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Conserved domains on  [gi|22328183|ref|NP_191975|]
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RNAhelicase-like 8 [Arabidopsis thaliana]

Protein Classification

DDX6/DHH1 family DEAD/DEAH box RNA helicase( domain architecture ID 13028552)

DDX6/DHH1 family DEAD/DEAH box containing ATP-dependent RNA helicase catalyzes the unwinding of RNA; such as ATP-dependent RNA helicase DHH1 that is involved in mRNA turnover, and more specifically in mRNA decapping

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
133-333 1.83e-146

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: 417.47  E-value: 1.83e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELA 212
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 213 LQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQP 292
Cdd:cd17940  81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 22328183 293 SVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVIN 333
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
343-472 2.03e-56

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: 184.25  E-value: 2.03e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 343 ITQFYAFVEERQKIHCLN-TLFSKLQINQSIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRN 421
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22328183 422 LVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSGRFGHLGLAVNLI 472
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
133-333 1.83e-146

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: 417.47  E-value: 1.83e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELA 212
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 213 LQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQP 292
Cdd:cd17940  81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 22328183 293 SVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVIN 333
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
133-497 1.71e-143

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 418.40  E-value: 1.71e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQD-NNVIQAVIIVPTREL 211
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPTREL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 212 ALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQ 291
Cdd:COG0513  84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 292 PSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVINLM-DELTLKGITQFYAFVEERQKIHCLNTLFSKLQINQ 370
Cdd:COG0513 164 EDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVApENATAETIEQRYYLVDKRDKLELLRRLLRDEDPER 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 371 SIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAE 450
Cdd:COG0513 244 AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPE 323
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 22328183 451 TYLHRVGRSGRFGHLGLAVNLITYEDRFNLYRIEQELGTEIKQIPPH 497
Cdd:COG0513 324 DYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELP 370
PTZ00424 PTZ00424
helicase 45; Provisional
133-498 7.56e-110

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 331.79  E-value: 7.56e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELA 212
Cdd:PTZ00424  30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  213 LQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQP 292
Cdd:PTZ00424 110 QQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKG 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  293 SVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVINL-MDELTLKGITQFYAFVE-ERQKIHCLNTLFSKLQINQ 370
Cdd:PTZ00424 190 QIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVkKDELTLEGIRQFYVAVEkEEWKFDTLCDLYETLTITQ 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  371 SIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAE 450
Cdd:PTZ00424 270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 22328183  451 TYLHRVGRSGRFGHLGLAVNLITYEDRFNLYRIEQELGTEIKQIPPHI 498
Cdd:PTZ00424 350 NYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEV 397
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
155-321 5.86e-63

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 202.47  E-value: 5.86e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   155 SPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELALQTSQVCKELGKHLKIQVMVTT 234
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   235 GGTSLKDDIMRLYQPvHLLVGTPGRILDLTKKGVcVLKDCSVLVMDEADKLLSQEFQPSVEHLISFLPESRQILMFSATF 314
Cdd:pfam00270  81 GGDSRKEQLEKLKGP-DILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158

                  ....*..
gi 22328183   315 PVTVKDF 321
Cdd:pfam00270 159 PRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
343-472 2.03e-56

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: 184.25  E-value: 2.03e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 343 ITQFYAFVEERQKIHCLN-TLFSKLQINQSIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRN 421
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22328183 422 LVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSGRFGHLGLAVNLI 472
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
146-346 1.20e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 176.91  E-value: 1.20e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183    146 IYEKGFERPSPIQEESIPIALTG-RDILARAKNGTGKTAAFCIPVLEKIDQDNNvIQAVIIVPTRELALQTSQVCKELGK 224
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKG-GRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183    225 HLKIQVMVTTGGTSLKDDIMRLYQ-PVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLISFLPE 303
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 22328183    304 SRQILMFSATFPVTVKDFKDRFLTNPYVINLmDELTLKGITQF 346
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV-GFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
354-463 4.82e-34

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: 123.86  E-value: 4.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   354 QKIHCLNTLFSKLQINQSIIFCNSVNRVEllAKKITEL-GYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGI 432
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 22328183   433 DIQAVNVVINFDFPKNAETYLHRVGRSGRFG 463
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
382-463 3.44e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 104.22  E-value: 3.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183    382 ELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSGR 461
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 22328183    462 FG 463
Cdd:smart00490  81 AG 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
273-490 4.81e-14

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 74.41  E-value: 4.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 273 DCSVLVMDEAdkllsqefqpsveHLIS-----FLPESRQI------------LMFSATF-PVTVKDFKDRF-LTNPYVI- 332
Cdd:COG0514 131 KISLFAIDEA-------------HCISqwghdFRPDYRRLgelrerlpnvpvLALTATAtPRVRADIAEQLgLEDPRVFv 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 333 ------NLmdeltlkgitqFYAFVE--ERQKIHCLNTLFSKLQiNQS-IIFCNSVNRVELLAKKITELGYSCFYIHAKML 403
Cdd:COG0514 198 gsfdrpNL-----------RLEVVPkpPDDKLAQLLDFLKEHP-GGSgIVYCLSRKKVEELAEWLREAGIRAAAYHAGLD 265
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 404 QDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSGRFGHLGLAVNLITYEDRFNL-YR 482
Cdd:COG0514 266 AEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQrFF 345

                ....*...
gi 22328183 483 IEQELGTE 490
Cdd:COG0514 346 IEQSPPDE 353
mfd TIGR00580
transcription-repair coupling factor (mfd); All proteins in this family for which functions ...
378-464 1.18e-05

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: 48.12  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   378 VNRVE-------LLAKKITELGYScfYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFdfpkNAE 450
Cdd:TIGR00580 667 HNRIEsieklatQLRELVPEARIA--IAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIE----RAD 740
                          90       100
                  ....*....|....*....|..
gi 22328183   451 TY----LH----RVGRSGRFGH 464
Cdd:TIGR00580 741 KFglaqLYqlrgRVGRSKKKAY 762
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
372-476 2.70e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 43.73  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   372 IIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACrNLVC-TDLFTRGIDIQAVNVVINFDFPKNAE 450
Cdd:PLN03137  684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEI-NIICaTVAFGMGINKPDVRFVIHHSLPKSIE 762
                          90       100
                  ....*....|....*....|....*.
gi 22328183   451 TYLHRVGRSGRFGHLGLAVNLITYED 476
Cdd:PLN03137  763 GYHQECGRAGRDGQRSSCVLYYSYSD 788
 
Name Accession Description Interval E-value
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
133-333 1.83e-146

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: 417.47  E-value: 1.83e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELA 212
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 213 LQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQP 292
Cdd:cd17940  81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 22328183 293 SVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVIN 333
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
133-497 1.71e-143

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 418.40  E-value: 1.71e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQD-NNVIQAVIIVPTREL 211
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPTREL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 212 ALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQ 291
Cdd:COG0513  84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 292 PSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVINLM-DELTLKGITQFYAFVEERQKIHCLNTLFSKLQINQ 370
Cdd:COG0513 164 EDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVApENATAETIEQRYYLVDKRDKLELLRRLLRDEDPER 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 371 SIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAE 450
Cdd:COG0513 244 AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPE 323
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 22328183 451 TYLHRVGRSGRFGHLGLAVNLITYEDRFNLYRIEQELGTEIKQIPPH 497
Cdd:COG0513 324 DYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELP 370
PTZ00424 PTZ00424
helicase 45; Provisional
133-498 7.56e-110

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 331.79  E-value: 7.56e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELA 212
Cdd:PTZ00424  30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  213 LQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQP 292
Cdd:PTZ00424 110 QQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKG 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  293 SVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVINL-MDELTLKGITQFYAFVE-ERQKIHCLNTLFSKLQINQ 370
Cdd:PTZ00424 190 QIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVkKDELTLEGIRQFYVAVEkEEWKFDTLCDLYETLTITQ 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  371 SIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAE 450
Cdd:PTZ00424 270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 22328183  451 TYLHRVGRSGRFGHLGLAVNLITYEDRFNLYRIEQELGTEIKQIPPHI 498
Cdd:PTZ00424 350 NYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEV 397
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
138-492 1.71e-95

