 265
Cdd:cd17957  84 SKGTGLRIVL-LSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEP-GFREQTDEILA 161

                       170       180       190
                ....*....|....*....|....*....|...
gi 15231748 266 DIgrVNPNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17957 162 AC--TNPNLQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 102-301 2.79e-24

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: 100.14  E-value: 2.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 102 LMKGLYvEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVD--PTLRE---PQALCICPTRELAN 176
Cdd:cd17966   1 VMDELK-RQGFTEPTAIQAQGWPMALS--GRDMVGIAQTGSGKTLAFLLPAIVHINaqPPLERgdgPIVLVLAPTRELAQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 177 QNMEVLQKMGKFTGITAELAVPDSTRGAPAA--TRGApvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATd 254
Cdd:cd17966  78 QIQQEANKFGGSSRLRNTCVYGGAPKGPQIRdlRRGV----EICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDM- 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15231748 255 GFRDdslKIMKDIGRVNPNFQVLLFSATFNETVKDFVARTVKDPNQL 301
Cdd:cd17966 153 GFEP---QIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 102-307 3.68e-23

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: 98.08  E-value: 3.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 102 LMKGLYvEMKFEKPSKIQAISLPMIMTPpHKHLIAQAHNGSGKTTCFVLGML--------SRVDPTL-REPQALCICPTR 172
Cdd:cd17946   1 ILRALA-DLGFSEPTPIQALALPAAIRD-GKDVIGAAETGSGKTLAFGIPILerllsqksSNGVGGKqKPLRALILTPTR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 173 ELANQNMEVLQKMGKFTGITAELAVpdstrGAPAAT---RGAPVSAHVVIGTPGTLKKWMAFKRLGLN---HLKILVFDE 246
Cdd:cd17946  79 ELAVQVKDHLKAIAKYTNIKIASIV-----GGLAVQkqeRLLKKRPEIVVATPGRLWELIQEGNEHLAnlkSLRFLVLDE 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231748 247 ADHMLATDGFRDDSlKIMKDIGRVNPNF----QVLLFSATFNEtVKDFVARTVKDPNQLFVKRED 307
Cdd:cd17946 154 ADRMLEKGHFAELE-KILELLNKDRAGKkrkrQTFVFSATLTL-DHQLPLKLNSKKKKKKKEKKQ 216
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 109-298 4.06e-23

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: 97.45  E-value: 4.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 109 EMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRV--DPTLRE---PQALCICPTRELANQNMEVLQ 183
Cdd:cd17953  29 KLGYEKPTPIQAQALPAIMS--GRDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPgegPIGLIMAPTRELALQIYVECK 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 184 KMGKFTGITAelavpdstrgaPAATRGAPVS---------AHVVIGTPGTLKKWMAF---KRLGLNHLKILVFDEADHML 251
Cdd:cd17953 107 KFSKALGLRV-----------VCVYGGSGISeqiaelkrgAEIVVCTPGRMIDILTAnngRVTNLRRVTYVVLDEADRMF 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15231748 252 ATdGFRDdslKIMKDIGRVNPNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17953 176 DM-GFEP---QIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 104-303 8.39e-23

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: 95.82  E-value: 8.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 104 KGLyVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVdptLREP-------QALCICPTRELAN 176
Cdd:cd17941   3 KGL-KEAGFIKMTEIQRDSIPHALQ--GRDILGAAKTGSGKTLAFLVPLLEKL---YRERwtpedglGALIISPTRELAM 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 177 QNMEVLQKMGKFTGITAELAVPdstrGAPAATRGAPVSA-HVVIGTPGTLKKWM-AFKRLGLNHLKILVFDEADHMLATd 254
Cdd:cd17941  77 QIFEVLRKVGKYHSFSAGLIIG----GKDVKEEKERINRmNILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDM- 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15231748 255 GFRDDSLKIMKDIGrvnPNFQVLLFSATFNETVKDFVARTVKDPNQLFV 303
Cdd:cd17941 152 GFKETLDAIVENLP---KSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
HELICc smart00490
helicase superfamily c-terminal domain;
354-442 1.22e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 1.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748    354 QKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPtkyetgePDYEVYLH 433
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-------WSPASYIQ 73


                   ....*....
gi 15231748    434 RVGRAGRFG 442
Cdd:smart00490  74 RIGRAGRAG 82
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 102-298 1.24e-22

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: 95.73  E-value: 1.24e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 102 LMKGLYVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSR---VDPTL-RE--PQALCICPTRELA 175
Cdd:cd17949   1 LVSHLKSKMGIEKPTAIQKLAIPVLLQ--GRDVLVRSQTGSGKTLAYLLPIIQRllsLEPRVdRSdgTLALVLVPTRELA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 176 NQNMEVLQKMGK-FTGITAELAVPDSTRGAPAAT--RGAPvsahVVIGTPGTL----KKWMAFKrlgLNHLKILVFDEAD 248
Cdd:cd17949  79 LQIYEVLEKLLKpFHWIVPGYLIGGEKRKSEKARlrKGVN----ILIATPGRLldhlKNTQSFD---VSNLRWLVLDEAD 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231748 249 HMLatD-GFRDDSLKIMK--DIGRVN--------PNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17949 152 RLL--DmGFEKDITKILEllDDKRSKaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDP 210
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 108-298 8.51e-22

