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Conserved domains on  [gi|164419732|ref|NP_037396|]
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ATP-dependent RNA helicase DDX25 isoform 1 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030634)

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_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
80-308 3.05e-166

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: 467.96  E-value: 3.05e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  80 HRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLS 159
Cdd:cd18048    1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 160 RVNALELFPQCLCLAPTYELALQTGRVVEQMGKFCVDVQVMYAIRGNRIPRGTDITKQIIIGTPGTVLDWCFKLKLIDLT 239
Cdd:cd18048   81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164419732 240 KIRVFVLDEADVMIDTQGFSDHSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELT 308
Cdd:cd18048  161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
312-448 1.31e-50

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


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 168.45  E-value: 1.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 312 IRQYYVLCEHRKDKYQALCNIYGSITIGQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKV 391
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 164419732 392 LITTNVCARGIDVKQVTIVVNFDLPvkqgeePDYETYLHRIGRTGRFGKKGLAFNMI 448
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLP------RDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
80-308 3.05e-166

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: 467.96  E-value: 3.05e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  80 HRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLS 159
Cdd:cd18048    1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 160 RVNALELFPQCLCLAPTYELALQTGRVVEQMGKFCVDVQVMYAIRGNRIPRGTDITKQIIIGTPGTVLDWCFKLKLIDLT 239
Cdd:cd18048   81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164419732 240 KIRVFVLDEADVMIDTQGFSDHSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELT 308
Cdd:cd18048  161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
114-482 3.88e-116

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 347.90  E-value: 3.88e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 114 AMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNA-LELFPQCLCLAPTYELALQTGRVVEQMGK 192
Cdd:COG0513   19 ELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPTRELALQVAEELRKLAK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 193 FC-VDVQVMYairGnriprGTDITKQ---------IIIGTPGTVLDWcFKLKLIDLTKIRVFVLDEADVMIDtQGFSDHS 262
Cdd:COG0513   97 YLgLRVATVY---G-----GVSIGRQiralkrgvdIVVATPGRLLDL-IERGALDLSGVETLVLDEADRMLD-MGFIEDI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 263 IRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELTLNNIRQYYVLCEHRkDKYQALCNIYGSITIGQAI 342
Cdd:COG0513  167 ERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR-DKLELLRRLLRDEDPERAI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 343 IFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPvkqgee 422
Cdd:COG0513  246 VFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP------ 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 423 PDYETYLHRIGRTGRFGKKGLAFNMIEVDELPSLMKIQDHFNSSIKQLNAEDMDEIEKID 482
Cdd:COG0513  320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKR 379
PTZ00424 PTZ00424
helicase 45; Provisional
111-476 7.17e-96

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 295.20  E-value: 7.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQM 190
Cdd:PTZ00424  42 GIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLAL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 191 GKFCvDVQVmYAIRGNRIPRgTDITK-----QIIIGTPGTVLDWCFKlKLIDLTKIRVFVLDEADVMIdTQGFSDHSIRI 265
Cdd:PTZ00424 120 GDYL-KVRC-HACVGGTVVR-DDINKlkagvHMVVGTPGRVYDMIDK-RHLRVDDLKLFILDEADEML-SRGFKGQIYDV 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 266 QRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELTLNNIRQYYVLCEHRKDKYQALCNIYGSITIGQAIIFC 345
Cdd:PTZ00424 195 FKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYC 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 346 QTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVKQgeepdy 425
Cdd:PTZ00424 275 NTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP------ 348
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164419732 426 ETYLHRIGRTGRFGKKGLAFNMIEVDELPSLMKIQDHFNSSIKQLNAEDMD 476
Cdd:PTZ00424 349 ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVAD 399
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
312-448 1.31e-50

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 168.45  E-value: 1.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 312 IRQYYVLCEHRKDKYQALCNIYGSITIGQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKV 391
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 164419732 392 LITTNVCARGIDVKQVTIVVNFDLPvkqgeePDYETYLHRIGRTGRFGKKGLAFNMI 448
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLP------RDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
121-286 4.06e-36

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: 131.21  E-value: 4.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  121 SKIQEMALPmmLAHPPQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQMGKFcVDVQVM 200
Cdd:pfam00270   1 TPIQAEAIP--AILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKG-LGLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  201 YAIRGNRIP--RGTDITKQIIIGTPGTVLDWCFKLKLIDltKIRVFVLDEADVMIDtQGFSDHSIRIQRALPSECQMLLF 278
Cdd:pfam00270  78 SLLGGDSRKeqLEKLKGPDILVGTPGRLLDLLQERKLLK--NLKLLVLDEAHRLLD-MGFGPDLEEILRRLPKKRQILLL 154

                  ....*...
gi 164419732  279 SATFEDSV 286
Cdd:pfam00270 155 SATLPRNL 162
DEXDc smart00487
DEAD-like helicases superfamily;
112-315 2.23e-34

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 127.99  E-value: 2.23e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732   112 IYAMGFNRPSKIQEMALPMMLAHPpQNLIAQSQSGTGKTAAFVLAMLSRVNAlELFPQCLCLAPTYELALQTGRVVEQMG 191
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732   192 KFCVDVQVMYAIRGNRIPRGTDITK---QIIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMIDtQGFSDHSIRIQRA 268
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLD-LLENDKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 164419732   269 LPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLrkEELTLNNIRQY 315
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
324-439 7.26e-30

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 112.30  E-value: 7.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  324 DKYQALCNIYGSITIGQAIIFCQTRRNAKwLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGID 403
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 164419732  404 VKQVTIVVNFDLPvkqgeePDYETYLHRIGRTGRFG 439
Cdd:pfam00271  80 LPDVDLVINYDLP------WNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
352-439 1.30e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 1.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732   352 KWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVkqgeepDYETYLHR 431
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPW------SPASYIQR 74

                   ....*...
gi 164419732   432 IGRTGRFG 439
Cdd:smart00490  75 IGRAGRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
290-441 1.93e-10

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 63.21  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 290 AERIIPDPNVIKLRK--EELTLnnirqyyvlcEHRKDKY--QALCNIYGSITIGQAIIFCQTRRnakwlTVEMI-----Q 360
Cdd:COG1111  311 SKRLVSDPRFRKAMRlaEEADI----------EHPKLSKlrEILKEQLGTNPDSRIIVFTQYRD-----TAEMIveflsE 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 361 DGHQVSLLSGE--------LTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDlPVkqgeePDYETYLHRI 432
Cdd:COG1111  376 PGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PV-----PSEIRSIQRK 449

                 ....*....
gi 164419732 433 GRTGRFGKK 441
Cdd:COG1111  450 GRTGRKREG 458
PRK13766 PRK13766
Hef nuclease; Provisional
290-437 3.37e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 43.32  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 290 AERIIPDPNVIKL--RKEELTLnnirqyyvlcEHrkDKYQALCNIYGSITIGQ----AIIFCQTRRNAKWLTVEMIQDG- 362
Cdd:PRK13766 323 SKRLVEDPRFRKAvrKAKELDI----------EH--PKLEKLREIVKEQLGKNpdsrIIVFTQYRDTAEKIVDLLEKEGi 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 363 ------HQVSLLSGE-LTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVnFDLPVkqgeePDYETYLHRIGRT 435
Cdd:PRK13766 391 kavrfvGQASKDGDKgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRSIQRKGRT 464

                 ..
gi 164419732 436 GR 437
Cdd:PRK13766 465 GR 466
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
80-308 3.05e-166

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: 467.96  E-value: 3.05e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  80 HRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLS 159
Cdd:cd18048    1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 160 RVNALELFPQCLCLAPTYELALQTGRVVEQMGKFCVDVQVMYAIRGNRIPRGTDITKQIIIGTPGTVLDWCFKLKLIDLT 239
Cdd:cd18048   81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164419732 240 KIRVFVLDEADVMIDTQGFSDHSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELT 308
Cdd:cd18048  161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
111-301 5.85e-120

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: 349.18  E-value: 5.85e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQM 190
Cdd:cd17963    8 GLYAMGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQIGEVVEKM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 191 GKFCvDVQVMYAIRGNRIPRGTDITKQIIIGTPGTVLDWCFKlKLIDLTKIRVFVLDEADVMIDTQGFSDHSIRIQRALP 270
Cdd:cd17963   88 GKFT-GVKVALAVPGNDVPRGKKITAQIVIGTPGTVLDWLKK-RQLDLKKIKILVLDEADVMLDTQGHGDQSIRIKRMLP 165
                        170       180       190
                 ....*....|....*....|....*....|.
gi 164419732 271 SECQMLLFSATFEDSVWHFAERIIPDPNVIK 301
Cdd:cd17963  166 RNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
114-482 3.88e-116

