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Conserved domains on  [gi|2462632188|ref|XP_054184363|]
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ATP-dependent RNA helicase DDX3Y isoform X4 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030640)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

EC:  3.6.4.-
PubMed:  20206133
SCOP:  3002019

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
1-224 0e+00

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: 528.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   1 MGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALkaVKENGRYGRRKQY 80
Cdd:cd18051    28 LGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESL--PSESGYYGRRKQY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  81 PISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVL 160
Cdd:cd18051   106 PLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVL 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462632188 161 DEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGS 224
Cdd:cd18051   186 DEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVGRVGS 249
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
229-359 1.22e-60

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: 194.26  E-value: 1.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 229 ITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 308
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462632188 309 LVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 359
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
1-224 0e+00

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: 528.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   1 MGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALkaVKENGRYGRRKQY 80
Cdd:cd18051    28 LGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESL--PSESGYYGRRKQY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  81 PISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVL 160
Cdd:cd18051   106 PLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVL 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462632188 161 DEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGS 224
Cdd:cd18051   186 DEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
14-382 8.73e-166

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 474.25  E-value: 8.73e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEalkavkengrygrrkqyPISLVLAPTRELA 93
Cdd:COG0513    22 YTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA-----------------PQALILAPTRELA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  94 VQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEP 173
Cdd:COG0513    85 LQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 174 QIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEDLDKRSFLLDILGATG 253
Cdd:COG0513   165 DIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 254 SDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLP 333
Cdd:COG0513   241 PER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462632188 334 SDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLveaKQEVP 382
Cdd:COG0513   320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLI---GQKIE 365
PTZ00110 PTZ00110
helicase; Provisional
5-410 3.21e-130

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 387.98  E-value: 3.21e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgealkAVKENGRYGrrkQYPISL 84
Cdd:PTZ00110  141 ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI----------NAQPLLRYG---DGPIVL 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 164
Cdd:PTZ00110  208 VLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEAD 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 165 RMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL-DEYIFLAVGRVG-STSENITQKVVWVEDLDKR 242
Cdd:PTZ00110  288 RMLDMGFEPQIRKIVSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKR 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 243 SFLLDILGATGSD-SLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI 321
Cdd:PTZ00110  364 GKLKMLLQRIMRDgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDV 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 322 SNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLVEAKQEVPSWLENMAYEHHYKGGSRGR 401
Cdd:PTZ00110  444 KDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRW 523

                  ....*....
gi 2462632188 402 SKSNRFSGG 410
Cdd:PTZ00110  524 GGYGRFSNN 532
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
18-206 4.29e-62

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: 199.39  E-value: 4.29e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  18 TPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengrygrrkqyPISLVLAPTRELAVQIY 97
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG------------------PQALVLAPTRELAEQIY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  98 EEARKFSYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDFCKYLVLDEADRMLDMGFEPQIRR 177
Cdd:pfam00270  63 EELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEE 140
                         170       180
                  ....*....|....*....|....*....
gi 2462632188 178 IVEQdtMPPKgvRHTMMFSATFPKEIQML 206
Cdd:pfam00270 141 ILRR--LPKK--RQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
229-359 1.22e-60

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: 194.26  E-value: 1.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 229 ITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 308
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462632188 309 LVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 359
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
9-232 2.51e-58

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 191.17  E-value: 2.51e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188    9 IELTRYTRPTPVQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkavkengRYGRRKQYPISLVLA 87
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-------------------EALKRGKGGRVLVLV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   88 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 166
Cdd:smart00487  62 PTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRL 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462632188  167 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRvgSTSENITQK 232
Cdd:smart00487 142 LDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
240-350 7.03e-37

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: 131.18  E-value: 7.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 240 DKRSFLLDILgATGSDSLTLVFVETKKGADsLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGL 319
Cdd:pfam00271   1 EKLEALLELL-KKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462632188 320 DISNVRHVINFDLPSDIEEYVHRIGRTGRVG 350
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
269-350 2.39e-30

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 112.69  E-value: 2.39e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  269 DSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGR 348
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 2462632188  349 VG 350
Cdd:smart00490  81 AG 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
118-372 9.10e-21

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 94.82  E-value: 9.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 118 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdfckyLVLDEA--------DrmldmgFEP---QIRRIVE 180
Cdd:COG0514    94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 181 QDTMPPkgvrhTMMFSATFPKE-----IQMLARDflDEYIFLA-VGRvgstsENITQKVVWVEDLDKRSFLLDILGATGS 254
Cdd:COG0514   163 RLPNVP-----VLALTATATPRvradiAEQLGLE--DPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPG 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 255 DSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATaVA-ARGLDISNVRHVINFDLP 333
Cdd:COG0514   231 GS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLP 308
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2462632188 334 SDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLD 372
Cdd:COG0514   309 KSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
PRK13766 PRK13766
Hef nuclease; Provisional
255-348 1.65e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 57.19  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 255 DSLTLVFVETKKGADSLEDFLYHEGYAC------TSIHGDR--SQRDREEALHQFRSGKSPILVATAVAARGLDISNVRH 326
Cdd:PRK13766  365 DSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444
                          90       100
                  ....*....|....*....|...
gi 2462632188 327 VINFD-LPSDIeEYVHRIGRTGR 348
Cdd:PRK13766  445 VIFYEpVPSEI-RSIQRKGRTGR 466
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
158-350 9.78e-05

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 44.37  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 158 LVLDEADRMLDmgfEPQIRRIVEQDTMPPKGVRHTMMfSATFPKEIQMLARDFldEYIFLAVGRVGSTSENITQKVVWVE 237
Cdd:TIGR01587 128 LIFDEVHFYDE---YTLALILAVLEVLKDNDVPILLM-SATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILI 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 238 DLDKR---SFLLDILGATGSDSLTLVFVET-----------KKGADSLEDFLYHEGYActsiHGDRSQRDREEALHQFRS 303
Cdd:TIGR01587 202 ESDKVgeiSSLERLLEFIKKGGSIAIIVNTvdraqefyqqlKEKAPEEEIILYHSRFT----EKDRAKKEAELLREMKKS 277
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462632188 304 GKSPILVATAVAARGLDISnvrhvinFDL----PSDIEEYVHRIGRTGRVG 350
Cdd:TIGR01587 278 NEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYG 321
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
1-224 0e+00

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: 528.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   1 MGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALkaVKENGRYGRRKQY 80
Cdd:cd18051    28 LGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESL--PSESGYYGRRKQY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  81 PISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVL 160
Cdd:cd18051   106 PLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVL 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462632188 161 DEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGS 224
Cdd:cd18051   186 DEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
14-382 8.73e-166

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 474.25  E-value: 8.73e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEalkavkengrygrrkqyPISLVLAPTRELA 93
Cdd:COG0513    22 YTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA-----------------PQALILAPTRELA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  94 VQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEP 173
Cdd:COG0513    85 LQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 174 QIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEDLDKRSFLLDILGATG 253
Cdd:COG0513   165 DIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 254 SDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLP 333
Cdd:COG0513   241 PER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462632188 334 SDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLveaKQEVP 382
Cdd:COG0513   320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLI---GQKIE 365
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
1-223 1.70e-159

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: 450.40  E-value: 1.70e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   1 MGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkavkENGRYGRRKQY 80
Cdd:cd17967     7 LRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGP--------PSVGRGRRKAY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  81 PISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVL 160
Cdd:cd17967    79 PSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462632188 161 DEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVG 223
Cdd:cd17967   159 DEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
PTZ00110 PTZ00110
helicase; Provisional
5-410 3.21e-130