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: 92.86  E-value: 8.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 108 VEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRV--DPTLRE---PQALCICPTRELANQNMEVL 182
Cdd:cd17952   6 RKQEYEQPTPIQAQALPVALS--GRDMIGIAKTGSGKTAAFIWPMLVHImdQRELEKgegPIAVIVAPTRELAQQIYLEA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 183 QKMGKFTGI--TAELAVPDSTRGAPAATRGApvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATdGFRDDS 260
Cdd:cd17952  84 KKFGKAYNLrvVAVYGGGSKWEQAKALQEGA----EIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDM-GFEYQV 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15231748 261 LKImkdIGRVNPNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17952 159 RSI---VGHVRPDRQTLLFSATFKKKIEQLARDILSDP 193
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 102-298 1.87e-21

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: 92.40  E-value: 1.87e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 102 LMKGLyVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGML------SRVDPTLRE--PQALCICPTRE 173
Cdd:cd17951   1 ILKGL-KKKGIKKPTPIQMQGLPTILS--GRDMIGIAFTGSGKTLVFTLPLImfaleqEKKLPFIKGegPYGLIVCPSRE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 174 LANQNMEVLQKM------GKFTGITAELAVPdstrGAPAATRGAPVS--AHVVIGTPGTLKKWMAFKRLGLNHLKILVFD 245
Cdd:cd17951  78 LARQTHEVIEYYckalqeGGYPQLRCLLCIG----GMSVKEQLEVIRkgVHIVVATPGRLMDMLNKKKINLDICRYLCLD 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15231748 246 EADHMLATdGFRDDSLKIMKDIGRVNpnfQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17951 154 EADRMIDM-GFEEDIRTIFSYFKGQR---QTLLFSATMPKKIQNFAKSALVKP 202
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 98-289 4.11e-21

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: 91.11  E-value: 4.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  98 LSPELMKGLyVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRV------DPTLREPQALCICPT 171
Cdd:cd17961   1 LDPRLLKAI-AKLGWEKPTLIQSKAIPLALE--GKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 172 RELANQNMEVLQKMGKFTGI---TAELAVPDSTRGAPAATRGAPvsaHVVIGTPGTLKKWMAFKRLGL-NHLKILVFDEA 247
Cdd:cd17961  78 RELAQQVSKVLEQLTAYCRKdvrVVNLSASSSDSVQRALLAEKP---DIVVSTPARLLSHLESGSLLLlSTLKYLVIDEA 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15231748 248 DHMLaTDGFRDDslkiMKDIGRVNP-NFQVLLFSATFNETVKD 289
Cdd:cd17961 155 DLVL-SYGYEED----LKSLLSYLPkNYQTFLMSATLSEDVEA 192
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 93-298 5.43e-21

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: 90.84  E-value: 5.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  93 FEDLNLSPELMKGLYvEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLgmlsrvdPTLREPQALCICPTR 172
Cdd:cd17938   1 FEELGVMPELIKAVE-ELDWLLPTDIQAEAIPLILG--GGDVLMAAETGSGKTGAFCL-------PVLQIVVALILEPSR 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 173 ELANQNMEVLQKMGKF-TGITAELAVPDSTRGAPAATRGAPVSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHML 251
Cdd:cd17938  71 ELAEQTYNCIENFKKYlDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLL 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15231748 252 aTDGFRDDSLKI---MKDIGRVNPNFQVLLFSATFNET-VKDFVARTVKDP 298
Cdd:cd17938 151 -SQGNLETINRIynrIPKITSDGKRLQVIVCSATLHSFeVKKLADKIMHFP 200
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 110-298 7.22e-20

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: 87.52  E-value: 7.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 110 MKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVD--PTLRE----PQALCICPTRELANQ-NMEV- 181
Cdd:cd17958   8 QGFEKPSPIQSQAWPIILQ--GIDLIGVAQTGTGKTLAYLLPGFIHLDlqPIPREqrngPGVLVLTPTRELALQiEAECs 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 182 ------LQKMGKFTGITAELAVPDSTRGApaatrgapvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATdG 255
Cdd:cd17958  86 kysykgLKSVCVYGGGNRNEQIEDLSKGV-----------DIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDM-G 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15231748 256 FRDDSLKIMKDIgrvNPNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17958 154 FEPQIRKILLDI---RPDRQTIMTSATWPDGVRRLAQSYLKDP 193
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 109-298 1.16e-19

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: 87.38  E-value: 1.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 109 EMKFEKPSKIQAISLPMIMTPphKHLIAQAHNGSGKTTCFVLGMLSRVD--PTLRE------PQALCICPTRELANQNME 180
Cdd:cd17945   7 KLGYKEPTPIQRQAIPIGLQN--RDIIGIAETGSGKTAAFLIPLLVYISrlPPLDEetkddgPYALILAPTRELAQQIEE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 181 VLQKMGKFTGITAELAVPDSTRG--APAATRGApvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLatD-GFR 257
Cdd:cd17945  85 ETQKFAKPLGIRVVSIVGGHSIEeqAFSLRNGC----EILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMI--DmGFE 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231748 258 DDSLKIMKDIGRVNPNF-----------------QVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17945 159 PQVTKILDAMPVSNKKPdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRP 216
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 109-291 1.56e-19

