NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19075832|ref|NP_588332|]
View 

ATP-dependent RNA helicase Dbp6 [Schizosaccharomyces pombe]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13028779)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
137-380 7.00e-116

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: 344.23  E-value: 7.00e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLQDGRHGPmYSYGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLRCVVIVPTRE 216
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKSTP-PYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 217 LTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQL---NGDENECRIDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDE 293
Cdd:cd17956  80 LVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLlvdTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFLVIDE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 294 ADRLLDQSFQDWVDTVMMEISHPKCLQNKSNildldqnisptflpdIDTLLPYRLPSPLQKLVFSATLTRDPSKIASLKL 373
Cdd:cd17956 160 ADRLLNQSFQDWLETVMKALGRPTAPDLGSF---------------GDANLLERSVRPLQKLLFSATLTRDPEKLSSLKL 224

                ....*..
gi 19075832 374 HNPRLVL 380
Cdd:cd17956 225 HRPRLFT 231
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
408-541 6.66e-42

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: 147.27  E-value: 6.66e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 408 QEYHVSVSSEKPILLYHLIHSKNLTN-ILCFVKSNEAAARLHRLLEliheslNQSFSCGLFTSSLSRDERKKIISRFATG 486
Cdd:cd18787   3 QLYVVVEEEEKKLLLLLLLLEKLKPGkAIIFVNTKKRVDRLAELLE------ELGIKVAALHGDLSQEERERALKKFRSG 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19075832 487 DLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGREGFAWTLV 541
Cdd:cd18787  77 KVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
137-380 7.00e-116

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: 344.23  E-value: 7.00e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLQDGRHGPmYSYGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLRCVVIVPTRE 216
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKSTP-PYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 217 LTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQL---NGDENECRIDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDE 293
Cdd:cd17956  80 LVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLlvdTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFLVIDE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 294 ADRLLDQSFQDWVDTVMMEISHPKCLQNKSNildldqnisptflpdIDTLLPYRLPSPLQKLVFSATLTRDPSKIASLKL 373
Cdd:cd17956 160 ADRLLNQSFQDWLETVMKALGRPTAPDLGSF---------------GDANLLERSVRPLQKLLFSATLTRDPEKLSSLKL 224

                ....*..
gi 19075832 374 HNPRLVL 380
Cdd:cd17956 225 HRPRLFT 231
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
128-566 1.35e-97

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 304.38  E-value: 1.35e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 128 FSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLR 207
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILA----------GRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 208 CVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLNGdenecRIDVLVSTPGRLVDHIRNdESFSLQHLR 287
Cdd:COG0513  74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKR-----GVDIVVATPGRLLDLIER-GALDLSGVE 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 288 YMVIDEADRLLDqsfqdwvdtvmMEishpkclqnksnildldqnisptFLPDIDTLLPyRLPSPLQKLVFSATLTRDPSK 367
Cdd:COG0513 148 TLVLDEADRMLD-----------MG-----------------------FIEDIERILK-LLPKERQTLLFSATMPPEIRK 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 368 IASLKLHNPRLVLVQNKDMEVDDggeIEddaivfsvpptlQEYHVSVSSEKPILLYHLIHSKNLTNILCFVKSNEAAARL 447
Cdd:COG0513 193 LAKRYLKNPVRIEVAPENATAET---IE------------QRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRL 257
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 448 HRLLEliheslNQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGR 527
Cdd:COG0513 258 AEKLQ------KRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGR 331
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 19075832 528 TARAGREGFAWTLVQSHEGHHFSKLVKQLRRTLPIKRIK 566
Cdd:COG0513 332 TGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELP 370
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
128-568 8.96e-55

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 192.08  E-value: 8.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  128 FSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLqDGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQCLSH--RTVP- 204
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPAL-DGR---------DVLGSAPTGTGKTAAFLLPALQHLLDfpRRKSg 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  205 RLRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSlrhetYQLNGDENECRIDVLVSTPGRLVDHIRNdESFSLQ 284
Cdd:PRK11192  73 PPRILILTPTRELAMQVADQARELAKHTHLDIATITGGVA-----YMNHAEVFSENQDIVVATPGRLLQYIKE-ENFDCR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  285 HLRYMVIDEADRLLDQSFQDWVDTVMMEISHPKclqnksnildldqnisptflpdidtllpyrlpsplQKLVFSATLT-R 363
Cdd:PRK11192 147 AVETLILDEADRMLDMGFAQDIETIAAETRWRK-----------------------------------QTLLFSATLEgD 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  364 DPSKIASLKLHNPRlvlvqnkdmevddggEIEDDaivfsvPPT------LQEYHVSVSSE-KPILLYHLIHSKNLTNILC 436
Cdd:PRK11192 192 AVQDFAERLLNDPV---------------EVEAE------PSRrerkkiHQWYYRADDLEhKTALLCHLLKQPEVTRSIV 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  437 FVKSNEaaaRLHRLLELIHEslnQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPL 516
Cdd:PRK11192 251 FVRTRE---RVHELAGWLRK---AGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPR 324
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19075832  517 SVRSYVHRIGRTARAGREGFAWTLVQSHEghhfSKLVKQLRRTL--PIKRIKIE 568
Cdd:PRK11192 325 SADTYLHRIGRTGRAGRKGTAISLVEAHD----HLLLGKIERYIeePLKARVID 374
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
151-368 3.00e-42

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: 149.70  E-value: 3.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832   151 AVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRTvPRLRCVVIVPTRELTVQVAKTFEYYMS 230
Cdd:pfam00270   2 PIQAEAIPAILE----------GRDVLVQAPTGSGKTLAFLLPALEALDKLD-NGPQALVLAPTRELAEQIYEELKKLGK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832   231 GAGLQVCAWTGQKSLRHETYQLNGdenecrIDVLVSTPGRLVDHIRNDEsfSLQHLRYMVIDEADRLLDQSFQDWVDTVM 310
Cdd:pfam00270  71 GLGLKVASLLGGDSRKEQLEKLKG------PDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFGPDLEEIL 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19075832   311 MeishpkclqnksnildldqnisptflpdidtllpyRLPSPLQKLVFSATLTRDPSKI 368
Cdd:pfam00270 143 R-----------------------------------RLPKKRQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
408-541 6.66e-42

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: 147.27  E-value: 6.66e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 408 QEYHVSVSSEKPILLYHLIHSKNLTN-ILCFVKSNEAAARLHRLLEliheslNQSFSCGLFTSSLSRDERKKIISRFATG 486
Cdd:cd18787   3 QLYVVVEEEEKKLLLLLLLLEKLKPGkAIIFVNTKKRVDRLAELLE------ELGIKVAALHGDLSQEERERALKKFRSG 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19075832 487 DLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGREGFAWTLV 541
Cdd:cd18787  77 KVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
150-381 7.63e-33

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 124.91  E-value: 7.63e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832    150 FAVQAAVLPLLLQDGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQCLSHRTVPrlRCVVIVPTRELTVQVAKTFEYYM 229
Cdd:smart00487  10 RPYQKEAIEALLSGLR---------DVILAAPTGSGKTLAALLPALEALKRGKGG--RVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832    230 SGAGLQVCAWTGQKSLRHETYQLNGDenecRIDVLVSTPGRLVDHIRNDeSFSLQHLRYMVIDEADRLLDQSFQDWVDTV 309
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESG----KTDILVTTPGRLLDLLEND-KLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075832    310 MMeishpkclqnksnildldqnisptflpdidtllpyRLPSPLQKLVFSATLTRDPSKIASLKLHNPRLVLV 381
Cdd:smart00487 154 LK-----------------------------------LLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV 190
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
417-532 8.77e-26

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: 101.90  E-value: 8.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832   417 EKPILLYHLIHSKNLTNILCFVKSNEAAArlhrlLELIHESLNqsFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDL 496
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-----AELLLEKEG--IKVARLHGDLSQEEREEILEDFRKGKIDVLVATDV 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19075832   497 MARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAG 532
Cdd:pfam00271  74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
452-532 1.02e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 1.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832    452 ELIHESLNQ-SFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTAR 530
Cdd:smart00490   1 EELAELLKElGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 19075832    531 AG 532
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
451-534 3.21e-10

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 63.21  E-value: 3.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 451 LELIHESLNQ-SFSCGLFT--SS------LSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDP-PLSVRS 520
Cdd:COG1111 366 AEMIVEFLSEpGIKAGRFVgqASkegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPvPSEIRS 445
                        90
                ....*....|....*.
gi 19075832 521 yVHRIGRTAR--AGRE 534
Cdd:COG1111 446 -IQRKGRTGRkrEGRV 460
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
407-535 1.44e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 41.62  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  407 LQEYHVSVSS-EKPILLYHLIHS-KNLTNILCFV----------------KSNEAAARLHrlleliheslNQSFSCGLFT 468
Cdd:PRK11057 198 LNDPLIQISSfDRPNIRYTLVEKfKPLDQLMRYVqeqrgksgiiycnsraKVEDTAARLQ----------SRGISAAAYH 267
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075832  469 SSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGrtaRAGREG 535
Cdd:PRK11057 268 AGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG---RAGRDG 331
mfd TIGR00580
transcription-repair coupling factor (mfd); All proteins in this family for which functions ...
474-580 2.12e-03

transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273152 [Multi-domain]  Cd Length: 926  Bit Score: 41.19  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832   474 DERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRI-GRTARAGREGFAWTLVQSHEghhfsKL 552
Cdd:TIGR00580 699 NELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKKKAYAYLLYPHQK-----AL 773
                          90       100
                  ....*....|....*....|....*....
gi 19075832   553 VKQ-LRRTLPIKrikiEFSHISEEFVVAY 580
Cdd:TIGR00580 774 TEDaQKRLEAIQ----EFSELGAGFKIAL 798
 
Name Accession Description Interval E-value
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
137-380 7.00e-116

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: 344.23  E-value: 7.00e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLQDGRHGPmYSYGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLRCVVIVPTRE 216
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKSTP-PYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 217 LTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQL---NGDENECRIDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDE 293
Cdd:cd17956  80 LVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLlvdTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFLVIDE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 294 ADRLLDQSFQDWVDTVMMEISHPKCLQNKSNildldqnisptflpdIDTLLPYRLPSPLQKLVFSATLTRDPSKIASLKL 373
Cdd:cd17956 160 ADRLLNQSFQDWLETVMKALGRPTAPDLGSF---------------GDANLLERSVRPLQKLLFSATLTRDPEKLSSLKL 224

                ....*..
gi 19075832 374 HNPRLVL 380
Cdd:cd17956 225 HRPRLFT 231
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
128-566 1.35e-97

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 304.38  E-value: 1.35e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 128 FSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLR 207
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILA----------GRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 208 CVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLNGdenecRIDVLVSTPGRLVDHIRNdESFSLQHLR 287
Cdd:COG0513  74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKR-----GVDIVVATPGRLLDLIER-GALDLSGVE 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 288 YMVIDEADRLLDqsfqdwvdtvmMEishpkclqnksnildldqnisptFLPDIDTLLPyRLPSPLQKLVFSATLTRDPSK 367
Cdd:COG0513 148 TLVLDEADRMLD-----------MG-----------------------FIEDIERILK-LLPKERQTLLFSATMPPEIRK 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 368 IASLKLHNPRLVLVQNKDMEVDDggeIEddaivfsvpptlQEYHVSVSSEKPILLYHLIHSKNLTNILCFVKSNEAAARL 447
Cdd:COG0513 193 LAKRYLKNPVRIEVAPENATAET---IE------------QRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRL 257
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 448 HRLLEliheslNQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGR 527
Cdd:COG0513 258 AEKLQ------KRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGR 331
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 19075832 528 TARAGREGFAWTLVQSHEGHHFSKLVKQLRRTLPIKRIK 566
Cdd:COG0513 332 TGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELP 370
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
137-379 1.87e-56