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 297.10  E-value: 1.71e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  138 LKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELAlqtSQ 217
Cdd:PRK11776  11 LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELA---DQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  218 VCKEL-----GKHlKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQP 292
Cdd:PRK11776  88 VAKEIrrlarFIP-NIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  293 SVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVINLMDELTLKGITQ-FYAfVEERQKIHCLNTLFSKLQINQS 371
Cdd:PRK11776 167 AIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQrFYE-VSPDERLPALQRLLLHHQPESC 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  372 IIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAET 451
Cdd:PRK11776 246 VVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEV 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 22328183  452 YLHRVGRSGRFGHLGLAVNLITYEDRFNLYRIEQELGTEIK 492
Cdd:PRK11776 326 HVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
142-332 2.39e-84

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: 258.91  E-value: 2.39e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 142 LLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQD----NNVIQAVIIVPTRELALQTSQ 217
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEpkkkGRGPQALVLAPTRELAMQIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 218 VCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHL 297
Cdd:cd00268  81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 22328183 298 ISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
133-492 1.27e-77

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 249.86  E-value: 1.27e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEK-ID---QDNNVIQAVIIVPT 208
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHlLDfprRKSGPPRILILTPT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  209 RELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQ 288
Cdd:PRK11192  83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  289 EFQPSVEHLISflpESR---QILMFSATFP-VTVKDFKDRFLTNPYVINLMDELTLKG-ITQFYAFVEERQ-KIHCLNTL 362
Cdd:PRK11192 163 GFAQDIETIAA---ETRwrkQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKkIHQWYYRADDLEhKTALLCHL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  363 FSKLQINQSIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVIN 442
Cdd:PRK11192 240 LKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVIN 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 22328183  443 FDFPKNAETYLHRVGRSGRFGHLGLAVNLITYEDRFNLYRIEQELGTEIK 492
Cdd:PRK11192 320 FDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLK 369
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
133-494 3.32e-75

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 244.33  E-value: 3.32e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDN------NVIQAVIIV 206
Cdd:PRK10590   3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphakgrRPVRALILT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  207 PTRELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLL 286
Cdd:PRK10590  83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  287 SQEFQPSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVINLMDELTL-KGITQFYAFVEERQKIHCLNTLFSK 365
Cdd:PRK10590 163 DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTAsEQVTQHVHFVDKKRKRELLSQMIGK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  366 LQINQSIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDF 445
Cdd:PRK10590 243 GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYEL 322
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 22328183  446 PKNAETYLHRVGRSGRFGHLGLAVNLITYEDRFNLYRIEQELGTEIKQI 494
Cdd:PRK10590 323 PNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRI 371
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
133-494 2.73e-70

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 235.90  E-value: 2.73e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELA 212
Cdd:PRK11634   8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  213 LQTSQVCKELGKHLK-IQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQ 291
Cdd:PRK11634  88 VQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  292 PSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVINLMDELTLK-GITQFYAFVEERQKIHCLNTLFSKLQINQ 370
Cdd:PRK11634 168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRpDISQSYWTVWGMRKNEALVRFLEAEDFDA 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  371 SIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAE 450
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 22328183  451 TYLHRVGRSGRFGHLGLAVNLITYEDRFNLYRIEQELGTEIKQI 494
Cdd:PRK11634 328 SYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEV 371
PTZ00110 PTZ00110
helicase; Provisional
133-498 2.98e-70

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 233.90  E-value: 2.98e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  133 FEDYFLKrellmGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQA-----VIIVP 207
Cdd:PTZ00110 137 FPDYILK-----SLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGdgpivLVLAP 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  208 TRELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLS 287
Cdd:PTZ00110 212 TRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLD 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  288 QEFQPSVEHLISFLPESRQILMFSATFPVTVKDF-KDRFLTNPYVINL--MDELTLKGITQFYAFVEERQKIHCLNTLFS 364
Cdd:PTZ00110 292 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLaRDLCKEEPVHVNVgsLDLTACHNIKQEVFVVEEHEKRGKLKMLLQ 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  365 KLQINQS--IIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVIN 442
Cdd:PTZ00110 372 RIMRDGDkiLIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVIN 451
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22328183  443 FDFPKNAETYLHRVGRSGRFGHLGLAVNLITyEDRFNLYRIEQELGTEIKQ-IPPHI 498
Cdd:PTZ00110 452 FDFPNQIEDYVHRIGRTGRAGAKGASYTFLT-PDKYRLARDLVKVLREAKQpVPPEL 507
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
110-496 1.42e-69

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 230.18  E-value: 1.42e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  110 RLKLPAPDTRYRTED--VTATKG-NEFEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFC 186
Cdd:PRK01297  63 RERKPKPASLWKLEDfvVEPQEGkTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFL 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  187 IPVLEKIDQDNNVIQ-------AVIIVPTRELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRL-YQPVHLLVGTPG 258
Cdd:PRK01297 143 ISIINQLLQTPPPKErymgeprALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPG 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  259 RILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLISFLP--ESRQILMFSATFPVTVKDFKDRFLTNPYVINLMD 336
Cdd:PRK01297 223 RLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEP 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  337 E-LTLKGITQFYAFVEERQKIHCLNTLFSKLQINQSIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFR 415
Cdd:PRK01297 303 EnVASDTVEQHVYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFR 382
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  416 NGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSGRFGHLGLAVNLITYEDRFNLYRIEQELGTEIK-QI 494
Cdd:PRK01297 383 EGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEM 462

                 ..
gi 22328183  495 PP 496
Cdd:PRK01297 463 PP 464
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
135-332 2.36e-65

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: 209.87  E-value: 2.36e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 135 DYFLKRELLMGIYEKGFERPSPIQEESI-PIaLTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELAL 213
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIvPI-IKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 214 QTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPS 293
Cdd:cd17939  80 QIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 22328183 294 VEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd17939 160 IYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
155-321 5.86e-63

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 202.47  E-value: 5.86e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   155 SPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELALQTSQVCKELGKHLKIQVMVTT 234
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   235 GGTSLKDDIMRLYQPvHLLVGTPGRILDLTKKGVcVLKDCSVLVMDEADKLLSQEFQPSVEHLISFLPESRQILMFSATF 314
Cdd:pfam00270  81 GGDSRKEQLEKLKGP-DILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158

                  ....*..
gi 22328183   315 PVTVKDF 321
Cdd:pfam00270 159 PRNLEDL 165
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
142-332 1.60e-61

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: 199.80  E-value: 1.60e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 142 LLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELALQTSQVCKE 221
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 222 LGKHLK-IQVMVTTGGTSLKDDIMRLYQPvHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLISF 300
Cdd:cd17943  81 IGKKLEgLKCEVFIGGTPVKEDKKKLKGC-HIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
                       170       180       190
                ....*....|....*....|....*....|..
gi 22328183 301 LPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
138-332 2.76e-58

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: 191.63  E-value: 2.76e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 138 LKRELLMGIYEKGFERPSPIQEESIPIALTG--RDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELALQT 215
Cdd:cd17963   1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 216 SQVCKELGKHLKIQVMVttggtSLKDDIMRLYQPV--HLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLL-SQEFQP 292
Cdd:cd17963  81 GEVVEKMGKFTGVKVAL-----AVPGNDVPRGKKItaQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGHGD 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 22328183 293 SVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd17963 156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
133-332 7.00e-58

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: 190.76  E-value: 7.00e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELA 212
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 213 LQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQP 292
Cdd:cd18045  81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 22328183 293 SVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
133-332 1.59e-57

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: 189.58  E-value: 1.59e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELA 212
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 213 LQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQP 292
Cdd:cd18046  81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 22328183 293 SVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
133-481 1.59e-57

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 199.24  E-value: 1.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVL--------EKIDQDNNVIqAVI 204
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrcctirsGHPSEQRNPL-AMV 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  205 IVPTRELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADK 284
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  285 LLSQEFQPSVEHLISFLPESrQILMFSATFPVTVKDFKDRFLTNPYVINL-MDELTLKGITQFYAFVEERQKihcLNTLF 363
Cdd:PLN00206 282 MLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIgNPNRPNKAVKQLAIWVETKQK---KQKLF 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  364 SKLQINQ-----SIIFCNSVNRVELLAKKITEL-GYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAV 437
Cdd:PLN00206 358 DILKSKQhfkppAVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRV 437
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 22328183  438 NVVINFDFPKNAETYLHRVGRSGRFGHLGLAVNLITYEDRfNLY 481
Cdd:PLN00206 438 RQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDR-NLF 480
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
343-472 2.03e-56