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 387.98  E-value: 3.21e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgealkAVKENGRYGrrkQYPISL 84
Cdd:PTZ00110  141 ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI----------NAQPLLRYG---DGPIVL 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 164
Cdd:PTZ00110  208 VLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEAD 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 165 RMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL-DEYIFLAVGRVG-STSENITQKVVWVEDLDKR 242
Cdd:PTZ00110  288 RMLDMGFEPQIRKIVSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKR 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 243 SFLLDILGATGSD-SLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI 321
Cdd:PTZ00110  364 GKLKMLLQRIMRDgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDV 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 322 SNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLVEAKQEVPSWLENMAYEHHYKGGSRGR 401
Cdd:PTZ00110  444 KDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRW 523

                  ....*....
gi 2462632188 402 SKSNRFSGG 410
Cdd:PTZ00110  524 GGYGRFSNN 532
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
3-223 4.89e-127

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: 369.68  E-value: 4.89e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   3 EIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGpgeaLKAVKENGrygrrKQYPI 82
Cdd:cd18052    52 ETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEG----LTASSFSE-----VQEPQ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  83 SLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDE 162
Cdd:cd18052   123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462632188 163 ADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE-YIFLAVGRVG 223
Cdd:cd18052   203 ADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFLKEdYLFLTVGRVG 264
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
14-364 4.41e-99

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 305.19  E-value: 4.41e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgealkavkeNGRYgRRKQypiSLVLAPTRELA 93
Cdd:PRK11776   24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--------------DVKR-FRVQ---ALVLCPTRELA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  94 VQIYEEARKFSyrsRVRP-------CvvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 166
Cdd:PRK11776   86 DQVAKEIRRLA---RFIPnikvltlC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 167 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYifLAVgRVGSTSEN--ITQKVVWVEDLDKRSF 244
Cdd:PRK11776  160 LDMGFQDAIDAIIRQ--APAR--RQTLLFSATYPEGIAAISQRFQRDP--VEV-KVESTHDLpaIEQRFYEVSPDERLPA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 245 LLDILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNV 324
Cdd:PRK11776  233 LQRLLLHHQPES-CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2462632188 325 RHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNM 364
Cdd:PRK11776  312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEM 351
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
5-217 3.59e-97

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 290.88  E-value: 3.59e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkavkengrygRRKQYPISL 84
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK--------------KKGRGPQAL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 164
Cdd:cd00268    67 VLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEAD 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462632188 165 RMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFL 217
Cdd:cd00268   147 RMLDMGFEEDVEKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
5-382 7.30e-97

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 299.42  E-value: 7.30e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkAVKengryGRRkqyPI-S 83
Cdd:PRK10590   12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQP-----HAK-----GRR---PVrA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  84 LVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 163
Cdd:PRK10590   79 LILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 164 DRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEDLDKRS 243
Cdd:PRK10590  159 DRMLDMGFIHDIRRVLAK--LPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 244 FLLDILGaTGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISN 323
Cdd:PRK10590  235 LLSQMIG-KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462632188 324 VRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLveaKQEVP 382
Cdd:PRK10590  314 LPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL---KKEIP 369
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
5-407 7.33e-91

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 285.91  E-value: 7.33e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILS---QIYTDGPGEalkavkengrygRRKqyP 81
Cdd:PLN00206  132 LLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTIRSGHPSE------------QRN--P 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  82 ISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLD 161
Cdd:PLN00206  198 LAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLD 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 162 EADRMLDMGFEPQIRRIVEQDTMPpkgvrHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEDLDK 241
Cdd:PLN00206  278 EVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQK 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 242 RSFLLDILgaTGSDSLT---LVFVETKKGADSLEDFL-YHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAAR 317
Cdd:PLN00206  353 KQKLFDIL--KSKQHFKppaVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGR 430
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 318 GLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLVEAKQEVPSWLENmayeHHYKGG 397
Cdd:PLN00206  431 GVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELAN----SRYLGS 506
                         410
                  ....*....|
gi 2462632188 398 SRGRSKSNRF 407
Cdd:PLN00206  507 GRKRKKKRRY 516
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
5-361 4.10e-90

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 282.57  E-value: 4.10e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEAlkavkengrygRRKQYPISL 84
Cdd:PRK01297   98 LMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKE-----------RYMGEPRAL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLE-RGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 163
Cdd:PRK01297  167 IIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 164 DRMLDMGFEPQIRRIVEQDtmPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEDLDKRS 243
Cdd:PRK01297  247 DRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYK 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 244 FLLDILGATGSDSLtLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISN 323
Cdd:PRK01297  325 LLYNLVTQNPWERV-MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2462632188 324 VRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNE 361
Cdd:PRK01297  404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGE 441
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
5-217 1.45e-84

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: 258.45  E-value: 1.45e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIyTDGPgealkavkengrYGRRKQYPISL 84
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI-NAQP------------PLERGDGPIVL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 164
Cdd:cd17966    68 VLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEAD 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462632188 165 RMLDMGFEPQIRRIVEQdTMPPkgvRHTMMFSATFPKEIQMLARDFLDEYIFL 217
Cdd:cd17966   148 RMLDMGFEPQIRKIVDQ-IRPD---RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
5-383 2.68e-81

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 262.58  E-value: 2.68e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgPGEAlkavkengryGRRKQYPISL 84
Cdd:PRK04537   20 LLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSR-PALA----------DRKPEDPRAL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI-GLDFCKYLVLDEA 163
Cdd:PRK04537   89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 164 DRMLDMGFEPQIRRIVEQdtMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEDLDKRS 243
Cdd:PRK04537  169 DRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 244 FLLDILgATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISN 323
Cdd:PRK04537  247 LLLGLL-SRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 324 VRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKnmnITKDLLDLLVEAKQEVPS 383
Cdd:PRK04537  326 VKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACER---YAMSLPDIEAYIEQKIPV 382
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
14-358 8.92e-81

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 257.18  E-value: 8.92e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsQIYTDGPgealkavkengrygRRKQYPIS-LVLAPTREL 92
Cdd:PRK11192   21 YTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAL-QHLLDFP--------------RRKSGPPRiLILTPTREL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  93 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 172
Cdd:PRK11192   86 AMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 173 PQIRRIVEQdtmpPKGVRHTMMFSATFPKE-IQMLARDFLDEYIFLAVGrvGSTSE--NITQKVVWVEDLD-KRSFLLDI 248
Cdd:PRK11192  166 QDIETIAAE----TRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAE--PSRRErkKIHQWYYRADDLEhKTALLCHL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 249 LgATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVI 328
Cdd:PRK11192  240 L-KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
                         330       340       350
                  ....*....|....*....|....*....|
gi 2462632188 329 NFDLPSDIEEYVHRIGRTGRVGNLGLATSF 358
Cdd:PRK11192  319 NFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
18-358 5.68e-78

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 249.50  E-value: 5.68e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  18 TPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEalkavkengryGRRKQYPISLVLAPTRELAVQIY 97
Cdd:PRK04837   32 TPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPE-----------DRKVNQPRALIMAPTRELAVQIH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  98 EEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRR 177
Cdd:PRK04837  101 ADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRW 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 178 IVEQdtMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEDLDKRSFLLDILGATGSDSl 257
Cdd:PRK04837  181 LFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEWPDR- 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 258 TLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIE 337
Cdd:PRK04837  258 AIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCE 337
                         330       340
                  ....*....|....*....|.
gi 2462632188 338 EYVHRIGRTGRVGNLGLATSF 358
Cdd:PRK04837  338 DYVHRIGRTGRAGASGHSISL 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
14-358 4.24e-72

