NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|40538825|ref|NP_081432|]
View 

ATP-dependent RNA helicase DDX51 [Mus musculus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13028779)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
181-425 2.76e-116

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


:

Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 346.54  E-value: 2.76e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRANGITSYFPVQAAVIPALLESADHGfligrGGYQPSDLCVSAPTGSGKTLAFVIPVVQALLHRVVCHIRALVVL 260
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKST-----PPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 261 PTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKTADGFRCLADIVVATPGRLVDHIDQTPGFSLQQLRFL 340
Cdd:cd17956  76 PTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 341 IIDEADRMIDSMHQSWLPRVVAAAFYSEGPtgscallqrTQPQALTAASTCVPQMPLQKLLFSATLTQDPEKLQRLGLYQ 420
Cdd:cd17956 156 VIDEADRLLNQSFQDWLETVMKALGRPTAP---------DLGSFGDANLLERSVRPLQKLLFSATLTRDPEKLSSLKLHR 226

                ....*
gi 40538825 421 PRLFS 425
Cdd:cd17956 227 PRLFT 231
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
452-582 2.00e-41

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: 146.50  E-value: 2.00e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 452 LTHHYVPCRLSSKPLIVL-HLVLRMSCSRALCFTNSRENSHRLY-LLAQAfgGVSVAEFSSRYGPGQRKKILKQFEQGKI 529
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAeLLEEL--GIKVAALHGDLSQEERERALKKFRSGKV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 40538825 530 QLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTARAGKTGQAFTLL 582
Cdd:cd18787  79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
181-425 2.76e-116

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


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 346.54  E-value: 2.76e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRANGITSYFPVQAAVIPALLESADHGfligrGGYQPSDLCVSAPTGSGKTLAFVIPVVQALLHRVVCHIRALVVL 260
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKST-----PPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 261 PTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKTADGFRCLADIVVATPGRLVDHIDQTPGFSLQQLRFL 340
Cdd:cd17956  76 PTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 341 IIDEADRMIDSMHQSWLPRVVAAAFYSEGPtgscallqrTQPQALTAASTCVPQMPLQKLLFSATLTQDPEKLQRLGLYQ 420
Cdd:cd17956 156 VIDEADRLLNQSFQDWLETVMKALGRPTAP---------DLGSFGDANLLERSVRPLQKLLFSATLTRDPEKLSSLKLHR 226

                ....*
gi 40538825 421 PRLFS 425
Cdd:cd17956 227 PRLFT 231
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
177-639 6.08e-91

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 287.81  E-value: 6.08e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 177 VHPDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVCHIRA 256
Cdd:COG0513   9 LSPPLLKALAELGYTTPTPIQAQAIPLILA--------GR------DVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 257 LVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDHIDQtpG-FSLQ 335
Cdd:COG0513  75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRG--------VDIVVATPGRLLDLIER--GaLDLS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 336 QLRFLIIDEADRM-----IDSMHQswlprvvaaafysegptgscaLLQRTQPQAltaastcvpqmplQKLLFSATLtqdP 410
Cdd:COG0513 145 GVETLVLDEADRMldmgfIEDIER---------------------ILKLLPKER-------------QTLLFSATM---P 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 411 EKLQRLglyqprlfSTRLgQQSPKdTAEVDENSGKytfPVGLTHHYVPCRLSSKPLIVLHLVLRMSCSRALCFTNSRENS 490
Cdd:COG0513 188 PEIRKL--------AKRY-LKNPV-RIEVAPENAT---AETIEQRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGA 254
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 491 HRL--YLLAQafgGVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGR 568
Cdd:COG0513 255 DRLaeKLQKR---GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGR 331
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40538825 569 TARAGKTGQAFTLLLKvQERKFLQMvseagVPELTHHEIPRKLLQPLVARYETALSQLEKTVKEEQKLKAA 639
Cdd:COG0513 332 TGRAGAEGTAISLVTP-DERRLLRA-----IEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKA 396
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
176-639 1.28e-46

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 170.51  E-value: 1.28e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  176 EVHPDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALL---HRVVC 252
Cdd:PRK11192   7 ELDESLLEALQDKGYTRPTAIQAEAIPPALD--------GR------DVLGSAPTGTGKTAAFLLPALQHLLdfpRRKSG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  253 HIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAkEQESLVQKTadgfrclADIVVATPGRLVDHIDQTpGF 332
Cdd:PRK11192  73 PPRILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYM-NHAEVFSEN-------QDIVVATPGRLLQYIKEE-NF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  333 SLQQLRFLIIDEADRMIDsMhqswlprvvaaafysegptGSCALLQRtqpqalTAASTcvpQMPLQKLLFSATLtqDPEK 412
Cdd:PRK11192 144 DCRAVETLILDEADRMLD-M-------------------GFAQDIET------IAAET---RWRKQTLLFSATL--EGDA 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  413 LQRlglyqprlFSTRLgqqsPKDTAEVDENSGKYTFPVGLTHHYVPCRLSSKPLIVLHLVLRMSCSRALCFTNSRENSHR 492
Cdd:PRK11192 193 VQD--------FAERL----LNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHE 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  493 LY-LLAQAfgGVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTAR 571
Cdd:PRK11192 261 LAgWLRKA--GINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGR 338
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40538825  572 AGKTGQAFTL-------LLKVQERKFLQMVSEAGVPEL--THHEIPRKLLQPLVARyeTALSQLEKTVKEEQKLKAA 639
Cdd:PRK11192 339 AGRKGTAISLveahdhlLLGKIERYIEEPLKARVIDELrpKTKAPSEKKTGKPSKK--VLAKRAEKKEKEKEKPKVK 413
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
452-582 2.00e-41

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: 146.50  E-value: 2.00e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 452 LTHHYVPCRLSSKPLIVL-HLVLRMSCSRALCFTNSRENSHRLY-LLAQAfgGVSVAEFSSRYGPGQRKKILKQFEQGKI 529
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAeLLEEL--GIKVAALHGDLSQEERERALKKFRSGKV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 40538825 530 QLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTARAGKTGQAFTLL 582
Cdd:cd18787  79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
195-413 1.68e-40

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: 145.08  E-value: 1.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825   195 PVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVcHIRALVVLPTKELAQQVSKVFN 274
Cdd:pfam00270   2 PIQAEAIPAILE--------GR------DVLVQAPTGSGKTLAFLLPALEALDKLDN-GPQALVLAPTRELAEQIYEELK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825   275 IYTDTTPLRVALVTGQKSLAKEQESLVQktadgfrclADIVVATPGRLVDHIDQTPgfSLQQLRFLIIDEADRMIDSMHQ 354
Cdd:pfam00270  67 KLGKGLGLKVASLLGGDSRKEQLEKLKG---------PDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFG 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 40538825   355 SWLPRVVaaafysegptgscallqrtqpqaltaasTCVPQmPLQKLLFSATLTQDPEKL 413
Cdd:pfam00270 136 PDLEEIL----------------------------RRLPK-KRQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
185-427 2.82e-33

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 126.45  E-value: 2.82e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825    185 LRANGITSYFPVQAAVIPALLESadhgfligrggyqPSDLCVSAPTGSGKTLAFVIPVVQALLHRVvcHIRALVVLPTKE 264
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSG-------------LRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTRE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825    265 LAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLvqktadgFRCLADIVVATPGRLVDHIDQTPgFSLQQLRFLIIDE 344
Cdd:smart00487  66 LAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKL-------ESGKTDILVTTPGRLLDLLENDK-LSLSNVDLVILDE 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825    345 ADRMIDSMHQSWLPRvvaaafysegptgscaLLQRTQPQaltaastcvpqmpLQKLLFSATLTQDPEKLQRLGLYQPRLF 424
Cdd:smart00487 138 AHRLLDGGFGDQLEK----------------LLKLLPKN-------------VQLLLLSATPPEEIENLLELFLNDPVFI 188

                   ...
gi 40538825    425 STR 427
Cdd:smart00487 189 DVG 191
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
463-573 7.43e-26