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: 184.25  E-value: 2.03e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 343 ITQFYAFVEERQKIHCLN-TLFSKLQINQSIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRN 421
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22328183 422 LVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSGRFGHLGLAVNLI 472
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
133-471 2.58e-55

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 194.40  E-value: 2.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKI-------DQDNNVIQAVII 205
Cdd:PRK04537  11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALIL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  206 VPTRELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKK-GVCVLKDCSVLVMDEADK 284
Cdd:PRK04537  91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEADR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  285 LLSQEFQPSVEHLISFLPE--SRQILMFSATFPVTVKDFKDRFLTNPYVINLMDE-LTLKGITQFYAFVEERQKIHCLNT 361
Cdd:PRK04537 171 MFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETEtITAARVRQRIYFPADEEKQTLLLG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  362 LFSKLQINQSIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVI 441
Cdd:PRK04537 251 LLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVY 330
                        330       340       350
                 ....*....|....*....|....*....|
gi 22328183  442 NFDFPKNAETYLHRVGRSGRFGHLGLAVNL 471
Cdd:PRK04537 331 NYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
133-333 5.62e-54

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: 180.58  E-value: 5.62e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNV--IQAVIIVPTRE 210
Cdd:cd17959   3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTvgARALILSPTRE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 211 LALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEF 290
Cdd:cd17959  83 LALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGF 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 22328183 291 QPSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVIN 333
Cdd:cd17959 163 AEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
142-329 1.95e-53

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: 178.60  E-value: 1.95e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 142 LLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKI---DQDNNVIQAVIIVPTRELALQTSQV 218
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 219 CKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCV-LKDCSVLVMDEADKLLSQEFQPSVEHL 297
Cdd:cd17947  81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFdLDSIEILVLDEADRMLEEGFADELKEI 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 22328183 298 ISFLPESRQILMFSATFPVTVKDFKDRFLTNP 329
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
133-491 2.58e-53

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 185.56  E-value: 2.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCI---------PVLEkiDQDNNVIQAV 203
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTatfhyllshPAPE--DRKVNQPRAL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  204 IIVPTRELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEAD 283
Cdd:PRK04837  88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  284 KLLSQEFQPSVEHLISFLPESRQIL--MFSATFPVTVKDFKDRFLTNP-YVINLMDELTLKGITQ--FYAFVEErqKIHC 358
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMPPANQRLnmLFSATLSYRVRELAFEHMNNPeYVEVEPEQKTGHRIKEelFYPSNEE--KMRL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  359 LNTLFSKLQINQSIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVN 438
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 22328183  439 VVINFDFPKNAETYLHRVGRSGRFGHLGLAVNLITYEDRFNLYRIEQELGTEI 491
Cdd:PRK04837 326 HVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
DEXDc smart00487
DEAD-like helicases superfamily;
146-346 1.20e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 176.91  E-value: 1.20e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183    146 IYEKGFERPSPIQEESIPIALTG-RDILARAKNGTGKTAAFCIPVLEKIDQDNNvIQAVIIVPTRELALQTSQVCKELGK 224
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKG-GRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183    225 HLKIQVMVTTGGTSLKDDIMRLYQ-PVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLISFLPE 303
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 22328183    304 SRQILMFSATFPVTVKDFKDRFLTNPYVINLmDELTLKGITQF 346
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV-GFTPLEPIEQF 201
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
133-329 4.05e-52

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 175.58  E-value: 4.05e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELA 212
Cdd:cd17954   2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 213 LQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTK--KGVCvLKDCSVLVMDEADKLLSQEF 290
Cdd:cd17954  82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEntKGFS-LKSLKFLVMDEADRLLNMDF 160
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 22328183 291 QPSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNP 329
Cdd:cd17954 161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP 199
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
138-334 5.64e-52

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: 175.08  E-value: 5.64e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 138 LKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKI------DQDNNVIQAVIIVPTREL 211
Cdd:cd17961   1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 212 ALQTSQVCKELGKHL--KIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKD-CSVLVMDEADKLLSQ 288
Cdd:cd17961  81 AQQVSKVLEQLTAYCrkDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLSY 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 22328183 289 EFQPSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVINL 334
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
142-332 2.18e-51

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: 174.05  E-value: 2.18e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 142 LLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQ-----DNNVIQ---AVIIVPTRELAL 213
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppldEETKDDgpyALILAPTRELAQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 214 QTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPS 293
Cdd:cd17945  81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 22328183 294 VEHLISFLPES--------------------RQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd17945 161 VTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
133-332 4.24e-51

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: 172.79  E-value: 4.24e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELA 212
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 213 LQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTK---KGVCVLKDCSVLVMDEADKLLSQE 289
Cdd:cd17955  81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGS 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 22328183 290 FQPSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFW 203
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
133-331 9.24e-51

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: 172.67  E-value: 9.24e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLkRELLMGIYEK-GFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKI--DQDNNVI--------Q 201
Cdd:cd17967   2 FEEAGL-RELLLENIKRaGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLleDGPPSVGrgrrkaypS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 202 AVIIVPTRELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDE 281
Cdd:cd17967  81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 22328183 282 ADKLLSQEFQPSVEHLISF----LPESRQILMFSATFPVTVKDFKDRFLTNpYV 331
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKN-YI 213
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
141-321 2.14e-50

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: 171.23  E-value: 2.14e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 141 ELLMGIYEKGFERPSPIQEESIPIAL-TGRDILARAKNGTGKTAAFCIPVLE-----KIDQDNNVIQAVIIVPTRELALQ 214
Cdd:cd17964   4 SLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQsllntKPAGRRSGVSALIISPTRELALQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 215 TSQVCKELGKHLK---IQVMVttGGTSLKDDIMRLY-QPVHLLVGTPGRILD-LTKKGVC-VLKDCSVLVMDEADKLLSQ 288
Cdd:cd17964  84 IAAEAKKLLQGLRklrVQSAV--GGTSRRAELNRLRrGRPDILVATPGRLIDhLENPGVAkAFTDLDYLVLDEADRLLDM 161
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 22328183 289 EFQPSVEHLISFLPES----RQILMFSATFPVTVKDF 321
Cdd:cd17964 162 GFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQI 198
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
133-332 3.15e-50

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: 170.60  E-value: 3.15e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELA 212
Cdd:cd17950   4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 213 LQTSQVCKELGKHLK-IQVMVTTGGTSLKDDIMRLYQPV-HLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQ-E 289
Cdd:cd17950  84 FQISNEYERFSKYMPnVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQlD 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 22328183 290 FQPSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
133-329 4.40e-50

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: 170.19  E-value: 4.40e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEkidqdnnVIQAVIIVPTRELA 212
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------IVVALILEPSRELA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 213 LQTSQVCKELGKHL---KIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQE 289
Cdd:cd17938  74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 22328183 290 FQPSVEHLISFLP-----ESR-QILMFSATFPVT-VKDFKDRFLTNP 329
Cdd:cd17938 154 NLETINRIYNRIPkitsdGKRlQVIVCSATLHSFeVKKLADKIMHFP 200
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
143-334 1.09e-48

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: 166.31  E-value: 1.09e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 143 LMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDN----NVIQAVIIVPTRELALQTSQV 218
Cdd:cd17941   2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwtpeDGLGALIISPTRELAMQIFEV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 219 CKELGKHLKIQVMVTTGGTSLKDDIMRLYQpVHLLVGTPGRIL---DLTkkgvcVLKDCS---VLVMDEADKLLSQEFQP 292
Cdd:cd17941  82 LRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLqhmDET-----PGFDTSnlqMLVLDEADRILDMGFKE 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 22328183 293 SVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVINL 334
Cdd:cd17941 156 TLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
131-331 2.45e-47

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: 165.14  E-value: 2.45e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 131 NEFEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDN------NVIQ--- 201
Cdd:cd18052  43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGltassfSEVQepq 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 202 AVIIVPTRELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDE 281
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 22328183 282 ADKLLSQEFQPSVEHLISFL----PESRQILMFSATFPVTVKDFKDRFLTNPYV 331
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKEDYL 256
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
146-333 4.49e-46

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: 159.46  E-value: 4.49e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 146 IYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKID------QDNNVIqAVIIVPTRELALQTSQVC 219
Cdd:cd17966   5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINaqppleRGDGPI-VLVLAPTRELAQQIQQEA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 220 KELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLIS 299
Cdd:cd17966  84 NKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVD 163
                       170       180       190
                ....*....|....*....|....*....|....
gi 22328183 300 FLPESRQILMFSATFPVTVKDFKDRFLTNPYVIN 333
Cdd:cd17966 164 QIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
142-333 1.26e-45