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 239.75  E-value: 4.24e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaLKAvkengrygrrkqyPISLVLAPTRELA 93
Cdd:PRK11634   26 YEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE-----LKA-------------PQILVLAPTRELA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  94 VQIYEEARKFSYRSR-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 172
Cdd:PRK11634   88 VQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 173 PQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEDLDKRSFLLDILGAT 252
Cdd:PRK11634  168 EDVETIMAQ--IPEG--HQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 253 GSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDL 332
Cdd:PRK11634  244 DFDA-AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDI 322
                         330       340
                  ....*....|....*....|....*.
gi 2462632188 333 PSDIEEYVHRIGRTGRVGNLGLATSF 358
Cdd:PRK11634  323 PMDSESYVHRIGRTGRAGRAGRALLF 348
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
5-215 7.93e-68

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: 215.36  E-value: 7.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYtdgpgealkavkeNGRYGRRKQYPISL 84
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-------------DQRELEKGEGPIAV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 164
Cdd:cd17952    68 IVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEAD 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462632188 165 RMLDMGFEPQIRRIVEQdTMPPkgvRHTMMFSATFPKEIQMLARDFLDEYI 215
Cdd:cd17952   148 RMFDMGFEYQVRSIVGH-VRPD---RQTLLFSATFKKKIEQLARDILSDPI 194
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
5-211 1.25e-67

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: 216.09  E-value: 1.25e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEAlkavkENGrygrrkqyPISL 84
Cdd:cd17953    23 VLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKP-----GEG--------PIGL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDM--MERGKI-GLDFCKYLVLD 161
Cdd:cd17953    90 IMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDIltANNGRVtNLRRVTYVVLD 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462632188 162 EADRMLDMGFEPQIRRIVeqDTMPPKgvRHTMMFSATFPKEIQMLARDFL 211
Cdd:cd17953   170 EADRMFDMGFEPQIMKIV--NNIRPD--RQTVLFSATFPRKVEALARKVL 215
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
5-220 2.09e-67

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: 216.03  E-value: 2.09e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgealkavkENGRYGRRKQYPISL 84
Cdd:cd18049    35 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI-------------NHQPFLERGDGPICL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 164
Cdd:cd18049   102 VLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462632188 165 RMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVG 220
Cdd:cd18049   182 RMLDMGFEPQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
13-220 4.46e-66

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: 213.72  E-value: 4.46e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  13 RYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgealkavkENGRYGRRKQYPISLVLAPTREL 92
Cdd:cd18050    81 NFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI-------------NHQPYLERGDGPICLVLAPTREL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  93 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 172
Cdd:cd18050   148 AQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFE 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462632188 173 PQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVG 220
Cdd:cd18050   228 PQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
9-211 2.53e-65

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: 209.87  E-value: 2.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   9 IELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALKavKENGrygrrkqyPISLVLAP 88
Cdd:cd17945     5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEET--KDDG--------PYALILAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  89 TRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLD 168
Cdd:cd17945    75 TRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMID 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462632188 169 MGFEPQIRRIVeqDTMPP------------------KGVRHTMMFSATFPKEIQMLARDFL 211
Cdd:cd17945   155 MGFEPQVTKIL--DAMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYL 213
PTZ00424 PTZ00424
helicase 45; Provisional
14-370 2.98e-62

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 207.76  E-value: 2.98e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaLKAVKengrygrrkqypiSLVLAPTREL 92
Cdd:PTZ00424   48 FEKPSAIQQRGIkPILDG-YDTIGQAQSGTGKTATFVIAALQLIDYD-----LNACQ-------------ALILAPTREL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  93 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 172
Cdd:PTZ00424  109 AQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 173 PQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEDLDKRSFLLDILGAT 252
Cdd:PTZ00424  189 GQIYDVFKK--LPPD--VQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYET 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 253 GSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDL 332
Cdd:PTZ00424  265 LTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDL 344
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2462632188 333 PSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDL 370
Cdd:PTZ00424  345 PASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
18-206 4.29e-62

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: 199.39  E-value: 4.29e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  18 TPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengrygrrkqyPISLVLAPTRELAVQIY 97
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG------------------PQALVLAPTRELAEQIY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  98 EEARKFSYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDFCKYLVLDEADRMLDMGFEPQIRR 177
Cdd:pfam00270  63 EELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEE 140
                         170       180
                  ....*....|....*....|....*....
gi 2462632188 178 IVEQdtMPPKgvRHTMMFSATFPKEIQML 206
Cdd:pfam00270 141 ILRR--LPKK--RQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
229-359 1.22e-60

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: 194.26  E-value: 1.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 229 ITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 308
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462632188 309 LVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 359
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
13-208 3.84e-59

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


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 193.57  E-value: 3.84e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  13 RYTRPTPVQKHAI-PIIKGKRDLMACAQTGSGKTAAFLLPilsqiytdgpgeALKAVKENGRYGRRKQYPIsLVLAPTRE 91
Cdd:cd17964    13 GFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLP------------AIQSLLNTKPAGRRSGVSA-LIISPTRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  92 LAVQIYEEARKFSYRSR-VRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMME--RGKIGLDFCKYLVLDEADRML 167
Cdd:cd17964    80 LALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462632188 168 DMGFEPQIRRIVeqDTMPPKGVRH--TMMFSATFPKEIQMLAR 208
Cdd:cd17964   160 DMGFRPDLEQIL--RHLPEKNADPrqTLLFSATVPDEVQQIAR 200
DEXDc smart00487
DEAD-like helicases superfamily;
9-232 2.51e-58

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 191.17  E-value: 2.51e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188    9 IELTRYTRPTPVQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkavkengRYGRRKQYPISLVLA 87
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-------------------EALKRGKGGRVLVLV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   88 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 166
Cdd:smart00487  62 PTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRL 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462632188  167 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRvgSTSENITQK 232
Cdd:smart00487 142 LDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
14-212 1.16e-57

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: 189.00  E-value: 1.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQ-IYTDgpgealkavkengrygRRKQYPISLVLAPTREL 92
Cdd:cd17947    10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERlLYRP----------------KKKAATRVLVLVPTREL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  93 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDFCKYLVLDEADRMLDMGF 171
Cdd:cd17947    74 AMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGF 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462632188 172 EPQIRRIVEqdtMPPKGvRHTMMFSATFPKEIQMLARDFLD 212
Cdd:cd17947   154 ADELKEILR---LCPRT-RQTMLFSATMTDEVKDLAKLSLN 190
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
5-220 1.41e-57

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: 188.95  E-value: 1.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALKAvkengrygrrkqypisL 84
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRA----------------L 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGG-ADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 163
Cdd:cd17957    65 ILAPTRELASQIYRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEA 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462632188 164 DRMLDMGFEPQIRRIVEQDTMPPKgvrHTMMFSATFPKEIQMLARDFLDEYIFLAVG 220
Cdd:cd17957   145 DKLFEPGFREQTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
14-216 1.15e-55

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: 184.35  E-value: 1.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIP-IIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDGpgealkavkengrYGrrkqyPISLVLAPTREL 92
Cdd:cd17955    19 IKEPTPIQKLCIPeILAG-RDVIGGAKTGSGKTAAFALPILQRLSEDP-------------YG-----IFALVLTPTREL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  93 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMME---RGKIGLDFCKYLVLDEADRMLDM 169
Cdd:cd17955    80 AYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462632188 170 GFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIF 216
Cdd:cd17955   160 SFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
5-213 2.37e-55

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: 183.05  E-value: 2.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqIYTDGpgEALKAVKENGrygrrkqyPISL 84
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF--IHLDL--QPIPREQRNG--------PGVL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKFSYRSRVRPCVvYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 164
Cdd:cd17958    69 VLTPTRELALQIEAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEAD 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462632188 165 RMLDMGFEPQIRRIVeQDTMPPkgvRHTMMFSATFPKEIQMLARDFLDE 213
Cdd:cd17958   148 RMLDMGFEPQIRKIL-LDIRPD---RQTIMTSATWPDGVRRLAQSYLKD 192
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
16-211 2.79e-54