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 347.90  E-value: 3.88e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 114 AMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNA-LELFPQCLCLAPTYELALQTGRVVEQMGK 192
Cdd:COG0513   19 ELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPTRELALQVAEELRKLAK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 193 FC-VDVQVMYairGnriprGTDITKQ---------IIIGTPGTVLDWcFKLKLIDLTKIRVFVLDEADVMIDtQGFSDHS 262
Cdd:COG0513   97 YLgLRVATVY---G-----GVSIGRQiralkrgvdIVVATPGRLLDL-IERGALDLSGVETLVLDEADRMLD-MGFIEDI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 263 IRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELTLNNIRQYYVLCEHRkDKYQALCNIYGSITIGQAI 342
Cdd:COG0513  167 ERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR-DKLELLRRLLRDEDPERAI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 343 IFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPvkqgee 422
Cdd:COG0513  246 VFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP------ 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 423 PDYETYLHRIGRTGRFGKKGLAFNMIEVDELPSLMKIQDHFNSSIKQLNAEDMDEIEKID 482
Cdd:COG0513  320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKR 379
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
97-301 6.04e-107

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: 316.66  E-value: 6.04e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  97 KTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPT 176
Cdd:cd18047    1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 177 YELALQTGRVVEQMGKFCVDVQVMYAIRGNRIPRGTDITKQIIIGTPGTVLDWCFKLKLIDLTKIRVFVLDEADVMIDTQ 256
Cdd:cd18047   81 YELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQ 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 164419732 257 GFSDHSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIK 301
Cdd:cd18047  161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
PTZ00424 PTZ00424
helicase 45; Provisional
111-476 7.17e-96

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 295.20  E-value: 7.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQM 190
Cdd:PTZ00424  42 GIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLAL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 191 GKFCvDVQVmYAIRGNRIPRgTDITK-----QIIIGTPGTVLDWCFKlKLIDLTKIRVFVLDEADVMIdTQGFSDHSIRI 265
Cdd:PTZ00424 120 GDYL-KVRC-HACVGGTVVR-DDINKlkagvHMVVGTPGRVYDMIDK-RHLRVDDLKLFILDEADEML-SRGFKGQIYDV 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 266 QRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELTLNNIRQYYVLCEHRKDKYQALCNIYGSITIGQAIIFC 345
Cdd:PTZ00424 195 FKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYC 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 346 QTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVKQgeepdy 425
Cdd:PTZ00424 275 NTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP------ 348
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164419732 426 ETYLHRIGRTGRFGKKGLAFNMIEVDELPSLMKIQDHFNSSIKQLNAEDMD 476
Cdd:PTZ00424 349 ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVAD 399
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
114-468 4.05e-65

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 217.36  E-value: 4.05e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 114 AMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELAlqtgrvveqmgkf 193
Cdd:PRK11776  21 ELGYTEMTPIQAQSLPAILAG--KDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELA------------- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 194 cvDvQVMYAIRgnRIPRGTDITK---------------------QIIIGTPGTVLDWCFKLKLiDLTKIRVFVLDEADVM 252
Cdd:PRK11776  86 --D-QVAKEIR--RLARFIPNIKvltlcggvpmgpqidslehgaHIIVGTPGRILDHLRKGTL-DLDALNTLVLDEADRM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 253 IDtQGFSDHSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEElTLNNIRQYYVLCEhRKDKYQALCNI 332
Cdd:PRK11776 160 LD-MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH-DLPAIEQRFYEVS-PDERLPALQRL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 333 YGSITIGQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELtvEQ--RASIIQRFRDGKEKVLITTNVCARGIDVKQVTIV 410
Cdd:PRK11776 237 LLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDL--EQrdRDQVLVRFANRSCSVLVATDVAARGLDIKALEAV 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164419732 411 VNFDLPvkqgeePDYETYLHRIGRTGRFGKKGLAFNMIEVDELPSLMKIQDHFNSSIK 468
Cdd:PRK11776 315 INYELA------RDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
114-468 4.66e-62

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 208.26  E-value: 4.66e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 114 AMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRvnaLELFPQ-------CLCLAPTYELALQTGRV 186
Cdd:PRK11192  18 DKGYTRPTAIQAEAIPPALDG--RDVLGSAPTGTGKTAAFLLPALQH---LLDFPRrksgpprILILTPTRELAMQVADQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 187 VEQMGKFC-VDVQVmyaIRGNrIPRGT--DI---TKQIIIGTPGTVLDWcFKLKLIDLTKIRVFVLDEADVMIDtQGFSD 260
Cdd:PRK11192  93 ARELAKHThLDIAT---ITGG-VAYMNhaEVfseNQDIVVATPGRLLQY-IKEENFDCRAVETLILDEADRMLD-MGFAQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 261 HSIRIQralpSEC----QMLLFSATFE-DSVWHFAERIIPDPNVIKL---RKEEltlNNIRQYYVLCEHRKDKYQALCNI 332
Cdd:PRK11192 167 DIETIA----AETrwrkQTLLFSATLEgDAVQDFAERLLNDPVEVEAepsRRER---KKIHQWYYRADDLEHKTALLCHL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 333 YGSITIGQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVN 412
Cdd:PRK11192 240 LKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVIN 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 164419732 413 FDLPVKQgeepdyETYLHRIGRTGRFGKKGLAFNMIEVDELPSLMKIQDHFNSSIK 468
Cdd:PRK11192 320 FDMPRSA------DTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLK 369
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
115-473 2.62e-57

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 200.46  E-value: 2.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 115 MGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQMGKFC 194
Cdd:PRK11634  24 LGYEKPSPIQAECIPHLLNG--RDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHM 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 195 VDVQVMYAIRGNRIP---RGTDITKQIIIGTPGTVLDWcFKLKLIDLTKIRVFVLDEADVMIdTQGFSDHSIRIQRALPS 271
Cdd:PRK11634 102 RGVNVVALYGGQRYDvqlRALRQGPQIVVGTPGRLLDH-LKRGTLDLSKLSGLVLDEADEML-RMGFIEDVETIMAQIPE 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 272 ECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELTLNNIRQ-YYVLCEHRKDkyQALCNIYGSITIGQAIIFCQTRrN 350
Cdd:PRK11634 180 GHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQsYWTVWGMRKN--EALVRFLEAEDFDAAIIFVRTK-N 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 351 AKWLTVEMIQ-DGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVkqgeepDYETYL 429
Cdd:PRK11634 257 ATLEVAEALErNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM------DSESYV 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 164419732 430 HRIGRTGRFGKKGLAFNMIEVDELPSLMKIQDHFNSSIKQL---NAE 473
Cdd:PRK11634 331 HRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVelpNAE 377
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
112-468 5.17e-56

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 193.59  E-value: 5.17e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 112 IYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNAL----ELF---PQCLCLAPTYELALQTG 184
Cdd:PRK01297 102 IHDLGFPYCTPIQAQVLGYTLAG--HDAIGRAQTGTGKTAAFLISIINQLLQTpppkERYmgePRALIIAPTRELVVQIA 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 185 RVVEQMGKFcVDVQVMYAIRGnriprgTDITKQ----------IIIGTPGTVLDWCfKLKLIDLTKIRVFVLDEADVMID 254
Cdd:PRK01297 180 KDAAALTKY-TGLNVMTFVGG------MDFDKQlkqlearfcdILVATPGRLLDFN-QRGEVHLDMVEVMVLDEADRMLD 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 255 tQGFSDHSIRIQRALP--SECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELTLNNIRQYyVLCEHRKDKYQALCNI 332
Cdd:PRK01297 252 -MGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQH-VYAVAGSDKYKLLYNL 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 333 YGSITIGQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVN 412
Cdd:PRK01297 330 VTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVIN 409
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 164419732 413 FDLPvkqgEEPDyeTYLHRIGRTGRFGKKGLAFNMIEVDELPSLMKIQDHFNSSIK 468
Cdd:PRK01297 410 FTLP----EDPD--DYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS 459
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
114-301 1.13e-52

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: 176.09  E-value: 1.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 114 AMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALEL----FPQCLCLAPTYELALQTGRVVEQ 189
Cdd:cd00268    7 KLGFEKPTPIQAQAIPLILSG--RDVIGQAQTGSGKTLAFLLPILEKLLPEPKkkgrGPQALVLAPTRELAMQIAEVARK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 190 MGKFCvDVQVMyAIRGnriprGTDITKQ---------IIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMIDtQGFSD 260
Cdd:cd00268   85 LGKGT-GLKVA-AIYG-----GAPIKKQiealkkgpdIVVGTPGRLLD-LIERGKLDLSNVKYLVLDEADRMLD-MGFEE 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 164419732 261 HSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIK 301
Cdd:cd00268  156 DVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
116-460 7.15e-52