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 102.29  E-value: 7.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825   463 SKPLIVLHLVLRMSCSRALCFTNSRENSHRLYLLAQAfgGVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGI 542
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEAELLLEKE--GIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 40538825   543 DVQGVELVINYDAPQYLRTYVHRVGRTARAG 573
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
502-573 2.32e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 85.73  E-value: 2.32e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40538825    502 GVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTARAG 573
Cdd:smart00490  11 GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
478-584 6.51e-11

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 65.52  E-value: 6.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 478 SRALCFTNSRENSHRLY-LLAQAfgGVSVAEF---SSRYGPG-----QRKKILKQFEQGKIQLLISTDATARGIDVQGVE 548
Cdd:COG1111 354 SRIIVFTQYRDTAEMIVeFLSEP--GIKAGRFvgqASKEGDKgltqkEQIEILERFRAGEFNVLVATSVAEEGLDIPEVD 431
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 40538825 549 LVINYDA-PQYLRtYVHRVGRTARAGKtGQAFTLLLK 584
Cdd:COG1111 432 LVIFYEPvPSEIR-SIQRKGRTGRKRE-GRVVVLIAK 466
PRK13766 PRK13766
Hef nuclease; Provisional
478-584 6.27e-07

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 52.57  E-value: 6.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  478 SRALCFTNSRENSHRLY-LLAQAfgGVSVAEF---SSRYGP-G----QRKKILKQFEQGKIQLLISTDATARGIDVQGVE 548
Cdd:PRK13766 366 SRIIVFTQYRDTAEKIVdLLEKE--GIKAVRFvgqASKDGDkGmsqkEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVD 443
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 40538825  549 LVINYDA-PQYLRTyVHRVGRTARaGKTGQAFTLLLK 584
Cdd:PRK13766 444 LVIFYEPvPSEIRS-IQRKGRTGR-QEEGRVVVLIAK 478
 
Name Accession Description Interval E-value
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
181-425 2.76e-116

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


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 346.54  E-value: 2.76e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRANGITSYFPVQAAVIPALLESADHGfligrGGYQPSDLCVSAPTGSGKTLAFVIPVVQALLHRVVCHIRALVVL 260
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKST-----PPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 261 PTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKTADGFRCLADIVVATPGRLVDHIDQTPGFSLQQLRFL 340
Cdd:cd17956  76 PTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 341 IIDEADRMIDSMHQSWLPRVVAAAFYSEGPtgscallqrTQPQALTAASTCVPQMPLQKLLFSATLTQDPEKLQRLGLYQ 420
Cdd:cd17956 156 VIDEADRLLNQSFQDWLETVMKALGRPTAP---------DLGSFGDANLLERSVRPLQKLLFSATLTRDPEKLSSLKLHR 226

                ....*
gi 40538825 421 PRLFS 425
Cdd:cd17956 227 PRLFT 231
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
177-639 6.08e-91

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 287.81  E-value: 6.08e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 177 VHPDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVCHIRA 256
Cdd:COG0513   9 LSPPLLKALAELGYTTPTPIQAQAIPLILA--------GR------DVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 257 LVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDHIDQtpG-FSLQ 335
Cdd:COG0513  75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRG--------VDIVVATPGRLLDLIER--GaLDLS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 336 QLRFLIIDEADRM-----IDSMHQswlprvvaaafysegptgscaLLQRTQPQAltaastcvpqmplQKLLFSATLtqdP 410
Cdd:COG0513 145 GVETLVLDEADRMldmgfIEDIER---------------------ILKLLPKER-------------QTLLFSATM---P 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 411 EKLQRLglyqprlfSTRLgQQSPKdTAEVDENSGKytfPVGLTHHYVPCRLSSKPLIVLHLVLRMSCSRALCFTNSRENS 490
Cdd:COG0513 188 PEIRKL--------AKRY-LKNPV-RIEVAPENAT---AETIEQRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGA 254
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 491 HRL--YLLAQafgGVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGR 568
Cdd:COG0513 255 DRLaeKLQKR---GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGR 331
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40538825 569 TARAGKTGQAFTLLLKvQERKFLQMvseagVPELTHHEIPRKLLQPLVARYETALSQLEKTVKEEQKLKAA 639
Cdd:COG0513 332 TGRAGAEGTAISLVTP-DERRLLRA-----IEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKA 396
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
181-421 2.89e-50

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: 173.01  E-value: 2.89e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVC---HIRAL 257
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILS--------GR------DVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrGPQAL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 258 VVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDHIDQTPgFSLQQL 337
Cdd:cd00268  67 VLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKG--------PDIVVGTPGRLLDLIERGK-LDLSNV 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 338 RFLIIDEADRMIDsmhQSWLPRVVaaafysegptgscALLQRTQPQaltaastcvpqmpLQKLLFSATLTQDPEKLQRLG 417
Cdd:cd00268 138 KYLVLDEADRMLD---MGFEEDVE-------------KILSALPKD-------------RQTLLFSATLPEEVKELAKKF 188

                ....
gi 40538825 418 LYQP 421
Cdd:cd00268 189 LKNP 192
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
176-639 1.28e-46

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 170.51  E-value: 1.28e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  176 EVHPDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALL---HRVVC 252
Cdd:PRK11192   7 ELDESLLEALQDKGYTRPTAIQAEAIPPALD--------GR------DVLGSAPTGTGKTAAFLLPALQHLLdfpRRKSG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  253 HIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAkEQESLVQKTadgfrclADIVVATPGRLVDHIDQTpGF 332
Cdd:PRK11192  73 PPRILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYM-NHAEVFSEN-------QDIVVATPGRLLQYIKEE-NF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  333 SLQQLRFLIIDEADRMIDsMhqswlprvvaaafysegptGSCALLQRtqpqalTAASTcvpQMPLQKLLFSATLtqDPEK 412
Cdd:PRK11192 144 DCRAVETLILDEADRMLD-M-------------------GFAQDIET------IAAET---RWRKQTLLFSATL--EGDA 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  413 LQRlglyqprlFSTRLgqqsPKDTAEVDENSGKYTFPVGLTHHYVPCRLSSKPLIVLHLVLRMSCSRALCFTNSRENSHR 492
Cdd:PRK11192 193 VQD--------FAERL----LNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHE 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  493 LY-LLAQAfgGVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTAR 571
Cdd:PRK11192 261 LAgWLRKA--GINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGR 338
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40538825  572 AGKTGQAFTL-------LLKVQERKFLQMVSEAGVPEL--THHEIPRKLLQPLVARyeTALSQLEKTVKEEQKLKAA 639
Cdd:PRK11192 339 AGRKGTAISLveahdhlLLGKIERYIEEPLKARVIDELrpKTKAPSEKKTGKPSKK--VLAKRAEKKEKEKEKPKVK 413
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
78-616 1.07e-45

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 168.94  E-value: 1.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825   78 GSATPNSEAPRAKRRKADKDVDAGRGEEAPEELSAGAEDPGAnpqedvqRPPAPGRvlgdfaRRKTPKVQPfLPAWlaKP 157
Cdd:PRK01297  12 GEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRA-------EKPKKDK------PRRERKPKP-ASLW--KL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  158 SCVKKSVTEDLTPIEDIpEVHPDLQKQLRANGITSYFPVQAAVIPALLESADhgfLIGRggyqpsdlcvsAPTGSGKTLA 237
Cdd:PRK01297  76 EDFVVEPQEGKTRFHDF-NLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHD---AIGR-----------AQTGTGKTAA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  238 FVIPVVQALLH------RVVCHIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrcL 311
Cdd:PRK01297 141 FLISIINQLLQtpppkeRYMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEAR-------F 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  312 ADIVVATPGRLVDhIDQTPGFSLQQLRFLIIDEADRMIDsmhQSWLPRVvaaafysegptgscALLQRTQPqaltaastc 391
Cdd:PRK01297 214 CDILVATPGRLLD-FNQRGEVHLDMVEVMVLDEADRMLD---MGFIPQV--------------RQIIRQTP--------- 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  392 vPQMPLQKLLFSATLTQDPEKLQRLGLYQPRLFSTRlGQQSPKDTAEvdensgkytfpvglTHHYVPCRlSSKPLIVLHL 471
Cdd:PRK01297 267 -RKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIE-PENVASDTVE--------------QHVYAVAG-SDKYKLLYNL 329
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  472 VLRMSCSRALCFTNSRENSHRLYLLAQAfGGVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVI 551
Cdd:PRK01297 330 VTQNPWERVMVFANRKDEVRRIEERLVK-DGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVI 408
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40538825  552 NYDAPQYLRTYVHRVGRTARAGKTGQAFTLLLKvQERKFLQMVSEAGVPELTHHEIPRKLLQPLV 616
Cdd:PRK01297 409 NFTLPEDPDDYVHRIGRTGRAGASGVSISFAGE-DDAFQLPEIEELLGRKISCEMPPAELLKPVP 472
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
452-582 2.00e-41