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: 188.80  E-value: 1.87e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCL---SHRTVPRLRCVVIVP 213
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILS----------GRDVIGQAQTGSGKTLAFLLPILEKLlpePKKKGRGPQALVLAP 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 214 TRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLngdenECRIDVLVSTPGRLVDHIRNDeSFSLQHLRYMVIDE 293
Cdd:cd00268  71 TRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEAL-----KKGPDIVVGTPGRLLDLIERG-KLDLSNVKYLVLDE 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 294 ADRLLDQSFQDWVDTvmmeishpkclqnksnILDldqnisptflpdidtllpyRLPSPLQKLVFSATLTRDPSKIASLKL 373
Cdd:cd00268 145 ADRMLDMGFEEDVEK----------------ILS-------------------ALPKDRQTLLFSATLPEEVKELAKKFL 189

                ....*.
gi 19075832 374 HNPRLV 379
Cdd:cd00268 190 KNPVRI 195
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
128-568 8.96e-55

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 192.08  E-value: 8.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  128 FSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLqDGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQCLSH--RTVP- 204
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPAL-DGR---------DVLGSAPTGTGKTAAFLLPALQHLLDfpRRKSg 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  205 RLRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSlrhetYQLNGDENECRIDVLVSTPGRLVDHIRNdESFSLQ 284
Cdd:PRK11192  73 PPRILILTPTRELAMQVADQARELAKHTHLDIATITGGVA-----YMNHAEVFSENQDIVVATPGRLLQYIKE-ENFDCR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  285 HLRYMVIDEADRLLDQSFQDWVDTVMMEISHPKclqnksnildldqnisptflpdidtllpyrlpsplQKLVFSATLT-R 363
Cdd:PRK11192 147 AVETLILDEADRMLDMGFAQDIETIAAETRWRK-----------------------------------QTLLFSATLEgD 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  364 DPSKIASLKLHNPRlvlvqnkdmevddggEIEDDaivfsvPPT------LQEYHVSVSSE-KPILLYHLIHSKNLTNILC 436
Cdd:PRK11192 192 AVQDFAERLLNDPV---------------EVEAE------PSRrerkkiHQWYYRADDLEhKTALLCHLLKQPEVTRSIV 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  437 FVKSNEaaaRLHRLLELIHEslnQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPL 516
Cdd:PRK11192 251 FVRTRE---RVHELAGWLRK---AGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPR 324
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19075832  517 SVRSYVHRIGRTARAGREGFAWTLVQSHEghhfSKLVKQLRRTL--PIKRIKIE 568
Cdd:PRK11192 325 SADTYLHRIGRTGRAGRKGTAISLVEAHD----HLLLGKIERYIeePLKARVID 374
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
123-547 4.13e-44

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 163.43  E-value: 4.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  123 NTTVEFSSLNISSKLVERLQkqniTRGFA----VQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIvqcL 198
Cdd:PRK11776   1 MSMTAFSTLPLPPALLANLN----ELGYTemtpIQAQSLPAILA----------GKDVIAQAKTGSGKTAAFGLGL---L 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  199 SHRTVPRLRC--VVIVPTRELTVQVAK------TFEyymsgAGLQVCAWTGQKSLRHetyQLNGDENECRIdvLVSTPGR 270
Cdd:PRK11776  64 QKLDVKRFRVqaLVLCPTRELADQVAKeirrlaRFI-----PNIKVLTLCGGVPMGP---QIDSLEHGAHI--IVGTPGR 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  271 LVDHIRNdESFSLQHLRYMVIDEADRLLDQSFQDWVDTVmmeISHpkclqnksnildldqnisptflpdidtllpyrLPS 350
Cdd:PRK11776 134 ILDHLRK-GTLDLDALNTLVLDEADRMLDMGFQDAIDAI---IRQ--------------------------------APA 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  351 PLQKLVFSATLTRDPSKIASLKLHNPRLVLVQnkdmEVDDGGEIEDdaiVFsvpptlqeYHVSvSSEKPILLYHLI--HS 428
Cdd:PRK11776 178 RRQTLLFSATYPEGIAAISQRFQRDPVEVKVE----STHDLPAIEQ---RF--------YEVS-PDERLPALQRLLlhHQ 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  429 KNLTNILCFVKSN--EAAARLHrlleliheslNQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANT 506
Cdd:PRK11776 242 PESCVVFCNTKKEcqEVADALN----------AQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 19075832  507 QNVINYDPPLSVRSYVHRIGRTARAGREGFAWTLVQSHEGH 547
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQ 352
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
45-535 8.06e-43

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 160.46  E-value: 8.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832   45 LKKSASFSQAAQQALKQSRKEDNERDIEMQDVDAEAQPHDLLPIPQPSVEDFVDSKPHVKNITSVLPKWLAEPITVDPNT 124
Cdd:PRK01297   5 LKKIFGKGEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKPKPASLWKLEDFVVEPQE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  125 -TVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRTV 203
Cdd:PRK01297  85 gKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLA----------GHDAIGRAQTGTGKTAAFLISIINQLLQTPP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  204 PR------LRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLngDENECriDVLVSTPGRLVDHIRN 277
Cdd:PRK01297 155 PKerymgePRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQL--EARFC--DILVATPGRLLDFNQR 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  278 DESFsLQHLRYMVIDEADRLLDQSFqdwvdtvmmeishpkclqnksnildldqnisptfLPDIDTLLPYRLP-SPLQKLV 356
Cdd:PRK01297 231 GEVH-LDMVEVMVLDEADRMLDMGF----------------------------------IPQVRQIIRQTPRkEERQTLL 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  357 FSATLTRDPSKIASLKLHNPRLVLVQNKDMEVDDggeIEddaivfsvpptlQEYHVSVSSEKPILLYHLIHSKNLTNILC 436
Cdd:PRK01297 276 FSATFTDDVMNLAKQWTTDPAIVEIEPENVASDT---VE------------QHVYAVAGSDKYKLLYNLVTQNPWERVMV 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  437 FVKSNEAAARLHRLLelihesLNQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPL 516
Cdd:PRK01297 341 FANRKDEVRRIEERL------VKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPE 414
                        490
                 ....*....|....*....
gi 19075832  517 SVRSYVHRIGRTARAGREG 535
Cdd:PRK01297 415 DPDDYVHRIGRTGRAGASG 433
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
151-368 3.00e-42

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: 149.70  E-value: 3.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832   151 AVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRTvPRLRCVVIVPTRELTVQVAKTFEYYMS 230
Cdd:pfam00270   2 PIQAEAIPAILE----------GRDVLVQAPTGSGKTLAFLLPALEALDKLD-NGPQALVLAPTRELAEQIYEELKKLGK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832   231 GAGLQVCAWTGQKSLRHETYQLNGdenecrIDVLVSTPGRLVDHIRNDEsfSLQHLRYMVIDEADRLLDQSFQDWVDTVM 310
Cdd:pfam00270  71 GLGLKVASLLGGDSRKEQLEKLKG------PDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFGPDLEEIL 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19075832   311 MeishpkclqnksnildldqnisptflpdidtllpyRLPSPLQKLVFSATLTRDPSKI 368
Cdd:pfam00270 143 R-----------------------------------RLPKKRQILLLSATLPRNLEDL 165
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
122-537 5.84e-42

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 159.73  E-value: 5.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  122 PNTTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHR 201
Cdd:PRK04537   5 PLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALP----------GGDVAGQAQTGTGKTLAFLVAVMNRLLSR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  202 tvPRL--------RCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTG------QKSLRHETyqlngdenecrIDVLVST 267
Cdd:PRK04537  75 --PALadrkpedpRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGgvdydkQRELLQQG-----------VDVIIAT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  268 PGRLVDHIRNDESFSLQHLRYMVIDEADRLLDQSfqdwvdtvmmeishpkclqnksnildldqnisptFLPDIDTLLpYR 347
Cdd:PRK04537 142 PGRLIDYVKQHKVVSLHACEICVLDEADRMFDLG----------------------------------FIKDIRFLL-RR 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  348 LP--SPLQKLVFSATLTRDPSKIASLKLHNPRLVLVQNKDMevddggeieddaivfSVPPTLQEYHVSVSSEKPILLYHL 425
Cdd:PRK04537 187 MPerGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETI---------------TAARVRQRIYFPADEEKQTLLLGL 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  426 IHSKNLTNILCFVKSNEAAARLHRLLEliheslNQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVAN 505
Cdd:PRK04537 252 LSRSEGARTMVFVNTKAFVERVARTLE------RHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
                        410       420       430
                 ....*....|....*....|....*....|..
gi 19075832  506 TQNVINYDPPLSVRSYVHRIGRTARAGREGFA 537
Cdd:PRK04537 326 VKYVYNYDLPFDAEDYVHRIGRTARLGEEGDA 357
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
408-541 6.66e-42

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: 147.27  E-value: 6.66e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 408 QEYHVSVSSEKPILLYHLIHSKNLTN-ILCFVKSNEAAARLHRLLEliheslNQSFSCGLFTSSLSRDERKKIISRFATG 486
Cdd:cd18787   3 QLYVVVEEEEKKLLLLLLLLEKLKPGkAIIFVNTKKRVDRLAELLE------ELGIKVAALHGDLSQEERERALKKFRSG 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19075832 487 DLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGREGFAWTLV 541
Cdd:cd18787  77 KVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
128-568 7.36e-42

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 157.28  E-value: 7.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  128 FSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPR-- 205
Cdd:PRK10590   3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLE----------GRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAkg 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  206 ---LRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLNGDenecrIDVLVSTPGRLVDhIRNDESFS 282
Cdd:PRK10590  73 rrpVRALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGG-----VDVLVATPGRLLD-LEHQNAVK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  283 LQHLRYMVIDEADRLLDQSFqdwvdtvmmeishpkclqnksnildldqnisptfLPDIDTLLPyRLPSPLQKLVFSATLT 362
Cdd:PRK10590 147 LDQVEILVLDEADRMLDMGF----------------------------------IHDIRRVLA-KLPAKRQNLLFSATFS 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  363 RDPSKIASLKLHNPRLVLVQNKDMEVDdggEIEddaivfsvpptlQEYHVSVSSEKPILLYHLIHSKNLTNILCFVKSNE 442
Cdd:PRK10590 192 DDIKALAEKLLHNPLEIEVARRNTASE---QVT------------QHVHFVDKKRKRELLSQMIGKGNWQQVLVFTRTKH 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  443 AAARLHrllelihESLNQSfscGLFTSSL----SRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSV 518
Cdd:PRK10590 257 GANHLA-------EQLNKD---GIRSAAIhgnkSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVP 326
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19075832  519 RSYVHRIGRTARAGREGFAWTLVQSHEghhfSKLVKQLRRTL--PIKRIKIE 568
Cdd:PRK10590 327 EDYVHRIGRTGRAAATGEALSLVCVDE----HKLLRDIEKLLkkEIPRIAIP 374
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
137-376 9.71e-39

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: 141.24  E-value: 9.71e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRT--VPRLRCVVIVPT 214
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALL----------GKDICASAVTGSGKTAAFLLPILERLLYRPkkKAATRVLVLVPT 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 215 RELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLngdenECRIDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDEA 294
Cdd:cd17947  71 RELAMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAAL-----RARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 295 DRLLDQSFQDwvdtVMMEIshpkcLQnksnildldqnisptflpdidtllpyRLPSPLQKLVFSATLTRDPSKIASLKLH 374
Cdd:cd17947 146 DRMLEEGFAD----ELKEI-----LR--------------------------LCPRTRQTMLFSATMTDEVKDLAKLSLN 190