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 181.93  E-value: 7.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 116 GFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQ------CLCLAPTYELALQTGRVVEQ 189
Cdd:PRK10590  20 GYREPTPIQQQAIPAVLEG--RDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrALILTPTRELAAQIGENVRD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 190 MGKF------------CVDVQVMyAIRGnriprGTDItkqiIIGTPGTVLDWCFKlKLIDLTKIRVFVLDEADVMIDtQG 257
Cdd:PRK10590  98 YSKYlnirslvvfggvSINPQMM-KLRG-----GVDV----LVATPGRLLDLEHQ-NAVKLDQVEILVLDEADRMLD-MG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 258 FSdHSIR-IQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELTLNNIRQYYVLCEhRKDKYQALCNIYGSI 336
Cdd:PRK10590 166 FI-HDIRrVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVD-KKRKRELLSQMIGKG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 337 TIGQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLP 416
Cdd:PRK10590 244 NWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELP 323
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 164419732 417 vkqgEEPdyETYLHRIGRTGRFGKKGLAFNMIEVDELPSLMKIQ 460
Cdd:PRK10590 324 ----NVP--EDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIE 361
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
312-448 1.31e-50

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 168.45  E-value: 1.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 312 IRQYYVLCEHRKDKYQALCNIYGSITIGQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKV 391
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 164419732 392 LITTNVCARGIDVKQVTIVVNFDLPvkqgeePDYETYLHRIGRTGRFGKKGLAFNMI 448
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLP------RDAEDYVHRIGRTGRAGRKGTAITFV 131
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
92-444 8.78e-48

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 173.60  E-value: 8.78e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  92 PLYSVkTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLahPPQNLIAQSQSGTGKTAAFVLAMLSR-------VNAL 164
Cdd:PRK04537   5 PLTDL-TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVAL--PGGDVAGQAQTGTGKTLAFLVAVMNRllsrpalADRK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 165 ELFPQCLCLAPTYELALQtgrVVEQMGKFCVDVQVMYAIrgnrIPRGTDITKQ---------IIIGTPGTVLDWCFKLKL 235
Cdd:PRK04537  82 PEDPRALILAPTRELAIQ---IHKDAVKFGADLGLRFAL----VYGGVDYDKQrellqqgvdVIIATPGRLIDYVKQHKV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 236 IDLTKIRVFVLDEADVMIDTQGFSDhsIR-IQRALPSEC--QMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELTLNNI 312
Cdd:PRK04537 155 VSLHACEICVLDEADRMFDLGFIKD--IRfLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 313 RQ--YYVLCEhrkDKYQALCNIYGSITIGQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEK 390
Cdd:PRK04537 233 RQriYFPADE---EKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLE 309
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 164419732 391 VLITTNVCARGIDVKQVTIVVNFDLPVkqgeepDYETYLHRIGRTGRFGKKGLA 444
Cdd:PRK04537 310 ILVATDVAARGLHIDGVKYVYNYDLPF------DAEDYVHRIGRTARLGEEGDA 357
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
111-444 9.77e-47

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 167.46  E-value: 9.77e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLA----MLS-------RVNAlelfPQCLCLAPTYEL 179
Cdd:PRK04837  22 ALEKKGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAFLTAtfhyLLShpapedrKVNQ----PRALIMAPTREL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 180 ALQTGRVVEQMGKFC-VDVQVMYAIRG-----NRIPRGTDItkqiIIGTPGTVLDWcFKLKLIDLTKIRVFVLDEADVMI 253
Cdd:PRK04837  96 AVQIHADAEPLAQATgLKLGLAYGGDGydkqlKVLESGVDI----LIGTTGRLIDY-AKQNHINLGAIQVVVLDEADRMF 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 254 DTqGFSDhSIR-IQRALPSECQML--LFSATFEDSVWHFAERIIPDPNVIKLRKEELTLNNIRQ--YYVLCEhrkDKYQA 328
Cdd:PRK04837 171 DL-GFIK-DIRwLFRRMPPANQRLnmLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNE---EKMRL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 329 LCNIYGSITIGQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVT 408
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 164419732 409 IVVNFDLPvkqgeePDYETYLHRIGRTGRFGKKGLA 444
Cdd:PRK04837 326 HVFNYDLP------DDCEDYVHRIGRTGRAGASGHS 355
PTZ00110 PTZ00110
helicase; Provisional
112-452 1.77e-45

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 166.49  E-value: 1.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 112 IYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELF-----PQCLCLAPTYELALQtgrV 186
Cdd:PTZ00110 145 LKNAGFTEPTPIQVQGWPIALSG--RDMIGIAETGSGKTLAFLLPAIVHINAQPLLrygdgPIVLVLAPTRELAEQ---I 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 187 VEQMGKFCVDVQVMYAIRGNRIPRGTDITK-----QIIIGTPGTVLDWcFKLKLIDLTKIRVFVLDEADVMIDtQGFSDH 261
Cdd:PTZ00110 220 REQCNKFGASSKIRNTVAYGGVPKRGQIYAlrrgvEILIACPGRLIDF-LESNVTNLRRVTYLVLDEADRMLD-MGFEPQ 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 262 SIRIQRALPSECQMLLFSATFEDSVWHFAeRIIPDPNVIKLRKEELTL---NNIRQY-YVLCEHrkDKYQALCNIYGSIT 337
Cdd:PTZ00110 298 IRKIVSQIRPDRQTLMWSATWPKEVQSLA-RDLCKEEPVHVNVGSLDLtacHNIKQEvFVVEEH--EKRGKLKMLLQRIM 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 338 I--GQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDL 415
Cdd:PTZ00110 375 RdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDF 454
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 164419732 416 PVKqgeepdYETYLHRIGRTGRFGKKGLAFNMIEVDE 452
Cdd:PTZ00110 455 PNQ------IEDYVHRIGRTGRAGAKGASYTFLTPDK 485
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
111-300 5.95e-44

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: 153.61  E-value: 5.95e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQM 190
Cdd:cd17940   13 GIFEKGFEKPSPIQEESIPIALSG--RDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELALQTSQVCKEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 191 GKFCvDVQVMYAIRG-------NRIPRGTditkQIIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMIDtQGFSDHSI 263
Cdd:cd17940   91 GKHM-GVKVMVTTGGtslrddiMRLYQTV----HVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLS-QDFQPIIE 163
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 164419732 264 RIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVI 300
Cdd:cd17940  164 KILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
111-300 4.49e-43

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 150.94  E-value: 4.49e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMA-LPMMLAHppqNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQ 189
Cdd:cd17939   11 GIYAYGFEKPSAIQQRAiVPIIKGR---DVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 190 MGKFcVDVQVMYAIRGNRIprGTDITK-----QIIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMIDtQGFSDHSIR 264
Cdd:cd17939   88 LGDY-MGVKVHACIGGTSV--REDRRKlqygpHIVVGTPGRVFD-MLQRRSLRTDKIKMFVLDEADEMLS-RGFKDQIYD 162
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 164419732 265 IQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVI 300
Cdd:cd17939  163 IFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
112-444 4.31e-37

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 143.00  E-value: 4.31e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 112 IYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELF-------PQCLCLAPTYELALQTG 184
Cdd:PLN00206 136 LETAGYEFPTPIQMQAIPAALSG--RSLLVSADTGSGKTASFLVPIISRCCTIRSGhpseqrnPLAMVLTPTRELCVQVE 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 185 RVVEQMGKfCVDVQVMYAIRGNRIPRGTDITKQ---IIIGTPGTVLDWCFKLKlIDLTKIRVFVLDEADVMIDtQGFSDH 261
Cdd:PLN00206 214 DQAKVLGK-GLPFKTALVVGGDAMPQQLYRIQQgveLIVGTPGRLIDLLSKHD-IELDNVSVLVLDEVDCMLE-RGFRDQ 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 262 SIRIQRALpSECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELTLNNIRQYYVLCEhRKDKYQALCNIYGSITIGQ- 340
Cdd:PLN00206 291 VMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVE-TKQKKQKLFDILKSKQHFKp 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 341 -AIIFCQTRRNAKWLTVEM-IQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVK 418
Cdd:PLN00206 369 pAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNT 448
                        330       340
                 ....*....|....*....|....*.
gi 164419732 419 QGEepdyetYLHRIGRTGRFGKKGLA 444
Cdd:PLN00206 449 IKE------YIHQIGRASRMGEKGTA 468
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
111-297 1.81e-36

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: 133.34  E-value: 1.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMA-LPMMLAHppqNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQ 189
Cdd:cd18046   13 GIYAYGFEKPSAIQQRAiMPCIKGY---DVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELAQQIQKVVMA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 190 MGKFCvDVQVMYAIRGNRI---PRGTDITKQIIIGTPGTVLDWCFKlKLIDLTKIRVFVLDEADVMIdTQGFSDHSIRIQ 266
Cdd:cd18046   90 LGDYM-GIKCHACIGGTSVrddAQKLQAGPHIVVGTPGRVFDMINR-RYLRTDYIKMFVLDEADEML-SRGFKDQIYDIF 166
                        170       180       190
                 ....*....|....*....|....*....|.
gi 164419732 267 RALPSECQMLLFSATFEDSVWHFAERIIPDP 297
Cdd:cd18046  167 QKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
121-286 4.06e-36