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: 158.51  E-value: 1.26e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 142 LLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKI-----DQDNNVIQAVIIVPTRELALQTS 216
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 217 QVCKELGKH--LKIQVMVTTGGTS-LKDDIMRLYQPVHLLVGTPGRILDLTKKGVCV--LKDCSVLVMDEADKLLSQEFQ 291
Cdd:cd17960  81 EVLQSFLEHhlPKLKCQLLIGGTNvEEDVKKFKRNGPNILVGTPGRLEELLSRKADKvkVKSLEVLVLDEADRLLDLGFE 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 22328183 292 PSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVIN 333
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
142-332 1.66e-45

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: 157.96  E-value: 1.66e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 142 LLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKI-DQDNNVIQ----AVIIVPTRELALQTS 216
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImDQRELEKGegpiAVIVAPTRELAQQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 217 QVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEH 296
Cdd:cd17952  81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 22328183 297 LISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
143-320 3.87e-45

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: 157.14  E-value: 3.87e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 143 LMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDN----NVIQAVIIVPTRELALQTSQV 218
Cdd:cd17942   2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKfkprNGTGVIIISPTRELALQIYGV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 219 CKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILD-LTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHL 297
Cdd:cd17942  82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQI 161
                       170       180
                ....*....|....*....|...
gi 22328183 298 ISFLPESRQILMFSATFPVTVKD 320
Cdd:cd17942 162 IKLLPKRRQTMLFSATQTRKVED 184
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
142-332 9.13e-44

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


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 153.09  E-value: 9.13e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 142 LLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELALQTSQVCKE 221
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 222 LGK---HLKIQVMVttGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLI 298
Cdd:cd17962  81 LMKglpPMKTALLV--GGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 22328183 299 SFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd17962 159 ENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
138-332 8.98e-43

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: 151.38  E-value: 8.98e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 138 LKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKI-DQ-----DNNVIqAVIIVPTREL 211
Cdd:cd17953  19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIkDQrpvkpGEGPI-GLIMAPTREL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 212 ALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDL--TKKG-VCVLKDCSVLVMDEADKLLSQ 288
Cdd:cd17953  98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDIltANNGrVTNLRRVTYVVLDEADRMFDM 177
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 22328183 289 EFQPSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd17953 178 GFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
142-333 3.53e-40

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: 144.02  E-value: 3.53e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 142 LLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIP-VLEKIDQDNN--VIQ-----AVIIVPTRELAL 213
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEKKlpFIKgegpyGLIVCPSRELAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 214 QTSQVCKELGKHLK------IQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLS 287
Cdd:cd17951  81 QTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 22328183 288 QEFQPSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVIN 333
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
142-329 5.78e-39

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: 140.42  E-value: 5.78e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 142 LLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNN--VIQAVIIVPTRELALQTSQVC 219
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKkkGLRALILAPTRELASQIYREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 220 KELGKHLKIQVMVTTGGTSLK-DDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLI 298
Cdd:cd17957  81 LKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 22328183 299 SFLPESR-QILMFSATFPVTVKDFKDRFLTNP 329
Cdd:cd17957 161 AACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
133-339 1.37e-38

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: 140.54  E-value: 1.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTG--RDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRE 210
Cdd:cd18048  20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 211 LALQTSQVCKELGKH-LKIQVMVTTGGTSLKDDIMRLYQpvhLLVGTPGRILDLT-KKGVCVLKDCSVLVMDEADKLLsq 288
Cdd:cd18048 100 LALQTGKVVEEMGKFcVGIQVIYAIRGNRPGKGTDIEAQ---IVIGTPGTVLDWCfKLRLIDVTNISVFVLDEADVMI-- 174
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22328183 289 EFQPSVEHLISF---LPESRQILMFSATFPVTVKDFKDRFLTNPYVINL-MDELT 339
Cdd:cd18048 175 NVQGHSDHSVRVkrsMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLkKEELT 229
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
131-328 7.95e-38

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: 139.02  E-value: 7.95e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 131 NEFEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQD---NNVIQ------ 201
Cdd:cd18051  21 ETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgESLPSesgyyg 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 202 -------AVIIVPTRELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDC 274
Cdd:cd18051 101 rrkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYC 180
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 22328183 275 SVLVMDEADKLLSQEFQPSVEHLIS--FLPES--RQILMFSATFPVTVKDFKDRFLTN 328
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPKEIQMLARDFLDN 238
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
150-332 2.01e-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: 136.95  E-value: 2.01e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 150 GFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQ------AVIIVPTRELALQTSQVCKELG 223
Cdd:cd17949  10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKLL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 224 KHLK-IQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVC-VLKDCSVLVMDEADKLLSQEFQPSVEHLISFL 301
Cdd:cd17949  90 KPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMGFEKDITKILELL 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 22328183 302 -------------PESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd17949 170 ddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
142-314 6.32e-36

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: 133.52  E-value: 6.32e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 142 LLMGIYEKGFERPSPIQEESIPIALT-GRDILARAKNGTGKTAAFCIPVLEKI---DQDNNVIQ------AVIIVPTREL 211
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlsqKSSNGVGGkqkplrALILTPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 212 ALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKG---VCVLKDCSVLVMDEADKLLS- 287
Cdd:cd17946  81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEk 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 22328183 288 ---QEFqpsvEHLISFLPES-------RQILMFSATF 314
Cdd:cd17946 161 ghfAEL----EKILELLNKDragkkrkRQTFVFSATL 193
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
117-334 9.69e-36

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: 132.83  E-value: 9.69e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 117 DTRYRTEDVTATKGN------EFEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVL 190
Cdd:cd18049   4 EQYRRSKEITVRGHNcpkpvlNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 191 EKIDQDNNVIQA-----VIIVPTRELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTK 265
Cdd:cd18049  84 VHINHQPFLERGdgpicLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLE 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328183 266 KGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVINL 334
Cdd:cd18049 164 AGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
146-334 1.81e-35

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: 133.21  E-value: 1.81e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 146 IYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQA-----VIIVPTRELALQTSQVCK 220
Cdd:cd18050  77 LLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLVLAPTRELAQQVQQVAD 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 221 ELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLISF 300
Cdd:cd18050 157 DYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ 236
                       170       180       190
                ....*....|....*....|....*....|....
gi 22328183 301 LPESRQILMFSATFPVTVKDFKDRFLTNPYVINL 334
Cdd:cd18050 237 IRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
143-332 4.33e-34

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: 127.20  E-value: 4.33e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 143 LMGIYEK-GFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQD------NNVIQAVIIVPTRELALQT 215
Cdd:cd17958   1 IMKEIKKqGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQpipreqRNGPGVLVLTPTRELALQI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 216 SQVCKELgKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVE 295
Cdd:cd17958  81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 22328183 296 HLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
354-463 4.82e-34

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: 123.86  E-value: 4.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   354 QKIHCLNTLFSKLQINQSIIFCNSVNRVEllAKKITEL-GYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGI 432
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 22328183   433 DIQAVNVVINFDFPKNAETYLHRVGRSGRFG 463
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
133-332 3.41e-32

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: 122.52  E-value: 3.41e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 133 FEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTG--RDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRE 210
Cdd:cd18047   3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 211 LALQTSQVCKELGK-HLKIQVMVTTGGTSLKDDIMRLYQpvhLLVGTPGRILD-LTKKGVCVLKDCSVLVMDEADKLL-S 287
Cdd:cd18047  83 LALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaT 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 22328183 288 QEFQPSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVI 332
Cdd:cd18047 160 QGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
142-320 4.53e-31

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 120.16  E-value: 4.53e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 142 LLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDN-------NVIQAVIIVPTRELALQ 214
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKllaegpfNAPRGLVITPSRELAEQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 215 TSQVCKELGKHLKIQVMVTTGGtSLKDDIMRLYQP-VHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPS 293
Cdd:cd17948  81 IGSVAQSLTEGLGLKVKVITGG-RTKRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 22328183 294 VEHLISFLP-------------ESRQILMFSATFPVTVKD 320
Cdd:cd17948 160 LSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGE 199
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
148-313 9.20e-30