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: 86.48  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 109 EMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRV-----DPTLREPQALCICPTRELANQNMEVLQ 183
Cdd:cd17960   7 ELGFTSMTPVQAATIPLFLS--NKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIYEVLQ 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 184 KMGKFTG--ITAELAVpdstrGAPAATRGAP----VSAHVVIGTPGTL-------KKWMAFKrlglnHLKILVFDEADHM 250
Cdd:cd17960  85 SFLEHHLpkLKCQLLI-----GGTNVEEDVKkfkrNGPNILVGTPGRLeellsrkADKVKVK-----SLEVLVLDEADRL 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15231748 251 LatD-GFRDDSLKIMkdiGRVNPNFQVLLFSATFNETVKDFV 291
Cdd:cd17960 155 L--DlGFEADLNRIL---SKLPKQRRTGLFSATQTDAVEELI 191
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 112-298 2.19e-19

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: 86.06  E-value: 2.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 112 FEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTRELANQNMEVLQKMGKftGI 191
Cdd:cd17962  10 YEVPTPIQMQMIPVGLL--GRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMK--GL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 192 ----TAELavpdsTRGAPAATRGAPVSAHV--VIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATdGFRDDSLKIMK 265
Cdd:cd17962  86 ppmkTALL-----VGGLPLPPQLYRLQQGVkvIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKM-GFQQQVLDILE 159

                       170       180       190
                ....*....|....*....|....*....|...
gi 15231748 266 DIGRvnpNFQVLLFSATFNETVKDFVARTVKDP 298
Cdd:cd17962 160 NISH---DHQTILVSATIPRGIEQLAGQLLQNP 189
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 131-282 2.34e-19

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: 84.38  E-value: 2.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 131 HKHLIAQAHNGSGKTTCFVLGMLSRVDPtlREPQALCICPTRELANQNMEVLQKMGKfTGITAELAVPDSTRGAPAATRG 210
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKL 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231748 211 APvsAHVVIGTPGTL-KKWMAFKRLGLNHLKILVFDEADHML-ATDGFRDDSLKIMKdigRVNPNFQVLLFSAT 282
Cdd:cd00046  78 GD--ADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLiDSRGALILDLAVRK---AGLKNAQVILLSAT 146
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 103-303 2.40e-19

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: 85.88  E-value: 2.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 103 MKGLyVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFV---LGMLSRVDPTLREPQA-LCICPTRELANQN 178
Cdd:cd17942   2 LKAI-EEMGFTKMTEIQAKSIPPLLE--GRDVLGAAKTGSGKTLAFLipaIELLYKLKFKPRNGTGvIIISPTRELALQI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 179 MEVLQKMGKFTGITAELAVPDSTRGAPAATRGAPVSahVVIGTPGTL-------KKWMaFKrlglnHLKILVFDEADHML 251
Cdd:cd17942  79 YGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVN--ILVATPGRLldhlqntKGFL-YK-----NLQCLIIDEADRIL 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15231748 252 ATdGFRDDSLKIMKDIGRvnpNFQVLLFSATFNETVKDfVARTVKDPNQLFV 303
Cdd:cd17942 151 EI-GFEEEMRQIIKLLPK---RRQTMLFSATQTRKVED-LARISLKKKPLYV 197
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 73-283 1.68e-17

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: 82.01  E-value: 1.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  73 EDSNIKAvTSGDTPyTSASRFEDLNLSpELMKGLYVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGM 152
Cdd:cd18051   5 EDIPVEA-TGENCP-PHIETFSDLDLG-EIIRNNIELARYTKPTPVQKHAIPIIKS--KRDLMACAQTGSGKTAAFLLPI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 153 LSRV------DPTLRE----------PQALCICPTRELANQNMEVLQKMGKFTGITaelavPDSTRGapaatrGAPVSA- 215
Cdd:cd18051  80 LSQIyeqgpgESLPSEsgyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVR-----PCVVYG------GADIGQq 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231748 216 --------HVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATdGFRDDSLKIM-KDIGRVNPNFQVLLFSATF 283
Cdd:cd18051 149 mrdlergcHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDM-GFEPQIRRIVeQDTMPPTGERQTLMFSATF 224
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 109-295 3.11e-17

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: 80.87  E-value: 3.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 109 EMKFEKPSKIQAISLPMIMTPPHKhLIAqAHNGSGKTTCFVLGMLSRV-------DPTLREPQALCICPTRELANQNMEV 181
Cdd:cd17948   7 RQGITKPTTVQKQGIPSILRGRNT-LCA-AETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQIGSV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 182 LQKMGKFTGITAELAVPDSTRGAPAATRGApvSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLaTDGFRDDSL 261
Cdd:cd17948  85 AQSLTEGLGLKVKVITGGRTKRQIRNPHFE--EVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLL-DDSFNEKLS 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15231748 262 KIMK----------DIGRVNPNFQVLLFSATFNETVKDFVARTV 295
Cdd:cd17948 162 HFLRrfplasrrseNTDGLDPGTQLVLVSATMPSGVGEVLSKVI 205
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 100-301 4.38e-17