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: 131.21  E-value: 4.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  121 SKIQEMALPmmLAHPPQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQMGKFcVDVQVM 200
Cdd:pfam00270   1 TPIQAEAIP--AILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKG-LGLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  201 YAIRGNRIP--RGTDITKQIIIGTPGTVLDWCFKLKLIDltKIRVFVLDEADVMIDtQGFSDHSIRIQRALPSECQMLLF 278
Cdd:pfam00270  78 SLLGGDSRKeqLEKLKGPDILVGTPGRLLDLLQERKLLK--NLKLLVLDEAHRLLD-MGFGPDLEEILRRLPKKRQILLL 154

                  ....*...
gi 164419732  279 SATFEDSV 286
Cdd:pfam00270 155 SATLPRNL 162
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
111-301 3.08e-35

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


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 129.69  E-value: 3.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQM 190
Cdd:cd17943    4 GLKAAGFQRPSPIQLAAIPLGLAG--HDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 191 GKFCVDVQVMYAIRGnrIPRGTDITK----QIIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMIDtQGFSDHSIRIQ 266
Cdd:cd17943   82 GKKLEGLKCEVFIGG--TPVKEDKKKlkgcHIAVGTPGRIKQ-LIELGALNVSHVRLFVLDEADKLME-GSFQKDVNWIF 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 164419732 267 RALPSECQMLLFSATFEDSVWHFAERIIPDPNVIK 301
Cdd:cd17943  158 SSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEXDc smart00487
DEAD-like helicases superfamily;
112-315 2.23e-34

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 127.99  E-value: 2.23e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732   112 IYAMGFNRPSKIQEMALPMMLAHPpQNLIAQSQSGTGKTAAFVLAMLSRVNAlELFPQCLCLAPTYELALQTGRVVEQMG 191
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732   192 KFCVDVQVMYAIRGNRIPRGTDITK---QIIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMIDtQGFSDHSIRIQRA 268
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLD-LLENDKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 164419732   269 LPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLrkEELTLNNIRQY 315
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
111-300 7.82e-34

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


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 126.43  E-value: 7.82e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQM 190
Cdd:cd18045   13 GIYAYGFEKPSAIQQRAIKPIIKG--RDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELAVQIQKVLLAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 191 GKFcVDVQVMYAIRGNRIprGTDITK-----QIIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMIdTQGFSDHSIRI 265
Cdd:cd18045   91 GDY-MNVQCHACIGGTSV--GDDIRKldygqHIVSGTPGRVFD-MIRRRSLRTRHIKMLVLDEADEML-NKGFKEQIYDV 165
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 164419732 266 QRALPSECQMLLFSATFEDSVWHFAERIIPDPNVI 300
Cdd:cd18045  166 YRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
111-301 1.66e-32

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: 122.80  E-value: 1.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAhpPQNLIAQSQSGTGKTAAFVLAMLSRVNALElfPQ----CLCLAPTYELALQTGRV 186
Cdd:cd17959   15 AIKKKGYKVPTPIQRKTIPLILD--GRDVVAMARTGSGKTAAFLIPMIEKLKAHS--PTvgarALILSPTRELALQTLKV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 187 VEQMGKFcVDVQVMYAIRGNRIPRG-TDITKQ--IIIGTPGTVLDWCFKLKLiDLTKIRVFVLDEADVMIDtQGFSDHSI 263
Cdd:cd17959   91 TKELGKF-TDLRTALLVGGDSLEEQfEALASNpdIIIATPGRLLHLLVEMNL-KLSSVEYVVFDEADRLFE-MGFAEQLH 167
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 164419732 264 RIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIK 301
Cdd:cd17959  168 EILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
111-286 3.37e-30

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: 116.20  E-value: 3.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVnaleLF-------PQCLCLAPTYELALQT 183
Cdd:cd17947    4 ALSSLGFTKPTPIQAAAIPLALLG--KDICASAVTGSGKTAAFLLPILERL----LYrpkkkaaTRVLVLVPTRELAMQC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 184 GRVVEQMGKFCvDVQVMYAIrGnriprGTDITKQ---------IIIGTPGTVLDWCFKLKLIDLTKIRVFVLDEADVMID 254
Cdd:cd17947   78 FSVLQQLAQFT-DITFALAV-G-----GLSLKAQeaalrarpdIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLE 150
                        170       180       190
                 ....*....|....*....|....*....|..
gi 164419732 255 TqGFSDHSIRIQRALPSECQMLLFSATFEDSV 286
Cdd:cd17947  151 E-GFADELKEILRLCPRTRQTMLFSATMTDEV 181
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
324-439 7.26e-30

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 112.30  E-value: 7.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  324 DKYQALCNIYGSITIGQAIIFCQTRRNAKwLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGID 403
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 164419732  404 VKQVTIVVNFDLPvkqgeePDYETYLHRIGRTGRFG 439
Cdd:pfam00271  80 LPDVDLVINYDLP------WNPASYIQRIGRAGRAG 109
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
82-290 4.16e-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: 112.37  E-value: 4.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732  82 VEVLQKDPSSPlysVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAML--- 158
Cdd:cd18052   31 VEVTGRNPPPA---ILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPVLtgm 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 159 -------SRVNALELfPQCLCLAPTYELALQtgrVVEQMGKFCVD-----------VQVMYAIRgnRIPRGTDitkqIII 220
Cdd:cd18052  106 mkegltaSSFSEVQE-PQALIVAPTRELANQ---IFLEARKFSYGtcirpvvvyggVSVGHQIR--QIEKGCH----ILV 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164419732 221 GTPGTVLDWCFKLKlIDLTKIRVFVLDEADVMIDtQGFSD--HSIRIQRALPS--ECQMLLFSATFEDSVWHFA 290
Cdd:cd18052  176 ATPGRLLDFIGRGK-ISLSKLKYLILDEADRMLD-MGFGPeiRKLVSEPGMPSkeDRQTLMFSATFPEEIQRLA 247
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
115-290 9.23e-28

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: 110.27  E-value: 9.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 115 MGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRV--NALEL--------FPQCLCLAPTYELALQTG 184
Cdd:cd17967   18 AGYTKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPIISKLleDGPPSvgrgrrkaYPSALILAPTRELAIQIY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 185 RVVEqmgKFC----VDVQVMY---AIRG--NRIPRGTDItkqiIIGTPGTVLDWCFKLKlIDLTKIRVFVLDEADVMIDt 255
Cdd:cd17967   96 EEAR---KFSyrsgVRSVVVYggaDVVHqqLQLLRGCDI----LVATPGRLVDFIERGR-ISLSSIKFLVLDEADRMLD- 166
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 164419732 256 QGFSDHSIRI--QRALPS--ECQMLLFSATFEDSVWHFA 290
Cdd:cd17967  167 MGFEPQIRKIveHPDMPPkgERQTLMFSATFPREIQRLA 205
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
115-286 2.59e-27

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: 108.56  E-value: 2.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 115 MGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLsrvNALELFPQ---CLCLAPTYELALQTGRVVEQMG 191
Cdd:cd17954   18 LGWKKPTKIQEEAIPVALQG--RDIIGLAETGSGKTAAFALPIL---QALLENPQrffALVLAPTRELAQQISEQFEALG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 192 KfcvDVQVMYAIrgnrIPRGTDITKQ---------IIIGTPGTVLDWCFKLKLIDLTKIRVFVLDEADVMIDTQgFSDHS 262
Cdd:cd17954   93 S---SIGLKSAV----LVGGMDMMAQaialakkphVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLNMD-FEPEI 164
                        170       180
                 ....*....|....*....|....
gi 164419732 263 IRIQRALPSECQMLLFSATFEDSV 286
Cdd:cd17954  165 DKILKVIPRERTTYLFSATMTTKV 188
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
111-300 7.88e-27

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: 107.28  E-value: 7.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAhPPQNLIAQSQSGTGKTAAFVLAMLSRVnaLELFPQ-------CLCLAPTYELALQT 183
Cdd:cd17964    8 ALTRMGFETMTPVQQKTLKPILS-TGDDVLARAKTGTGKTLAFLLPAIQSL--LNTKPAgrrsgvsALIISPTRELALQI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 184 GRVVEQMGKFCVDVQVMYAIRGNRIPRGT-DITKQ---IIIGTPGTVLDWCFK-LKLIDLTKIRVFVLDEADVMIDtQGF 258
Cdd:cd17964   85 AAEAKKLLQGLRKLRVQSAVGGTSRRAELnRLRRGrpdILVATPGRLIDHLENpGVAKAFTDLDYLVLDEADRLLD-MGF 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 164419732 259 SDHSIRIQRALPSEC----QMLLFSATFEDSVWHFAERII-PDPNVI 300
Cdd:cd17964  164 RPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTLkKDYKFI 210
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
111-302 1.07e-26