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 116.58  E-value: 9.20e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 148 EKGFERPSPIQEESIPIALTG---------RDILARAKNGTGKTAAFCIPVLEKI-DQDNNVIQAVIIVPTRELALQTSQ 217
Cdd:cd17956   7 NNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKELVQQVYK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 218 VCKELGKHLKIQVMVTTGGTSLKDDIM--------RLYQPVHLLVGTPGRILD-LTKKGVCVLKDCSVLVMDEADKLLSQ 288
Cdd:cd17956  87 VFESLCKGTGLKVVSLSGQKSFKKEQKlllvdtsgRYLSRVDILVATPGRLVDhLNSTPGFTLKHLRFLVIDEADRLLNQ 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 22328183 289 EFQPSVEHLIS--------------------FLPESRQILMFSAT 313
Cdd:cd17956 167 SFQDWLETVMKalgrptapdlgsfgdanlleRSVRPLQKLLFSAT 211
HELICc smart00490
helicase superfamily c-terminal domain;
382-463 3.44e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 104.22  E-value: 3.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183    382 ELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSGR 461
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 22328183    462 FG 463
Cdd:smart00490  81 AG 82
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
156-330 4.19e-27

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: 108.01  E-value: 4.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 156 PIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVI------QAVIIVPTRELALQTSQVCKELGKhlKIQ 229
Cdd:cd17944  15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVTKDFKDITR--KLS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 230 VMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLISFL-----PES 304
Cdd:cd17944  93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdsEDN 172
                       170       180
                ....*....|....*....|....*.
gi 22328183 305 RQILMFSATFPVTVKDFKDRFLTNPY 330
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYMKSQY 198
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
154-335 7.89e-22

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: 94.75  E-value: 7.89e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 154 PSPIQEESIPI---ALTGRDILAR-------------AKNGTGKTAAFCIPVLEKIDQ-----------------DNNVI 200
Cdd:cd17965  31 PSPIQTLAIKKllkTLMRKVTKQTsneepklevfllaAETGSGKTLAYLAPLLDYLKRqeqepfeeaeeeyesakDTGRP 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 201 QAVIIVPTRELALQTSQVCKELGK--HLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLV 278
Cdd:cd17965 111 RSVILVPTHELVEQVYSVLKKLSHtvKLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLV 190
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 22328183 279 MDEADKLLSQEFQPSVEHLISFLPESRQILMFSATFPvtvKDFkDRFLTN--PYVINLM 335
Cdd:cd17965 191 VDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP---KEF-DKTLRKlfPDVVRIA 245
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
178-458 1.61e-20

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 94.71  E-value: 1.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 178 GTGKT--AAFCIpvlEKIDQDNNVIqavIIVPTRELALQTSqvcKELGKHLKIQvmvttGGTSLKDDIMRlyqpvHLLVG 255
Cdd:COG1061 110 GTGKTvlALALA---AELLRGKRVL---VLVPRRELLEQWA---EELRRFLGDP-----LAGGGKKDSDA-----PITVA 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 256 TP---GRILDLTKkgvcVLKDCSVLVMDEADKLLSQEFQPSVEHLisflpESRQILMFSAT------FPVTVKDF----- 321
Cdd:COG1061 171 TYqslARRAHLDE----LGDRFGLVIIDEAHHAGAPSYRRILEAF-----PAAYRLGLTATpfrsdgREILLFLFdgivy 241
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 322 --------KDRFLTNPYVINLMDELTLKG---------ITQFYAFVEERqKIHCLNTLFSKL-QINQSIIFCNSVNRVEL 383
Cdd:COG1061 242 eyslkeaiEDGYLAPPEYYGIRVDLTDERaeydalserLREALAADAER-KDKILRELLREHpDDRKTLVFCSSVDHAEA 320
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328183 384 LAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGR 458
Cdd:COG1061 321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
168-313 8.68e-15

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: 71.67  E-value: 8.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 168 GRDILARAKNGTGKTAAFCIPVLEKIDQdnNVIQAVIIVPTRELALQTSQVCKEL-GKHLKIQVMvtTGGTSLKDDIMRL 246
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLRELfGPGIRVAVL--VGGSSAEEREKNK 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328183 247 YQPVHLLVGTPGRIL-DLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLI---SFLPESRQILMfSAT 313
Cdd:cd00046  77 LGDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAvrkAGLKNAQVILL-SAT 146
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
372-463 3.49e-14

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: 69.54  E-value: 3.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 372 IIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAET 451
Cdd:cd18794  34 IIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMES 113
                        90
                ....*....|..
gi 22328183 452 YLHRVGRSGRFG 463
Cdd:cd18794 114 YYQESGRAGRDG 125
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
273-490 4.81e-14

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 74.41  E-value: 4.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 273 DCSVLVMDEAdkllsqefqpsveHLIS-----FLPESRQI------------LMFSATF-PVTVKDFKDRF-LTNPYVI- 332
Cdd:COG0514 131 KISLFAIDEA-------------HCISqwghdFRPDYRRLgelrerlpnvpvLALTATAtPRVRADIAEQLgLEDPRVFv 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 333 ------NLmdeltlkgitqFYAFVE--ERQKIHCLNTLFSKLQiNQS-IIFCNSVNRVELLAKKITELGYSCFYIHAKML 403
Cdd:COG0514 198 gsfdrpNL-----------RLEVVPkpPDDKLAQLLDFLKEHP-GGSgIVYCLSRKKVEELAEWLREAGIRAAAYHAGLD 265
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 404 QDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSGRFGHLGLAVNLITYEDRFNL-YR 482
Cdd:COG0514 266 AEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQrFF 345

                ....*...
gi 22328183 483 IEQELGTE 490
Cdd:COG0514 346 IEQSPPDE 353
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
150-463 7.48e-14

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 73.98  E-value: 7.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  150 GFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLekidqdnnVIQAVIIVPTRELALQTSQVCKELGKHLKIQ 229
Cdd:PRK11057  22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL--------VLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  230 VMVTTGGTSLKDDIMRLYQP--VHLLVGTPGRILdlTKKGVCVLKDC--SVLVMDEAdkllsqefqpsveHLIS-----F 300
Cdd:PRK11057  94 CLNSTQTREQQLEVMAGCRTgqIKLLYIAPERLM--MDNFLEHLAHWnpALLAVDEA-------------HCISqwghdF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  301 LPESRQILMFSATFP-------------VTVKDFKDRF-LTNPYV-INLMDELTLKgitqfYAFVEERQKIHCLnTLFSK 365
Cdd:PRK11057 159 RPEYAALGQLRQRFPtlpfmaltataddTTRQDIVRLLgLNDPLIqISSFDRPNIR-----YTLVEKFKPLDQL-MRYVQ 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  366 LQINQS-IIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFD 444
Cdd:PRK11057 233 EQRGKSgIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFD 312
                        330
                 ....*....|....*....
gi 22328183  445 FPKNAETYLHRVGRSGRFG 463
Cdd:PRK11057 313 IPRNIESYYQETGRAGRDG 331
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
356-458 3.63e-09

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 55.29  E-value: 3.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 356 IHCLNTLFSKLQINQSIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNR---------------VFHDFRNGACR 420
Cdd:cd18802  13 IEILREYFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGFLIGRGNSsqrkrslmtqrkqkeTLDKFRDGELN 92
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 22328183 421 NLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGR 458
Cdd:cd18802  93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
422-463 8.32e-09

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 52.32  E-value: 8.32e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 22328183 422 LVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSGRFG 463
Cdd:cd18785  26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
362-461 2.53e-08

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: 53.04  E-value: 2.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 362 LFSKLQINQSIIFCNSVNRVELLAKKITELGYSC-----FYIHAKML-QDHRNRVFHDFRNGACRNLVCT---DLftrGI 432
Cdd:cd18796  32 IFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRvppdfIALHHGSLsRELREEVEAALKRGDLKVVVATsslEL---GI 108
                        90       100
                ....*....|....*....|....*....
gi 22328183 433 DIQAVNVVINFDFPKNAETYLHRVGRSGR 461
Cdd:cd18796 109 DIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
148-469 3.35e-08