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: 180.61  E-value: 2.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  16 RPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgeaLKAVKENGRYG-RRKQYPISLVLAPTRELAV 94
Cdd:cd17951    12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI-----------MFALEQEKKLPfIKGEGPYGLIVCPSRELAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  95 QIYEEARKFSYR------SRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLD 168
Cdd:cd17951    81 QTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462632188 169 MGFEPQIRRIVEQDtmppKGVRHTMMFSATFPKEIQMLARDFL 211
Cdd:cd17951   161 MGFEEDIRTIFSYF----KGQRQTLLFSATMPKKIQNFAKSAL 199
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
14-208 1.61e-52

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: 175.97  E-value: 1.61e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgealkavkengrygrrKQYPISLVLAPTRELA 93
Cdd:cd17954    20 WKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN------------------PQRFFALVLAPTRELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  94 VQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDFCKYLVLDEADRMLDMGFE 172
Cdd:cd17954    82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNMDFE 161
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462632188 173 PQIRRIVEqdTMPPKgvRHTMMFSATFPKEIQMLAR 208
Cdd:cd17954   162 PEIDKILK--VIPRE--RTTYLFSATMTTKVAKLQR 193
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
3-215 3.67e-50

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: 169.79  E-value: 3.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   3 EIIMGNIELTrYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengrygrrkqypI 82
Cdd:cd17940     9 ELLMGIFEKG-FEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV-------------------I 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  83 -SLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLD 161
Cdd:cd17940    69 qALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLD 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462632188 162 EADRMLDMGFEPQIRRIVeqDTMPPKgvRHTMMFSATFPKEIQmlarDFLDEYI 215
Cdd:cd17940   149 EADKLLSQDFQPIIEKIL--NFLPKE--RQILLFSATFPLTVK----NFMDRHM 194
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
13-217 7.38e-49

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: 166.61  E-value: 7.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  13 RYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealkavkengRYgRRKQYPISLVLAPTREL 92
Cdd:cd17949    10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEP-----------RV-DRSDGTLALVLVPTREL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  93 AVQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDFCKYLVLDEADRMLDMG 170
Cdd:cd17949    78 ALQIYEVLEKLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462632188 171 FEPQIRRIVE--------QDTMPPKGV-RHTMMFSATFPKEIQMLARDFLDEYIFL 217
Cdd:cd17949   158 FEKDITKILEllddkrskAGGEKSKPSrRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
14-217 9.97e-49

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: 165.94  E-value: 9.97e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgEALKAvkENGRYGRRkqypiSLVLAPTRELA 93
Cdd:cd17959    21 YKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMI---------EKLKA--HSPTVGAR-----ALILSPTRELA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  94 VQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEP 173
Cdd:cd17959    85 LQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAE 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462632188 174 QIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFL 217
Cdd:cd17959   165 QLHEILSR--LPEN--RQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
14-211 2.49e-48

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: 165.06  E-value: 2.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYtdgpgealkavkeNGRYGRRKQYPISLVLAPTRELA 93
Cdd:cd17960    10 FTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILL-------------KRKANLKKGQVGALIISPTRELA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  94 VQIYEEARKF--SYRSRVRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMMERGKIGLDF--CKYLVLDEADRMLD 168
Cdd:cd17960    77 TQIYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKVksLEVLVLDEADRLLD 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462632188 169 MGFEPQIRRIVEQdtmPPKGvRHTMMFSATFPKEIQMLARDFL 211
Cdd:cd17960   157 LGFEADLNRILSK---LPKQ-RRTGLFSATQTDAVEELIKAGL 195
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
1-198 7.15e-47

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: 160.95  E-value: 7.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   1 MGEIIMGnIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkavkengrygrrkQY 80
Cdd:cd17938     7 MPELIKA-VEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------------------------QI 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  81 PISLVLAPTRELAVQIYEEARKFSY---RSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKY 157
Cdd:cd17938    61 VVALILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRF 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462632188 158 LVLDEADRMLDMGFEPQIRRIVEQdtMPPKGVR----HTMMFSAT 198
Cdd:cd17938   141 FVLDEADRLLSQGNLETINRIYNR--IPKITSDgkrlQVIVCSAT 183
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
14-219 2.06e-45

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: 157.07  E-value: 2.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIY------TDGPGealkavkengrygrrkqypiSLVLA 87
Cdd:cd17941    10 FIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwtpEDGLG--------------------ALIIS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  88 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQirdLER--GCHLLVATPGRLVDMMERgKIGLDF--CKYLVLDEA 163
Cdd:cd17941    70 PTRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE---KERinRMNILVCTPGRLLQHMDE-TPGFDTsnLQMLVLDEA 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462632188 164 DRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAV 219
Cdd:cd17941   146 DRILDMGFKETLDAIVEN--LPKS--RQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
8-215 2.94e-44

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: 153.86  E-value: 2.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   8 NIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTdgpgealkavkengrygrRKQYPISLVLA 87
Cdd:cd17962     4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT------------------EHRNPSALILT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  88 PTRELAVQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 166
Cdd:cd17962    66 PTRELAVQIEDQAKELmKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTM 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462632188 167 LDMGFEPQIRRIVEQDTMPPKgvrhTMMFSATFPKEIQMLARDFLDEYI 215
Cdd:cd17962   146 LKMGFQQQVLDILENISHDHQ----TILVSATIPRGIEQLAGQLLQNPV 190
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
13-208 1.62e-43

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: 153.16  E-value: 1.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  13 RYTRPTPVQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeaLKAVKENGRYGRRKqYPISLVLAPTRE 91
Cdd:cd17946     9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERL--------LSQKSSNGVGGKQK-PLRALILTPTRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  92 LAVQI---YEEARKFsyrSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL---DFCKYLVLDEADR 165
Cdd:cd17946    80 LAVQVkdhLKAIAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLanlKSLRFLVLDEADR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462632188 166 MLDMG-FEP--QIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLAR 208
Cdd:cd17946   157 MLEKGhFAEleKILELLNKDRAGKKRKRQTFVFSATLTLDHQLPLK 202
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
5-208 2.04e-40

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: 143.65  E-value: 2.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   5 IMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTdgpgeaLKAVKENGRYGrrkqypisL 84
Cdd:cd17942     1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK------LKFKPRNGTGV--------I 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  85 VLAPTRELAVQIYEEARKF-SYRSRVRPCVVyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKiglDF----CKYLV 159
Cdd:cd17942    67 IISPTRELALQIYGVAKELlKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTK---GFlyknLQCLI 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462632188 160 LDEADRMLDMGFEPQIRRIVEqdtMPPKGvRHTMMFSATFPKEIQMLAR 208
Cdd:cd17942   143 IDEADRILEIGFEEEMRQIIK---LLPKR-RQTMLFSATQTRKVEDLAR 187
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
14-211 1.12e-39

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: 141.69  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDGPgeALKAvkengrygrrkqypisLVLAPTREL 92
Cdd:cd17939    17 FEKPSAIQQRAIvPIIKG-RDVIAQAQSGTGKTATFSIGALQRIDTTVR--ETQA----------------LVLAPTREL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  93 AVQIYE--EARKFSYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMG 170
Cdd:cd17939    78 AQQIQKvvKALGDYMGVKVHACI--GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRG 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462632188 171 FEPQIRRIVeqdTMPPKGVRhTMMFSATFPKEIQMLARDFL 211
Cdd:cd17939   156 FKDQIYDIF---QFLPPETQ-VVLFSATMPHEVLEVTKKFM 192
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
14-211 1.73e-39