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: 146.50  E-value: 2.00e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 452 LTHHYVPCRLSSKPLIVL-HLVLRMSCSRALCFTNSRENSHRLY-LLAQAfgGVSVAEFSSRYGPGQRKKILKQFEQGKI 529
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAeLLEEL--GIKVAALHGDLSQEERERALKKFRSGKV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 40538825 530 QLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTARAGKTGQAFTLL 582
Cdd:cd18787  79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
181-424 1.42e-40

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: 146.63  E-value: 1.42e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHR--VVCHIRALV 258
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALL--------GK------DICASAVTGSGKTAAFLLPILERLLYRpkKKAATRVLV 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 259 VLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLaKEQESLVqktadgfRCLADIVVATPGRLVDHIDQTPGFSLQQLR 338
Cdd:cd17947  67 LVPTRELAMQCFSVLQQLAQFTDITFALAVGGLSL-KAQEAAL-------RARPDIVIATPGRLIDHLRNSPSFDLDSIE 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 339 FLIIDEADRMIDsmhqswlprvvaaafysEGPTGSCALLQRTQPQAltaastcvpqmpLQKLLFSATLTQDPEKLQRLGL 418
Cdd:cd17947 139 ILVLDEADRMLE-----------------EGFADELKEILRLCPRT------------RQTMLFSATMTDEVKDLAKLSL 189

                ....*..
gi 40538825 419 YQP-RLF 424
Cdd:cd17947 190 NKPvRVF 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
195-413 1.68e-40

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: 145.08  E-value: 1.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825   195 PVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVcHIRALVVLPTKELAQQVSKVFN 274
Cdd:pfam00270   2 PIQAEAIPAILE--------GR------DVLVQAPTGSGKTLAFLLPALEALDKLDN-GPQALVLAPTRELAEQIYEELK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825   275 IYTDTTPLRVALVTGQKSLAKEQESLVQktadgfrclADIVVATPGRLVDHIDQTPgfSLQQLRFLIIDEADRMIDSMHQ 354
Cdd:pfam00270  67 KLGKGLGLKVASLLGGDSRKEQLEKLKG---------PDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFG 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 40538825   355 SWLPRVVaaafysegptgscallqrtqpqaltaasTCVPQmPLQKLLFSATLTQDPEKL 413
Cdd:pfam00270 136 PDLEEIL----------------------------RRLPK-KRQILLLSATLPRNLEDL 165
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
176-581 7.80e-40

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 153.95  E-value: 7.80e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  176 EVHPDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVC--- 252
Cdd:PRK04537  15 DLHPALLAGLESAGFTRCTPIQALTLPVALP--------GG------DVAGQAQTGTGKTLAFLVAVMNRLLSRPALadr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  253 ---HIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDHIDQT 329
Cdd:PRK04537  81 kpeDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQG--------VDVIIATPGRLIDYVKQH 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  330 PGFSLQQLRFLIIDEADRMIDSmhqswlprvvaaafyseGPTGSCALLQRTQPQALTAastcvpqmplQKLLFSATLTQ- 408
Cdd:PRK04537 153 KVVSLHACEICVLDEADRMFDL-----------------GFIKDIRFLLRRMPERGTR----------QTLLFSATLSHr 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  409 ----------DPEKLQrlgLYQPRLFSTRLGQQSpkdtaevdensgkytfpvglthhYVPCRLSSKPLIvLHLVLRMSCS 478
Cdd:PRK04537 206 vlelayehmnEPEKLV---VETETITAARVRQRI-----------------------YFPADEEKQTLL-LGLLSRSEGA 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  479 RALCFTNSRENSHRlylLAQAF--GGVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAP 556
Cdd:PRK04537 259 RTMVFVNTKAFVER---VARTLerHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLP 335
                        410       420
                 ....*....|....*....|....*
gi 40538825  557 QYLRTYVHRVGRTARAGKTGQAFTL 581
Cdd:PRK04537 336 FDAEDYVHRIGRTARLGEEGDAISF 360
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
178-581 5.56e-39

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 149.57  E-value: 5.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  178 HPDLQKQLRANGITSYFPVQAAVIPALLESADhgfLIGRggyqpsdlcvsAPTGSGKTLAFVIpvvqALLHRV-VCHIR- 255
Cdd:PRK11776  12 PPALLANLNELGYTEMTPIQAQSLPAILAGKD---VIAQ-----------AKTGSGKTAAFGL----GLLQKLdVKRFRv 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  256 -ALVVLPTKELAQQVSKVF--------NIytdttplRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDHI 326
Cdd:PRK11776  74 qALVLCPTRELADQVAKEIrrlarfipNI-------KVLTLCGGVPMGPQIDSLEHG--------AHIIVGTPGRILDHL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  327 DQTpGFSLQQLRFLIIDEADRMIDSMHQSWLPRVVAAAfysegPTgscallQRtqpqaltaastcvpqmplQKLLFSATL 406
Cdd:PRK11776 139 RKG-TLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQA-----PA------RR------------------QTLLFSATY 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  407 TQDPEKLQRLGLYQPRLFSTrlgqQSPKDTAEVD------ENSGKYTFPVGLTHHYVPcrlsskplivlhlvlrMSCsra 480
Cdd:PRK11776 189 PEGIAAISQRFQRDPVEVKV----ESTHDLPAIEqrfyevSPDERLPALQRLLLHHQP----------------ESC--- 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  481 LCFTNSRENSHRLYLLAQAFGGVSVA---EFSSRygpgQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQ 557
Cdd:PRK11776 246 VVFCNTKKECQEVADALNAQGFSALAlhgDLEQR----DRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELAR 321
                        410       420
                 ....*....|....*....|....
gi 40538825  558 YLRTYVHRVGRTARAGKTGQAFTL 581
Cdd:PRK11776 322 DPEVHVHRIGRTGRAGSKGLALSL 345
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
181-415 1.18e-38

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: 141.19  E-value: 1.18e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALL-HRVVCHIRALVV 259
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLH--------GR------DLLACAPTGSGKTLAFLIPILQKLGkPRKKKGLRALIL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 260 LPTKELAQQVSKVFNIYTDTTPLRVALVtgQKSLAKEQESLVQKTADgfrclADIVVATPGRLVDHIDQTPgFSLQQLRF 339
Cdd:cd17957  67 APTRELASQIYRELLKLSKGTGLRIVLL--SKSLEAKAKDGPKSITK-----YDILVSTPLRLVFLLKQGP-IDLSSVEY 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40538825 340 LIIDEADRMIDSMHQSWLPRVVAAafysegptgsCallqrTQPQaltaastcvpqmpLQKLLFSATLTQDPEKLQR 415
Cdd:cd17957 139 LVLDEADKLFEPGFREQTDEILAA----------C-----TNPN-------------LQRSLFSATIPSEVEELAR 186
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
195-421 4.17e-38