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: 81.21  E-value: 4.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 100 PELMKGLYVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVD--PTLRE---PQALCICPTREL 174
Cdd:cd18050  70 PQYVMDVLLDQNFKEPTPIQCQGFPLALS--GRDMVGIAQTGSGKTLAYLLPAIVHINhqPYLERgdgPICLVLAPTREL 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 175 ANQNMEVLQKMGKFTGITAELAVPDSTRGApaATRGAPVSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATd 254
Cdd:cd18050 148 AQQVQQVADDYGKSSRLKSTCIYGGAPKGP--QIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDM- 224

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15231748 255 GFRDdslKIMKDIGRVNPNFQVLLFSATFNETVKDFVARTVKDPNQL 301
Cdd:cd18050 225 GFEP---QIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 92-297 2.16e-16

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: 78.51  E-value: 2.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  92 RFEDLNLSPELMKgLYVEMKFEKPSKIQAISLPMIMTppHKHLIAQAHNGSGKTTCFVLGMLSRVD--PTLRE---PQAL 166
Cdd:cd18049  25 NFYEANFPANVMD-VIARQNFTEPTAIQAQGWPVALS--GLDMVGVAQTGSGKTLSYLLPAIVHINhqPFLERgdgPICL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 167 CICPTRELANQNMEVLQKMGKFTGITAELAVPDSTRGApaATRGAPVSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDE 246
Cdd:cd18049 102 VLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGP--QIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDE 179

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15231748 247 ADHMLATdGFRDdslKIMKDIGRVNPNFQVLLFSATFNETVKDFVARTVKD 297
Cdd:cd18049 180 ADRMLDM-GFEP---QIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 109-282 4.73e-16

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: 77.29  E-value: 4.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 109 EMKFEKPSKIQAISLPMIMtPPHKHLIAQ--------AHNGSGKTTCFVLGML----SRVDPTLRepqALCICPTRELAN 176
Cdd:cd17956   7 NNGITSAFPVQAAVIPWLL-PSSKSTPPYrpgdlcvsAPTGSGKTLAYVLPIVqalsKRVVPRLR---ALIVVPTKELVQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 177 QNMEVLQKMGKFTGITAELA-----VPDSTRGAPAATRGA-PVSAHVVIGTPGTL----KKWMAFKrlgLNHLKILVFDE 246
Cdd:cd17956  83 QVYKVFESLCKGTGLKVVSLsgqksFKKEQKLLLVDTSGRyLSRVDILVATPGRLvdhlNSTPGFT---LKHLRFLVIDE 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15231748 247 ADHML-------------ATDGFRDDSLKIMKDIGRVNP---NFQVLLFSAT 282
Cdd:cd17956 160 ADRLLnqsfqdwletvmkALGRPTAPDLGSFGDANLLERsvrPLQKLLFSAT 211
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 132-282 5.41e-15

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: 73.73  E-value: 5.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 132 KHLIAQAHNGSGKTTCFVLGMLSRVDPTL------REPQALCICPTRELANQNMEvlqkmgKFTGITAELAVPDSTRGAP 205
Cdd:cd17944  28 KDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTK------DFKDITRKLSVACFYGGTP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 206 AATRGAPVSA--HVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATdGFRDDSLKIMKDIGRVNP--NFQVLLFSA 281
Cdd:cd17944 102 YQQQIFAIRNgiDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDM-GFAEQVEEILSVSYKKDSedNPQTLLFSA 180


                .
gi 15231748 282 T 282
Cdd:cd17944 181 T 181
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
132-477 2.02e-12

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 69.15  E-value: 2.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 132 KHLIAQAHNGSGKTTCFVLGMLSRVdptLREPQALCICPTRELANQNMEVLQKMGKFTGITAELAVPDSTRGAPAATRga 211
Cdd:COG1204  39 KNLVVSAPTASGKTLIAELAILKAL---LNGGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGR-- 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 212 pvsAHVVIGTPgtlKKWMAFKRLG---LNHLKILVFDEAdHMLATD--GFRDDSL--KIMkdigRVNPNFQVLLFSATfn 284
Cdd:COG1204 114 ---YDILVATP---EKLDSLLRNGpswLRDVDLVVVDEA-HLIDDEsrGPTLEVLlaRLR----RLNPEAQIVALSAT-- 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 285 etvkdfvartVKDPnqlfvkrEDLA--LDS---------VKQYK-VVCPKE---QNKIEVIKDQI-----MELGDIGQTI 344
Cdd:COG1204 181 ----------IGNA-------EEIAewLDAelvksdwrpVPLNEgVLYDGVlrfDDGSRRSKDPTlalalDLLEEGGQVL 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 345 IFVKTKASAQKVHKALA-----------------------------EMGYDVTSV--------HGNLTESDRDKIVKEFK 387
Cdd:COG1204 244 VFVSSRRDAESLAKKLAdelkrrltpeereeleelaeellevseetHTNEKLADClekgvafhHAGLPSELRRLVEDAFR 323