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: 141.57  E-value: 1.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeaLKAVKENGRYgrrkQYPISLVLAPTRELA 93
Cdd:cd17961    14 WEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKI--------LKAKAESGEE----QGTRALILVPTRELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  94 VQIYEEARKFSY--RSRVRpCV-VYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL-DFCKYLVLDEADRMLDM 169
Cdd:cd17961    82 QQVSKVLEQLTAycRKDVR-VVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462632188 170 GFEPQIRRIVEqdtMPPKGVRHTMMfSATFPKEIQMLARDFL 211
Cdd:cd17961   161 GYEEDLKSLLS---YLPKNYQTFLM-SATLSEDVEALKKLVL 198
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
14-210 7.01e-39

DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 139.63  E-value: 7.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGK--RDLMACAQTGSGKTAAFLLPILSQIYTdgpgealkavkengrygrRKQYPISLVLAPTRE 91
Cdd:cd17963    14 FNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDP------------------TLKSPQALCLAPTRE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  92 LAVQIYEEARKF-SY-----RSRVRPCVVYGGADIGQQIrdlergchlLVATPGRLVDMMERGKIGLDFCKYLVLDEADR 165
Cdd:cd17963    76 LARQIGEVVEKMgKFtgvkvALAVPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQLDLKKIKILVLDEADV 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462632188 166 MLDM-GFEPQIRRIVEqdtMPPKGVRhTMMFSATFPKEIQMLARDF 210
Cdd:cd17963   147 MLDTqGHGDQSIRIKR---MLPRNCQ-ILLFSATFPDSVRKFAEKI 188
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
240-350 7.03e-37

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: 131.18  E-value: 7.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 240 DKRSFLLDILgATGSDSLTLVFVETKKGADsLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGL 319
Cdd:pfam00271   1 EKLEALLELL-KKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462632188 320 DISNVRHVINFDLPSDIEEYVHRIGRTGRVG 350
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
14-211 3.40e-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: 132.57  E-value: 3.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaLKAVKengrygrrkqypiSLVLAPTREL 92
Cdd:cd18046    19 FEKPSAIQQRAImPCIKG-YDVIAQAQSGTGKTATFSISILQQIDTS-----LKATQ-------------ALVLAPTREL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  93 AVQIYE--EARKFSYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMG 170
Cdd:cd18046    80 AQQIQKvvMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRG 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462632188 171 FEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL 211
Cdd:cd18046   158 FKDQIYDIFQK--LPPD--TQVVLLSATMPNDVLEVTTKFM 194
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
17-211 4.48e-36

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


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 132.47  E-value: 4.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  17 PTPVQKHAIP-IIKGKrDLMACAQTGSGKTAAFLLPILSQIYTDgPGEalkavkengrygrrkqypIS-LVLAPTRELAV 94
Cdd:cd17950    25 PSEVQHECIPqAILGM-DVLCQAKSGMGKTAVFVLSTLQQLEPV-DGQ------------------VSvLVICHTRELAF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  95 QIYEEARKFS-YRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM---LDM 169
Cdd:cd17950    85 QISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleqLDM 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462632188 170 gfepqiRRIVeQD--TMPPKGvRHTMMFSATFPKEIQMLARDFL 211
Cdd:cd17950   165 ------RRDV-QEifRATPHD-KQVMMFSATLSKEIRPVCKKFM 200
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
14-216 4.18e-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: 129.31  E-value: 4.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPilsqiytdgpgeALKAVKengrygRRKQYPISLVLAPTRELA 93
Cdd:cd17943    10 FQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVI------------ALESLD------LERRHPQVLILAPTREIA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  94 VQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 172
Cdd:cd17943    72 VQIHDVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQ 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462632188 173 PQIRRIveqDTMPPKGvRHTMMFSATFPKE-IQMLARdFLDEYIF 216
Cdd:cd17943   151 KDVNWI---FSSLPKN-KQVIAFSATYPKNlDNLLAR-YMRKPVL 190
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
14-213 4.32e-32

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: 121.42  E-value: 4.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAI-PIIKGkRDLMACAQTGSGKTAAFLLPILSQIYTdgpgealkAVKEngrygrrkqyPISLVLAPTREL 92
Cdd:cd18045    19 FEKPSAIQQRAIkPIIKG-RDVIAQSQSGTGKTATFSISVLQCLDI--------QVRE----------TQALILSPTREL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  93 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 172
Cdd:cd18045    80 AVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462632188 173 PQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDE 213
Cdd:cd18045   160 EQIYDVYRY--LPPA--TQVVLVSATLPQDILEMTNKFMTD 196
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
11-201 2.63e-31

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 120.16  E-value: 2.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  11 LTRY--TRPTPVQKHAIP-IIKGKRDLMAcAQTGSGKTAAFLLPILSQIYTDgpgEALKAVKENGrygrrkqyPISLVLA 87
Cdd:cd17948     5 LQRQgiTKPTTVQKQGIPsILRGRNTLCA-AETGSGKTLTYLLPIIQRLLRY---KLLAEGPFNA--------PRGLVIT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  88 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIgQQIRDLERG-CHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 166
Cdd:cd17948    73 PSRELAEQIGSVAQSLTEGLGLKVKVITGGRTK-RQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462632188 167 LDMGFEPQIRRIVEQ-----------DTMPPKGvrHTMMFSATFPK 201
Cdd:cd17948   152 LDDSFNEKLSHFLRRfplasrrsentDGLDPGT--QLVLVSATMPS 195
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
19-211 1.48e-30

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: 117.26  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  19 PVQ-KHAIPIIKGKrDLMACAQTGSGKTAAFLLPILsqiytdgpgEALKAVKENGRYGRRkqyPISLVLAPTRELAVQIY 97
Cdd:cd17944    15 PIQvKTFHPVYSGK-DLIAQARTGTGKTFSFAIPLI---------EKLQEDQQPRKRGRA---PKVLVLAPTRELANQVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  98 EEARKFSYRSRVrpCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRR 177
Cdd:cd17944    82 KDFKDITRKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462632188 178 IV-EQDTMPPKGVRHTMMFSATFPKEIQMLARDFL 211
Cdd:cd17944   160 ILsVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
HELICc smart00490
helicase superfamily c-terminal domain;
269-350 2.39e-30

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 112.69  E-value: 2.39e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  269 DSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGR 348
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 2462632188  349 VG 350
Cdd:smart00490  81 AG 82
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
13-206 1.62e-26

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: 106.95  E-value: 1.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  13 RYTRPTPVQKHAIP-IIKG--------KRDLMACAQTGSGKTAAFLLPILsQIYTDGPGEALKAvkengrygrrkqypis 83
Cdd:cd17956     9 GITSAFPVQAAVIPwLLPSskstppyrPGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVPRLRA---------------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  84 LVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL--------LVATPGRLVDMMERGK-IGLDF 154
Cdd:cd17956    72 LIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGrylsrvdiLVATPGRLVDHLNSTPgFTLKH 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462632188 155 CKYLVLDEADRMLDMGFE---PQIRRIVEQDTMP------------PKGVR-HTMMFSATF---PKEIQML 206
Cdd:cd17956   152 LRFLVIDEADRLLNQSFQdwlETVMKALGRPTAPdlgsfgdanlleRSVRPlQKLLFSATLtrdPEKLSSL 222
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
1-210 8.78e-25