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: 106.90  E-value: 1.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRV------NALELFPQCLCLAPTYELALQTG 184
Cdd:cd17961    8 AIAKLGWEKPTLIQSKAIPLALEG--KDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQVS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 185 RVVEQMGKFC-VDVQVMyAIRGNriprgTDITKQ---------IIIGTPGTVLDWCFKLKLIDLTKIRVFVLDEADVMId 254
Cdd:cd17961   86 KVLEQLTAYCrKDVRVV-NLSAS-----SSDSVQrallaekpdIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVL- 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 164419732 255 TQGFSDHSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIKL 302
Cdd:cd17961  159 SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
116-297 1.20e-26

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: 106.66  E-value: 1.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 116 GFNRPSKIQEMALPM-MLAHppqNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQMGKFC 194
Cdd:cd17950   21 GFEHPSEVQHECIPQaILGM---DVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISNEYERFSKYM 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 195 VDVQVMYAIRGNRIPRGTDITK----QIIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMIDTQGFSDHSIRIQRALP 270
Cdd:cd17950   98 PNVKTAVFFGGVPIKKDIEVLKnkcpHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDKMLEQLDMRRDVQEIFRATP 176
                        170       180
                 ....*....|....*....|....*..
gi 164419732 271 SECQMLLFSATFEDSVWHFAERIIPDP 297
Cdd:cd17950  177 HDKQVMMFSATLSKEIRPVCKKFMQDP 203
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
112-297 9.45e-26

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: 103.78  E-value: 9.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 112 IYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQMG 191
Cdd:cd17962    5 LKKAGYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 192 KFCVDVQVMYAIRGNRIPRGTDITKQ---IIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMIDtQGFSDHSIRIQRA 268
Cdd:cd17962   83 KGLPPMKTALLVGGLPLPPQLYRLQQgvkVIIATPGRLLD-ILKQSSVELDNIKIVVVDEADTMLK-MGFQQQVLDILEN 160
                        170       180
                 ....*....|....*....|....*....
gi 164419732 269 LPSECQMLLFSATFEDSVWHFAERIIPDP 297
Cdd:cd17962  161 ISHDHQTILVSATIPRGIEQLAGQLLQNP 189
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
114-297 1.64e-25

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: 103.46  E-value: 1.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 114 AMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQtgrVVEQMGKF 193
Cdd:cd17955   16 SLGIKEPTPIQKLCIPEILAG--RDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELAYQ---IAEQFRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 194 CVDVQVMYAIrgnrIPRGTDITKQ---------IIIGTPGTVLD---------WCFKlklidltKIRVFVLDEADVMIDT 255
Cdd:cd17955   91 GAPLGLRCCV----IVGGMDMVKQalelskrphIVVATPGRLADhlrssddttKVLS-------RVKFLVLDEADRLLTG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 164419732 256 QgFSDHSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDP 297
Cdd:cd17955  160 S-FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
115-297 1.41e-24

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: 100.86  E-value: 1.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 115 MGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVnalelfpQCLCLAPTYELALQTGRVVEQMGKFC 194
Cdd:cd17938   17 LDWLLPTDIQAEAIPLILGG--GDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELAEQTYNCIENFKKYL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 195 VD--VQVMYAIRG-------NRIPRGTDItkqiIIGTPGTVLDWcFKLKLIDLTKIRVFVLDEADVMIDtQGFSDHSIRI 265
Cdd:cd17938   88 DNpkLRVALLIGGvkareqlKRLESGVDI----VVGTPGRLEDL-IKTGKLDLSSVRFFVLDEADRLLS-QGNLETINRI 161
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 164419732 266 QRALPS------ECQMLLFSATFE-DSVWHFAERIIPDP 297
Cdd:cd17938  162 YNRIPKitsdgkRLQVIVCSATLHsFEVKKLADKIMHFP 200
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
115-301 1.54e-24

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: 101.12  E-value: 1.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 115 MGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELF------PQCLCLAPTYELALQTGRVVE 188
Cdd:cd17949    9 MGIEKPTAIQKLAIPVLLQG--RDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrsdgTLALVLVPTRELALQIYEVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 189 QMGKFCVDVQVMYAIRGN-------RIPRGtdITkqIIIGTPGTVLDWCFKLKLIDLTKIRVFVLDEADVMIDtQGFSDH 261
Cdd:cd17949   87 KLLKPFHWIVPGYLIGGEkrksekaRLRKG--VN--ILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLD-MGFEKD 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164419732 262 SIRIQRAL-------------PSECQMLLFSATFEDSVWHFAERIIPDPNVIK 301
Cdd:cd17949  162 ITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
111-286 1.53e-23

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: 98.03  E-value: 1.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQ-----CLCLAPTYELALQTGR 185
Cdd:cd17960    4 VVAELGFTSMTPVQAATIPLFLSN--KDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKkgqvgALIISPTRELATQIYE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 186 VVEQMGKFCVD-VQVMYAIRGNRIPRGTDITK----QIIIGTPGTVLD-WCFKLKLIDLTKIRVFVLDEADVMIDTqGFS 259
Cdd:cd17960   82 VLQSFLEHHLPkLKCQLLIGGTNVEEDVKKFKrngpNILVGTPGRLEElLSRKADKVKVKSLEVLVLDEADRLLDL-GFE 160
                        170       180
                 ....*....|....*....|....*..
gi 164419732 260 DHSIRIQRALPSECQMLLFSATFEDSV 286
Cdd:cd17960  161 ADLNRILSKLPKQRRTGLFSATQTDAV 187
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
112-297 2.88e-23

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: 97.05  E-value: 2.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 112 IYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELF-----PQCLCLAPTYELALQtgrV 186
Cdd:cd17966    5 LKRQGFTEPTAIQAQGWPMALSG--RDMVGIAQTGSGKTLAFLLPAIVHINAQPPLergdgPIVLVLAPTRELAQQ---I 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 187 VEQMGKFCVDVQV-MYAIRGNrIPRGTDITK-----QIIIGTPGTVLDWcFKLKLIDLTKIRVFVLDEADVMIDtQGFSD 260
Cdd:cd17966   80 QQEANKFGGSSRLrNTCVYGG-APKGPQIRDlrrgvEICIATPGRLIDF-LDQGKTNLRRVTYLVLDEADRMLD-MGFEP 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 164419732 261 H------SIRIQRalpsecQMLLFSATFEDSVWHFAERIIPDP 297
Cdd:cd17966  157 QirkivdQIRPDR------QTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
112-293 4.85e-23

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: 97.01  E-value: 4.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 112 IYAMGFNRPSKIQEMALPMMLAhpPQNLIAQSQSGTGKTAAFVLAMLSRVNAL--------ELFPQCLCLAPTYELALQt 183
Cdd:cd17945    5 IRKLGYKEPTPIQRQAIPIGLQ--NRDIIGIAETGSGKTAAFLIPLLVYISRLppldeetkDDGPYALILAPTRELAQQ- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 184 grVVEQMGKFCV--DVQVMYAIRG-------NRIPRGTDitkqIIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMID 254
Cdd:cd17945   82 --IEEETQKFAKplGIRVVSIVGGhsieeqaFSLRNGCE----ILIATPGRLLD-CLERRLLVLNQCTYVVLDEADRMID 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 164419732 255 tQGFSDHSIRIQRALPSEC--------------------QMLLFSATFEDSVwhfaERI 293
Cdd:cd17945  155 -MGFEPQVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAV----EKI 208
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
116-297 5.41e-23

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: 96.12  E-value: 5.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 116 GFNRPSKIQEMALPMMLAHPpqNLIAQSQSGTGKTAAFVLAMLSRVNAL--ELFPQCLCLAPTYELALQTGRVVEQMGKF 193
Cdd:cd17957    9 GYREPTPIQMQAIPILLHGR--DLLACAPTGSGKTLAFLIPILQKLGKPrkKKGLRALILAPTRELASQIYRELLKLSKG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 194 CvDVQVMYAIRGNR-IPRGTDITKQ---IIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMIDTqGFSDHSIRIQRAL 269
Cdd:cd17957   87 T-GLRIVLLSKSLEaKAKDGPKSITkydILVSTPLRLVF-LLKQGPIDLSSVEYLVLDEADKLFEP-GFREQTDEILAAC 163
                        170       180
                 ....*....|....*....|....*....
gi 164419732 270 PSEC-QMLLFSATFEDSVWHFAERIIPDP 297
Cdd:cd17957  164 TNPNlQRSLFSATIPSEVEELARSVMKDP 192
HELICc smart00490
helicase superfamily c-terminal domain;
352-439 1.30e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 1.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732   352 KWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVkqgeepDYETYLHR 431
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPW------SPASYIQR 74

                   ....*...
gi 164419732   432 IGRTGRFG 439
Cdd:smart00490  75 IGRAGRAG 82
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
117-290 2.88e-22