                ..
gi 19075832 375 NP 376
Cdd:cd17947 191 KP 192
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
124-560 1.11e-38

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 150.77  E-value: 1.11e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  124 TTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLqDGRhgpmysyggDVCVSAATGSGKTLSYVIPivqcLSHRTV 203
Cdd:PRK11634   4 FETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLL-NGR---------DVLGMAQTGSGKTAAFSLP----LLHNLD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  204 PRLRC---VVIVPTRELTVQVAKT---FEYYMSGAGLqVCAWTGQkslRHETyQLNGDENECRIdvLVSTPGRLVDHIRN 277
Cdd:PRK11634  70 PELKApqiLVLAPTRELAVQVAEAmtdFSKHMRGVNV-VALYGGQ---RYDV-QLRALRQGPQI--VVGTPGRLLDHLKR 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  278 DeSFSLQHLRYMVIDEADRLLDQSFQDWVDTVMMEIshpkclqnksnildldqnisptflpdidtllpyrlPSPLQKLVF 357
Cdd:PRK11634 143 G-TLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQI-----------------------------------PEGHQTALF 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  358 SATLTRDPSKIASLKLHNPRLVLVQNKdmevddggeieddaiVFSVPPTLQEYHVSVSSEKPILLYHLIHSKNLTNILCF 437
Cdd:PRK11634 187 SATMPEAIRRITRRFMKEPQEVRIQSS---------------VTTRPDISQSYWTVWGMRKNEALVRFLEAEDFDAAIIF 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  438 VKSNEAAarlhrlLElIHESLNQS-FSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPL 516
Cdd:PRK11634 252 VRTKNAT------LE-VAEALERNgYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 19075832  517 SVRSYVHRIGRTARAGREGFAWTLVQSHEghhfSKLVKQLRRTL 560
Cdd:PRK11634 325 DSESYVHRIGRTGRAGRAGRALLFVENRE----RRLLRNIERTM 364
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
128-376 6.76e-38

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: 138.99  E-value: 6.76e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 128 FSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRTvPRLR 207
Cdd:cd17954   2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQ----------GRDIIGLAETGSGKTAAFALPILQALLENP-QRFF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 208 CVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLNGdenecRIDVLVSTPGRLVDHIRNDESFSLQHLR 287
Cdd:cd17954  71 ALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAK-----KPHVIVATPGRLVDHLENTKGFSLKSLK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 288 YMVIDEADRLLDQSFQdwvdtvmmeishpkclqnksnildldqnisptflPDIDTLLPYrLPSPLQKLVFSATLTrdpSK 367
Cdd:cd17954 146 FLVMDEADRLLNMDFE----------------------------------PEIDKILKV-IPRERTTYLFSATMT---TK 187
                       250
                ....*....|..
gi 19075832 368 IASLK---LHNP 376
Cdd:cd17954 188 VAKLQrasLKNP 199
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
137-379 4.24e-37

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: 137.33  E-value: 4.24e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERL-QKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLS------HRTVPrLRCV 209
Cdd:cd17949   1 LVSHLkSKMGIEKPTAIQKLAIPVLLQ----------GRDVLVRSQTGSGKTLAYLLPIIQRLLsleprvDRSDG-TLAL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 210 VIVPTRELTVQVAKTFEYYmsgagLQVCAW------TGQKSLRHETYQLngdenecR--IDVLVSTPGRLVDHIRNDESF 281
Cdd:cd17949  70 VLVPTRELALQIYEVLEKL-----LKPFHWivpgylIGGEKRKSEKARL-------RkgVNILIATPGRLLDHLKNTQSF 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 282 SLQHLRYMVIDEADRLLDQSFQDWVDTVMmeishpKCLQNKSNildldqnisptflpdiDTLLPYRLPSPLQKLVFSATL 361
Cdd:cd17949 138 DVSNLRWLVLDEADRLLDMGFEKDITKIL------ELLDDKRS----------------KAGGEKSKPSRRQTVLVSATL 195
                       250
                ....*....|....*...
gi 19075832 362 TRDPSKIASLKLHNPRLV 379
Cdd:cd17949 196 TDGVKRLAGLSLKDPVYI 213
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
128-376 4.35e-37

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: 136.97  E-value: 4.35e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 128 FSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLShrTVPR-L 206
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILA----------GRDVIGGAKTGSGKTAAFALPILQRLS--EDPYgI 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 207 RCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLNGdenecRIDVLVSTPGRLVDHIRN--DESFSLQ 284
Cdd:cd17955  69 FALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSK-----RPHIVVATPGRLADHLRSsdDTTKVLS 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 285 HLRYMVIDEADRLLDQSFQDWVDTVmmeISHpkclqnksnildldqnisptflpdidtllpyrLPSPLQKLVFSATLTRD 364
Cdd:cd17955 144 RVKFLVLDEADRLLTGSFEDDLATI---LSA--------------------------------LPPKRQTLLFSATLTDA 188
                       250
                ....*....|..
gi 19075832 365 PSKIASLKLHNP 376
Cdd:cd17955 189 LKALKELFGNKP 200
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
137-381 1.33e-36

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: 135.41  E-value: 1.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLQdGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQCL-SHRTVPRLRCVVIVPTR 215
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLH-GR---------DLLACAPTGSGKTLAFLIPILQKLgKPRKKKGLRALILAPTR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 216 ELTVQVAKTFEYYMSGAGLQVCAWtgQKSLrhETYQLNGDENECRIDVLVSTPGRLVDHIRNDESfSLQHLRYMVIDEAD 295
Cdd:cd17957  71 ELASQIYRELLKLSKGTGLRIVLL--SKSL--EAKAKDGPKSITKYDILVSTPLRLVFLLKQGPI-DLSSVEYLVLDEAD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 296 RLLDQSFQDWVDTVMMEISHPKclqnksnildldqnisptflpdidtllpyrlpspLQKLVFSATLTRDPSKIASLKLHN 375
Cdd:cd17957 146 KLFEPGFREQTDEILAACTNPN----------------------------------LQRSLFSATIPSEVEELARSVMKD 191

                ....*.
gi 19075832 376 PRLVLV 381
Cdd:cd17957 192 PIRIIV 197
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
124-537 9.51e-35

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 136.25  E-value: 9.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  124 TTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQ-CLSH-- 200
Cdd:PRK04837   6 TEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLA----------GRDVAGQAQTGTGKTMAFLTATFHyLLSHpa 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  201 ---RTVPRLRCVVIVPTRELTVQVAKTFEYYMSGAGLQV-CAWTGqkslrhETYQLNGDENECRIDVLVSTPGRLVDHIR 276
Cdd:PRK04837  76 pedRKVNQPRALIMAPTRELAVQIHADAEPLAQATGLKLgLAYGG------DGYDKQLKVLESGVDILIGTTGRLIDYAK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  277 NDeSFSLQHLRYMVIDEADRLLDQSFqdwvdtvmmeishpkclqnksnildldqnisptfLPDIDTLLpYRLPSPLQKL- 355
Cdd:PRK04837 150 QN-HINLGAIQVVVLDEADRMFDLGF----------------------------------IKDIRWLF-RRMPPANQRLn 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  356 -VFSATLTRDPSKIASLKLHNPRLVlvqnkdmevddggEIEDDaivfsvpptlqeyhvsvssEKPillyhlihSKNLTNI 434
Cdd:PRK04837 194 mLFSATLSYRVRELAFEHMNNPEYV-------------EVEPE-------------------QKT--------GHRIKEE 233
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  435 LcFVKSNEAAARLhrLLELIHESL--------NQSFSC--------------GLFTSSLSRDERKKIISRFATGDLNLLV 492
Cdd:PRK04837 234 L-FYPSNEEKMRL--LQTLIEEEWpdraiifaNTKHRCeeiwghlaadghrvGLLTGDVAQKKRLRILEEFTRGDLDILV 310
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 19075832  493 CSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGREGFA 537
Cdd:PRK04837 311 ATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHS 355
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
133-373 1.05e-34

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: 130.40  E-value: 1.05e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 133 ISSKLVERLQKQNITRGFAVQAAVLPLLLQDGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQCL----SHRTVPRLRC 208
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGD---------DVLARAKTGTGKTLAFLLPAIQSLlntkPAGRRSGVSA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 209 VVIVPTRELTVQVAKTFE---YYMSGAGLQVCawTGQKSLRhetyqlngdENECRI-----DVLVSTPGRLVDHIRNdES 280
Cdd:cd17964  72 LIISPTRELALQIAAEAKkllQGLRKLRVQSA--VGGTSRR---------AELNRLrrgrpDILVATPGRLIDHLEN-PG 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 281 F--SLQHLRYMVIDEADRLLDQSFQDwvdtvmmeishpkclqnksnilDLDQnisptflpdIDTLLPYRLPSPLQKLVFS 358
Cdd:cd17964 140 VakAFTDLDYLVLDEADRLLDMGFRP----------------------DLEQ---------ILRHLPEKNADPRQTLLFS 188
                       250
                ....*....|....*
gi 19075832 359 ATLTRDPSKIASLKL 373
Cdd:cd17964 189 ATVPDEVQQIARLTL 203
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
152-381 2.88e-33

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: 125.87  E-value: 2.88e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 152 VQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLShrtvpRLR--------CVVIVPTRELTVQVAK 223
Cdd:cd17941  16 IQRDSIPHALQ----------GRDILGAAKTGSGKTLAFLVPLLEKLY-----RERwtpedglgALIISPTRELAMQIFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 224 TF----EYYMSGAGLqvcaWTGQKSLRHETYQLNgdenecRIDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDEADRLLD 299
Cdd:cd17941  81 VLrkvgKYHSFSAGL----IIGGKDVKEEKERIN------RMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 300 QSFQDWVDTVMMEishpkclqnksnildldqnisptflpdidtllpyrLPSPLQKLVFSATLTRDPSKIASLKLHNPRLV 379
Cdd:cd17941 151 MGFKETLDAIVEN-----------------------------------LPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195

                ..
gi 19075832 380 LV 381
Cdd:cd17941 196 SV 197
DEXDc smart00487
DEAD-like helicases superfamily;
150-381 7.63e-33

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 124.91  E-value: 7.63e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832    150 FAVQAAVLPLLLQDGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQCLSHRTVPrlRCVVIVPTRELTVQVAKTFEYYM 229
Cdd:smart00487  10 RPYQKEAIEALLSGLR---------DVILAAPTGSGKTLAALLPALEALKRGKGG--RVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832    230 SGAGLQVCAWTGQKSLRHETYQLNGDenecRIDVLVSTPGRLVDHIRNDeSFSLQHLRYMVIDEADRLLDQSFQDWVDTV 309
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESG----KTDILVTTPGRLLDLLEND-KLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075832    310 MMeishpkclqnksnildldqnisptflpdidtllpyRLPSPLQKLVFSATLTRDPSKIASLKLHNPRLVLV 381
Cdd:smart00487 154 LK-----------------------------------LLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV 190
PTZ00110 PTZ00110
helicase; Provisional
122-557 6.31e-32