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 388 ECLTQVLIATDVIARGfdqqrVNL----VVNYNlpTKYETGEP----DyevYLHRVGRAGRFGR--KGAVFnlLLDDGwD 457
Cdd:COG1204 324 EGLIKVLVATPTLAAG-----VNLparrVIIRD--TKRGGMVPipvlE---FKQMAGRAGRPGYdpYGEAI--LVAKS-S 390

                       410       420
                ....*....|....*....|
gi 15231748 458 KEVMEKIEKYFEANVKEIKS 477
Cdd:COG1204 391 DEADELFERYILGEPEPIRS 410
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 131-282 2.55e-12

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: 65.36  E-value: 2.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 131 HKHLIAQAHNGSGKTTCFVLGMLSRVdptLREPQ-ALCICPTRELANQNMEVLQKMGKFTGITAELAVPDSTRgapaaTR 209
Cdd:cd17921  17 GDSVLVSAPTSSGKTLIAELAILRAL---ATSGGkAVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSV-----NK 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231748 210 GAPVSAHVVIGTP----GTLKKWmafKRLGLNHLKILVFDEAdHMLAtDGFRDDSLK-IMKDIGRVNPNFQVLLFSAT 282
Cdd:cd17921  89 LLLAEADILVATPekldLLLRNG---GERLIQDVRLVVVDEA-HLIG-DGERGVVLElLLSRLLRINKNARFVGLSAT 161
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
236-440 2.84e-10

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 62.47  E-value: 2.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 236 LNHLKI--LVFDEAdHMLATDG--FRDDSLKIMKDIGRVnPNFQVLLFSATFNETVKDFVART--VKDPNQL---FVkRE 306
Cdd:COG0514 127 LRRLKIslFAIDEA-HCISQWGhdFRPDYRRLGELRERL-PNVPVLALTATATPRVRADIAEQlgLEDPRVFvgsFD-RP 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 307 DLaldsvkQYKVVCPKEQNKIEVIKDQIMELGDiGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEF 386
Cdd:COG0514 204 NL------RLEVVPKPPDDKLAQLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRF 276

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15231748 387 KECLTQVLIATdvIA--RGFDQQRVNLVVNYNLPtkyetgePDYEVYLHRVGRAGR 440
Cdd:COG0514 277 LRDEVDVIVAT--IAfgMGIDKPDVRFVIHYDLP-------KSIEAYYQEIGRAGR 323
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 314-448 9.15e-10

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: 56.72  E-value: 9.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 314 KQYKVVCPKeqnkIEVIKDQIMELGDIGQ-TIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLT- 391
Cdd:cd18793   4 KIEEVVSGK----LEALLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDi 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231748 392 -QVLIATDVIARGFDQQRVNLVVNYNLPtkyetGEPDYEvyLHRVGRAGRFGRKGAVF 448
Cdd:cd18793  80 rVFLLSTKAGGVGLNLTAANRVILYDPW-----WNPAVE--EQAIDRAHRIGQKKPVV 130
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 324-440 5.44e-09

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 54.87  E-value: 5.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 324 QNKIEVIKdqIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDvtsvHGNLTESDRDKIVKEFKECLTQVLIATDVIARG 403
Cdd:cd18795  29 SDIIVLLK--IETVSEGKPVLVFCSSRKECEKTAKDLAGIAFH----HAGLTREDRELVEELFREGLIKVLVATSTLAAG 102

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15231748 404 fdqqrVNL----VVnYNLPTKYETGEPDY----EvYLHRVGRAGR 440
Cdd:cd18795 103 -----VNLpartVI-IKGTQRYDGKGYRElsplE-YLQMIGRAGR 140
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 316-443 5.64e-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: 54.52  E-value: 5.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 316 YKVVcPKEQNKIEVI-KDQIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVL 394
Cdd:cd18794   6 YSVR-PKDKKDEKLDlLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15231748 395 IATDVIARGFDQQRVNLVVNYNLPtkyetgePDYEVYLHRVGRAGRFGR 443
Cdd:cd18794  85 VATVAFGMGIDKPDVRFVIHYSLP-------KSMESYYQESGRAGRDGL 126
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
291-490 1.11e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 57.82  E-value: 1.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 291 VARTVKDPNqlfVKRedlALDSVKQYKVVCPKeQNKIEVIKDQIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVT-- 368
Cdd:COG1111 311 SKRLVSDPR---FRK---AMRLAEEADIEHPK-LSKLREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrf 383

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 369 ----SVHGN--LTESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNY-NLPTkyetgepdyEV-YLHRVGRAGR 440
Cdd:COG1111 384 vgqaSKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYePVPS---------EIrSIQRKGRTGR 454

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 441 FgRKGAVFNLLLDDGWD---------KE-VMEKIEKYFEANVKEIKSWNSEEEYKSALKE 490
Cdd:COG1111 455 K-REGRVVVLIAKGTRDeayywssrrKEkKMKSILKKLKKLLDKQEKEKLKESAQATLDE 513
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
 230-469 2.12e-07