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


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 102.84  E-value: 8.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188   1 MGEIIMGNIELTRYTRPTPVQKHAIPIIKGKR----------------DLMACAQTGSGKTAAFLLPILSQIY---TDGP 61
Cdd:cd17965    15 IKEILKGSNKTDEEIKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKrqeQEPF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  62 GEALKAVKENGRYGRrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVV-YGGADIGQQIRDLERG-CHLLVATPG 139
Cdd:cd17965    95 EEAEEEYESAKDTGR----PRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLAFKGrIDILVTTPG 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462632188 140 RLVDMME-RGKIgLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgVRHTMMFSATFPKEIQMLARDF 210
Cdd:cd17965   171 KLASLAKsRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APK--LKHLILCSATIPKEFDKTLRKL 237
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
29-345 2.50e-21

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 97.02  E-value: 2.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  29 KGKRDLMACAQTGSGKTAAfllpilsqiytdgpgeALKAVKENGRYGRrkqypiSLVLAPTRELAVQIYEEARKFsyrsr 108
Cdd:COG1061    98 RGGGRGLVVAPTGTGKTVL----------------ALALAAELLRGKR------VLVLVPRRELLEQWAEELRRF----- 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 109 vrpcvvYGGADIGQQIRDleRGCHLLVATPGRLVDMMERGKIGlDFCKYLVLDEADRmldmGFEPQIRRIVEQdtMPPKg 188
Cdd:COG1061   151 ------LGDPLAGGGKKD--SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEA--FPAA- 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 189 vrHTMMFSAT------FPKEI-------------QMLARDFLDEYIFLAV--------GRVGSTSENITQKVVwVEDLDK 241
Cdd:COG1061   215 --YRLGLTATpfrsdgREILLflfdgivyeyslkEAIEDGYLAPPEYYGIrvdltderAEYDALSERLREALA-ADAERK 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 242 RSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI 321
Cdd:COG1061   292 DKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
                         330       340
                  ....*....|....*....|....
gi 2462632188 322 SNVRHVINFDLPSDIEEYVHRIGR 345
Cdd:COG1061   372 PRLDVAILLRPTGSPREFIQRLGR 395
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
118-372 9.10e-21

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 94.82  E-value: 9.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 118 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdfckyLVLDEA--------DrmldmgFEP---QIRRIVE 180
Cdd:COG0514    94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 181 QDTMPPkgvrhTMMFSATFPKE-----IQMLARDflDEYIFLA-VGRvgstsENITQKVVWVEDLDKRSFLLDILGATGS 254
Cdd:COG0514   163 RLPNVP-----VLALTATATPRvradiAEQLGLE--DPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPG 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 255 DSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATaVA-ARGLDISNVRHVINFDLP 333
Cdd:COG0514   231 GS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLP 308
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2462632188 334 SDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLD 372
Cdd:COG0514   309 KSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
14-207 3.91e-17

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: 80.45  E-value: 3.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGK--RDLMACAQTGSGKTAAFLLPILSqiytdgpgealkavkengRYGRRKQYPISLVLAPTRE 91
Cdd:cd18048    38 FNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLS------------------RVDALKLYPQCLCLSPTFE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  92 LAVQ---IYEEARKFSYRSRV----RPCVVYGGADIGQQIrdlergchlLVATPGRLVDMMERGK-IGLDFCKYLVLDEA 163
Cdd:cd18048   100 LALQtgkVVEEMGKFCVGIQViyaiRGNRPGKGTDIEAQI---------VIGTPGTVLDWCFKLRlIDVTNISVFVLDEA 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462632188 164 DRMLDM-GFEPQIRRIveQDTMPPKGvrHTMMFSATFPKEIQMLA 207
Cdd:cd18048   171 DVMINVqGHSDHSVRV--KRSMPKEC--QMLLFSATFEDSVWAFA 211
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
241-348 1.60e-14

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 75.92  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 241 KRSFLLDILG---ATGSDSLTLVFVETKKGADSLEDFLYHEGYACT------SIHGDR--SQRDREEALHQFRSGKSPIL 309
Cdd:COG1111   336 KLSKLREILKeqlGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGEFNVL 415
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462632188 310 VATAVAARGLDISNVRHVINFDL-PSDIeEYVHRIGRTGR 348
Cdd:COG1111   416 VATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR 454
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
258-345 7.05e-14

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: 68.77  E-value: 7.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 258 TLVFVETKKGADSLEDFLYHEGYACTSI-------HGDRSQ--------RDREEALHQFRSGKSPILVATAVAARGLDIS 322
Cdd:cd18802    28 GIIFVERRATAVVLSRLLKEHPSTLAFIrcgfligRGNSSQrkrslmtqRKQKETLDKFRDGELNLLIATSVLEEGIDVP 107
                          90       100
                  ....*....|....*....|...
gi 2462632188 323 NVRHVINFDLPSDIEEYVHRIGR 345
Cdd:cd18802   108 ACNLVIRFDLPKTLRSYIQSRGR 130
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
36-198 1.45e-13

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: 67.81  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  36 ACAQTGSGKTAAFLLPILSQIYTDGPGealkavkengrygrrkqypiSLVLAPTRELAVQIYEEARK-FSYRSRVRpcVV 114
Cdd:cd00046     6 ITAPTGSGKTLAALLAALLLLLKKGKK--------------------VLVLVPTKALALQTAERLRElFGPGIRVA--VL 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 115 YGGADIGQQIRDLERGCHLLVATPGRLVDMMER-GKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMpPKGVRhTM 193
Cdd:cd00046    64 VGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAG-LKNAQ-VI 141

                  ....*
gi 2462632188 194 MFSAT 198
Cdd:cd00046   142 LLSAT 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
14-207 2.23e-13

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: 68.98  E-value: 2.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  14 YTRPTPVQKHAIPIIKGK--RDLMACAQTGSGKTAAFLLPILSQIytdgpGEALKavkengrygrrkqYPISLVLAPTRE 91
Cdd:cd18047    21 FNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-----EPANK-------------YPQCLCLSPTYE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  92 LAVQ---IYEEARKFSyrsrvrPCVVYGGADIGQQirdLERGC----HLLVATPGRLVDMMERGK-IGLDFCKYLVLDEA 163
Cdd:cd18047    83 LALQtgkVIEQMGKFY------PELKLAYAVRGNK---LERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEA 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462632188 164 DRML-DMGFEPQIRRIveqDTMPPKGVRhTMMFSATFPKEIQMLA 207
Cdd:cd18047   154 DVMIaTQGHQDQSIRI---QRMLPRNCQ-MLLFSATFEDSVWKFA 194
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
226-350 1.00e-12

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: 65.31  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 226 SENITQKVVWVEDLDKRSFLLD-ILGATGSDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSG 304
Cdd:cd18794     1 RPNLFYSVRPKDKKDEKLDLLKrIKVEHLGGS-GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462632188 305 KSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVG 350
Cdd:cd18794    80 KIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
259-344 8.33e-12

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: 62.49  E-value: 8.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 259 LVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP--ILVATAVAARGLDISNVRHVINFDL---P 333
Cdd:cd18793    31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPwwnP 110
                          90
                  ....*....|....
gi 2462632188 334 SDIE---EYVHRIG 344
Cdd:cd18793   111 AVEEqaiDRAHRIG 124
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
15-355 7.10e-10