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 130.28  E-value: 6.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  122 PNTTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIP-IVQCLSH 200
Cdd:PTZ00110 126 PKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALS----------GRDMIGIAETGSGKTLAFLLPaIVHINAQ 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  201 rtvPRLR------CVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQL-NGdenecrIDVLVSTPGRLVD 273
Cdd:PTZ00110 196 ---PLLRygdgpiVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALrRG------VEILIACPGRLID 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  274 HIRNDESfSLQHLRYMVIDEADRLLDQSFQDWVDTVMMEIShpkclqnksnildldqnisptflPDIDTLLpyrlpsplq 353
Cdd:PTZ00110 267 FLESNVT-NLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIR-----------------------PDRQTLM--------- 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  354 klvFSATLTRDPSKIA-SLKLHNPRLVLVQNKDMEVDDggEIEddaivfsvpptlQEYHVSVSSEKPILLYHLIHS--KN 430
Cdd:PTZ00110 314 ---WSATWPKEVQSLArDLCKEEPVHVNVGSLDLTACH--NIK------------QEVFVVEEHEKRGKLKMLLQRimRD 376
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  431 LTNILCFVKSNEAAARLHRLLEL-------IHESLNQsfscglftsslsrDERKKIISRFATGDLNLLVCSDLMARGIDV 503
Cdd:PTZ00110 377 GDKILIFVETKKGADFLTKELRLdgwpalcIHGDKKQ-------------EERTWVLNEFKTGKSPIMIATDVASRGLDV 443
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19075832  504 ANTQNVINYDPPLSVRSYVHRIGRTARAGREGFAWTLVQSHEGHHFSKLVKQLR 557
Cdd:PTZ00110 444 KDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLR 497
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
151-310 5.55e-31

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: 119.60  E-value: 5.55e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 151 AVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRTV----PRLRCVVIVPTRELTVQVAKTFE 226
Cdd:cd17960  15 PVQAATIPLFLS----------NKDVVVEAVTGSGKTLAFLIPVLEILLKRKAnlkkGQVGALIISPTRELATQIYEVLQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 227 YYMSGAGLQVCA--WTGQKSLRHETYQLNgdENECriDVLVSTPGRLVDHI-RNDESFSLQHLRYMVIDEADRLLDQSFQ 303
Cdd:cd17960  85 SFLEHHLPKLKCqlLIGGTNVEEDVKKFK--RNGP--NILVGTPGRLEELLsRKADKVKVKSLEVLVLDEADRLLDLGFE 160

                ....*..
gi 19075832 304 DWVDTVM 310
Cdd:cd17960 161 ADLNRIL 167
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
137-372 6.61e-31

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: 120.42  E-value: 6.61e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLQDGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQ-CLSHR-------TVPRLRC 208
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPAAIRDGK---------DVIGAAETGSGKTLAFGIPILErLLSQKssngvggKQKPLRA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 209 VVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTG----QKSLRhetyQLNGdenecRIDVLVSTPGRLVDHIRNDESF--S 282
Cdd:cd17946  72 LILTPTRELAVQVKDHLKAIAKYTNIKIASIVGglavQKQER----LLKK-----RPEIVVATPGRLWELIQEGNEHlaN 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 283 LQHLRYMVIDEADRLL-DQSFQdwvdtvmmEISHpkclqnksnILDLDQNISPTFLPDIdtllpyrlpsplQKLVFSATL 361
Cdd:cd17946 143 LKSLRFLVLDEADRMLeKGHFA--------ELEK---------ILELLNKDRAGKKRKR------------QTFVFSATL 193
                       250
                ....*....|.
gi 19075832 362 TRDPSKIASLK 372
Cdd:cd17946 194 TLDHQLPLKLN 204
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
135-376 6.98e-31

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: 119.61  E-value: 6.98e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 135 SKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHR-----TVPRLRCV 209
Cdd:cd17961   3 PRLLKAIAKLGWEKPTLIQSKAIPLALE----------GKDILARARTGSGKTAAYALPIIQKILKAkaesgEEQGTRAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 210 VIVPTRELTVQVAKTFE---YYMSGAgLQVCAWTGQKSLRHETYQLNGdenecRIDVLVSTPGRLVDHIRNDESFSLQHL 286
Cdd:cd17961  73 ILVPTRELAQQVSKVLEqltAYCRKD-VRVVNLSASSSDSVQRALLAE-----KPDIVVSTPARLLSHLESGSLLLLSTL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 287 RYMVIDEADRLLDQSFQDwvdtvmmeishpkclqnksnildldqnisptflpDIDTLLPYrLPSPLQKLVFSATLTRDPS 366
Cdd:cd17961 147 KYLVIDEADLVLSYGYEE----------------------------------DLKSLLSY-LPKNYQTFLMSATLSEDVE 191
                       250
                ....*....|
gi 19075832 367 KIASLKLHNP 376
Cdd:cd17961 192 ALKKLVLHNP 201
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
121-557 8.11e-30

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 123.36  E-value: 8.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  121 DPNTTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIV-QCLS 199
Cdd:PLN00206 116 VPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALS----------GRSLLVSADTGSGKTASFLVPIIsRCCT 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  200 HRT--VPRLR---CVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQL-NGdenecrIDVLVSTPGRLVD 273
Cdd:PLN00206 186 IRSghPSEQRnplAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIqQG------VELIVGTPGRLID 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  274 HIRNDEsFSLQHLRYMVIDEADRLLDQSFQDWVDTVMMEISHPkclqnksnildldqnisptflpdidtllpyrlpsplQ 353
Cdd:PLN00206 260 LLSKHD-IELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP------------------------------------Q 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  354 KLVFSATLTRDPSKIASLKLHNPRLVLVQNKDMevddggeieddaivfsvpPTLQEYHVSV---SSEKPILLYHLIHSKN 430
Cdd:PLN00206 303 VLLFSATVSPEVEKFASSLAKDIILISIGNPNR------------------PNKAVKQLAIwveTKQKKQKLFDILKSKQ 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  431 --LTNILCFVKSNEAAarlhrllELIHESLnqSFSCGLFTSSL----SRDERKKIISRFATGDLNLLVCSDLMARGIDVA 504
Cdd:PLN00206 365 hfKPPAVVFVSSRLGA-------DLLANAI--TVVTGLKALSIhgekSMKERREVMKSFLVGEVPVIVATGVLGRGVDLL 435
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19075832  505 NTQNVINYDPPLSVRSYVHRIGRTARAGREGFAWTLVQSHEGHHFSKLVKQLR 557
Cdd:PLN00206 436 RVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLK 488
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
128-379 1.70e-29

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: 115.86  E-value: 1.70e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 128 FSSLNISSKLVERLQKqnitRGFAV----QAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCL-SHRT 202
Cdd:cd17959   3 FQSMGLSPPLLRAIKK----KGYKVptpiQRKTIPLILD----------GRDVVAMARTGSGKTAAFLIPMIEKLkAHSP 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 203 VPRLRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLNGDEnecriDVLVSTPGRLVdHIRNDESFS 282
Cdd:cd17959  69 TVGARALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNP-----DIIIATPGRLL-HLLVEMNLK 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 283 LQHLRYMVIDEADRLLDQSFQDWVDtvmmEISHpkclqnksnildldqnisptflpdidtllpyRLPSPLQKLVFSATLT 362
Cdd:cd17959 143 LSSVEYVVFDEADRLFEMGFAEQLH----EILS-------------------------------RLPENRQTLLFSATLP 187
                       250
                ....*....|....*..
gi 19075832 363 RDPSKIASLKLHNPRLV 379
Cdd:cd17959 188 KLLVEFAKAGLNEPVLI 204
PTZ00424 PTZ00424
helicase 45; Provisional
128-541 2.94e-29

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 119.93  E-value: 2.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  128 FSSLNISSKLVERLQKQNITRGFAVQA-AVLPLLlqDGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQCLSHRTVPrL 206
Cdd:PTZ00424  30 FDALKLNEDLLRGIYSYGFEKPSAIQQrGIKPIL--DGY---------DTIGQAQSGTGKTATFVIAALQLIDYDLNA-C 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  207 RCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLNGDenecrIDVLVSTPGRLVDHIrNDESFSLQHL 286
Cdd:PTZ00424  98 QALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAG-----VHMVVGTPGRVYDMI-DKRHLRVDDL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  287 RYMVIDEADRLLDQSFqdwvdtvmmeishpkclqnKSNILDLDQnisptflpdidtllpyRLPSPLQKLVFSATLTRDPS 366
Cdd:PTZ00424 172 KLFILDEADEMLSRGF-------------------KGQIYDVFK----------------KLPPDVQVALFSATMPNEIL 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  367 KIASLKLHNPRLVLVQNKDMEVDDggeieddaivfsvpptLQEYHVSVSSE--KPILLYHLIHSKNLTNILCFVKSNEaa 444
Cdd:PTZ00424 217 ELTTKFMRDPKRILVKKDELTLEG----------------IRQFYVAVEKEewKFDTLCDLYETLTITQAIIYCNTRR-- 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  445 aRLHRLLELIHEslnQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHR 524
Cdd:PTZ00424 279 -KVDYLTKKMHE---RDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHR 354
                        410
                 ....*....|....*..
gi 19075832  525 IGRTARAGREGFAWTLV 541
Cdd:PTZ00424 355 IGRSGRFGRKGVAINFV 371
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
128-375 6.33e-28

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


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 111.81  E-value: 6.33e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 128 FSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQ------CLSHR 201
Cdd:cd17967   2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILA-GR---------DLMACAQTGSGKTAAFLLPIISklledgPPSVG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 202 TVPRL---RCVVIVPTRELTVQ---VAKTFEYymsGAGLQVCAWTGQKSLRHETYQLngdENECriDVLVSTPGRLVDHI 275
Cdd:cd17967  72 RGRRKaypSALILAPTRELAIQiyeEARKFSY---RSGVRSVVVYGGADVVHQQLQL---LRGC--DILVATPGRLVDFI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 276 rNDESFSLQHLRYMVIDEADRLLDQSfqdwvdtvmmeishpkclqnksnildldqnisptFLPDIDTLLPY-RLPSPL-- 352
Cdd:cd17967 144 -ERGRISLSSIKFLVLDEADRMLDMG----------------------------------FEPQIRKIVEHpDMPPKGer 188
                       250       260
                ....*....|....*....|...
gi 19075832 353 QKLVFSATLTRDPSKIASLKLHN 375
Cdd:cd17967 189 QTLMFSATFPREIQRLAADFLKN 211
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
141-378 2.25e-26

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: 106.68  E-value: 2.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 141 LQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSH-RTVPR--LRCVVIVPTREL 217
Cdd:cd17942   5 IEEMGFTKMTEIQAKSIPPLLE----------GRDVLGAAKTGSGKTLAFLIPAIELLYKlKFKPRngTGVIIISPTREL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 218 TVQ---VAKTFEYYMSGAGLQVcawTGQKSLRHETYQL-NGdenecrIDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDE 293
Cdd:cd17942  75 ALQiygVAKELLKYHSQTFGIV---IGGANRKAEAEKLgKG------VNILVATPGRLLDHLQNTKGFLYKNLQCLIIDE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 294 ADRLLDQSFQDwvdtvmmeishpkclqnksnilDLDQNISptflpdidtllpyRLPSPLQKLVFSATLTRDPSKIASLKL 373
Cdd:cd17942 146 ADRILEIGFEE----------------------EMRQIIK-------------LLPKRRQTMLFSATQTRKVEDLARISL 190

                ....*
gi 19075832 374 HNPRL 378
Cdd:cd17942 191 KKKPL 195
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
417-532 8.77e-26

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: 101.90  E-value: 8.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832   417 EKPILLYHLIHSKNLTNILCFVKSNEAAArlhrlLELIHESLNqsFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDL 496
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-----AELLLEKEG--IKVARLHGDLSQEEREEILEDFRKGKIDVLVATDV 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19075832   497 MARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAG 532
Cdd:pfam00271  74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
152-379 3.96e-25