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


Pssm-ID: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 140.14  E-value: 4.17e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 195 PVQAAVIPALLESADhgfLIGRggyqpsdlcvsAPTGSGKTLAFVIPVVQALLHRVVcHIRALVVLPTKELAQQVSKVFN 274
Cdd:cd17954  25 KIQEEAIPVALQGRD---IIGL-----------AETGSGKTAAFALPILQALLENPQ-RFFALVLAPTRELAQQISEQFE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 275 IYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDHIDQTPGFSLQQLRFLIIDEADRMIDSMHQ 354
Cdd:cd17954  90 ALGSSIGLKSAVLVGGMDMMAQAIALAKK--------PHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLNMDFE 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40538825 355 SWLPRVVAaafysegptgscallqrtqpqaltaastcvpQMPLQK--LLFSATLTQDPEKLQRLGLYQP 421
Cdd:cd17954 162 PEIDKILK-------------------------------VIPRERttYLFSATMTTKVAKLQRASLKNP 199
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
182-422 1.04e-36

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: 135.88  E-value: 1.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 182 QKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQaLLHRV----VCHIRAL 257
Cdd:cd17941   2 LKGLKEAGFIKMTEIQRDSIPHALQ--------GR------DILGAAKTGSGKTLAFLVPLLE-KLYRErwtpEDGLGAL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 258 VVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQktadgfrclADIVVATPGRLVDHIDQTPGFSLQQL 337
Cdd:cd17941  67 IISPTRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINR---------MNILVCTPGRLLQHMDETPGFDTSNL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 338 RFLIIDEADRMIDSMHQSWLPRVVaaafySEGPTgscallQRtqpqaltaastcvpqmplQKLLFSATLTQDPEKLQRLG 417
Cdd:cd17941 138 QMLVLDEADRILDMGFKETLDAIV-----ENLPK------SR------------------QTLLFSATQTKSVKDLARLS 188

                ....*
gi 40538825 418 LYQPR 422
Cdd:cd17941 189 LKNPE 193
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
179-609 1.44e-36

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 142.64  E-value: 1.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  179 PDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVcH----- 253
Cdd:PRK10590  10 PDILRAVAEQGYREPTPIQQQAIPAVLE--------GR------DLMASAQTGTGKTAGFTLPLLQHLITRQP-Hakgrr 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  254 -IRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLvqktadgfRCLADIVVATPGRLVDhIDQTPGF 332
Cdd:PRK10590  75 pVRALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKL--------RGGVDVLVATPGRLLD-LEHQNAV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  333 SLQQLRFLIIDEADRMIDSMHQSWLPRVVAaafysegptgscallqrtqpqaltaastcvpQMPL--QKLLFSATLTQDP 410
Cdd:PRK10590 146 KLDQVEILVLDEADRMLDMGFIHDIRRVLA-------------------------------KLPAkrQNLLFSATFSDDI 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  411 EKLQRLGLYQPRLFS-TRLGQQSPKDTAEVdensgkytfpvglthHYVPCRlsSKPLIVLHLVLRMSCSRALCFTNSREN 489
Cdd:PRK10590 195 KALAEKLLHNPLEIEvARRNTASEQVTQHV---------------HFVDKK--RKRELLSQMIGKGNWQQVLVFTRTKHG 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  490 SHRlylLAQAFG--GVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVG 567
Cdd:PRK10590 258 ANH---LAEQLNkdGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIG 334
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 40538825  568 RTARAGKTGQAFTLLLkVQERKFLQmvseaGVPELTHHEIPR 609
Cdd:PRK10590 335 RTGRAAATGEALSLVC-VDEHKLLR-----DIEKLLKKEIPR 370
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
177-425 1.92e-36

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: 135.43  E-value: 1.92e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 177 VHPDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVcHIRA 256
Cdd:cd17955   6 LSSWLVKQCASLGIKEPTPIQKLCIPEILA--------GR------DVIGGAKTGSGKTAAFALPILQRLSEDPY-GIFA 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 257 LVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDHIDQTPG--FSL 334
Cdd:cd17955  71 LVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKR--------PHIVVATPGRLADHLRSSDDttKVL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 335 QQLRFLIIDEADRMIDSMHQSWLPRVVAaafysegptgscallqrtqpqaltaastCVPQMPlQKLLFSATLTQDPEKLQ 414
Cdd:cd17955 143 SRVKFLVLDEADRLLTGSFEDDLATILS----------------------------ALPPKR-QTLLFSATLTDALKALK 193
                       250
                ....*....|.
gi 40538825 415 RLGLYQPRLFS 425
Cdd:cd17955 194 ELFGNKPFFWE 204
DEXDc smart00487
DEAD-like helicases superfamily;
185-427 2.82e-33

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 126.45  E-value: 2.82e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825    185 LRANGITSYFPVQAAVIPALLESadhgfligrggyqPSDLCVSAPTGSGKTLAFVIPVVQALLHRVvcHIRALVVLPTKE 264
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSG-------------LRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTRE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825    265 LAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLvqktadgFRCLADIVVATPGRLVDHIDQTPgFSLQQLRFLIIDE 344
Cdd:smart00487  66 LAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKL-------ESGKTDILVTTPGRLLDLLENDK-LSLSNVDLVILDE 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825    345 ADRMIDSMHQSWLPRvvaaafysegptgscaLLQRTQPQaltaastcvpqmpLQKLLFSATLTQDPEKLQRLGLYQPRLF 424
Cdd:smart00487 138 AHRLLDGGFGDQLEK----------------LLKLLPKN-------------VQLLLLSATPPEEIENLLELFLNDPVFI 188

                   ...
gi 40538825    425 STR 427
Cdd:smart00487 189 DVG 191
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
181-421 1.17e-32

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: 124.61  E-value: 1.17e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRANGITSYFPVQAAVIPALLESadhgfligrggyqpSDLCVSAPTGSGKTLAFVIPVVQALLHRVVC----HIRA 256
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSN--------------KDVVVEAVTGSGKTLAFLIPVLEILLKRKANlkkgQVGA 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 257 LVVLPTKELAQQVSKVFNIYTD--TTPLRVALVTGQKSLAKEQESLVQKTadgfrclADIVVATPGRLVDHID-QTPGFS 333
Cdd:cd17960  67 LIISPTRELATQIYEVLQSFLEhhLPKLKCQLLIGGTNVEEDVKKFKRNG-------PNILVGTPGRLEELLSrKADKVK 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 334 LQQLRFLIIDEADRMID-----SMHQ--SWLPRvvaaafysegptgscallQRTqpqalTAastcvpqmplqklLFSATL 406
Cdd:cd17960 140 VKSLEVLVLDEADRLLDlgfeaDLNRilSKLPK------------------QRR-----TG-------------LFSATQ 183
                       250
                ....*....|....*
gi 40538825 407 TQDPEKLQRLGLYQP 421
Cdd:cd17960 184 TDAVEELIKAGLRNP 198
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
177-418 2.45e-31

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: 121.15  E-value: 2.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 177 VHPDLQKQLRANGITSYFPVQAAVIPALLESADhgfligrggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHR----VVC 252
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGD-------------DVLARAKTGTGKTLAFLLPAIQSLLNTkpagRRS 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 253 HIRALVVLPTKELAQQVSKVFN-IYTDTTPLRVALVTGQKSLAKEQESLVQktadgFRClaDIVVATPGRLVDHI-DQTP 330
Cdd:cd17964  68 GVSALIISPTRELALQIAAEAKkLLQGLRKLRVQSAVGGTSRRAELNRLRR-----GRP--DILVATPGRLIDHLeNPGV 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 331 GFSLQQLRFLIIDEADRMIDSMHQSWLPRVVaaafysegptgscallqrtqpQALTAAStcvpQMPLQKLLFSATLTQDP 410
Cdd:cd17964 141 AKAFTDLDYLVLDEADRLLDMGFRPDLEQIL---------------------RHLPEKN----ADPRQTLLFSATVPDEV 195

                ....*...
gi 40538825 411 EKLQRLGL 418
Cdd:cd17964 196 QQIARLTL 203
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
178-581 2.48e-31