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: 61.39  E-value: 7.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  15 TRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEAlkavkengrygrrkqypisLVLAPTRELAV 94
Cdd:COG1205    55 ERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGATA-------------------LYLYPTKALAR 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  95 QIYEEARKF--SYRSRVRPCVVYGgaDIGQQIRD--LERGcHLLVATPgrlvDMMERgkiGL--------DF---CKYLV 159
Cdd:COG1205   116 DQLRRLRELaeALGLGVRVATYDG--DTPPEERRwiREHP-DIVLTNP----DMLHY---GLlphhtrwaRFfrnLRYVV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 160 LDEA---------------DRMldmgfepqiRRIVEQdtmppKGVRHTMMF-SATF--PKEiqmLARDFLDEYiFLAVGR 221
Cdd:COG1205   186 IDEAhtyrgvfgshvanvlRRL---------RRICRH-----YGSDPQFILaSATIgnPAE---HAERLTGRP-VTVVDE 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 222 VGSTSENITQkVVW----VEDLDKRSFLL---DILG-ATGSDSLTLVFVETKKGA----DSLEDFLYHEGYAcTSIHGDR 289
Cdd:COG1205   248 DGSPRGERTF-VLWnpplVDDGIRRSALAeaaRLLAdLVREGLRTLVFTRSRRGAellaRYARRALREPDLA-DRVAAYR 325
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 290 SQ---RDREEALHQFRSGKSPILVAT-AVAArGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLA 355
Cdd:COG1205   326 AGylpEERREIERGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
259-349 9.40e-10

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 61.01  E-value: 9.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 259 LVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP--ILVATAVAARGLDISNVRHVINFDLP--S 334
Cdd:COG0553   553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWwnP 632
                          90
                  ....*....|....*....
gi 2462632188 335 DIEEY----VHRIGRTGRV 349
Cdd:COG0553   633 AVEEQaidrAHRIGQTRDV 651
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
290-348 1.71e-09

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: 56.21  E-value: 1.71e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 290 SQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFD-LPSDIeEYVHRIGRTGR 348
Cdd:cd18801    75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
PRK13766 PRK13766
Hef nuclease; Provisional
255-348 1.65e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 57.19  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 255 DSLTLVFVETKKGADSLEDFLYHEGYAC------TSIHGDR--SQRDREEALHQFRSGKSPILVATAVAARGLDISNVRH 326
Cdd:PRK13766  365 DSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444
                          90       100
                  ....*....|....*....|...
gi 2462632188 327 VINFD-LPSDIeEYVHRIGRTGR 348
Cdd:PRK13766  445 VIFYEpVPSEI-RSIQRKGRTGR 466
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
308-348 1.67e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 51.17  E-value: 1.67e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462632188 308 ILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGR 348
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
18-163 2.10e-08

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 56.44  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  18 TPVQKHAIP--IIKGKRdLMACAQTGSGKTAafllpiLSQIYtdgpgeALKAVKENGRygrrkqypiSLVLAPTRELAVQ 95
Cdd:COG1204    24 YPPQAEALEagLLEGKN-LVVSAPTASGKTL------IAELA------ILKALLNGGK---------ALYIVPLRALASE 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  96 IYEEARKFSYRSRVRPCVVYGGADIGqqIRDLERgCHLLVATPGRLvDMMERGKIGL--DFcKYLVLDEA 163
Cdd:COG1204    82 KYREFKRDFEELGIKVGVSTGDYDSD--DEWLGR-YDILVATPEKL-DSLLRNGPSWlrDV-DLVVVDEA 146
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
16-198 2.80e-08

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 53.57  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  16 RPTPVQKHAIPIIKG------KRDLMACAQTGSGKTAAFLLPILsqiytdgpgealkAVKENGRYgrrkqypiSLVLAPT 89
Cdd:cd17918    15 SLTKDQAQAIKDIEKdlhspePMDRLLSGDVGSGKTLVALGAAL-------------LAYKNGKQ--------VAILVPT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  90 RELAVQIYEEARKfsYRSRVRPCVVYGG--ADIGQQIrDLERGCHLLVAtpgrlvdmMERGKIGLDFckyLVLDEADRMl 167
Cdd:cd17918    74 EILAHQHYEEARK--FLPFINVELVTGGtkAQILSGI-SLLVGTHALLH--------LDVKFKNLDL---VIVDEQHRF- 138
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462632188 168 dmgfepqirRIVEQDTMPPKGVRHTMMFSAT 198
Cdd:cd17918   139 ---------GVAQREALYNLGATHFLEATAT 160
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
13-66 3.28e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 52.80  E-value: 3.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462632188  13 RYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKT-AAFlLPILSQIYTDGPGEALK 66
Cdd:COG1201    21 RFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELP 74
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
21-163 3.29e-07

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


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 50.28  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  21 QKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgealkavkengrYGRRkqypiSLVLAPTRELAVQIYEEA 100
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD--------------PGSR-----ALYLYPTKALAQDQLRSL 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462632188 101 RKF--SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPgrlvDMME-----RGKIGLDFC---KYLVLDEA 163
Cdd:cd17923    66 RELleQLGLGIRVATYDGDTPREERRAIIRNPPRILLTNP----DMLHyallpHHDRWARFLrnlRYVVLDEA 134
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
22-199 2.10e-06

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 47.30  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  22 KHAIPIIKGKRDLMACAQTGSGKTA-AFLLPILsqiytdgpgealkavkengrygrRKQYPIsLVLAPTRELAVQIYEEA 100
Cdd:cd17926     9 LEAWLAHKNNRRGILVLPTGSGKTLtALALIAY-----------------------LKELRT-LIVVPTDALLDQWKERF 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 101 RKFSYRSRVrpCVVYGGADIGQqirdleRGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRmldmGFEPQIRRIVE 180
Cdd:cd17926    65 EDFLGDSSI--GLIGGGKKKDF------DDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEILK 132
                         170
                  ....*....|....*....
gi 2462632188 181 QDTMPPKgvrhtMMFSATF 199
Cdd:cd17926   133 ELNAKYR-----LGLTATP 146
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
31-163 3.93e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 47.65  E-value: 3.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  31 KRDLMACAQTGSGKT--AAFLLPILSQIytdgpgeaLKAVKENGRygrrkqypISLVLAPTRELAVQIYEEARKFSYrSR 108
Cdd:cd18034    16 KRNTIVVLPTGSGKTliAVMLIKEMGEL--------NRKEKNPKK--------RAVFLVPTVPLVAQQAEAIRSHTD-LK 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462632188 109 VRPCvvYGGADIGQQIRDLERGC----HLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 163
Cdd:cd18034    79 VGEY--SGEMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
276-372 5.50e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 48.94  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 276 YHEGYactsihgDRSQRDR-EEAlhqFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGL 354
Cdd:PRK11057  266 YHAGL-------DNDVRADvQEA---FQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAE 335
                          90
                  ....*....|....*...
gi 2462632188 355 ATSFFNEKNMNITKDLLD 372
Cdd:PRK11057  336 AMLFYDPADMAWLRRCLE 353
PRK13767 PRK13767
ATP-dependent helicase; Provisional
13-138 5.51e-06

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 49.11  E-value: 5.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  13 RYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALkavkENGRYgrrkqypiSLVLAPTREL 92
Cdd:PRK13767   29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGEL----EDKVY--------CLYVSPLRAL 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462632188  93 A-----------VQIYEEARKFSYR-SRVRPCVVYGGADIGQQIRDLERGCHLLVATP 138
Cdd:PRK13767   97 NndihrnleeplTEIREIAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTP 154
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
18-163 1.39e-05

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 45.72  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  18 TPVQKHAI-PIIKGKRDLMACAQTGSGKTAAFLLPIlsqiytdgpgeaLKAVKENGRygrrkqypISLVLAPTRELAVQI 96
Cdd:cd17921     3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAI------------LRALATSGG--------KAVYIAPTRALVNQK 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462632188  97 YEEARKFSYRSRVRPCVVYGGADIGqqiRDLERGCHLLVATPGRLVDMMERGKIGLDF-CKYLVLDEA 163
Cdd:cd17921    63 EADLRERFGPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGERLIQdVRLVVVDEA 127
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
158-350 9.78e-05