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: 103.17  E-value: 3.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 152 VQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQClshrtvprLRCVVIVPTRELTVQVA---KTFEYY 228
Cdd:cd17938  25 IQAEAIPLILG----------GGDVLMAAETGSGKTGAFCLPVLQI--------VVALILEPSRELAEQTYnciENFKKY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 229 MSGAGLQVCAWTGQKSLRHETYQLNGDenecrIDVLVSTPGRLVDHIRNdESFSLQHLRYMVIDEADRLLDQSFQDWVDT 308
Cdd:cd17938  87 LDNPKLRVALLIGGVKAREQLKRLESG-----VDIVVGTPGRLEDLIKT-GKLDLSSVRFFVLDEADRLLSQGNLETINR 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075832 309 vmmeishpkcLQNKsnildldqnisptfLPDIdTLLPYRlpspLQKLVFSATL-TRDPSKIASLKLHNPRLV 379
Cdd:cd17938 161 ----------IYNR--------------IPKI-TSDGKR----LQVIVCSATLhSFEVKKLADKIMHFPTWV 203
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
137-310 6.21e-24

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: 100.52  E-value: 6.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCL------SHRTVPRLRCVV 210
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILR----------GRNTLCAAETGSGKTLTYLLPIIQRLlrykllAEGPFNAPRGLV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 211 IVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHetyQLNGDENEcrIDVLVSTPGRLVDHIRNdESFSLQHLRYMV 290
Cdd:cd17948  71 ITPSRELAEQIGSVAQSLTEGLGLKVKVITGGRTKRQ---IRNPHFEE--VDILVATPGALSKLLTS-RIYSLEQLRHLV 144
                       170       180
                ....*....|....*....|
gi 19075832 291 IDEADRLLDQSFQDWVDTVM 310
Cdd:cd17948 145 LDEADTLLDDSFNEKLSHFL 164
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
153-376 2.34e-23

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: 98.17  E-value: 2.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 153 QAAVLPLLLqdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLShRTVPRLRCVVIVPTRELTVQVAKTFE---YYM 229
Cdd:cd17939  25 QRAIVPIIK-----------GRDVIAQAQSGTGKTATFSIGALQRID-TTVRETQALVLAPTRELAQQIQKVVKalgDYM 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 230 sgaGLQVCAWTGQKSLRHETYQLNGDenecrIDVLVSTPGRLVDHIRNDeSFSLQHLRYMVIDEADRLLDQSFQDwvdtv 309
Cdd:cd17939  93 ---GVKVHACIGGTSVREDRRKLQYG-----PHIVVGTPGRVFDMLQRR-SLRTDKIKMFVLDEADEMLSRGFKD----- 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075832 310 mmeishpkclqnksNILDLDQnisptflpdidtllpyRLPSPLQKLVFSATLTRDPSKIASLKLHNP 376
Cdd:cd17939 159 --------------QIYDIFQ----------------FLPPETQVVLFSATMPHEVLEVTKKFMRDP 195
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
152-376 4.10e-23

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


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 97.78  E-value: 4.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 152 VQAAVLPLLLQdGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQCLSHrtVPRL---------RCVVIVPTRELTVQVA 222
Cdd:cd17945  16 IQRQAIPIGLQ-NR---------DIIGIAETGSGKTAAFLIPLLVYISR--LPPLdeetkddgpYALILAPTRELAQQIE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 223 KTFEYYMSGAGLQVCAWTGQKSLRHETYQL-NGdenecrIDVLVSTPGRLVDHIRNdESFSLQHLRYMVIDEADRLLDQS 301
Cdd:cd17945  84 EETQKFAKPLGIRVVSIVGGHSIEEQAFSLrNG------CEILIATPGRLLDCLER-RLLVLNQCTYVVLDEADRMIDMG 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075832 302 FQDWVDTVMMEIshPKCLQNKSNILDLDQNISPTFLpdidtllpYRlpsplQKLVFSATLTRDPSKIASLKLHNP 376
Cdd:cd17945 157 FEPQVTKILDAM--PVSNKKPDTEEAEKLAASGKHR--------YR-----QTMMFTATMPPAVEKIAKGYLRRP 216
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
152-376 7.90e-23

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: 96.60  E-value: 7.90e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 152 VQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLsHRTVPRLRCVVIVPTREL---TVQVAKTFEYY 228
Cdd:cd17940  25 IQEESIPIALS----------GRDILARAKNGTGKTGAYLIPILEKI-DPKKDVIQALILVPTRELalqTSQVCKELGKH 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 229 MsgaGLQVCAWTGQKSLRHETYQLNGDenecrIDVLVSTPGRLVDHIRNDESfSLQHLRYMVIDEADRLLDQSFQdwvdt 308
Cdd:cd17940  94 M---GVKVMVTTGGTSLRDDIMRLYQT-----VHVLVGTPGRILDLAKKGVA-DLSHCKTLVLDEADKLLSQDFQ----- 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075832 309 vmmeishpkclqnksnildldqnisptflPDIDTLLPYrLPSPLQKLVFSATLTRDPSKIASLKLHNP 376
Cdd:cd17940 160 -----------------------------PIIEKILNF-LPKERQILLFSATFPLTVKNFMDRHMHNP 197
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
137-379 1.26e-22

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: 95.79  E-value: 1.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLqdgrhgpmysYGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVpRLRCVVIVPTRE 216
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGL----------AGHDLIVQAKSGTGKTLVFVVIALESLDLERR-HPQVLILAPTRE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 217 LTVQVAKTF-EYYMSGAGLQVCAWTGQKSLRHETYQLNGdeneCRIdvLVSTPGRLVdHIRNDESFSLQHLRYMVIDEAD 295
Cdd:cd17943  70 IAVQIHDVFkKIGKKLEGLKCEVFIGGTPVKEDKKKLKG----CHI--AVGTPGRIK-QLIELGALNVSHVRLFVLDEAD 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 296 RLLDQSFQdwvDTVMMEISHpkclqnksnildldqnisptflpdidtllpyrLPSPLQKLVFSATLTRDPSKIASLKLHN 375
Cdd:cd17943 143 KLMEGSFQ---KDVNWIFSS--------------------------------LPKNKQVIAFSATYPKNLDNLLARYMRK 187

                ....
gi 19075832 376 PRLV 379
Cdd:cd17943 188 PVLV 191
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
127-302 6.60e-22

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: 95.42  E-value: 6.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 127 EFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRL 206
Cdd:cd18052  44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILA-GR---------DLMACAQTGSGKTAAFLLPVLTGMMKEGLTAS 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 207 R--------CVVIVPTRELTVQV---AKTFEYymsGAGLQVCAWTGQKSLRHETYQLngdENECRIdvLVSTPGRLVDHI 275
Cdd:cd18052 114 SfsevqepqALIVAPTRELANQIfleARKFSY---GTCIRPVVVYGGVSVGHQIRQI---EKGCHI--LVATPGRLLDFI 185
                       170       180
                ....*....|....*....|....*..
gi 19075832 276 rNDESFSLQHLRYMVIDEADRLLDQSF 302
Cdd:cd18052 186 -GRGKISLSKLKYLILDEADRMLDMGF 211
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
137-313 6.97e-22

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: 93.68  E-value: 6.97e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLR-----CVVI 211
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQ----------GIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQrngpgVLVL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 212 VPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSlrhetyqlNGDENECR--IDVLVSTPGRLVDhIRNDESFSLQHLRYM 289
Cdd:cd17958  71 TPTRELALQIEAECSKYSYKGLKSVCVYGGGNR--------NEQIEDLSkgVDIIIATPGRLND-LQMNNVINLKSITYL 141
                       170       180
                ....*....|....*....|....
gi 19075832 290 VIDEADRLLDQSFQDWVDTVMMEI 313
Cdd:cd17958 142 VLDEADRMLDMGFEPQIRKILLDI 165
HELICc smart00490
helicase superfamily c-terminal domain;
452-532 1.02e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 1.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832    452 ELIHESLNQ-SFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTAR 530
Cdd:smart00490   1 EELAELLKElGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 19075832    531 AG 532
Cdd:smart00490  81 AG 82
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
137-376 1.11e-21

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


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 93.25  E-value: 1.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIP-IVQCLSHRTVPRLR---CVVIV 212
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALS----------GRDMIGIAKTGSGKTAAFIWPmLVHIMDQRELEKGEgpiAVIVA 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 213 PTRELTVQV---AKTF-EYYmsgaGLQVCAWTGQKSLRHETYQLngdenECRIDVLVSTPGRLVDHIRNdESFSLQHLRY 288
Cdd:cd17952  71 PTRELAQQIyleAKKFgKAY----NLRVVAVYGGGSKWEQAKAL-----QEGAEIVVATPGRLIDMVKK-KATNLQRVTY 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 289 MVIDEADRLLDQSFQDWVDTVMMEIShpkclqnksnildldqnisptflPDIDTLLpyrlpsplqklvFSATLTRDPSKI 368
Cdd:cd17952 141 LVLDEADRMFDMGFEYQVRSIVGHVR-----------------------PDRQTLL------------FSATFKKKIEQL 185

                ....*...
gi 19075832 369 ASLKLHNP 376
Cdd:cd17952 186 ARDILSDP 193
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
138-310 1.34e-21

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: 92.99  E-value: 1.34e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 138 VERLQKQNITRGFAVQAAVLplllqdgrhGPMYSyGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLR-----CVVIV 212
Cdd:cd17944   2 IKLLQARGVTYLFPIQVKTF---------HPVYS-GKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRgrapkVLVLA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 213 PTRELTVQVAKTFEYYMSgaGLQVCAWTGQKSlrhetYQLNGDENECRIDVLVSTPGRLVDHIRNDEsFSLQHLRYMVID 292
Cdd:cd17944  72 PTRELANQVTKDFKDITR--KLSVACFYGGTP-----YQQQIFAIRNGIDILVGTPGRIKDHLQNGR-LDLTKLKHVVLD 143
                       170
                ....*....|....*...
gi 19075832 293 EADRLLDQSFQDWVDTVM 310
Cdd:cd17944 144 EVDQMLDMGFAEQVEEIL 161
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
122-313 6.09e-21

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: 91.99  E-value: 6.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 122 PNTTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHR 201
Cdd:cd18049  20 PKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALS----------GLDMVGVAQTGSGKTLSYLLPAIVHINHQ 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 202 tvPRLR------CVVIVPTRELTVQVAKTFEYYMSGAGLQ-VCAWTGQKslrhETYQLNGDENEcrIDVLVSTPGRLVDH 274
Cdd:cd18049  90 --PFLErgdgpiCLVLAPTRELAQQVQQVAAEYGRACRLKsTCIYGGAP----KGPQIRDLERG--VEICIATPGRLIDF 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19075832 275 IRNDESfSLQHLRYMVIDEADRLLDQSFQDWVDTVMMEI 313
Cdd:cd18049 162 LEAGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI 199
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
152-302 1.91e-20

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: 90.90  E-value: 1.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 152 VQAAVLPLLLQDgrhgPMYSYGGDVC----------VSAATGSGKTLSYVIPIVQCL----------------SHRTVPR 205
Cdd:cd17965  34 IQTLAIKKLLKT----LMRKVTKQTSneepklevflLAAETGSGKTLAYLAPLLDYLkrqeqepfeeaeeeyeSAKDTGR 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 206 LRCVVIVPTRELTVQVAKTFEYYMSGAGLQVcawTGQKSLRHETYQLNGDENECRIDVLVSTPGRLVDhIRNDESFSLQH 285
Cdd:cd17965 110 PRSVILVPTHELVEQVYSVLKKLSHTVKLGI---KTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLAS-LAKSRPKILSR 185
                       170
                ....*....|....*..
gi 19075832 286 LRYMVIDEADRLLDQSF 302
Cdd:cd17965 186 VTHLVVDEADTLFDRSF 202
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
137-303 1.32e-19