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: 95.49  E-value: 2.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 117 FNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRV----------------NALELFPQCLCLAPTYELA 180
Cdd:cd18051   41 YTKPTPVQKHAIPIIKSK--RDLMACAQTGSGKTAAFLLPILSQIyeqgpgeslpsesgyyGRRKQYPLALVLAPTRELA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 181 LQtgrVVEQMGKF----CVDVQVMYAirgnriprGTDITKQI---------IIGTPGTVLDWCFKLKlIDLTKIRVFVLD 247
Cdd:cd18051  119 SQ---IYDEARKFayrsRVRPCVVYG--------GADIGQQMrdlergchlLVATPGRLVDMLERGK-IGLDYCKYLVLD 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 164419732 248 EADVMIDtQGFSDHSIRI--QRALP--SECQMLLFSATFEDSVWHFA 290
Cdd:cd18051  187 EADRMLD-MGFEPQIRRIveQDTMPptGERQTLMFSATFPKEIQMLA 232
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
112-300 5.09e-21

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: 90.55  E-value: 5.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 112 IYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNAL-ELFPQ----CLCLAPTYELALQTGRV 186
Cdd:cd17952    5 IRKQEYEQPTPIQAQALPVALSG--RDMIGIAKTGSGKTAAFIWPMLVHIMDQrELEKGegpiAVIVAPTRELAQQIYLE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 187 VEQMGK-FCVDVQVMYAIRG-----NRIPRGTDitkqIIIGTPGTVLDwCFKLKLIDLTKIRVFVLDEADVMIDTqGFSD 260
Cdd:cd17952   83 AKKFGKaYNLRVVAVYGGGSkweqaKALQEGAE----IVVATPGRLID-MVKKKATNLQRVTYLVLDEADRMFDM-GFEY 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 164419732 261 HSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVI 300
Cdd:cd17952  157 QVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
116-300 5.20e-21

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: 90.81  E-value: 5.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 116 GFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQ----CLCLAPTYELALQTGRVVEQMG 191
Cdd:cd17941    9 GFIKMTEIQRDSIPHALQG--RDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELAMQIFEVLRKVG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 192 KFcvdvQVMYA---IRGN-------RIPRgtditKQIIIGTPGTVLDWCFKLKLIDLTKIRVFVLDEADVMIDTqGFSDH 261
Cdd:cd17941   87 KY----HSFSAgliIGGKdvkeekeRINR-----MNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDM-GFKET 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 164419732 262 SIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVI 300
Cdd:cd17941  157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
112-297 1.11e-19

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: 87.43  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 112 IYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELF-----PQCLCLAPTYELALQtgrV 186
Cdd:cd17953   27 IKKLGYEKPTPIQAQALPAIMSG--RDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVkpgegPIGLIMAPTRELALQ---I 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 187 VEQMGKFC--VDVQVMYAIRGNRIP-------RGTDItkqiIIGTPGTVLDWcfkL-----KLIDLTKIRVFVLDEADVM 252
Cdd:cd17953  102 YVECKKFSkaLGLRVVCVYGGSGISeqiaelkRGAEI----VVCTPGRMIDI---LtanngRVTNLRRVTYVVLDEADRM 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 164419732 253 IDTqGFSDHSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDP 297
Cdd:cd17953  175 FDM-GFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
112-297 8.50e-19

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: 84.44  E-value: 8.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 112 IYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVL-AMLSRVNALELF-----PQCLCLAPTYELALQTGR 185
Cdd:cd17958    5 IKKQGFEKPSPIQSQAWPIILQG--IDLIGVAQTGTGKTLAYLLpGFIHLDLQPIPReqrngPGVLVLTPTRELALQIEA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 186 VVEQMGKFCVDVQVMYAiRGNRIPRGTDITK--QIIIGTPGTVLDWCFKlKLIDLTKIRVFVLDEADVMIDtQGFSDHSI 263
Cdd:cd17958   83 ECSKYSYKGLKSVCVYG-GGNRNEQIEDLSKgvDIIIATPGRLNDLQMN-NVINLKSITYLVLDEADRMLD-MGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 164419732 264 RIQRALPSECQMLLFSATFEDSVWHFAERIIPDP 297
Cdd:cd17958  160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
111-300 1.11e-18

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: 84.31  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLsrVNALEL----------FPQCLCLAPTYELA 180
Cdd:cd17951    4 GLKKKGIKKPTPIQMQGLPTILSG--RDMIGIAFTGSGKTLVFTLPLI--MFALEQekklpfikgeGPYGLIVCPSRELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 181 LQTGRVVEQMGKFCVD-----VQVMYAIRGNRIPRGTDITKQ---IIIGTPGTVLDWCFKlKLIDLTKIRVFVLDEADVM 252
Cdd:cd17951   80 RQTHEVIEYYCKALQEggypqLRCLLCIGGMSVKEQLEVIRKgvhIVVATPGRLMDMLNK-KKINLDICRYLCLDEADRM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 164419732 253 IDtQGFSDHSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVI 300
Cdd:cd17951  159 ID-MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
111-310 5.75e-18

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: 82.02  E-value: 5.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQ----CLCLAPTYELALQTGRV 186
Cdd:cd17942    4 AIEEMGFTKMTEIQAKSIPPLLEG--RDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQIYGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 187 VEQMGKFcvDVQVMYAIRG--NRIPRGTDITK--QIIIGTPGTVLD-------WCFKlklidltKIRVFVLDEADVMIDt 255
Cdd:cd17942   82 AKELLKY--HSQTFGIVIGgaNRKAEAEKLGKgvNILVATPGRLLDhlqntkgFLYK-------NLQCLIIDEADRILE- 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 164419732 256 QGFSDHSIRIQRALPSECQMLLFSATfedsvwhfAERIIPDPNVIKLRKEELTLN 310
Cdd:cd17942  152 IGFEEEMRQIIKLLPKRRQTMLFSAT--------QTRKVEDLARISLKKKPLYVG 198
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
117-296 1.23e-17

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: 81.98  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 117 FNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELF-----PQCLCLAPTYELALQTGRVVEQMG 191
Cdd:cd18049   44 FTEPTAIQAQGWPVALSG--LDMVGVAQTGSGKTLSYLLPAIVHINHQPFLergdgPICLVLAPTRELAQQVQQVAAEYG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 192 KFC-VDVQVMY--AIRGNRIpRGTDITKQIIIGTPGTVLDWcFKLKLIDLTKIRVFVLDEADVMIDtQGFSDHSIRIQRA 268
Cdd:cd18049  122 RACrLKSTCIYggAPKGPQI-RDLERGVEICIATPGRLIDF-LEAGKTNLRRCTYLVLDEADRMLD-MGFEPQIRKIVDQ 198
                        170       180
                 ....*....|....*....|....*...
gi 164419732 269 LPSECQMLLFSATFEDSVWHFAERIIPD 296
Cdd:cd18049  199 IRPDRQTLMWSATWPKEVRQLAEDFLKD 226
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
117-296 2.38e-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: 81.98  E-value: 2.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 117 FNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELF-----PQCLCLAPTYELALQTGRVVEQMG 191
Cdd:cd18050   82 FKEPTPIQCQGFPLALSG--RDMVGIAQTGSGKTLAYLLPAIVHINHQPYLergdgPICLVLAPTRELAQQVQQVADDYG 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 192 KfCVDVQVMYAIRGnrIPRGTDITK-----QIIIGTPGTVLDWcFKLKLIDLTKIRVFVLDEADVMIDtQGFSDHSIRIQ 266
Cdd:cd18050  160 K-SSRLKSTCIYGG--APKGPQIRDlergvEICIATPGRLIDF-LEAGKTNLRRCTYLVLDEADRMLD-MGFEPQIRKIV 234
                        170       180       190
                 ....*....|....*....|....*....|
gi 164419732 267 RALPSECQMLLFSATFEDSVWHFAERIIPD 296
Cdd:cd18050  235 DQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
137-292 3.55e-17

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: 79.89  E-value: 3.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 137 QNLIAQSQSGTGKTAAFVLAMLSRVNALE------LFPQCLCLAPTYELALQTGR----VVEQMGKFCVDVQVMYAIRGN 206
Cdd:cd17944   28 KDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTKdfkdITRKLSVACFYGGTPYQQQIF 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 207 RIPRGTDitkqIIIGTPGTVLDWCFKLKLiDLTKIRVFVLDEADVMIDtQGFSDH-----SIRIQRALPSECQMLLFSAT 281
Cdd:cd17944  108 AIRNGID----ILVGTPGRIKDHLQNGRL-DLTKLKHVVLDEVDQMLD-MGFAEQveeilSVSYKKDSEDNPQTLLFSAT 181
                        170
                 ....*....|.
gi 164419732 282 FEDSVWHFAER 292
Cdd:cd17944  182 CPDWVYNVAKK 192
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
111-315 4.74e-16