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 52.82  E-value: 2.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 230 AFKRLGLNHLKILVFDEAdHMLA--TDGFRDDSLKIMKDIGRvnpnfQVLLFSATFNETVKDFVARtvkdpNQLFVKRED 307
Cdd:cd09639 115 YEFTLASIANSLLIFDEV-HFYDeyTLALILAVLEVLKDNDV-----PILLMSATLPKFLKEYAEK-----IGYVEENEP 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 308 LALDSVKQYKVV-CPKEQN-KIEVIKDQIMELGDIGQTIIFVKTKASAQKVHKALAEMG--YDVTSVHGNLTESDRDKIV 383
Cdd:cd09639 184 LDLKPNERAPFIkIESDKVgEISSLERLLEFIKKGGSVAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSRFTEKDRAKKE 263

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 384 KEFKECLTQ----VLIATDVIARGFDQQrVNLVVNynlptkyETGEPDyeVYLHRVGRAGRFGRKGA----VFNLLLDDG 455
Cdd:cd09639 264 AELLLEFKKsekfVIVATQVIEASLDIS-VDVMIT-------ELAPID--SLIQRLGRLHRYGEKNGeevyIITDAPDGK 333

                       250
                ....*....|....*...
gi 15231748 456 ----WDKEVMEKIEKYFE 469
Cdd:cd09639 334 gqkpYPYDLVERTIELLE 351
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 315-438 2.73e-07

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: 49.90  E-value: 2.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 315 QYKVVCPKEQNKIEVIKDQIMELGDIgQTIIFVKTKASAQ----------------KVHkALAEMGYDVTSVHGNLTESD 378
Cdd:cd18802   1 EEIVVIPKLQKLIEILREYFPKTPDF-RGIIFVERRATAVvlsrllkehpstlafiRCG-FLIGRGNSSQRKRSLMTQRK 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 379 RDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPTkyetgepDYEVYLHRVGRA 438
Cdd:cd18802  79 QKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPK-------TLRSYIQSRGRA 131
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 308-466 8.41e-07

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 51.76  E-value: 8.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 308 LALDSVKQYKVVCPKEQNKIEVIkDQIMELGDigQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFK 387
Cdd:COG0553 520 LLLEEGAELSGRSAKLEALLELL-EELLAEGE--KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQ 596

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 388 ---EClTQVLIATDVIARGFDQQRVNLVVNYNL---PTKYEtgepdyevylHRVGRAGRFGRKGAVF--NLLLDDGWDKE 459
Cdd:COG0553 597 egpEA-PVFLISLKAGGEGLNLTAADHVIHYDLwwnPAVEE----------QAIDRAHRIGQTRDVQvyKLVAEGTIEEK 665


                ....*..
gi 15231748 460 VMEKIEK 466
Cdd:COG0553 666 ILELLEE 672
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 236-444 2.92e-06

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 50.28  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   236 LNHLKIL---------VFDEAdHMLATDG--FRDD--SLKIMKdigRVNPNFQVLLFSATFNETVKDFVARTVKDPN--- 299
Cdd:PLN03137  570 LRHLENLnsrgllarfVIDEA-HCVSQWGhdFRPDyqGLGILK---QKFPNIPVLALTATATASVKEDVVQALGLVNcvv 645

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748   300 --QLFvKREDLaldsvkQYKVVcPKEQNKIEVIKDQIME--LGDIGqtIIFVKTKASAQKVHKALAEMGYDVTSVHGNLT 375
Cdd:PLN03137  646 frQSF-NRPNL------WYSVV-PKTKKCLEDIDKFIKEnhFDECG--IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMD 715

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231748   376 ESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPTKYETgepdyevYLHRVGRAGRFGRK 444
Cdd:PLN03137  716 PAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG-------YHQECGRAGRDGQR 777
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 377-448 3.88e-06

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: 44.62  E-value: 3.88e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231748 377 SDRDKIVKEFKECLtQVLIATDVIARGFDQQRVNLVVNYNLPtkyetgePDYEVYLHRVGRAGRFGRKGAVF 448
Cdd:cd18785  10 TNSIEHAEEIASSL-EILVATNVLGEGIDVPSLDTVIFFDPP-------SSAASYIQRVGRAGRGGKDEGEV 73
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 132-293 8.02e-06

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: 46.42  E-value: 8.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 132 KHLIAQAHNGSGKTTCFVLGMLSRVdptLREP--QALCICPTRELANQNMEVLQK--MGKFTGITAELAVPDSTRGAPAA 207
Cdd:cd17923  16 RSVVVTTGTASGKSLCYQLPILEAL---LRDPgsRALYLYPTKALAQDQLRSLREllEQLGLGIRVATYDGDTPREERRA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 208 TRGAPvsAHVVIGTPGTL--------KKWMAFkrlgLNHLKILVFDEAD----------HMLatdgfrddsLKIMKDIGR 269
Cdd:cd17923  93 IIRNP--PRILLTNPDMLhyallphhDRWARF----LRNLRYVVLDEAHtyrgvfgshvALL---------LRRLRRLCR 157

                       170       180
                ....*....|....*....|....*
gi 15231748 270 V-NPNFQVLLFSATFNEtVKDFVAR 293
Cdd:cd17923 158 RyGADPQFILTSATIGN-PAEHART 181
PRK01172 PRK01172
ATP-dependent DNA helicase;
236-442 9.00e-06