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 126.62  E-value: 2.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  178 HPDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALL------HRVV 251
Cdd:PRK04837  16 HPQVVEALEKKGFHNCTPIQALALPLTLA--------GR------DVAGQAQTGTGKTMAFLTATFHYLLshpapeDRKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  252 CHIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDHIDQTPg 331
Cdd:PRK04837  82 NQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESG--------VDILIGTTGRLIDYAKQNH- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  332 FSLQQLRFLIIDEADRMIDsmhqswLPRVVAAAFysegptgscaLLQRtqpqaltaastcvpqMPLQK----LLFSATLT 407
Cdd:PRK04837 153 INLGAIQVVVLDEADRMFD------LGFIKDIRW----------LFRR---------------MPPANqrlnMLFSATLS 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  408 -----------QDPEK-----LQRLG------LYQP------RLFSTRLGQQSPkDTAEVDENsgkytfpvglTHHyvpc 459
Cdd:PRK04837 202 yrvrelafehmNNPEYvevepEQKTGhrikeeLFYPsneekmRLLQTLIEEEWP-DRAIIFAN----------TKH---- 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  460 rlsSKPLIVLHLVlrmscsralcftnsrENSHRLYLLAqafGGVSvaefssrygpgQRK--KILKQFEQGKIQLLISTDA 537
Cdd:PRK04837 267 ---RCEEIWGHLA---------------ADGHRVGLLT---GDVA-----------QKKrlRILEEFTRGDLDILVATDV 314
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 40538825  538 TARGIDVQGVELVINYDAPQYLRTYVHRVGRTARAGKTGQAFTL 581
Cdd:PRK04837 315 AARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
183-415 6.04e-30

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: 118.11  E-value: 6.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 183 KQLRANGITSYFPVQAAVIPALLesadhgfligRGGYqpsDLCVSAPTGSGKTLAFVIPVVQALL--------HRVVCHI 254
Cdd:cd17946   3 RALADLGFSEPTPIQALALPAAI----------RDGK---DVIGAAETGSGKTLAFGIPILERLLsqkssngvGGKQKPL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 255 RALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDHIDQTPGF-- 332
Cdd:cd17946  70 RALILTPTRELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKR--------PEIVVATPGRLWELIQEGNEHla 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 333 SLQQLRFLIIDEADRMIDSMHQSWLPRVVaaafysegptgscALLQRTQPQAltaastcVPQMplQKLLFSATLT---QD 409
Cdd:cd17946 142 NLKSLRFLVLDEADRMLEKGHFAELEKIL-------------ELLNKDRAGK-------KRKR--QTFVFSATLTldhQL 199

                ....*.
gi 40538825 410 PEKLQR 415
Cdd:cd17946 200 PLKLNS 205
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
195-594 6.52e-30

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 124.96  E-value: 6.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  195 PVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPvvqaLLHRVVCHIRA---LVVLPTKELAQQVSK 271
Cdd:PRK11634  31 PIQAECIPHLLN--------GR------DVLGMAQTGSGKTAAFSLP----LLHNLDPELKApqiLVLAPTRELAVQVAE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  272 VFNIYTDTTPLR--VALVTGQKSLakeqeslVQKTAdgFRCLADIVVATPGRLVDHIDQTPgFSLQQLRFLIIDEADRMI 349
Cdd:PRK11634  93 AMTDFSKHMRGVnvVALYGGQRYD-------VQLRA--LRQGPQIVVGTPGRLLDHLKRGT-LDLSKLSGLVLDEADEML 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  350 dsmhqswlprvvAAAFYSEgptgscallqrtqpqaltaASTCVPQMPL--QKLLFSATLtqdPEKLQRLglyqPRLFStr 427
Cdd:PRK11634 163 ------------RMGFIED-------------------VETIMAQIPEghQTALFSATM---PEAIRRI----TRRFM-- 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  428 lgqqspKDTAEVDENSGKYTFPvGLTHHYVPCRLSSKPLIVLHLVLRMSCSRALCFTNSRENSHRLyllAQAF--GGVSV 505
Cdd:PRK11634 203 ------KEPQEVRIQSSVTTRP-DISQSYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEV---AEALerNGYNS 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  506 AEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTARAGKTGQAFtLLLKV 585
Cdd:PRK11634 273 AALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRAL-LFVEN 351

                 ....*....
gi 40538825  586 QERKFLQMV 594
Cdd:PRK11634 352 RERRLLRNI 360
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
181-421 2.14e-29

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: 115.76  E-value: 2.14e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRAN-GITSYFPVQAAVIPALLesadhgfligrggyQPSDLCVSAPTGSGKTLAFVIPVVQaLLHRVVCHIR---- 255
Cdd:cd17949   1 LVSHLKSKmGIEKPTAIQKLAIPVLL--------------QGRDVLVRSQTGSGKTLAYLLPIIQ-RLLSLEPRVDrsdg 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 256 --ALVVLPTKELAQQVSKVFNIYTDTTP-LRVALVTGQKSLAKEQESLvqktadgfRCLADIVVATPGRLVDHIDQTPGF 332
Cdd:cd17949  66 tlALVLVPTRELALQIYEVLEKLLKPFHwIVPGYLIGGEKRKSEKARL--------RKGVNILIATPGRLLDHLKNTQSF 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 333 SLQQLRFLIIDEADRMIDSMHQSWLPRVVAAAfysegptgscallqRTQPQALTAASTCVPQmpLQKLLFSATLTQDPEK 412
Cdd:cd17949 138 DVSNLRWLVLDEADRLLDMGFEKDITKILELL--------------DDKRSKAGGEKSKPSR--RQTVLVSATLTDGVKR 201

                ....*....
gi 40538825 413 LQRLGLYQP 421
Cdd:cd17949 202 LAGLSLKDP 210
PTZ00110 PTZ00110
helicase; Provisional
179-582 2.23e-29

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 122.96  E-value: 2.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  179 PD-LQKQLRANGITSYFPVQAAVIPALLESADhgfLIGRggyqpsdlcvsAPTGSGKTLAFVIPVVqallhrvvCHIRA- 256
Cdd:PTZ00110 138 PDyILKSLKNAGFTEPTPIQVQGWPIALSGRD---MIGI-----------AETGSGKTLAFLLPAI--------VHINAq 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  257 -----------LVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDH 325
Cdd:PTZ00110 196 pllrygdgpivLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRG--------VEILIACPGRLIDF 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  326 IDQTPGfSLQQLRFLIIDEADRMIDSMHQSWLPRVVAAAfyseGPTGSCALLQRTQP---QALtAASTCvPQMPLQKLLF 402
Cdd:PTZ00110 268 LESNVT-NLRRVTYLVLDEADRMLDMGFEPQIRKIVSQI----RPDRQTLMWSATWPkevQSL-ARDLC-KEEPVHVNVG 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  403 SATLT------------QDPEKLQRLglyqpRLFSTRLGQQSPKDTAEVDENSGKYTFPVGLthhyvpcRLSSKPlivlh 470
Cdd:PTZ00110 341 SLDLTachnikqevfvvEEHEKRGKL-----KMLLQRIMRDGDKILIFVETKKGADFLTKEL-------RLDGWP----- 403
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  471 lvlrmscsrALCFTNSRENSHRLYllaqafggvsvaefssrygpgqrkkILKQFEQGKIQLLISTDATARGIDVQGVELV 550
Cdd:PTZ00110 404 ---------ALCIHGDKKQEERTW-------------------------VLNEFKTGKSPIMIATDVASRGLDVKDVKYV 449
                        410       420       430
                 ....*....|....*....|....*....|..
gi 40538825  551 INYDAPQYLRTYVHRVGRTARAGKTGQAFTLL 582
Cdd:PTZ00110 450 INFDFPNQIEDYVHRIGRTGRAGAKGASYTFL 481
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
179-421 2.35e-29