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: 56.38  E-value: 3.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 148 EKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNViQAVIIVPTRELA---LQT-SQVCKELG 223
Cdd:COG1205  51 KRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA-TALYLYPTKALArdqLRRlRELAEALG 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 224 khLKIQVMVTTGGTSLKDdimR--LYQPVHLLVGTP-----GrILDLTKKGVCVLKDCSVLVMDEA-------------- 282
Cdd:COG1205 130 --LGVRVATYDGDTPPEE---RrwIREHPDIVLTNPdmlhyG-LLPHHTRWARFFRNLRYVVIDEAhtyrgvfgshvanv 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 283 -DKLLsqefqpsveHLISFLPESRQILMFSAT-------------FPVTVKDF-------KDRFLTNPYVINlmdeltlK 341
Cdd:COG1205 204 lRRLR---------RICRHYGSDPQFILASATignpaehaerltgRPVTVVDEdgsprgeRTFVLWNPPLVD-------D 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 342 GITQfYAFVEERQkihclntLFSKLQIN--QSIIFCNSVNRVELLAKKITEL-----------GYscfyiHAKMLQDHRN 408
Cdd:COG1205 268 GIRR-SALAEAAR-------LLADLVREglRTLVFTRSRRGAELLARYARRAlrepdladrvaAY-----RAGYLPEERR 334
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328183 409 RVFHDFRNGACRNLVCT---DLftrGIDIQAVNVVINFDFPKNAETYLHRVGRSGRFGHLGLAV 469
Cdd:COG1205 335 EIERGLRSGELLGVVSTnalEL---GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
PRK00254 PRK00254
ski2-like helicase; Provisional
146-476 5.55e-08

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 55.59  E-value: 5.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  146 IYEKGFERPSPIQEESIPI-ALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNviQAVIIVPTRELALQTSQVCKELGK 224
Cdd:PRK00254  16 LKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGG--KAVYLVPLKALAEEKYREFKDWEK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  225 hLKIQVMVTTGGTSLKDDIMRLYQpvhLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLISFLPES 304
Cdd:PRK00254  94 -LGLRVAMTTGDYDSTDEWLGKYD---IIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGR 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  305 RQILMFSATF--------------------PVTVK------------DFK-DRFLTNpyvinlMDELTLKGI---TQFYA 348
Cdd:PRK00254 170 AQILGLSATVgnaeelaewlnaelvvsdwrPVKLRkgvfyqgflfweDGKiERFPNS------WESLVYDAVkkgKGALV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  349 FVEERQK--------------------IHCLNTLFSKLQINQSiifcnsvnrVELLAKKITelGYSCFYiHAKMLQDHRN 408
Cdd:PRK00254 244 FVNTRRSaekealelakkikrfltkpeLRALKELADSLEENPT---------NEKLKKALR--GGVAFH-HAGLGRTERV 311
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328183  409 RVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINfDFPKNAETYLHRV---------GRSGR--FGHLGLAVNLITYED 476
Cdd:PRK00254 312 LIEDAFREGLIKVITATPTLSAGINLPAFRVIIR-DTKRYSNFGWEDIpvleiqqmmGRAGRpkYDEVGEAIIVATTEE 389
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
156-315 6.20e-08

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: 52.65  E-value: 6.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 156 PIQEESI-PIALTGRDILARAKNGTGKT--AAFCIpvLEKIDQDNNVIqaVIIVPTRELALQTSQVCKELGKHLKIQVMV 232
Cdd:cd17921   4 PIQREALrALYLSGDSVLVSAPTSSGKTliAELAI--LRALATSGGKA--VYIAPTRALVNQKEADLRERFGPLGKNVGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 233 TTGGTSLKDDIMRLYQpvhLLVGTPgRILD--LTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLISFLP---ESRQI 307
Cdd:cd17921  80 LTGDPSVNKLLLAEAD---ILVATP-EKLDllLRNGGERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrinKNARF 155

                ....*...
gi 22328183 308 LMFSATFP 315
Cdd:cd17921 156 VGLSATLP 163
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
178-446 7.93e-08

CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 54.70  E-value: 7.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 178 GTGKTAAFCIPVLEKIDQDNN--VIqavIIVPTRELALQTSQVCKE-----LGKH--------LKIQVMVTTGGTSLKDD 242
Cdd:COG1203 157 GGGKTEAALLFALRLAAKHGGrrII---YALPFTSIINQTYDRLRDlfgedVLLHhsladldlLEEEEEYESEARWLKLL 233
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 243 IMRLYQPVhlLVGTPGRILDLT---KKGVCV----LKDcSVLVMDEADkLLSQEFQPSVEHLISFLPE--SRQILMfSAT 313
Cdd:COG1203 234 KELWDAPV--VVTTIDQLFESLfsnRKGQERrlhnLAN-SVIILDEVQ-AYPPYMLALLLRLLEWLKNlgGSVILM-TAT 308
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 314 FPvtvkDFKDRFLTNPYviNLMDELTLKGITQFYAFVEERQKIH--------CLNTLFSKLQINQSIIF-CNSVNRVELL 384
Cdd:COG1203 309 LP----PLLREELLEAY--ELIPDEPEELPEYFRAFVRKRVELKegplsdeeLAELILEALHKGKSVLViVNTVKDAQEL 382
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328183 385 AKKITELG--YSCFYIHAKMLQDHR----NRVFHDFRNGACRNLVCTDLFTRGIDIqavnvvinfDFP 446
Cdd:COG1203 383 YEALKEKLpdEEVYLLHSRFCPADRseieKEIKERLERGKPCILVSTQVVEAGVDI---------DFD 441
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
372-463 1.06e-07

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 54.74  E-value: 1.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 372 IIFCNSVNRVELLAKKITELGYSC--FYIHAK------MLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINF 443
Cdd:COG1111 357 IVFTQYRDTAEMIVEFLSEPGIKAgrFVGQASkegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFY 436
                        90       100
                ....*....|....*....|
gi 22328183 444 DFPKNAETYLHRVGRSGRFG 463
Cdd:COG1111 437 EPVPSEIRSIQRKGRTGRKR 456
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
275-463 1.22e-07

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 53.59  E-value: 1.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 275 SVLVMDEADkLLSQEFQPSVEHLISFLPESRQ-ILMFSATFPvtvKDFKDRFLTNPYVINLmdeltlkgITQFYAFVEER 353
Cdd:cd09639 125 SLLIFDEVH-FYDEYTLALILAVLEVLKDNDVpILLMSATLP---KFLKEYAEKIGYVEEN--------EPLDLKPNERA 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 354 QKIHCLN-TLFSKLQIN----------QSIIFCNSVNRVELLAKKITELGYS--CFYIHAKMLQDHR----NRVFHDFRN 416
Cdd:cd09639 193 PFIKIESdKVGEISSLErllefikkggSVAIIVNTVDRAQEFYQQLKEKGPEeeIMLIHSRFTEKDRakkeAELLLEFKK 272
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 22328183 417 GACRNLVCTDLFTRGIDIqAVNVVINFDFPKNAETylHRVGRSGRFG 463
Cdd:cd09639 273 SEKFVIVATQVIEASLDI-SVDVMITELAPIDSLI--QRLGRLHRYG 316
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
370-469 1.35e-07

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: 50.72  E-value: 1.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 370 QSIIFCNSVNRVELLAK-------KITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVIN 442
Cdd:cd18797  37 KTIVFCRSRKLAELLLRylkarlvEEGPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
                        90       100
                ....*....|....*....|....*..
gi 22328183 443 FDFPKNAETYLHRVGRSGRFGHLGLAV 469
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGKDSLVI 143
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
378-464 5.19e-07

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: 49.26  E-value: 5.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 378 VNRVELLAKKITELG-----YSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETY 452
Cdd:cd18810  32 HNRIESIEKLATQLRqlvpeARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQ 111
                        90
                ....*....|....*.
gi 22328183 453 LH----RVGRSGRFGH 464
Cdd:cd18810 112 LYqlrgRVGRSKERAY 127
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
371-463 8.10e-07