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 48.34  E-value: 9.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  236 LNHLKILVFDEAdHMLAtDGFRDDSLKIMKDIGR-VNPNFQVLLFSATF---NETVKDFVARTVKD-----PNQL-FVKR 305
Cdd:PRK01172 133 INDVGLIVADEI-HIIG-DEDRGPTLETVLSSARyVNPDARILALSATVsnaNELAQWLNASLIKSnfrpvPLKLgILYR 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  306 EDLALDSVKQYKVvcpkeqNKIEVIKDQImelGDIGQTIIFVKTKASAQKVHKALAEM---------------GYD---- 366
Cdd:PRK01172 211 KRLILDGYERSQV------DINSLIKETV---NDGGQVLVFVSSRKNAEDYAEMLIQHfpefndfkvssennnVYDdsln 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  367 ------VTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGfdqqrVNL---VVNYNLPTKYETgepDYEVYL----- 432
Cdd:PRK01172 282 emlphgVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAG-----VNLparLVIVRDITRYGN---GGIRYLsnmei 353

                        250
                 ....*....|.
gi 15231748  433 -HRVGRAGRFG 442
Cdd:PRK01172 354 kQMIGRAGRPG 364
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 365-464 1.95e-05

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: 44.64  E-value: 1.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 365 YDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNlPTKYETGEpdyevyLHRV-GRAGRfGR 443
Cdd:cd18811  62 LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED-AERFGLSQ------LHQLrGRVGR-GD 133

                        90       100
                ....*....|....*....|.
gi 15231748 444 KGAVFNLLLDDGWDKEVMEKI 464
Cdd:cd18811 134 HQSYCLLVYKDPLTETAKQRL 154
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 343-440 4.37e-05

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 42.93  E-value: 4.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 343 TIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRD--KIVKEFKECLT-QVLIATDVIARGFDQQRVNLVVnYNLPT 419
Cdd:cd18799   9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdeALILLFFGELKpPILVTVDLLTTGVDIPEVDNVV-FLRPT 87

                        90       100
                ....*....|....*....|.
gi 15231748 420 KYETgepdyeVYLHRVGRAGR 440
Cdd:cd18799  88 ESRT------LFLQMLGRGLR 102
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 141-267 6.23e-05

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 44.18  E-value: 6.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 141 GSGKTTCFVLG---MLSRVDPTLR-EPQALCICPTRELANQNMEVLQ-----KMGKFTGitaELAVPDSTRGApaaTRGA 211
Cdd:cd18034  26 GSGKTLIAVMLikeMGELNRKEKNpKKRAVFLVPTVPLVAQQAEAIRshtdlKVGEYSG---EMGVDKWTKER---WKEE 99

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15231748 212 PVSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATDGFRddslKIMKDI 267
Cdd:cd18034 100 LEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDECHHATGDHPYA----RIMKEF 151
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 352-416 1.83e-04

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: 41.87  E-value: 1.83e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231748 352 SAQKVHKALAEM--GYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYN 416
Cdd:cd18792  46 SIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED 112
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 141-283 2.34e-04

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 41.52  E-value: 2.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 141 GSGKTTCFVLGMLsrvdpTLREPQALCICPTRELANQNMEVLQK------MGKFTGitaelavpdstrGAPAATRGAPvs 214
Cdd:cd17926  28 GSGKTLTALALIA-----YLKELRTLIVVPTDALLDQWKERFEDflgdssIGLIGG------------GKKKDFDDAN-- 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231748 215 ahVVIGTPGTLKKWMAFKRLGLNHLKILVFDEAdHMLATDGFRddslKImkdIGRVNPNFQvLLFSATF 283
Cdd:cd17926  89 --VVVATYQSLSNLAEEEKDLFDQFGLLIVDEA-HHLPAKTFS----EI---LKELNAKYR-LGLTATP 146
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
 170-282 2.58e-04

DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 41.92  E-value: 2.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 170 PTRELANQNMEVLQK-MGKFTGITAELA--VPDSTRGAPAATRgapvsaHVVIGTPGTLKKWMAFKRLGLNHLKILVFDE 246
Cdd:cd18033  54 PTKPLVSQQIEACYKiTGIPSSQTAELTgsVPPTKRAELWASK------RVFFLTPQTLENDLKEGDCDPKSIVCLVIDE 127

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15231748 247 ADHmlATDGFRddSLKIMKDIGRVNPNFQVLLFSAT 282
Cdd:cd18033 128 AHR--ATGNYA--YCQVVRELMRYNSHFRILALTAT 159
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 314-451 3.28e-04

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 40.80  E-value: 3.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 314 KQYKVVCPKEQNKIEVIKDQIMELGDIGQT--IIFVKTKASAQKVHKALAEMGYDVTSV----HGN------LTESDRDK 381
Cdd:cd18801   2 RKVEKIHPKLEKLEEIVKEHFKKKQEGSDTrvIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASgksskgMSQKEQKE 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 382 IVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNlPTKYETGepdyevYLHRVGRAGRfGRKGAVFNLL 451
Cdd:cd18801  82 VIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPIR------MIQRMGRTGR-KRQGRVVVLL 143
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 141-247 3.52e-04