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: 77.28  E-value: 4.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 111 GIYAMGFNRPSKIQEMALPMMLaHPPQNLIAQSQSGTGKTAAF-------VLAMLSRVNALELF--PQCLCLAPTYELAL 181
Cdd:cd17946    4 ALADLGFSEPTPIQALALPAAI-RDGKDVIGAAETGSGKTLAFgipilerLLSQKSSNGVGGKQkpLRALILTPTRELAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 182 QTGRVVEQMGKFcVDVQVMyAIRGnriprGTDITKQ---------IIIGTPGTVLDwcfklkLID--------LTKIRVF 244
Cdd:cd17946   83 QVKDHLKAIAKY-TNIKIA-SIVG-----GLAVQKQerllkkrpeIVVATPGRLWE------LIQegnehlanLKSLRFL 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164419732 245 VLDEADVMIDTQGFSD-HSI--RIQRALPSEC---QMLLFSATFedSVWHFAeriiPDPNVIKLRKEELTLNNIRQY 315
Cdd:cd17946  150 VLDEADRMLEKGHFAElEKIleLLNKDRAGKKrkrQTFVFSATL--TLDHQL----PLKLNSKKKKKKKEKKQKLEL 220
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
138-281 1.29e-14

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: 70.90  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 138 NLIAQSQSGTGKTAAFVLAMLSRvnALELFPQCLCLAPTYELALQTGRVVEQMGKFCVDVQVMYA------IRGNRIPRg 211
Cdd:cd00046    3 NVLITAPTGSGKTLAALLAALLL--LLKKGKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGgssaeeREKNKLGD- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164419732 212 tditKQIIIGTPGTVLDWCFKLKLIDLTKIRVFVLDEADVM-IDTQGFSDHSIRIQRALPSECQMLLFSAT 281
Cdd:cd00046   80 ----ADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALlIDSRGALILDLAVRKAGLKNAQVILLSAT 146
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
115-295 2.21e-12

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: 66.62  E-value: 2.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 115 MGFNRPSKIQEMALPMMLAHppQNLIAQSQSGTGKTAAFVLAMLSRVNALELF-------PQCLCLAPTYELALQTGRVV 187
Cdd:cd17948    8 QGITKPTTVQKQGIPSILRG--RNTLCAAETGSGKTLTYLLPIIQRLLRYKLLaegpfnaPRGLVITPSRELAEQIGSVA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 188 EQMGK-FCVDVQVMYAIRGNRI---PRGTDItkQIIIGTPGTVLdwcfKL---KLIDLTKIRVFVLDEADVMIDtQGFSD 260
Cdd:cd17948   86 QSLTEgLGLKVKVITGGRTKRQirnPHFEEV--DILVATPGALS----KLltsRIYSLEQLRHLVLDEADTLLD-DSFNE 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 164419732 261 -----------HSIRIQRA--LPSECQMLLFSATFEDSVWHFAERIIP 295
Cdd:cd17948  159 klshflrrfplASRRSENTdgLDPGTQLVLVSATMPSGVGEVLSKVID 206
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
290-441 1.93e-10

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 63.21  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 290 AERIIPDPNVIKLRK--EELTLnnirqyyvlcEHRKDKY--QALCNIYGSITIGQAIIFCQTRRnakwlTVEMI-----Q 360
Cdd:COG1111  311 SKRLVSDPRFRKAMRlaEEADI----------EHPKLSKlrEILKEQLGTNPDSRIIVFTQYRD-----TAEMIveflsE 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 361 DGHQVSLLSGE--------LTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDlPVkqgeePDYETYLHRI 432
Cdd:COG1111  376 PGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PV-----PSEIRSIQRK 449

                 ....*....
gi 164419732 433 GRTGRFGKK 441
Cdd:COG1111  450 GRTGRKREG 458
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
146-411 5.97e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 61.58  E-value: 5.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 146 GTGKT--AAFVLAMLSRVnalelfPQCLCLAPTYELALQTgrvVEQMGKFCVDVqvmyAIRGNRIprgtDITKQIIIGTP 223
Cdd:COG1061  110 GTGKTvlALALAAELLRG------KRVLVLVPRRELLEQW---AEELRRFLGDP----LAGGGKK----DSDAPITVATY 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 224 GTVLDWCFKLKLIDltKIRVFVLDEAdvmidtqgfsdHSI------RIQRALPSECqMLLFSAT--FEDSVWHFAER--- 292
Cdd:COG1061  173 QSLARRAHLDELGD--RFGLVIIDEA-----------HHAgapsyrRILEAFPAAY-RLGLTATpfRSDGREILLFLfdg 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 293 ----------------------IIPDPNVIKLRKEELTLNNIRQYYVLCEHRKDK-YQALCNIYGSItiGQAIIFCQTRR 349
Cdd:COG1061  239 ivyeyslkeaiedgylappeyyGIRVDLTDERAEYDALSERLREALAADAERKDKiLRELLREHPDD--RKTLVFCSSVD 316
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164419732 350 NAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVV 411
Cdd:COG1061  317 HAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
114-281 2.07e-09

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: 57.64  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 114 AMGFNRPSKIQEMALPMMLA-------HPPQNLIAQSQSGTGKTAAFVL----AMLSRVNAlELfpQCLCLAPTYELALQ 182
Cdd:cd17956    7 NNGITSAFPVQAAVIPWLLPsskstppYRPGDLCVSAPTGSGKTLAYVLpivqALSKRVVP-RL--RALIVVPTKELVQQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 183 tgrVVEQMGKFC--VDVQVMyAIRGNR--------IPRGT----DITKQIIIGTPGTVLDWCFKLKLIDLTKIRVFVLDE 248
Cdd:cd17956   84 ---VYKVFESLCkgTGLKVV-SLSGQKsfkkeqklLLVDTsgryLSRVDILVATPGRLVDHLNSTPGFTLKHLRFLVIDE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 164419732 249 ADVMIDT--QGFSDHSI-RIQRA----------------LPSECQMLLFSAT 281
Cdd:cd17956  160 ADRLLNQsfQDWLETVMkALGRPtapdlgsfgdanllerSVRPLQKLLFSAT 211
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
120-300 2.38e-09

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


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 57.77  E-value: 2.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 120 PSKIQEMALPMMLAHPPQN---------------LIAqSQSGTGKTAAFVLAMLSRVNALELF----------------- 167
Cdd:cd17965   31 PSPIQTLAIKKLLKTLMRKvtkqtsneepklevfLLA-AETGSGKTLAYLAPLLDYLKRQEQEpfeeaeeeyesakdtgr 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 168 PQCLCLAPTYELALQTGRVVEQM--------GKFCVDVQVMYAIRGNRIPRGTDItkqiIIGTPGTVLDwCFKLKLIDLT 239
Cdd:cd17965  110 PRSVILVPTHELVEQVYSVLKKLshtvklgiKTFSSGFGPSYQRLQLAFKGRIDI----LVTTPGKLAS-LAKSRPKILS 184
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164419732 240 KIRVFVLDEADVMIDtQGFSDHSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVI 300
Cdd:cd17965  185 RVTHLVVDEADTLFD-RSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRI 244
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
322-416 6.37e-09

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 54.52  E-value: 6.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 322 RKDKYQALCNI----YGSITIGQAIIFCQTRRNAKWLTvEMIQD--------------GHQVSLLSGELTVEQRA--SII 381
Cdd:cd18802    5 VIPKLQKLIEIlreyFPKTPDFRGIIFVERRATAVVLS-RLLKEhpstlafircgfliGRGNSSQRKRSLMTQRKqkETL 83
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 164419732 382 QRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLP 416
Cdd:cd18802   84 DKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLP 118
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
339-440 9.16e-08

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


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 51.06  E-value: 9.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 339 GQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPvk 418
Cdd:cd18794   31 GSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLP-- 108
                         90       100
                 ....*....|....*....|..
gi 164419732 419 qgeePDYETYLHRIGRTGRFGK 440
Cdd:cd18794  109 ----KSMESYYQESGRAGRDGL 126
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
341-416 3.05e-07

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: 49.40  E-value: 3.05e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164419732 341 AIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEK--VLITTNVCARGIDVKQVTIVVNFDLP 416
Cdd:cd18793   30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPW 107
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
341-439 3.16e-06

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 49.84  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 341 AIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEK--VLITTNVCARGIDVKQVTIVVNFDLP-- 416
Cdd:COG0553  552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWwn 631
                         90       100
                 ....*....|....*....|....*.
gi 164419732 417 ---VKQgeepdyetylhRIGRTGRFG 439
Cdd:COG0553  632 pavEEQ-----------AIDRAHRIG 646
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
340-444 6.97e-06

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: 45.71  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 340 QAIIFCQTRRNA----KWLTVEMIQDGHQVSLLS---GELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVN 412
Cdd:cd18797   37 KTIVFCRSRKLAelllRYLKARLVEEGPLASKVAsyrAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
                         90       100       110
                 ....*....|....*....|....*....|..
gi 164419732 413 FDLPvkqgeePDYETYLHRIGRTGRFGKKGLA 444
Cdd:cd18797  117 AGYP------GSLASLWQQAGRAGRRGKDSLV 142
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
340-445 9.42e-06