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 48.24  E-value: 8.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 371 SIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRN--GACRNLVCTDLFTRGIDIQAVNVVINFDFPKN 448
Cdd:cd18793  30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGVGLNLTAANRVILYDPWWN 109
                        90
                ....*....|....*
gi 22328183 449 AETYLHRVGRSGRFG 463
Cdd:cd18793 110 PAVEEQAIDRAHRIG 124
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
151-460 1.21e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 51.26  E-value: 1.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 151 FERPSPIQEESIPIALTGRDILARAKNGTGKT-AAFCIPVLEKIDQDNNV-----IQAVIIVPTRELA------LQTsqV 218
Cdd:COG1201  22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDELARRPRPGelpdgLRVLYISPLKALAndiernLRA--P 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 219 CKELGKHLK-----IQVMVTTGGTSLKDdimR---LYQPVHLLVGTPGR--ILdLT-KKGVCVLKDCSVLVMDE-----A 282
Cdd:COG1201 100 LEEIGEAAGlplpeIRVGVRTGDTPASE---RqrqRRRPPHILITTPESlaLL-LTsPDARELLRGVRTVIVDEihalaG 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 283 DK---LLSQefqpSVEHLISFLPESRQILMFSATfpvtVKDFKD--RFL-----TNPYVI------------------NL 334
Cdd:COG1201 176 SKrgvHLAL----SLERLRALAPRPLQRIGLSAT----VGPLEEvaRFLvgyedPRPVTIvdagagkkpdlevlvpveDL 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 335 MDELTLKGITQFYafVEERqkIHCLntlfsklqINQS---IIFCNSVNRVELLAKKITELGYSCFYI----HAKMLQDHR 407
Cdd:COG1201 248 IERFPWAGHLWPH--LYPR--VLDL--------IEAHrttLVFTNTRSQAERLFQRLNELNPEDALPiaahHGSLSREQR 315
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 22328183 408 NRVFHDFRNGACRNLVCT---DLftrGIDIQAVNVVINFDFPKNAETYLHRVGRSG 460
Cdd:COG1201 316 LEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
372-458 2.44e-06

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 46.40  E-value: 2.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 372 IIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNR-VFHDFRNG--ACRNLVCTDLFTRGIDIQAVNVVInFDFPKN 448
Cdd:cd18799  10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV-FLRPTE 88
                        90
                ....*....|.
gi 22328183 449 AET-YLHRVGR 458
Cdd:cd18799  89 SRTlFLQMLGR 99
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
380-470 7.50e-06

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: 46.11  E-value: 7.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 380 RVELLAKKITEL--GYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFdfpkNAETY----L 453
Cdd:cd18792  46 SIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIE----DADRFglsqL 121
                        90       100
                ....*....|....*....|.
gi 22328183 454 H----RVGRSGRFGHLGLAVN 470
Cdd:cd18792 122 HqlrgRVGRGKHQSYCYLLYP 142
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
402-461 7.51e-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: 45.81  E-value: 7.51e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 402 MLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSGR 461
Cdd:cd18801  74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
mfd TIGR00580
transcription-repair coupling factor (mfd); All proteins in this family for which functions ...
378-464 1.18e-05

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: 48.12  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   378 VNRVE-------LLAKKITELGYScfYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFdfpkNAE 450
Cdd:TIGR00580 667 HNRIEsieklatQLRELVPEARIA--IAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIE----RAD 740
                          90       100
                  ....*....|....*....|..
gi 22328183   451 TY----LH----RVGRSGRFGH 464
Cdd:TIGR00580 741 KFglaqLYqlrgRVGRSKKKAY 762
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
275-487 1.27e-05

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


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 47.45  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   275 SVLVMDEADkLLSQEFQPSVEHLISFLPESRQ-ILMFSATFPvtvKDFKDRFLTNPYVINLmDELTLKGITQFyafveER 353
Cdd:TIGR01587 126 SLLIFDEVH-FYDEYTLALILAVLEVLKDNDVpILLMSATLP---KFLKEYAEKIGYVEFN-EPLDLKEERRF-----EN 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   354 QKIH-CLNTLFSKLQINQSI-----------IFCNSVNRVELLAKKITELG--YSCFYIHAKMLQDHR----NRVFHDF- 414
Cdd:TIGR01587 196 HRFIlIESDKVGEISSLERLlefikkggsiaIIVNTVDRAQEFYQQLKEKApeEEIILYHSRFTEKDRakkeAELLREMk 275
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328183   415 RNGACRNLVCTDLFTRGIDIqAVNVVINFDFPKNAETylHRVGRSGRFGHlglavnliTYEDRFNLYRIEQEL 487
Cdd:TIGR01587 276 KSNEKFVIVATQVIEASLDI-SADVMITELAPIDSLI--QRLGRLHRYGR--------KIGENFEVYIITIAP 337
CMS1 pfam14617
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant ...
160-324 1.37e-05

U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant CMS1-like proteins. The family has similarity to the DEAD-box helicases.


Pssm-ID: 373164  Cd Length: 250  Bit Score: 46.78  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   160 ESIPiALTGRDILARAKNGTGKTAAFCIPVLEKIDqdnnviqavIIVPTRELALQTSQVCKELGKHLKIQVMVTTGGTSl 239
Cdd:pfam14617 106 EHLP-GFTKKLSQRPKSNGSPHTLVLTIAALRAAD---------VLRPLKKLQTKGFKVAKLFAKHIKLEEHITYCKAS- 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   240 kddimrlyqPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEAdkllsqeFQPSVEHLISFLPESRQILMFSATFPVTVK 319
Cdd:pfam14617 175 ---------RIGIGVGTPGRIADLLENESLSVDNLKYIILDAS-------FRDIKNRGILDIRETRKAVIKFLTSKTVLE 238

                  ....*
gi 22328183   320 DFKDR 324
Cdd:pfam14617 239 RMAEG 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
372-463 1.66e-05

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 47.53  E-value: 1.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 372 IIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNG--ACRNLVCTDLFTRGIDIQAVNVVINFDFPKNA 449
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGEGLNLTAADHVIHYDLWWNP 632
                        90
                ....*....|....
gi 22328183 450 ETYLHRVGRSGRFG 463
Cdd:COG0553 633 AVEEQAIDRAHRIG 646
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
156-315 3.06e-05

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: 44.63  E-value: 3.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 156 PIQEESIPIAL-TGRDILARAKNGTGKTAAFCIPVLEKIDQDNnviQAVIIVPTRELALQTSQVCKELGKhLKIQVMVTT 234
Cdd:cd18028   4 PPQAEAVRAGLlKGENLLISIPTASGKTLIAEMAMVNTLLEGG---KALYLVPLRALASEKYEEFKKLEE-IGLKVGIST 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 235 GGTSLKDDIMRLYqpvHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLIS---FLPESRQILMFS 311
Cdd:cd18028  80 GDYDEDDEWLGDY---DIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVArlrRLNPNTQIIGLS 156

                ....
gi 22328183 312 ATFP 315
Cdd:cd18028 157 ATIG 160
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
352-441 5.67e-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: 5.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 352 ERQKIHCLNTlfSKLQI-----------NQSIIFCNSVNRVELLAKKITELGyscfyIHAKMLQDHRNRVFHDFRNGACR 420
Cdd:cd18789  24 KRRLLAAMNP--NKLRAleellkrheqgDKIIVFTDNVEALYRYAKRLLKPF-----ITGETPQSEREEILQNFREGEYN 96
                        90       100
                ....*....|....*....|.
gi 22328183 421 NLVCTDLFTRGIDIQAVNVVI 441
Cdd:cd18789  97 TLVVSKVGDEGIDLPEANVAI 117
PRK13767 PRK13767
ATP-dependent helicase; Provisional
151-460 5.79e-05

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 46.03  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  151 FERPSPIQEESIPIALTGRDILARAKNGTGKT-AAFC--IPVLEKIDQDN---NVIQAVIIVPTRELA----------LQ 214
Cdd:PRK13767  30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLaiIDELFRLGREGeleDKVYCLYVSPLRALNndihrnleepLT 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  215 -TSQVCKELGKHL-KIQVMVTTGGTSLKDDIMRLYQPVHLLVGTP---GRILDLTK---KgvcvLKDCSVLVMDEADKL- 285
Cdd:PRK13767 110 eIREIAKERGEELpEIRVAIRTGDTSSYEKQKMLKKPPHILITTPeslAILLNSPKfreK----LRTVKWVIVDEIHSLa 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  286 -------LSQefqpSVEHLISFLPESRQILMFSATF--PVTVKDF----KDRFLTNPYVI---NLMDELTLKGITQ---- 345
Cdd:PRK13767 186 enkrgvhLSL----SLERLEELAGGEFVRIGLSATIepLEEVAKFlvgyEDDGEPRDCEIvdaRFVKPFDIKVISPvddl 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  346 FYAFVEERQK-----IHCL-----NTLfsklqinqsiIFCNSVN---RVELLAKKITELGYSCFYI---HAKMLQDHRNR 409
Cdd:PRK13767 262 IHTPAEEISEalyetLHELikehrTTL----------IFTNTRSgaeRVLYNLRKRFPEEYDEDNIgahHSSLSREVRLE 331
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 22328183  410 VFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSG 460
Cdd:PRK13767 332 VEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
153-282 6.32e-05