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: 87.04  E-value: 1.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 137 LVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRtvPRLR------CVV 210
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALS----------GRDMVGIAQTGSGKTLAFLLPAIVHINAQ--PPLErgdgpiVLV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 211 IVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLngdenECRIDVLVSTPGRLVDHIRNDESfSLQHLRYMV 290
Cdd:cd17966  69 LAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDL-----RRGVEICIATPGRLIDFLDQGKT-NLRRVTYLV 142
                       170
                ....*....|...
gi 19075832 291 IDEADRLLDQSFQ 303
Cdd:cd17966 143 LDEADRMLDMGFE 155
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
122-376 3.46e-19

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 86.66  E-value: 3.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 122 PNTTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHR 201
Cdd:cd17953   8 PKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMS----------GRDVIGIAKTGSGKTLAFLLPMFRHIKDQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 202 tvPRLR------CVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLN-GDEnecridVLVSTPGRLVDH 274
Cdd:cd17953  78 --RPVKpgegpiGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKrGAE------IVVCTPGRMIDI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 275 I--RNDESFSLQHLRYMVIDEADRLLDQSFQDWVdtvmMEIshpkclqnksnildldqnisptflpdIDTLLPYRlpspl 352
Cdd:cd17953 150 LtaNNGRVTNLRRVTYVVLDEADRMFDMGFEPQI----MKI--------------------------VNNIRPDR----- 194
                       250       260
                ....*....|....*....|....
gi 19075832 353 QKLVFSATLTRDPSKIASLKLHNP 376
Cdd:cd17953 195 QTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
122-313 3.49e-18

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: 85.06  E-value: 3.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 122 PNTTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHR 201
Cdd:cd18050  58 PKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALS----------GRDMVGIAQTGSGKTLAYLLPAIVHINHQ 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 202 tvPRLR------CVVIVPTRELTVQVAK-TFEYYMSGAGLQVCAWTGQKslrhETYQLNGDENEcrIDVLVSTPGRLVDH 274
Cdd:cd18050 128 --PYLErgdgpiCLVLAPTRELAQQVQQvADDYGKSSRLKSTCIYGGAP----KGPQIRDLERG--VEICIATPGRLIDF 199
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19075832 275 IRNDESfSLQHLRYMVIDEADRLLDQSFQDWVDTVMMEI 313
Cdd:cd18050 200 LEAGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI 237
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
173-379 1.53e-17

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: 81.06  E-value: 1.53e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 173 GGDVCVSAATGSGKTLSYVIP-IVQCLSHRTVPrlRCVVIVPTRELTVQVAKTFEYYMSGA-GLQVCAWTGQKSLRHETY 250
Cdd:cd17962  27 GRDILASADTGSGKTAAFLLPvIIRCLTEHRNP--SALILTPTRELAVQIEDQAKELMKGLpPMKTALLVGGLPLPPQLY 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 251 QLNGDenecrIDVLVSTPGRLVDhIRNDESFSLQHLRYMVIDEADRLLDQSFQDWVdtvmmeishpkclqnksniLDLDQ 330
Cdd:cd17962 105 RLQQG-----VKVIIATPGRLLD-ILKQSSVELDNIKIVVVDEADTMLKMGFQQQV-------------------LDILE 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 19075832 331 NIsptflpdidtllpyrlPSPLQKLVFSATLTRDPSKIASLKLHNPRLV 379
Cdd:cd17962 160 NI----------------SHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
141-368 1.26e-16

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: 78.92  E-value: 1.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 141 LQKQNITRGFAVQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIP-IVQCLSHRT-VPRLR-----CVVIVP 213
Cdd:cd17951   5 LKKKGIKKPTPIQMQGLPTILS----------GRDMIGIAFTGSGKTLVFTLPlIMFALEQEKkLPFIKgegpyGLIVCP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 214 TRELTVQVAKTFEYY---MSGAG---LQVCAWTGQKSLRHetyQLNGDENECRIdvLVSTPGRLVDHIrNDESFSLQHLR 287
Cdd:cd17951  75 SRELARQTHEVIEYYckaLQEGGypqLRCLLCIGGMSVKE---QLEVIRKGVHI--VVATPGRLMDML-NKKKINLDICR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 288 YMVIDEADRLLDQSFQDWVDTVMmeiSHPKclqnksnildldqnisptflpdidtllpyrlpSPLQKLVFSATLtrdPSK 367
Cdd:cd17951 149 YLCLDEADRMIDMGFEEDIRTIF---SYFK--------------------------------GQRQTLLFSATM---PKK 190

                .
gi 19075832 368 I 368
Cdd:cd17951 191 I 191
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
173-308 1.64e-16

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: 76.67  E-value: 1.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 173 GGDVCVSAATGSGKTLSYVIPIVQCLSHRtvpRLRCVVIVPTRELTVQVAKTF-EYYMSGAGLQVCawTGQKSLRHETYQ 251
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLKK---GKKVLVLVPTKALALQTAERLrELFGPGIRVAVL--VGGSSAEEREKN 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19075832 252 LNGDEnecriDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDEADRLLDQSFQDWVDT 308
Cdd:cd00046  76 KLGDA-----DIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILD 127
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
132-537 1.31e-15

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: 80.26  E-value: 1.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 132 NISSKLVERLQKQNITRGFAVQAAVLPLLLQdGRHgpmysyggdVCVSAATGSGKTLSYVIPIVQCLSHRtvPRLRCVVI 211
Cdd:COG1205  40 WLPPELRAALKKRGIERLYSHQAEAIEAARA-GKN---------VVIATPTASGKSLAYLLPVLEALLED--PGATALYL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 212 VPTRELTV-QVAKtFEYYMS--GAGLQVCAWTG--QKSLRHETYQlNGdenecriDVLVSTPgrlvD--HI---RNDESF 281
Cdd:COG1205 108 YPTKALARdQLRR-LRELAEalGLGVRVATYDGdtPPEERRWIRE-HP-------DIVLTNP----DmlHYgllPHHTRW 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 282 S--LQHLRYMVIDEA---------------DRLLdqsfqdwvdtvmmEIshpkCLQNKSNildldqnisPTFlpdidtll 344
Cdd:COG1205 175 ArfFRNLRYVVIDEAhtyrgvfgshvanvlRRLR-------------RI----CRHYGSD---------PQF-------- 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 345 pyrlpsplqklVF-SATLtRDPSKIASlklhnpRLVlvqNKDMEV--DDG---GEIEddaIVFSVPPTLQE-YHVSVSSE 417
Cdd:COG1205 221 -----------ILaSATI-GNPAEHAE------RLT---GRPVTVvdEDGsprGERT---FVLWNPPLVDDgIRRSALAE 276
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 418 KPILLYHLIHSKNLTniLCFVKSneaaarlHRLLELIHESLNQSFSCGLFTSS-------LSRDERKKIISRFATGDLNL 490
Cdd:COG1205 277 AARLLADLVREGLRT--LVFTRS-------RRGAELLARYARRALREPDLADRvaayragYLPEERREIERGLRSGELLG 347
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 19075832 491 LVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGREGFA 537
Cdd:COG1205 348 VVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
141-360 4.08e-15

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: 74.15  E-value: 4.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 141 LQKQNITRGFAVQAAVLPLLLQDGRHgpmysyggDVCVSAATGSGKTLSYVIPIVQCLShRTVPRLRCVVIVPTRELTVQ 220
Cdd:cd17963   9 LYAMGFNKPSKIQETALPLILSDPPE--------NLIAQSQSGTGKTAAFVLAMLSRVD-PTLKSPQALCLAPTRELARQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 221 VAKTFEYYMSGAGLQVCAWTGQKSLRHE---TYQlngdenecridVLVSTPGRLVDHIRNdESFSLQHLRYMVIDEADRL 297
Cdd:cd17963  80 IGEVVEKMGKFTGVKVALAVPGNDVPRGkkiTAQ-----------IVIGTPGTVLDWLKK-RQLDLKKIKILVLDEADVM 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075832 298 LDQSfqdwvdtvmmeiSHPKCLQNKSNIldldqnisptflpdidtllpyrLPSPLQKLVFSAT 360
Cdd:cd17963 148 LDTQ------------GHGDQSIRIKRM----------------------LPRNCQILLFSAT 176
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
173-535 1.01e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 77.37  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 173 GGDVCVSAATGSGKTLsyvipIVQCLSHRTVPRLRCVVIVPTRELTVQVAKTFEYYMSGAGLqvcawtgqkslrhetyql 252
Cdd:COG1061 100 GGRGLVVAPTGTGKTV-----LALALAAELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLA------------------ 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 253 NGDENECRIDVLVSTPGRLVDHIRNDEsFSlQHLRYMVIDEADRLLDQSFQDwvdtvmmeishpkclqnksnILDLdqnI 332
Cdd:COG1061 157 GGGKKDSDAPITVATYQSLARRAHLDE-LG-DRFGLVIIDEAHHAGAPSYRR--------------------ILEA---F 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 333 SPTFLpdidtllpyrlpsplqkLVFSATLTRDpskiaslklhnprlvlvqnkdmevdDGGEIEDDA---IVFSV------ 403
Cdd:COG1061 212 PAAYR-----------------LGLTATPFRS-------------------------DGREILLFLfdgIVYEYslkeai 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 404 ------PPTLQEYHVSVSSEK----------------------PILLYHLIHSKNLTNILCFVKSNEAAARLHRLLElih 455
Cdd:COG1061 250 edgylaPPEYYGIRVDLTDERaeydalserlrealaadaerkdKILRELLREHPDDRKTLVFCSSVDHAEALAELLN--- 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 456 eslNQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGREG 535
Cdd:COG1061 327 ---EAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGK 403
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
122-303 1.19e-14

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: 73.92  E-value: 1.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 122 PNTTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQdGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQCLSHR 201
Cdd:cd18051  17 PPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKS-KR---------DLMACAQTGSGKTAAFLLPILSQIYEQ 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 202 TVPRLR---------------CVVIVPTRELTVQV---AKTFEYYmsgAGLQVCAWTGQKSLRhetYQLNGDENECRIdv 263
Cdd:cd18051  87 GPGESLpsesgyygrrkqyplALVLAPTRELASQIydeARKFAYR---SRVRPCVVYGGADIG---QQMRDLERGCHL-- 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19075832 264 LVSTPGRLVDHIRNDEsFSLQHLRYMVIDEADRLLDQSFQ 303
Cdd:cd18051 159 LVATPGRLVDMLERGK-IGLDYCKYLVLDEADRMLDMGFE 197
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
128-364 3.64e-14

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: 71.34  E-value: 3.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 128 FSSLNISSKLVERLQKQNITRGFAVQA-AVLPLLlqdgrhgpmysYGGDVCVSAATGSGKTLSYVIPIVQCLShRTVPRL 206
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQrAIKPII-----------KGRDVIAQSQSGTGKTATFSISVLQCLD-IQVRET 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 207 RCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLngdenECRIDVLVSTPGRLVDHIRNdESFSLQHL 286
Cdd:cd18045  69 QALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKL-----DYGQHIVSGTPGRVFDMIRR-RSLRTRHI 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075832 287 RYMVIDEADRLLDQSFQDWVDTVmmeishpkclqnksnildldqnisptflpdidtllpYR-LPSPLQKLVFSATLTRD 364
Cdd:cd18045 143 KMLVLDEADEMLNKGFKEQIYDV------------------------------------YRyLPPATQVVLVSATLPQD 185
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
153-304 5.47e-14