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: 115.37  E-value: 2.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 179 PDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHR--VVCH--- 253
Cdd:cd17961   3 PRLLKAIAKLGWEKPTLIQSKAIPLALE--------GK------DILARARTGSGKTAAYALPIIQKILKAkaESGEeqg 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 254 IRALVVLPTKELAQQVSKVFNIYTD--TTPLRVALVTGQKSlAKEQESLVqktadgfRCLADIVVATPGRLVDHIDQTPG 331
Cdd:cd17961  69 TRALILVPTRELAQQVSKVLEQLTAycRKDVRVVNLSASSS-DSVQRALL-------AEKPDIVVSTPARLLSHLESGSL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 332 FSLQQLRFLIIDEADRMIDSMHQSWLPRVVaaafySEGPTGscallqrtqpqaltaastcvpqmpLQKLLFSATLTQDPE 411
Cdd:cd17961 141 LLLSTLKYLVIDEADLVLSYGYEEDLKSLL-----SYLPKN------------------------YQTFLMSATLSEDVE 191
                       250
                ....*....|
gi 40538825 412 KLQRLGLYQP 421
Cdd:cd17961 192 ALKKLVLHNP 201
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
179-416 3.36e-29

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: 115.66  E-value: 3.36e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 179 PDLQKQLRAN----GITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALL------- 247
Cdd:cd17967   5 AGLRELLLENikraGYTKPTPVQKYAIPIILA--------GR------DLMACAQTGSGKTAAFLLPIISKLLedgppsv 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 248 --HRVVCHIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQktadGfrclADIVVATPGRLVDH 325
Cdd:cd17967  71 grGRRKAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLR----G----CDILVATPGRLVDF 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 326 IDQtpGF-SLQQLRFLIIDEADRMIDsmhQSWLP---RVVAAafysegptgscallqrtqpqaltaastcvPQMPL---- 397
Cdd:cd17967 143 IER--GRiSLSSIKFLVLDEADRMLD---MGFEPqirKIVEH-----------------------------PDMPPkger 188
                       250
                ....*....|....*....
gi 40538825 398 QKLLFSATLtqdPEKLQRL 416
Cdd:cd17967 189 QTLMFSATF---PREIQRL 204
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
182-424 1.38e-28

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: 113.22  E-value: 1.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 182 QKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQaLLHRVVCHIR----AL 257
Cdd:cd17942   2 LKAIEEMGFTKMTEIQAKSIPPLLE--------GR------DVLGAAKTGSGKTLAFLIPAIE-LLYKLKFKPRngtgVI 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 258 VVLPTKELAQQ---VSKVFNIYTDTTplrVALVTGQKSLAKEQESLVQKTadgfrclaDIVVATPGRLVDHIDQTPGFSL 334
Cdd:cd17942  67 IISPTRELALQiygVAKELLKYHSQT---FGIVIGGANRKAEAEKLGKGV--------NILVATPGRLLDHLQNTKGFLY 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 335 QQLRFLIIDEADRMI-----DSMHQ--SWLPRvvaaafysegptgscallQRtqpqaltaastcvpqmplQKLLFSATLT 407
Cdd:cd17942 136 KNLQCLIIDEADRILeigfeEEMRQiiKLLPK------------------RR------------------QTMLFSATQT 179
                       250
                ....*....|....*..
gi 40538825 408 QDPEKLQRLGLYQPRLF 424
Cdd:cd17942 180 RKVEDLARISLKKKPLY 196
PTZ00424 PTZ00424
helicase 45; Provisional
228-582 1.46e-27

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 115.31  E-value: 1.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  228 APTGSGKTLAFVIPVVQALLHRVVChIRALVVLPTKELAQQVSKVFNIYTDTTPLRV-ALVTGqkslakeqeSLVQKTAD 306
Cdd:PTZ00424  72 AQSGTGKTATFVIAALQLIDYDLNA-CQALILAPTRELAQQIQKVVLALGDYLKVRChACVGG---------TVVRDDIN 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  307 GFRCLADIVVATPGRLVDHIDQTpGFSLQQLRFLIIDEADRMIdsmhqswlprvvaaafySEGPTGSCALLQRTQPQALT 386
Cdd:PTZ00424 142 KLKAGVHMVVGTPGRVYDMIDKR-HLRVDDLKLFILDEADEML-----------------SRGFKGQIYDVFKKLPPDVQ 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  387 AAstcvpqmplqklLFSATLTQDPEKLQRLGLYQPRlfstRLGQQSPKDTAEvdensgkytfpvGLTHHYVPCRLSSKPL 466
Cdd:PTZ00424 204 VA------------LFSATMPNEILELTTKFMRDPK----RILVKKDELTLE------------GIRQFYVAVEKEEWKF 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  467 IVL-HLVLRMSCSRALCFTNSRENSHRLYLLAQAfGGVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQ 545
Cdd:PTZ00424 256 DTLcDLYETLTITQAIIYCNTRRKVDYLTKKMHE-RDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 40538825  546 GVELVINYDAPQYLRTYVHRVGRTARAGKTGQAFTLL 582
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFV 371
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
195-421 1.42e-26

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: 108.18  E-value: 1.42e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 195 PVQAAVIPALLESADhgfLIGrggyqpsdlcvSAPTGSGKTLAFVIPVVQALLHRVVCHIR-------ALVVLPTKELAQ 267
Cdd:cd17945  15 PIQRQAIPIGLQNRD---IIG-----------IAETGSGKTAAFLIPLLVYISRLPPLDEEtkddgpyALILAPTRELAQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 268 QVSKVFNIYTDTTPLRVALVTGQKSLaKEQESLVQKTadgfrclADIVVATPGRLVDHIDQTPgFSLQQLRFLIIDEADR 347
Cdd:cd17945  81 QIEEETQKFAKPLGIRVVSIVGGHSI-EEQAFSLRNG-------CEILIATPGRLLDCLERRL-LVLNQCTYVVLDEADR 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40538825 348 MIDSMHQSWLPRVVAAafysegpTGSCALLQRTQPQALTAASTcvPQMPLQKLLFSATLTQDPEKLQRLGLYQP 421
Cdd:cd17945 152 MIDMGFEPQVTKILDA-------MPVSNKKPDTEEAEKLAASG--KHRYRQTMMFTATMPPAVEKIAKGYLRRP 216
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
463-573 7.43e-26

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 102.29  E-value: 7.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825   463 SKPLIVLHLVLRMSCSRALCFTNSRENSHRLYLLAQAfgGVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGI 542
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEAELLLEKE--GIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 40538825   543 DVQGVELVINYDAPQYLRTYVHRVGRTARAG 573
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
179-612 9.69e-26

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 111.42  E-value: 9.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  179 PDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQAllhrvVCHIR--- 255
Cdd:PLN00206 130 PKLLLNLETAGYEFPTPIQMQAIPAALS--------GR------SLLVSADTGSGKTASFLVPIISR-----CCTIRsgh 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  256 --------ALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEqeslVQKTADGfrclADIVVATPGRLVDHID 327
Cdd:PLN00206 191 pseqrnplAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQ----LYRIQQG----VELIVGTPGRLIDLLS 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  328 QTpGFSLQQLRFLIIDEADRMIDSMHQSWLPRVVaaafysegptgscallqrtqpQALTAastcvPQMplqkLLFSATLT 407
Cdd:PLN00206 263 KH-DIELDNVSVLVLDEVDCMLERGFRDQVMQIF---------------------QALSQ-----PQV----LLFSATVS 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  408 QDPEKlqrlglyqprlFSTRLGqqspKDTAEVD-ENSGKYTFPVGLTHHYVPCRLSSKPLivlhLVLRMSCSR----ALC 482
Cdd:PLN00206 312 PEVEK-----------FASSLA----KDIILISiGNPNRPNKAVKQLAIWVETKQKKQKL----FDILKSKQHfkppAVV 372
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  483 FTNSRENSHrlyLLAQAFGGVSVAEFSSRYGP---GQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYL 559
Cdd:PLN00206 373 FVSSRLGAD---LLANAITVVTGLKALSIHGEksmKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTI 449
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 40538825  560 RTYVHRVGRTARAGKTGQAFTLLLKVQERKFLQMVS---EAGVPelthheIPRKLL 612
Cdd:PLN00206 450 KEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVAllkSSGAA------IPRELA 499
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
178-423 1.14e-25