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 44.37  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 158 LVLDEADRMLDmgfEPQIRRIVEQDTMPPKGVRHTMMfSATFPKEIQMLARDFldEYIFLAVGRVGSTSENITQKVVWVE 237
Cdd:TIGR01587 128 LIFDEVHFYDE---YTLALILAVLEVLKDNDVPILLM-SATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILI 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 238 DLDKR---SFLLDILGATGSDSLTLVFVET-----------KKGADSLEDFLYHEGYActsiHGDRSQRDREEALHQFRS 303
Cdd:TIGR01587 202 ESDKVgeiSSLERLLEFIKKGGSIAIIVNTvdraqefyqqlKEKAPEEEIILYHSRFT----EKDRAKKEAELLREMKKS 277
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462632188 304 GKSPILVATAVAARGLDISnvrhvinFDL----PSDIEEYVHRIGRTGRVG 350
Cdd:TIGR01587 278 NEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYG 321
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
285-350 2.16e-04

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


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 41.56  E-value: 2.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462632188 285 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVI-----NFDLpSDIEEYVHRIGRTGRVG 350
Cdd:cd18810    57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGL-AQLYQLRGRVGRSKERA 126
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
258-348 2.29e-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: 41.48  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 258 TLVFVETKKGADSLED---FLYHEGYACTSI---HG--DRSQRDR-EEALhqfRSGKSPILVATAVAARGLDISNVRHVI 328
Cdd:cd18796    41 TLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAAL---KRGDLKVVVATSSLELGIDIGDVDLVI 117
                          90       100
                  ....*....|....*....|
gi 2462632188 329 NFDLPSDIEEYVHRIGRTGR 348
Cdd:cd18796   118 QIGSPKSVARLLQRLGRSGH 137
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
258-345 3.09e-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: 40.24  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 258 TLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDRE-EALHQFRSGKS--PILVATAVAARGLDISNVRHVInFDLP- 333
Cdd:cd18799     9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV-FLRPt 87
                          90
                  ....*....|...
gi 2462632188 334 -SDIeEYVHRIGR 345
Cdd:cd18799    88 eSRT-LFLQMLGR 99
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
285-359 3.71e-04

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: 41.08  E-value: 3.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462632188 285 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI--SNVRHVINFDLPSDiEEYVHRIGRTGRVGNLGLATSFF 359
Cdd:cd18789    74 ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLpeANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
20-147 8.13e-04

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 40.80  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  20 VQKHAIP-IIKGKRDLMACAQTGSGKTAAFLLPILsqiytdgpgEALKAVKENGRYGRRKQYpislvLAPTRELAVQIYE 98
Cdd:cd18023     5 IQSEVFPdLLYSDKNFVVSAPTGSGKTVLFELAIL---------RLLKERNPLPWGNRKVVY-----IAPIKALCSEKYD 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462632188  99 EAR-KFsyrSRVRPCVVYGGADigQQIRDLE--RGCHLLVATPGRLvDMMER 147
Cdd:cd18023    71 DWKeKF---GPLGLSCAELTGD--TEMDDTFeiQDADIILTTPEKW-DSMTR 116
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
31-165 1.25e-03

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 39.81  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  31 KRDLMACAQTGSGKTAAFLLPILSQIytdgpgealkaVKENGRYgrrkqypisLVLAPTRELAVQIYEEARKFsyRSRVR 110
Cdd:cd18035    16 NGNTLIVLPTGLGKTIIAILVAADRL-----------TKKGGKV---------LILAPSRPLVEQHAENLKRV--LNIPD 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462632188 111 PCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADR 165
Cdd:cd18035    74 KITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
285-324 1.32e-03

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 39.56  E-value: 1.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462632188 285 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNV 324
Cdd:cd18792    66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA 105
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
32-162 1.46e-03

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


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 39.49  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  32 RDLMACAQTGSGKTAAFLLPILSQIYtDGPGEALKAvkengrygrrkqypisLVLAPTRELAVQIYE------EARKFSY 105
Cdd:cd17922     2 RNVLIAAPTGSGKTEAAFLPALSSLA-DEPEKGVQV----------------LYISPLKALINDQERrleeplDEIDLEI 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462632188 106 RSRVRpcvvYGgaDIGQQIRD--LERGCHLLVATPGRLVDMMERGKIGLDF--CKYLVLDE 162
Cdd:cd17922    65 PVAVR----HG--DTSQSEKAkqLKNPPGILITTPESLELLLVNKKLRELFagLRYVVVDE 119
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
284-393 1.70e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.06  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  284 SIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTG-RVGnlGLATSFFNEK 362
Cdd:PRK09751   306 SHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGLFFPR 383
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462632188  363 NmniTKDLLDLLVEAKQEVPSWLENMAYEHH 393
Cdd:PRK09751   384 T---RRDLVDSAVIVECMFAGRLENLTPPHN 411
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
19-203 2.08e-03

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 39.24  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  19 PVQKHAIP--IIKGKRdLMACAQTGSGKTaafLLPILSqiytdgpgeALKAVKENGRygrrkqypiSLVLAPTRELAVQI 96
Cdd:cd18028     4 PPQAEAVRagLLKGEN-LLISIPTASGKT---LIAEMA---------MVNTLLEGGK---------ALYLVPLRALASEK 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  97 YEEarkFSYRSRVrpcvvygGADIGQQIRDLERG------CHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMG 170
Cdd:cd18028    62 YEE---FKKLEEI-------GLKVGISTGDYDEDdewlgdYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEE 131
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462632188 171 FEPQIRRIVEQDTMPPKGVRhTMMFSATF--PKEI 203
Cdd:cd18028   132 RGPTLESIVARLRRLNPNTQ-IIGLSATIgnPDEL 165
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
255-349 3.30e-03

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 40.17  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  255 DSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFR---SGKSPILVATAVAARGLDISNVRHVINFD 331
Cdd:PLN03142   487 DSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkpgSEKFVFLLSTRAGGLGINLATADIVILYD 566
                           90       100
                   ....*....|....*....|....*.
gi 2462632188  332 lpSD--------IEEYVHRIGRTGRV 349
Cdd:PLN03142   567 --SDwnpqvdlqAQDRAHRIGQKKEV 590
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
285-348 4.49e-03

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


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 37.71  E-value: 4.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 285 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISN-----VRHVINFDLPSdieeyVHRI-GRTGR 348
Cdd:cd18811    67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGR 131
ResIII pfam04851
Type III restriction enzyme, res subunit;
17-200 6.80e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 37.27  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  17 PTPVQKHAI-----PIIKGKRDLMACAQTGSGKTaafllpilsqiYTdgpgeALKAVKEngrygRRKQYPIS--LVLAPT 89
Cdd:pfam04851   4 LRPYQIEAIenlleSIKNGQKRGLIVMATGSGKT-----------LT-----AAKLIAR-----LFKKGPIKkvLFLVPR 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188  90 RELAVQIYEEARKFSyrsrvrPCVVYGGADIGQQIRDLERG-CHLLVATPGRLV--DMMERGKIGLDFCKYLVLDEADRm 166
Cdd:pfam04851  63 KDLLEQALEEFKKFL------PNYVEIGEIISGDKKDESVDdNKIVVTTIQSLYkaLELASLELLPDFFDVIIIDEAHR- 135
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462632188 167 ldmGFEPQIRRIVEQDTmPPKGVRhtmmFSATFP 200
Cdd:pfam04851 136 ---SGASSYRNILEYFK-PAFLLG----LTATPE 161
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
258-348 8.74e-03

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB 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: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 37.22  E-value: 8.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632188 258 TLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDlpSDIE 337
Cdd:cd18790    30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKE 107
                          90
                  ....*....|....*...
gi 2462632188 338 EY-------VHRIGRTGR 348
Cdd:cd18790   108 GFlrsetslIQTIGRAAR 125
 
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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