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 48.29  E-value: 9.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 340 QAIIFCQTRRNAKwLTVEMIQDGHQVSLLSGELTV-------EQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVN 412
Cdd:COG1205  290 RTLVFTRSRRGAE-LLARYARRALREPDLADRVAAyragylpEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVL 368
                         90       100       110
                 ....*....|....*....|....*....|...
gi 164419732 413 FDLPvkqgeePDYETYLHRIGRTGRFGKKGLAF 445
Cdd:COG1205  369 AGYP------GTRASFWQQAGRAGRRGQDSLVV 395
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
390-442 1.09e-05

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 43.46  E-value: 1.09e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164419732 390 KVLITTNVCARGIDVKQVTIVVNFDLPvkqgeePDYETYLHRIGRTGRFGKKG 442
Cdd:cd18785   24 EILVATNVLGEGIDVPSLDTVIFFDPP------SSAASYIQRVGRAGRGGKDE 70
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
317-437 1.82e-05

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 44.65  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 317 VLCEHRKDKyQALCNiygsitiGQAIIFCQTRRNAKWLTVEMIQDGHQV--SLLSGELTVE--------QRASIIQRFRD 386
Cdd:cd18801   17 IVKEHFKKK-QEGSD-------TRVIIFSEFRDSAEEIVNFLSKIRPGIraTRFIGQASGKsskgmsqkEQKEVIEQFRK 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 164419732 387 GKEKVLITTNVCARGIDVKQVTIVVNFDL---PVKqgeepdyetYLHRIGRTGR 437
Cdd:cd18801   89 GGYNVLVATSIGEEGLDIGEVDLIICYDAspsPIR---------MIQRMGRTGR 133
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
294-444 6.40e-05

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 45.52  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 294 IPDPNVIKL---RKeeltlnNIRqYYVLCEHRKDKYQALCNIYGSITIGQAIIFCQTRRN----AKWLTvemiQDGHQVS 366
Cdd:COG0514  190 LEDPRVFVGsfdRP------NLR-LEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKveelAEWLR----EAGIRAA 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 367 LLSGELTVEQRASIIQRFRDGKEKVLITTNvcA--RGIDVKQVTIVVNFDLPvkqgeePDYETYLHRIGRTGRFGKKGLA 444
Cdd:COG0514  259 AYHAGLDAEEREANQDRFLRDEVDVIVATI--AfgMGIDKPDVRFVIHYDLP------KSIEAYYQEIGRAGRDGLPAEA 330
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
341-418 2.59e-04

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: 40.62  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 341 AIIFCQTRRNAKWLtVEMIQD-GHQVSLLSGELTVEQR--ASIIQ-RFRDGKEKVLITTNVCARGIDVKQVTIVVnFDLP 416
Cdd:cd18799    9 TLIFCVSIEHAEFM-AEAFNEaGIDAVALNSDYSDRERgdEALILlFFGELKPPILVTVDLLTTGVDIPEVDNVV-FLRP 86

                 ..
gi 164419732 417 VK 418
Cdd:cd18799   87 TE 88
PRK13766 PRK13766
Hef nuclease; Provisional
290-437 3.37e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 43.32  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 290 AERIIPDPNVIKL--RKEELTLnnirqyyvlcEHrkDKYQALCNIYGSITIGQ----AIIFCQTRRNAKWLTVEMIQDG- 362
Cdd:PRK13766 323 SKRLVEDPRFRKAvrKAKELDI----------EH--PKLEKLREIVKEQLGKNpdsrIIVFTQYRDTAEKIVDLLEKEGi 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 363 ------HQVSLLSGE-LTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVnFDLPVkqgeePDYETYLHRIGRT 435
Cdd:PRK13766 391 kavrfvGQASKDGDKgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRSIQRKGRT 464

                 ..
gi 164419732 436 GR 437
Cdd:PRK13766 465 GR 466
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
293-437 5.58e-04

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 40.33  E-value: 5.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 293 IIPDPNVIKLRKEELTLNNIRQY-YVLCEHRKdkyqalcniygsitigqAIIFCQTRRNAKWLTV------EMIQDGHQV 365
Cdd:cd18796    9 ILPVAPEIFPWAGESGADAYAEViFLLERHKS-----------------TLVFTNTRSQAERLAQrlrelcPDRVPPDFI 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164419732 366 SLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLP--VKQGeepdyetyLHRIGRTGR 437
Cdd:cd18796   72 ALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPksVARL--------LQRLGRSGH 137
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
303-411 2.08e-03

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 38.77  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 303 RKEELTLNNIRQYYVLCEHRKDKYQALCNIygsIT----IGQAIIFCQT----RRNAKWLTVEMIqdghqvsllSGELTV 374
Cdd:cd18789   13 YREYLGLGAHRKRRLLAAMNPNKLRALEEL---LKrheqGDKIIVFTDNvealYRYAKRLLKPFI---------TGETPQ 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 164419732 375 EQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVV 411
Cdd:cd18789   81 SEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAI 117
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
302-437 2.15e-03

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: 38.69  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 302 LRKEELTLNNIRQYYVLCEHRKDKyqalcniygsitigQAIIFCQTRRNAKWLTVEMIqdGhqVSLLSGELTVEQRASII 381
Cdd:cd18795   21 VDVMNKFDSDIIVLLKIETVSEGK--------------PVLVFCSSRKECEKTAKDLA--G--IAFHHAGLTREDRELVE 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164419732 382 QRFRDGKEKVLITT-------NVCARGIDVKQVTIvvnFDlpVKQGEEPDYETYLHRIGRTGR 437
Cdd:cd18795   83 ELFREGLIKVLVATstlaagvNLPARTVIIKGTQR---YD--GKGYRELSPLEYLQMIGRAGR 140
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
375-462 2.20e-03

C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain]  Cd Length: 238  Bit Score: 39.54  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 375 EQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIV--VNFD----LPVKQGEEPDYETYLHRIGRTGRFGKKGLAFNMI 448
Cdd:cd18804  131 GALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADsglnSPDFRASERAFQLLTQVSGRAGRGDKPGKVIIQT 210
                         90
                 ....*....|....
gi 164419732 449 EVDELPSLMKIQDH 462
Cdd:cd18804  211 YNPEHPLIQAAKEE 224
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
311-439 4.34e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 39.70  E-value: 4.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 311 NIRqyYVLCEhrkdKYQALCNIYGSITiGQ----AIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRD 386
Cdd:PRK11057 212 NIR--YTLVE----KFKPLDQLMRYVQ-EQrgksGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQR 284
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164419732 387 GKEKVLITTNVCARGIDVKQVTIVVNFDLPvkqgeePDYETYLHRIGRTGRFG 439
Cdd:PRK11057 285 DDLQIVVATVAFGMGINKPNVRFVVHFDIP------RNIESYYQETGRAGRDG 331
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
216-441 4.71e-03

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: 39.34  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 216 KQIIIGTPGTVL---DWCFKLKLIDLTKI--RVFVLDEADVMID-TQGFSDHSIRIQRALPSecQMLLFSATFEDSVWHF 289
Cdd:cd09639   94 DPITVCTIDQVLksvFGEFGHYEFTLASIanSLLIFDEVHFYDEyTLALILAVLEVLKDNDV--PILLMSATLPKFLKEY 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 290 AERIIPDPNviklrKEELTLNNIRQY-YVLCEHRKDKYQALCN--IYGSITIGQAIIFCQTRRNAKWLTVEMIQDGHQ-- 364
Cdd:cd09639  172 AEKIGYVEE-----NEPLDLKPNERApFIKIESDKVGEISSLErlLEFIKKGGSVAIIVNTVDRAQEFYQQLKEKGPEee 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 365 VSLLSGELT----VEQRASIIQRFRDGKEKVLITTNVCARGIDvkqvtivVNFDLPVKQGEEPDyeTYLHRIGRTGRFGK 440
Cdd:cd09639  247 IMLIHSRFTekdrAKKEAELLLEFKKSEKFVIVATQVIEASLD-------ISVDVMITELAPID--SLIQRLGRLHRYGE 317

                 .
gi 164419732 441 K 441
Cdd:cd09639  318 K 318
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
318-417 5.17e-03

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 39.09  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419732 318 LCEHRKDKYQALcniygsitigqaiIFCQTrrnakwltvemIQDGHQVS-LLSGEL------TV----EQRASIIQRFRD 386
Cdd:COG4098  312 LKKRLKEGRQLL-------------IFVPT-----------IELLEQLVaLLQKLFpeeriaGVhaedPERKEKVQAFRD 367
                         90       100       110
                 ....*....|....*....|....*....|..
gi 164419732 387 GKEKVLITTNVCARGIDVKQV-TIVVNFDLPV 417
Cdd:COG4098  368 GEIPILVTTTILERGVTFPNVdVAVLGADHPV 399
 
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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