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: 105.08  E-value: 1.14e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 178 HPDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQAL-LHRVVCHIRA 256
Cdd:cd17959   9 SPPLLRAIKKKGYKVPTPIQRKTIPLILD--------GR------DVVAMARTGSGKTAAFLIPMIEKLkAHSPTVGARA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 257 LVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDHIDQTpGFSLQQ 336
Cdd:cd17959  75 LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASN--------PDIIIATPGRLLHLLVEM-NLKLSS 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 337 LRFLIIDEADRMIDSMHQSWLPrvvaaafysegptgscALLQRTQPQAltaastcvpqmplQKLLFSATLtqdPEKL--- 413
Cdd:cd17959 146 VEYVVFDEADRLFEMGFAEQLH----------------EILSRLPENR-------------QTLLFSATL---PKLLvef 193
                       250
                ....*....|
gi 40538825 414 QRLGLYQPRL 423
Cdd:cd17959 194 AKAGLNEPVL 203
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
195-406 2.16e-25

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 103.94  E-value: 2.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 195 PVQAAVIPALLesadhgfligrGGyqpSDLCVSAPTGSGKTLAFVIPVVQAllhrvvchIRALVVLPTKELAQQVS---K 271
Cdd:cd17938  24 DIQAEAIPLIL-----------GG---GDVLMAAETGSGKTGAFCLPVLQI--------VVALILEPSRELAEQTYnciE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 272 VFNIYTDTTPLRVALVTGQKSlAKEQESLVQKTadgfrclADIVVATPGRLVDHIdQTPGFSLQQLRFLIIDEADRMIDS 351
Cdd:cd17938  82 NFKKYLDNPKLRVALLIGGVK-AREQLKRLESG-------VDIVVGTPGRLEDLI-KTGKLDLSSVRFFVLDEADRLLSQ 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 40538825 352 MHQSWLPRVvaaafYSEGPTGSCAlLQRtqpqaltaastcvpqmpLQKLLFSATL 406
Cdd:cd17938 153 GNLETINRI-----YNRIPKITSD-GKR-----------------LQVIVCSATL 184
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
176-416 2.39e-24

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: 102.74  E-value: 2.39e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 176 EVHPDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVCHIR 255
Cdd:cd18052  49 NLCETLLKNIRKAGYEKPTPVQKYAIPIILA--------GR------DLMACAQTGSGKTAAFLLPVLTGMMKEGLTASS 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 256 --------ALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAkEQESLVQKTADgfrcladIVVATPGRLVDHID 327
Cdd:cd18052 115 fsevqepqALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVG-HQIRQIEKGCH-------ILVATPGRLLDFIG 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 328 QTPgFSLQQLRFLIIDEADRMIDSMHQSWLPRVVAAafysegptgscallqrtqpqaltaastcvPQMPL----QKLLFS 403
Cdd:cd18052 187 RGK-ISLSKLKYLILDEADRMLDMGFGPEIRKLVSE-----------------------------PGMPSkedrQTLMFS 236
                       250
                ....*....|...
gi 40538825 404 ATLtqdPEKLQRL 416
Cdd:cd18052 237 ATF---PEEIQRL 246
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
185-350 6.75e-23

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: 97.82  E-value: 6.75e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 185 LRANGITSYFPVQAAVIPALLesadhgfligRGGYQpsdLCvSAPTGSGKTLAFVIPVVQALLHR-VVC-----HIRALV 258
Cdd:cd17948   5 LQRQGITKPTTVQKQGIPSIL----------RGRNT---LC-AAETGSGKTLTYLLPIIQRLLRYkLLAegpfnAPRGLV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 259 VLPTKELAQQVSKVFNIYTDTTPLRVALVTG----QKSLAKEQESlvqktadgfrclADIVVATPGRLV----DHIdqtp 330
Cdd:cd17948  71 ITPSRELAEQIGSVAQSLTEGLGLKVKVITGgrtkRQIRNPHFEE------------VDILVATPGALSklltSRI---- 134
                       170       180
                ....*....|....*....|
gi 40538825 331 gFSLQQLRFLIIDEADRMID 350
Cdd:cd17948 135 -YSLEQLRHLVLDEADTLLD 153
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
172-582 5.54e-22

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: 100.68  E-value: 5.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 172 EDIPE-VHPDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRV 250
Cdd:COG1205  35 APWPDwLPPELRAALKKRGIERLYSHQAEAIEAARA--------GK------NVVIATPTASGKSLAYLLPVLEALLEDP 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 251 VChiRALVVLPTKELAQ-QVSKvFNIYTDTTPL--RVALVTG-----QKSLAKEQeslvqktadgfrclADIVVATP--- 319
Cdd:COG1205 101 GA--TALYLYPTKALARdQLRR-LRELAEALGLgvRVATYDGdtppeERRWIREH--------------PDIVLTNPdml 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 320 --GRLVDHidqtPGFS--LQQLRFLIIDEAD--RMIDSMHQSW----LPRVvaAAFYSEGPTGSCAllqrtqpqaltaas 389
Cdd:COG1205 164 hyGLLPHH----TRWArfFRNLRYVVIDEAHtyRGVFGSHVANvlrrLRRI--CRHYGSDPQFILA-------------- 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 390 tcvpqmplqkllfSATLtQDPEKL-QRLglyqprlfstrLGQqspkDTAEVDENSGkytfPVGLTHHYV--------PCR 460
Cdd:COG1205 224 -------------SATI-GNPAEHaERL-----------TGR----PVTVVDEDGS----PRGERTFVLwnpplvddGIR 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 461 LSSKPL---IVLHLVLRMscSRALCFTNSRENSHRLYLLAQAF-----GGVSVAEFSSRYGPGQRKKILKQFEQGKIQLL 532
Cdd:COG1205 271 RSALAEaarLLADLVREG--LRTLVFTRSRRGAELLARYARRAlrepdLADRVAAYRAGYLPEERREIERGLRSGELLGV 348
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 40538825 533 ISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTARAGKTGQAFTLL 582
Cdd:COG1205 349 VSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVA 398
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
194-350 7.20e-22

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: 94.37  E-value: 7.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 194 FPVQAAVIPALLESADhgfLIGrggyqpsdlcvSAPTGSGKTLAFVIPVVQALLH-RVVCHIR---ALVVLPTKELAQQV 269
Cdd:cd17953  36 TPIQAQALPAIMSGRD---VIG-----------IAKTGSGKTLAFLLPMFRHIKDqRPVKPGEgpiGLIMAPTRELALQI 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 270 SKVFNIYTDTTPLRVALVTGQKSLaKEQESLVQKTadgfrclADIVVATPGRLVDHIDQTPG--FSLQQLRFLIIDEADR 347
Cdd:cd17953 102 YVECKKFSKALGLRVVCVYGGSGI-SEQIAELKRG-------AEIVVCTPGRMIDILTANNGrvTNLRRVTYVVLDEADR 173

                ...
gi 40538825 348 MID 350
Cdd:cd17953 174 MFD 176
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
183-350 2.14e-21

DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350709 [Multi-domain]  Cd Length: 206  Bit Score: 92.79  E-value: 2.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 183 KQLRANGITSYFPVQAAVIPALLESADhgfLIGrggyqpsdlcvSAPTGSGKTLAFVIPVV-QALLHRVVCHIR------ 255
Cdd:cd17951   3 KGLKKKGIKKPTPIQMQGLPTILSGRD---MIG-----------IAFTGSGKTLVFTLPLImFALEQEKKLPFIkgegpy 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 256 ALVVLPTKELAQQVSKVFNIYTDT------TPLRVALVTGQKSLaKEQESLVQKtadGFRcladIVVATPGRLVDHIdQT 329
Cdd:cd17951  69 GLIVCPSRELARQTHEVIEYYCKAlqeggyPQLRCLLCIGGMSV-KEQLEVIRK---GVH----IVVATPGRLMDML-NK 139
                       170       180
                ....*....|....*....|.
gi 40538825 330 PGFSLQQLRFLIIDEADRMID 350
Cdd:cd17951 140 KKINLDICRYLCLDEADRMID 160
HELICc smart00490
helicase superfamily c-terminal domain;
502-573 2.32e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 85.73  E-value: 2.32e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40538825    502 GVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTARAG 573
Cdd:smart00490  11 GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
181-421 3.72e-20