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: 70.94  E-value: 5.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 153 QAAVLPLLLqdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHrTVPRLRCVVIVPTRELTVQVAK---TFEYYM 229
Cdd:cd18046  27 QRAIMPCIK-----------GYDVIAQAQSGTGKTATFSISILQQIDT-SLKATQALVLAPTRELAQQIQKvvmALGDYM 94
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075832 230 sgaGLQVCAWTGQKSLRHETYQLNGDenecrIDVLVSTPGRLVDHIrNDESFSLQHLRYMVIDEADRLLDQSFQD 304
Cdd:cd18046  95 ---GIKCHACIGGTSVRDDAQKLQAG-----PHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSRGFKD 160
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
152-364 7.10e-14

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: 70.84  E-value: 7.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 152 VQAAVLPLLLQdgrhgpmysyGGDVCVSAATGSGKTLSYVIPIVQCLSHRTvPRLRCVVIVPTRELTVQVAKTFEY---Y 228
Cdd:cd17950  28 VQHECIPQAIL----------GMDVLCQAKSGMGKTAVFVLSTLQQLEPVD-GQVSVLVICHTRELAFQISNEYERfskY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 229 MSGAGLQVcaWTGQKSLRHETYQLngdENECRiDVLVSTPGRLVDHIRNdESFSLQHLRYMVIDEADRLLDQsfqdwvdt 308
Cdd:cd17950  97 MPNVKTAV--FFGGVPIKKDIEVL---KNKCP-HIVVGTPGRILALVRE-KKLKLSHVKHFVLDECDKMLEQ-------- 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075832 309 vmmeishpkclqnksniLDLDQNISPTFLpdidtllpyRLPSPLQKLVFSATLTRD 364
Cdd:cd17950 162 -----------------LDMRRDVQEIFR---------ATPHDKQVMMFSATLSKE 191
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
411-531 1.38e-13

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: 68.00  E-value: 1.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 411 HVSVSSEKPILLYHLIHS-KNLTNILC---FVKSNEAAARLHRLLELiHESLNQSFSCGLFT----------SSLSRDER 476
Cdd:cd18802   1 EEIVVIPKLQKLIEILREyFPKTPDFRgiiFVERRATAVVLSRLLKE-HPSTLAFIRCGFLIgrgnssqrkrSLMTQRKQ 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19075832 477 KKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRtARA 531
Cdd:cd18802  80 KETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
136-545 3.23e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 72.24  E-value: 3.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 136 KLVERLQKQNITRGFAVQAAVLPLLLQDGRHgpmysyggdVCVSAATGSGKTLSYVIPIVQCLSHrtvpRLRCVVIVPTR 215
Cdd:COG1204  10 KVIEFLKERGIEELYPPQAEALEAGLLEGKN---------LVVSAPTASGKTLIAELAILKALLN----GGKALYIVPLR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 216 ELTVQVAKTFEYYMSGAGLQVCAWTGQkslrhetYQLNGDENEcRIDVLVSTPGRLVDHIRNDESFsLQHLRYMVIDEAd 295
Cdd:COG1204  77 ALASEKYREFKRDFEELGIKVGVSTGD-------YDSDDEWLG-RYDILVATPEKLDSLLRNGPSW-LRDVDLVVVDEA- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 296 RLLDqsfqdwvD-----TVMMEISHPKCLQNKSNILDLdqniSPTfLPDIDTLL----------PYRlPSPLQKLVFSat 360
Cdd:COG1204 147 HLID-------DesrgpTLEVLLARLRRLNPEAQIVAL----SAT-IGNAEEIAewldaelvksDWR-PVPLNEGVLY-- 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 361 ltrdpskiaslklhnprlvlvqNKDMEVDDGGEIEDDAIVFSVPPTLQE------YhvsVSSEKPILLYHLIHSKNLTNI 434
Cdd:COG1204 212 ----------------------DGVLRFDDGSRRSKDPTLALALDLLEEggqvlvF---VSSRRDAESLAKKLADELKRR 266
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 435 LCFVKSN---EAAARLHRLLELIHES--LNQSFSCG-LF-TSSLSRDERKKIISRFATGDLNLLVC-SDLMArGIdvaNT 506
Cdd:COG1204 267 LTPEEREeleELAEELLEVSEETHTNekLADCLEKGvAFhHAGLPSELRRLVEDAFREGLIKVLVAtPTLAA-GV---NL 342
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 19075832 507 --QNVINYDP------PLSVRSYVHRIGRTARAGRE--GFAWTLVQSHE 545
Cdd:COG1204 343 paRRVIIRDTkrggmvPIPVLEFKQMAGRAGRPGYDpyGEAILVAKSSD 391
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
153-294 2.92e-12

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 65.36  E-value: 2.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 153 QAAVLPLLLQDGRHgpmysyggdVCVSAATGSGKTLSYVIPIVQCLshRTVPRlRCVVIVPTRELTVQVAKTFEYYMSGA 232
Cdd:cd17921   6 QREALRALYLSGDS---------VLVSAPTSSGKTLIAELAILRAL--ATSGG-KAVYIAPTRALVNQKEADLRERFGPL 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075832 233 GLQVCAWTGQKSLRhetyqlNGDENECriDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDEA 294
Cdd:cd17921  74 GKNVGLLTGDPSVN------KLLLAEA--DILVATPEKLDLLLRNGGERLIQDVRLVVVDEA 127
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
392-534 1.38e-11

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: 62.67  E-value: 1.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 392 GEIEDDAIVFSVP-PTLQEYHVSVSSEKPILLYHLIHSKNLTnilcFVKSNEAAARL-HRLLELIHESLNQSFScGLFTS 469
Cdd:cd18796   2 KKLDIKVILPVAPeIFPWAGESGADAYAEVIFLLERHKSTLV----FTNTRSQAERLaQRLRELCPDRVPPDFI-ALHHG 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075832 470 SLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGRE 534
Cdd:cd18796  77 SLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGA 141
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
451-534 3.21e-10

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 63.21  E-value: 3.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 451 LELIHESLNQ-SFSCGLFT--SS------LSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDP-PLSVRS 520
Cdd:COG1111 366 AEMIVEFLSEpGIKAGRFVgqASkegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPvPSEIRS 445
                        90
                ....*....|....*.
gi 19075832 521 yVHRIGRTAR--AGRE 534
Cdd:COG1111 446 -IQRKGRTGRkrEGRV 460
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
160-294 1.89e-08

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: 54.51  E-value: 1.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 160 LLQDGRHgpmysyggdVCVSAATGSGKTLSYVIPIVQCLSHRtvPRLRCVVIVPT-----------RELTVQVaktfeyy 228
Cdd:cd17923  11 AARAGRS---------VVVTTGTASGKSLCYQLPILEALLRD--PGSRALYLYPTkalaqdqlrslRELLEQL------- 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075832 229 msGAGLQVCAWTGQKSlrHETYQLNGDENEcriDVLVSTPGRLvdH---IRNDESF--SLQHLRYMVIDEA 294
Cdd:cd17923  73 --GLGIRVATYDGDTP--REERRAIIRNPP---RILLTNPDML--HyalLPHHDRWarFLRNLRYVVLDEA 134
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
472-536 2.75e-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: 2.75e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075832 472 SRDERKKIISRfatgdLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGREGF 536
Cdd:cd18785  12 SIEHAEEIASS-----LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEG 71
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
150-527 3.46e-08

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 56.65  E-value: 3.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 150 FAVQAAVLPLLLQdGRHgpmysyggdVCVSAATGSGKTLSYVIPIVQCLSHRTVP-----RLRCVVIVPTRELTVQVAKT 224
Cdd:COG1201  26 TPPQREAWPAIAA-GES---------TLLIAPTGSGKTLAAFLPALDELARRPRPgelpdGLRVLYISPLKALANDIERN 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 225 FEyyMSGAGLQVCAWTGQKSLRHETYqlNGD--ENECRI------DVLVSTPgrlvdhirndESFSL-----------QH 285
Cdd:COG1201  96 LR--APLEEIGEAAGLPLPEIRVGVR--TGDtpASERQRqrrrppHILITTP----------ESLALlltspdarellRG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 286 LRYMVIDEadrlldqsfqdW---VDT---VMMEIShpkclqnksnildldqnisptfLPDIDTLLPyrlpSPLQKLVFSA 359
Cdd:COG1201 162 VRTVIVDE-----------IhalAGSkrgVHLALS----------------------LERLRALAP----RPLQRIGLSA 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 360 TLtRDPSKIAS--LKLHNPRLV-LVQ---NKDMEVddggEIEddaivfsVPPTLQEY------HVSVSSEKPIllYHLIH 427
Cdd:COG1201 205 TV-GPLEEVARflVGYEDPRPVtIVDagaGKKPDL----EVL-------VPVEDLIErfpwagHLWPHLYPRV--LDLIE 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 428 SKNLTniLCFVKSNEAAARL-HRLLELIHESLNQSfscGLFTSSLSRDERKKIISRFATGDLNLLVCS---DLmarGIDV 503
Cdd:COG1201 271 AHRTT--LVFTNTRSQAERLfQRLNELNPEDALPI---AAHHGSLSREQRLEVEEALKAGELRAVVATsslEL---GIDI 342
                       410       420
                ....*....|....*....|....
gi 19075832 504 ANTQNVINYDPPLSVRSYVHRIGR 527
Cdd:COG1201 343 GDVDLVIQVGSPKSVARLLQRIGR 366
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
173-293 1.74e-07

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: 51.04  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 173 GGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLRCVVIVPTRELTVQVAKTFEYYMSGAGLQ--VCAWTGQKSLRHETY 250
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEipVAVRHGDTSQSEKAK 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19075832 251 QLngdenECRIDVLVSTP---GRLVDHIRNDESFSlqHLRYMVIDE 293
Cdd:cd17922  81 QL-----KNPPGILITTPeslELLLVNKKLRELFA--GLRYVVVDE 119
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
121-320 1.79e-07

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: 52.33  E-value: 1.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 121 DPNTTV----EFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQDGRHgpmysyggDVCVSAATGSGKTLSYVIPIVQ 196
Cdd:cd18048   9 DPTSPLfsvkSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQ--------NLIAQSQSGTGKTAAFVLAMLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 197 CL-SHRTVPRlrCVVIVPTRELTVQVAKTFEYYMS-GAGLQVcawtgqkslrheTYQLNGDE----NECRIDVLVSTPGR 270
Cdd:cd18048  81 RVdALKLYPQ--CLCLSPTFELALQTGKVVEEMGKfCVGIQV------------IYAIRGNRpgkgTDIEAQIVIGTPGT 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 19075832 271 LVDHIRNDESFSLQHLRYMVIDEADRLLD-QSFQDwvDTVMMEISHPKCLQ 320
Cdd:cd18048 147 VLDWCFKLRLIDVTNISVFVLDEADVMINvQGHSD--HSVRVKRSMPKECQ 195
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
173-296 8.94e-07

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 49.74  E-value: 8.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 173 GGDVCVSAATGSGKTLsyvIPIVQCLSH----RTVPRLRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHE 248
Cdd:cd17927  17 GKNTIICLPTGSGKTF---VAVLICEHHlkkfPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENVS 93
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 19075832 249 TYQLNGDEnecriDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDEADR 296
Cdd:cd17927  94 VEQIVESS-----DVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
ResIII pfam04851
Type III restriction enzyme, res subunit;
176-303 1.27e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.44  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832   176 VCVSAATGSGKTLSYVIPIVQCLSHRTVPrlRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSlrhetyqlngD 255
Cdd:pfam04851  26 GLIVMATGSGKTLTAAKLIARLFKKGPIK--KVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKK----------D 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 19075832   256 ENECRIDVLVSTPGRLVDHIRN-DESFSLQHLRYMVIDEADRLLDQSFQ 303
Cdd:pfam04851  94 ESVDDNKIVVTTIQSLYKALELaSLELLPDFFDVIIIDEAHRSGASSYR 142
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
177-297 1.72e-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: 48.07  E-value: 1.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 177 CVSAATGSGKTLsyvipiVQCLSHRTVPRLRCVVIVPTRELTVQVAKTFEyymsgaglqvcawtgQKSLRHETYQLNGDE 256
Cdd:cd17926  22 ILVLPTGSGKTL------TALALIAYLKELRTLIVVPTDALLDQWKERFE---------------DFLGDSSIGLIGGGK 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19075832 257 NECRID--VLVSTPGRLVDHIrNDESFSLQHLRYMVIDEADRL 297
Cdd:cd17926  81 KKDFDDanVVVATYQSLSNLA-EEEKDLFDQFGLLIVDEAHHL 122
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
452-535 1.82e-06