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: 43.29  E-value: 3.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 141 GSGKTTCFVLGMLSRVdptLREPQ--ALCICPTRELANQNMEVLQKMGKFTGITAELAV-----PDSTRgaPAATRgapv 213
Cdd:COG1205  81 ASGKSLAYLLPVLEAL---LEDPGatALYLYPTKALARDQLRRLRELAEALGLGVRVATydgdtPPEER--RWIRE---- 151

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15231748 214 SAHVVIGTP-----GTL---KKWMAFkrlgLNHLKILVFDEA 247
Cdd:COG1205 152 HPDIVLTNPdmlhyGLLphhTRWARF----FRNLRYVVIDEA 189
PRK13766 PRK13766
Hef nuclease; Provisional
 293-495 7.35e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 42.17  E-value: 7.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  293 RTVKDPNqlfVKRedlALDSVKQYKVVCPKEQNKIEVIKDQIMELGDiGQTIIFVKTKASAQKVHKALAEMGYDVTSVHG 372
Cdd:PRK13766 325 RLVEDPR---FRK---AVRKAKELDIEHPKLEKLREIVKEQLGKNPD-SRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVG 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  373 nltESDRD-----------KIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYnlptkyetgEPdyeV-----YLHRVG 436
Cdd:PRK13766 398 ---QASKDgdkgmsqkeqiEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFY---------EP---VpseirSIQRKG 462

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231748  437 RAGRfGRKGAVFNLL----LDDG--W---DKE-VMEKIEKYFEANVKEIKSW---NSEEEYKSALKEAGLLD 495
Cdd:PRK13766 463 RTGR-QEEGRVVVLIakgtRDEAyyWssrRKEkKMKEELKNLKGILNKKLQEldeEQKGEEEEKDEQLSLDD 533
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
 342-452 9.93e-04

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 39.55  E-value: 9.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 342 QTIIFVKTKASAQKVHKALAEM-------GYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVN 414
Cdd:cd18797  37 KTIVFCRSRKLAELLLRYLKARlveegplASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15231748 415 YNLPtkyetgePDYEVYLHRVGRAGRfGRKGAVFNLLL 452
Cdd:cd18797 117 AGYP-------GSLASLWQQAGRAGR-RGKDSLVILVA 146
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
 328-414 2.23e-03

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


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 38.48  E-value: 2.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 328 EVIKDQIM-ELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSV--HGNLTESDRDKIVKEFKECLTQVLIATDVIARGF 404
Cdd:cd18810  12 ELIREAIErELLRGGQVFYVHNRIESIEKLATQLRQLVPEARIAiaHGQMTENELEEVMLEFAKGEYDILVCTTIIESGI 91

                        90
                ....*....|.
gi 15231748 405 DQQRVN-LVVN 414
Cdd:cd18810  92 DIPNANtIIIE 102
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 233-442 3.76e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 39.70  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  233 RLGLNHLKILVFDEAdHMLATDG--FRDD--SLKIMKdigRVNPNFQVLLFSATFNETVKDFVARTVKDPNQLF----VK 304
Cdd:PRK11057 134 HLAHWNPALLAVDEA-HCISQWGhdFRPEyaALGQLR---QRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIqissFD 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748  305 REDLALDSVKQYKvvcPKEQnKIEVIKDQIMELGdigqtIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVK 384
Cdd:PRK11057 210 RPNIRYTLVEKFK---PLDQ-LMRYVQEQRGKSG-----IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQE 280

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231748  385 EFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPTKYETgepdyevYLHRVGRAGRFG 442
Cdd:PRK11057 281 AFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES-------YYQETGRAGRDG 331
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 132-246 4.23e-03

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: 38.49  E-value: 4.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 132 KHLIAQAHNGSGKTTCFVLGML----SRVDPTLREPQALCICPTRELANQNM-EVLQKMGKFTGITAELA---VPDSTRG 203
Cdd:cd18023  18 KNFVVSAPTGSGKTVLFELAILrllkERNPLPWGNRKVVYIAPIKALCSEKYdDWKEKFGPLGLSCAELTgdtEMDDTFE 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15231748 204 APaatrgapvSAHVVIGTPgtlKKWMAFKRLGLNH------LKILVFDE 246
Cdd:cd18023  98 IQ--------DADIILTTP---EKWDSMTRRWRDNgnlvqlVALVLIDE 135
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
351-400 5.11e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 39.65  E-value: 5.11e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15231748 351 ASAQKVHKALAEM--GYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVI 400
Cdd:COG1200 488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVI 539
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 303-447 5.78e-03

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 37.24  E-value: 5.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231748 303 VKREDLALDSVKQYKVVCPKEqnkiEVIKDQIMELGDIGQ----TIIFVKTKASAQKVHKALAEMGYDVTSV------HG 372
Cdd:cd18796   1 KKKLDIKVILPVAPEIFPWAG----ESGADAYAEVIFLLErhksTLVFTNTRSQAERLAQRLRELCPDRVPPdfialhHG 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231748 373 NLTESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPtkyetgepdYEV--YLHRVGRAGRfgRKGAV 447
Cdd:cd18796  77 SLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP---------KSVarLLQRLGRSGH--RPGAA 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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