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 44.18  E-value: 6.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 153 RPSPIQEESIPIALTgRDILARAKNGTGKT--AAFCIpvLEKIDQD----NNVIQAVIIVPTRELAlqtSQVCKELGKHL 226
Cdd:cd18034   2 TPRSYQLELFEAALK-RNTIVVLPTGSGKTliAVMLI--KEMGELNrkekNPKKRAVFLVPTVPLV---AQQAEAIRSHT 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328183 227 KIQVMVTTGGTSL-------KDDIMRLYQpvhLLVGTPGRILDLTKKGVCVLKDCSVLVMDEA 282
Cdd:cd18034  76 DLKVGEYSGEMGVdkwtkerWKEELEKYD---VLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
169-313 7.77e-05

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 43.56  E-value: 7.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 169 RDILARAKNGTGKTAAFCIPVLekiDQDNNVIQAVIIVPTRELALQTSQVCKELGKHLKIQVMvtTGGTSLKDDimrlyQ 248
Cdd:cd17918  37 MDRLLSGDVGSGKTLVALGAAL---LAYKNGKQVAILVPTEILAHQHYEEARKFLPFINVELV--TGGTKAQIL-----S 106
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22328183 249 PVHLLVGTPGRILDLTKKgvcvlKDCSVLVMDEADKLlsqefqpSVEHLISFLPESR-QILMFSAT 313
Cdd:cd17918 107 GISLLVGTHALLHLDVKF-----KNLDLVIVDEQHRF-------GVAQREALYNLGAtHFLEATAT 160
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
158-257 1.11e-04

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: 42.96  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 158 QEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNViQAVIIVPTRelALQTSQV--CKEL--GKHLKIQVMVT 233
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGS-RALYLYPTK--ALAQDQLrsLRELleQLGLGIRVATY 81
                        90       100
                ....*....|....*....|....
gi 22328183 234 TGGTSLKDDIMRLYQPVHLLVGTP 257
Cdd:cd17923  82 DGDTPREERRAIIRNPPRILLTNP 105
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
369-461 2.18e-04

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 41.77  E-value: 2.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 369 NQSIIFCNSVNRVELLAKKITELGyscfYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKN 448
Cdd:cd18795  44 KPVLVFCSSRKECEKTAKDLAGIA----FHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
                        90       100
                ....*....|....*....|.
gi 22328183 449 AET--------YLHRVGRSGR 461
Cdd:cd18795 120 GKGyrelspleYLQMIGRAGR 140
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
372-476 2.70e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 43.73  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183   372 IIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACrNLVC-TDLFTRGIDIQAVNVVINFDFPKNAE 450
Cdd:PLN03137  684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEI-NIICaTVAFGMGINKPDVRFVIHHSLPKSIE 762
                          90       100
                  ....*....|....*....|....*.
gi 22328183   451 TYLHRVGRSGRFGHLGLAVNLITYED 476
Cdd:PLN03137  763 GYHQECGRAGRDGQRSSCVLYYSYSD 788
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
154-282 4.25e-04

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: 41.65  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 154 PSPIQEESIPIALTGRDILARAKNGTGKT---AAFCIPVLEKIDQDNNViQAVIIVPTRELALQTSQVCKELGKHLKIQV 230
Cdd:cd17927   3 PRNYQLELAQPALKGKNTIICLPTGSGKTfvaVLICEHHLKKFPAGRKG-KVVFLANKVPLVEQQKEVFRKHFERPGYKV 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 22328183 231 MVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKG-VCVLKDCSVLVMDEA 282
Cdd:cd17927  82 TGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGtIVSLSDFSLLVFDEC 134
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
168-281 6.88e-04

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: 40.26  E-value: 6.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 168 GRDILARAKNGTGKTAAFCIPVLEKI-DQDNNVIQAVIIVPTRELA------LQTsqVCKELGkhLKIQVMVTTGGT--S 238
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALIndqerrLEE--PLDEID--LEIPVAVRHGDTsqS 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 22328183 239 LKDDIMRlyQPVHLLVGTPGRI-LDLTKKGVC-VLKDCSVLVMDE 281
Cdd:cd17922  77 EKAKQLK--NPPGILITTPESLeLLLVNKKLReLFAGLRYVVVDE 119
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
150-332 7.55e-04

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: 40.60  E-value: 7.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 150 GFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIP--VLEKIdqdnnviqAVIIVPTreLALQTSQV--CKELGkh 225
Cdd:cd17920   9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV--------TLVVSPL--ISLMQDQVdrLQQLG-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 226 lkIQVMVTTGGTSLKD-----DIMRLYQPVHLLVgTPGRILD----LTKKGVCVLKDCSVLVMDEAdKLLSQ---EFQPS 293
Cdd:cd17920  77 --IRAAALNSTLSPEEkrevlLRIKNGQYKLLYV-TPERLLSpdflELLQRLPERKRLALIVVDEA-HCVSQwghDFRPD 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 22328183 294 ---VEHLISFLPESrQILMFSATFPVTVK-DFKDR-FLTNPYVI 332
Cdd:cd17920 153 ylrLGRLRRALPGV-PILALTATATPEVReDILKRlGLRNPVIF 195
PRK01172 PRK01172
ATP-dependent DNA helicase;
168-472 9.36e-04

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 41.79  E-value: 9.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  168 GRDILARAKNGTGKTAAFCIPVLEKIDQDnnvIQAVIIVPTRELALQTSQVCKELgKHLKIQVMVTTGGTSLKDDIMRLY 247
Cdd:PRK01172  37 GENVIVSVPTAAGKTLIAYSAIYETFLAG---LKSIYIVPLRSLAMEKYEELSRL-RSLGMRVKISIGDYDDPPDFIKRY 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  248 QPVHLlvgTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLISFL----PESRqILMFSATF--------- 314
Cdd:PRK01172 113 DVVIL---TSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSAryvnPDAR-ILALSATVsnanelaqw 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  315 -----------PVTVKD---FKDRFLTNPYVINLMDELTLKGIT-----QFYAFVEERQKIHCLNTLFSKL--QINQSII 373
Cdd:PRK01172 189 lnasliksnfrPVPLKLgilYRKRLILDGYERSQVDINSLIKETvndggQVLVFVSSRKNAEDYAEMLIQHfpEFNDFKV 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183  374 FCNSVNRVELLAKKITELGYScfYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINfDFPKNAETYL 453
Cdd:PRK01172 269 SSENNNVYDDSLNEMLPHGVA--FHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVR-DITRYGNGGI 345
                        330       340
                 ....*....|....*....|....*...
gi 22328183  454 ---------HRVGRSGRFGHLGLAVNLI 472
Cdd:PRK01172 346 rylsnmeikQMIGRAGRPGYDQYGIGYI 373
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
398-470 1.01e-03

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


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 40.02  E-value: 1.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 398 IHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVInfdfPKNAETY----LH----RVGRSGRFGHLGLAV 469
Cdd:cd18811  67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMV----IEDAERFglsqLHqlrgRVGRGDHQSYCLLVY 142

                .
gi 22328183 470 N 470
Cdd:cd18811 143 K 143
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
178-228 1.75e-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: 40.74  E-value: 1.75e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 22328183 178 GTGKTAAFCIPVLEKIDQDNNVIqavIIVPTRELALQTSQVCKELGKHLKI 228
Cdd:COG3505   9 GSGKTVGLVIPNLTQLARGESVV---VTDPKGDLAELTAGFRRRAGYDVYV 56
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
399-460 2.59e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 40.68  E-value: 2.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328183   399 HAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSG 460
Cdd:PRK09751  308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
203-313 7.68e-03

DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 37.69  E-value: 7.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328183 203 VIIVPTRELALQTSQVCKELGKHLKIQVMVTTGGTSlKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEA 282
Cdd:cd18033  50 VFMAPTKPLVSQQIEACYKITGIPSSQTAELTGSVP-PTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEA 128
                        90       100       110
                ....*....|....*....|....*....|.
gi 22328183 283 DKLLSQEFQPSVEHLISFLPESRQILMFSAT 313
Cdd:cd18033 129 HRATGNYAYCQVVRELMRYNSHFRILALTAT 159
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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