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: 47.59  E-value: 1.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 452 ELIHESLNQS-FSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGrtaR 530
Cdd:cd18794  44 EQVAARLQSKgISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESG---R 120

                ....*
gi 19075832 531 AGREG 535
Cdd:cd18794 121 AGRDG 125
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
438-540 3.07e-06

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 50.14  E-value: 3.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 438 VKSNEAAARLHRLLELIHESLNQS----------------------FSCGLFTSSLSRDERKKIISRFATGDLNLLVC-S 494
Cdd:COG0514 209 VVPKPPDDKLAQLLDFLKEHPGGSgivyclsrkkveelaewlreagIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAtI 288
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 19075832 495 DL-MarGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGREGFAWTL 540
Cdd:COG0514 289 AFgM--GIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
411-534 3.32e-06

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 46.87  E-value: 3.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 411 HVSVSSEKPILLYHLIhsKNLTNILCFVKSNEAAARLHRLL--ELIHESLN----QSFSCGLftsslSRDERKKIISRFA 484
Cdd:cd18797  17 RGSARREAARLFADLV--RAGVKTIVFCRSRKLAELLLRYLkaRLVEEGPLaskvASYRAGY-----LAEDRREIEAELF 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 19075832 485 TGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGRE 534
Cdd:cd18797  90 NGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKD 139
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
468-535 4.02e-06

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 46.58  E-value: 4.02e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075832 468 TSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARaGREG 535
Cdd:cd18801  71 SKGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQG 137
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
178-294 4.50e-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: 4.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 178 VSAATGSGKTLSYVIPIVQcLSHR----TVPRLRCVVIVPTRELtvqVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLN 253
Cdd:cd18034  21 VVLPTGSGKTLIAVMLIKE-MGELnrkeKNPKKRAVFLVPTVPL---VAQQAEAIRSHTDLKVGEYSGEMGVDKWTKERW 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19075832 254 GDENEcRIDVLVSTPGRLVDHIRNDEsFSLQHLRYMVIDEA 294
Cdd:cd18034  97 KEELE-KYDVLVMTAQILLDALRHGF-LSLSDINLLIFDEC 135
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
474-545 3.11e-05

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: 44.26  E-value: 3.11e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075832 474 DERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRI-GRTARAGREGFAWTLVQSHE 545
Cdd:cd18810  64 NELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYAYFLYPDQK 136
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
420-535 6.61e-05

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: 43.39  E-value: 6.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 420 ILLYHlihsKNLTNILCFVKSNEAAARLHR--LLELIheslnqsfscglfTSSLSRDERKKIISRFATGDLNLLVCSDLM 497
Cdd:cd18789  42 LLKRH----EQGDKIIVFTDNVEALYRYAKrlLKPFI-------------TGETPQSEREEILQNFREGEYNTLVVSKVG 104
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19075832 498 ARGIDV--ANTQNVINYDPPlSVRSYVHRIGRTARAGREG 535
Cdd:cd18789 105 DEGIDLpeANVAIQISGHGG-SRRQEAQRLGRILRPKKGG 143
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
173-294 7.67e-05

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 44.06  E-value: 7.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 173 GGDVCVSAATGSGKTLSYVIPIVqcLSHRTVprlrcVVIVPTRELTV-QVAKtfeyyMSGAGLQVCAWTGQKSLRHETYQ 251
Cdd:cd17920  27 GRDVLVVMPTGGGKSLCYQLPAL--LLDGVT-----LVVSPLISLMQdQVDR-----LQQLGIRAAALNSTLSPEEKREV 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 19075832 252 LNG-DENECRIdVLVsTPGRLV-----DHIRNDESFSlqHLRYMVIDEA 294
Cdd:cd17920  95 LLRiKNGQYKL-LYV-TPERLLspdflELLQRLPERK--RLALIVVDEA 139
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
128-304 8.51e-05

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: 43.94  E-value: 8.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 128 FSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQDGRHgpmysyggDVCVSAATGSGKTLSYVIPIvqcLSH--RTVPR 205
Cdd:cd18047   3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQ--------NLIAQSQSGTGKTAAFVLAM---LSQvePANKY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 206 LRCVVIVPTRELTVQVAKTFEyymsgaglQVCAWTGQKSLrheTYQLNGDENE--CRI--DVLVSTPGRLVDHIRNDESF 281
Cdd:cd18047  72 PQCLCLSPTYELALQTGKVIE--------QMGKFYPELKL---AYAVRGNKLErgQKIseQIVIGTPGTVLDWCSKLKFI 140
                       170       180
                ....*....|....*....|....
gi 19075832 282 SLQHLRYMVIDEADRLL-DQSFQD 304
Cdd:cd18047 141 DPKKIKVFVLDEADVMIaTQGHQD 164
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
421-545 1.62e-04

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 42.25  E-value: 1.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 421 LLYHLIHSKNLTNilcfVKSNEAAARlhRLLELIHEslnqsFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARG 500
Cdd:cd18792  31 YVYPRIEESEKLD----LKSIEALAE--ELKELVPE-----ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVG 99
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19075832 501 IDVANTQNVINYDPPLSVRSYVHRI-GRTARAGREGFAWTLVQSHE 545
Cdd:cd18792 100 IDVPNANTMIIEDADRFGLSQLHQLrGRVGRGKHQSYCYLLYPDPK 145
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
151-293 2.23e-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: 42.73  E-value: 2.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 151 AVQAAVLPLLLQDGRhgpmysyggDVCVSAATGSGKTLSYVIPIVQCLSHRTVP---RLRCVVIVPTRELTVQVAKTFEY 227
Cdd:cd18023   4 RIQSEVFPDLLYSDK---------NFVVSAPTGSGKTVLFELAILRLLKERNPLpwgNRKVVYIAPIKALCSEKYDDWKE 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075832 228 YMSGAGLQVCAWTGQkslrhetYQLNGDENECRIDVLVSTPGR--LVDHIRNDESFSLQHLRYMVIDE 293
Cdd:cd18023  75 KFGPLGLSCAELTGD-------TEMDDTFEIQDADIILTTPEKwdSMTRRWRDNGNLVQLVALVLIDE 135
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
407-535 1.44e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 41.62  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832  407 LQEYHVSVSS-EKPILLYHLIHS-KNLTNILCFV----------------KSNEAAARLHrlleliheslNQSFSCGLFT 468
Cdd:PRK11057 198 LNDPLIQISSfDRPNIRYTLVEKfKPLDQLMRYVqeqrgksgiiycnsraKVEDTAARLQ----------SRGISAAAYH 267
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075832  469 SSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGrtaRAGREG 535
Cdd:PRK11057 268 AGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG---RAGRDG 331
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
183-297 2.05e-03

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins 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: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 39.47  E-value: 2.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 183 GSGKTLSyVIPIVQCLSHRTVPRLRCVVIVPT-------RELtvqvAKTFEyymsgaGLQVCAWTGQKSLRhetYQLNGD 255
Cdd:cd17919  29 GLGKTLQ-AIAFLAYLLKEGKERGPVLVVCPLsvlenweREF----EKWTP------DLRVVVYHGSQRER---AQIRAK 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19075832 256 ENECRIDVLVSTPGRLVDHIrndESFSLQHLRYMVIDEADRL 297
Cdd:cd17919  95 EKLDKFDVVLTTYETLRRDK---ASLRKFRWDLVVVDEAHRL 133
mfd TIGR00580
transcription-repair coupling factor (mfd); All proteins in this family for which functions ...
474-580 2.12e-03

transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273152 [Multi-domain]  Cd Length: 926  Bit Score: 41.19  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832   474 DERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRI-GRTARAGREGFAWTLVQSHEghhfsKL 552
Cdd:TIGR00580 699 NELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKKKAYAYLLYPHQK-----AL 773
                          90       100
                  ....*....|....*....|....*....
gi 19075832   553 VKQ-LRRTLPIKrikiEFSHISEEFVVAY 580
Cdd:TIGR00580 774 TEDaQKRLEAIQ----EFSELGAGFKIAL 798
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
470-527 2.99e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 40.68  E-value: 2.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19075832   470 SLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGR 527
Cdd:PRK09751  310 SVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGR 367
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
449-526 3.32e-03

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: 38.23  E-value: 3.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 449 RLLELIHESLNQ-SFSCGLFTSSLSRDERKKIISRFAT--GDLNLLVCSDLMARGID--VANTqnVINYDPPL--SV--- 518
Cdd:cd18793  38 DTLDILEEALRErGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGVGLNltAANR--VILYDPWWnpAVeeq 115
                        90
                ....*....|.
gi 19075832 519 ---RsyVHRIG 526
Cdd:cd18793 116 aidR--AHRIG 124
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
176-228 5.23e-03

Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442728 [Multi-domain]  Cd Length: 402  Bit Score: 39.58  E-value: 5.23e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 19075832 176 VCVSAATGSGKTLSYVIPIVQCLShrtvPRLRCVVIVPTRELtvqVAKTFEYY 228
Cdd:COG3505   2 VLVIGPTGSGKTVGLVIPNLTQLA----RGESVVVTDPKGDL---AELTAGFR 47
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
449-528 6.96e-03

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 39.44  E-value: 6.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 449 RLLELIHESLNQS-FSCGLFTSSLSRDERKKIISRFATGDLN--LLVCSDLMARGIDV--ANTqnVINYDPP--LSV--- 518
Cdd:COG0553 560 DTLDLLEERLEERgIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLtaADH--VIHYDLWwnPAVeeq 637
                        90
                ....*....|...
gi 19075832 519 ---RsyVHRIGRT 528
Cdd:COG0553 638 aidR--AHRIGQT 648
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
178-301 7.41e-03

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 38.08  E-value: 7.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 178 VSAATGSGKT---LSYVIPIVQclshrtvPRLRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCA--WTG--QKSLRHETY 250
Cdd:cd17924  37 IIAPTGVGKTtfgLATSLYLAS-------KGKRSYLIFPTKSLVKQAYERLSKYAEKAGVEVKIlvYHSrlKKKEKEELL 109
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 19075832 251 --QLNGDenecrIDVLVSTPGRLvdhIRNDESFSLQHLRYMVIDEADRLLDQS 301
Cdd:cd17924 110 ekIEKGD-----FDILVTTNQFL---SKNFDLLSNKKFDFVFVDDVDAVLKSS 154
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
173-293 9.06e-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: 37.70  E-value: 9.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075832 173 GGDVCVSAATGSGKTLSYVIPIVQCLSHRTvprlRCVVIVPTRELTVQVAKTFEYYmSGAGLQVCAWTGQkslrhetYQl 252
Cdd:cd18028  17 GENLLISIPTASGKTLIAEMAMVNTLLEGG----KALYLVPLRALASEKYEEFKKL-EEIGLKVGISTGD-------YD- 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19075832 253 NGDENECRIDVLVSTPGRLVDHIRNDESFsLQHLRYMVIDE 293
Cdd:cd18028  84 EDDEWLGDYDIIVATYEKFDSLLRHSPSW-LRDVGVVVVDE 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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