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: 89.01  E-value: 3.72e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRANGITSYFPVQAAVIPALLESADhgfLIGrggyqpsdlcvSAPTGSGKTLAFVIPVV-----QALLHRVVCHIr 255
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRD---MIG-----------IAKTGSGKTAAFIWPMLvhimdQRELEKGEGPI- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 256 ALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLvqktadgfRCLADIVVATPGRLVDHIdQTPGFSLQ 335
Cdd:cd17952  66 AVIVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKAL--------QEGAEIVVATPGRLIDMV-KKKATNLQ 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 336 QLRFLIIDEADRMIDsmhqswlprvvaAAFysegptgscallqrtQPQALTAASTCVPQMplQKLLFSATLTQDPEKLQR 415
Cdd:cd17952 137 RVTYLVLDEADRMFD------------MGF---------------EYQVRSIVGHVRPDR--QTLLFSATFKKKIEQLAR 187

                ....*.
gi 40538825 416 LGLYQP 421
Cdd:cd17952 188 DILSDP 193
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
181-350 7.38e-20

DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 87.81  E-value: 7.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVV-----QALLHRVVCHIr 255
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALS--------GR------DMVGIAQTGSGKTLAFLLPAIvhinaQPPLERGDGPI- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 256 ALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDHIDQ--TPgfs 333
Cdd:cd17966  66 VLVLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRG--------VEICIATPGRLIDFLDQgkTN--- 134
                       170
                ....*....|....*..
gi 40538825 334 LQQLRFLIIDEADRMID 350
Cdd:cd17966 135 LRRVTYLVLDEADRMLD 151
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
183-391 3.88e-18

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: 82.97  E-value: 3.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 183 KQLRANGITSYFPVQAAVIPALlesadhgfligrggYQPSDLCVSAPTGSGKTLAFVIPVVQAlLHRVVCHIR------A 256
Cdd:cd17944   3 KLLQARGVTYLFPIQVKTFHPV--------------YSGKDLIAQARTGTGKTFSFAIPLIEK-LQEDQQPRKrgrapkV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 257 LVVLPTKELAQQVSKVFNiyTDTTPLRVALVTGQKSLakeqeslvQKTADGFRCLADIVVATPGRLVDHIdQTPGFSLQQ 336
Cdd:cd17944  68 LVLAPTRELANQVTKDFK--DITRKLSVACFYGGTPY--------QQQIFAIRNGIDILVGTPGRIKDHL-QNGRLDLTK 136
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 40538825 337 LRFLIIDEADRMIDSMHQSWLPRVVAAAFYSEgptgscallQRTQPQALTAASTC 391
Cdd:cd17944 137 LKHVVLDEVDQMLDMGFAEQVEEILSVSYKKD---------SEDNPQTLLFSATC 182
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
178-405 5.45e-18

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: 82.62  E-value: 5.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 178 HPDLQKQLRANGITSYFPVQAAVIPALLESAdhgfligrggyqPSDLCVSAPTGSGKTLAFVIpvvqALLHRVVCHIR-- 255
Cdd:cd17963   2 KPELLKGLYAMGFNKPSKIQETALPLILSDP------------PENLIAQSQSGTGKTAAFVL----AMLSRVDPTLKsp 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 256 -ALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQktadgfrcladIVVATPGRLVDHIdQTPGFSL 334
Cdd:cd17963  66 qALCLAPTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKITAQ-----------IVIGTPGTVLDWL-KKRQLDL 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40538825 335 QQLRFLIIDEADRMIDSMHQSwlprvvaaafysegptGSCALLQRTQPQaltaastcvpqmPLQKLLFSAT 405
Cdd:cd17963 134 KKIKILVLDEADVMLDTQGHG----------------DQSIRIKRMLPR------------NCQILLFSAT 176
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
183-354 1.20e-17

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: 81.54  E-value: 1.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 183 KQLRANGITSYFPVQAAVIPallesadhgflIGRGGYqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVcHIRALVVLPT 262
Cdd:cd17943   3 EGLKAAGFQRPSPIQLAAIP-----------LGLAGH---DLIVQAKSGTGKTLVFVVIALESLDLERR-HPQVLILAPT 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 263 KELAQQVSKVF-NIYTDTTPLRVALVTGQKSLAKEQESLVQktadgfrclADIVVATPGRLVdHIDQTPGFSLQQLRFLI 341
Cdd:cd17943  68 REIAVQIHDVFkKIGKKLEGLKCEVFIGGTPVKEDKKKLKG---------CHIAVGTPGRIK-QLIELGALNVSHVRLFV 137
                       170
                ....*....|...
gi 40538825 342 IDEADRMIDSMHQ 354
Cdd:cd17943 138 LDEADKLMEGSFQ 150
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
223-351 2.60e-17

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: 80.83  E-value: 2.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 223 DLCVSAPTGSGKTLAFVIPVVQALlHRVVCHIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQ 302
Cdd:cd17939  36 DVIAQAQSGTGKTATFSIGALQRI-DTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQY 114
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 40538825 303 KTadgfrclaDIVVATPGRLVDHIdQTPGFSLQQLRFLIIDEADRMIDS 351
Cdd:cd17939 115 GP--------HIVVGTPGRVFDML-QRRSLRTDKIKMFVLDEADEMLSR 154
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
195-358 5.86e-17

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: 80.88  E-value: 5.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 195 PVQAAVIPALLESadhgfLIGRGGYQPSD-------LCVSAPTGSGKTLAFVIPVVQAL----------------LHRVV 251
Cdd:cd17965  33 PIQTLAIKKLLKT-----LMRKVTKQTSNeepklevFLLAAETGSGKTLAYLAPLLDYLkrqeqepfeeaeeeyeSAKDT 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 252 CHIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSlakeqeSLVQKTADGFRCLADIVVATPGRLVDhIDQTPG 331
Cdd:cd17965 108 GRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFG------PSYQRLQLAFKGRIDILVTTPGKLAS-LAKSRP 180
                       170       180
                ....*....|....*....|....*..
gi 40538825 332 FSLQQLRFLIIDEADRMIDsmhQSWLP 358
Cdd:cd17965 181 KILSRVTHLVVDEADTLFD---RSFLQ 204
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
226-357 7.85e-17

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: 77.83  E-value: 7.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 226 VSAPTGSGKTLAFVIPVVQALLHRvvcHIRALVVLPTKELAQQVSKVFNIYTDTtPLRVALVTGQKSlAKEQESLvqkta 305
Cdd:cd00046   6 ITAPTGSGKTLAALLAALLLLLKK---GKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSS-AEEREKN----- 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 40538825 306 dgFRCLADIVVATPGRLVDHIDQTPGFSLQQLRFLIIDEADRMIDSMHQSWL 357
Cdd:cd00046  76 --KLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALI 125
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
179-350 3.17e-16

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: 77.72  E-value: 3.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 179 PDLQKQLRANGITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALlHRVVCHIRALV 258
Cdd:cd17940   8 RELLMGIFEKGFEKPSPIQEESIPIALS--------GR------DILARAKNGTGKTGAYLIPILEKI-DPKKDVIQALI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 259 VLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKTadgfrclaDIVVATPGRLVDHIDQTPGfSLQQLR 338
Cdd:cd17940  73 LVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTV--------HVLVGTPGRILDLAKKGVA-DLSHCK 143
                       170
                ....*....|..
gi 40538825 339 FLIIDEADRMID 350
Cdd:cd17940 144 TLVLDEADKLLS 155
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
172-582 5.11e-15

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 78.14  E-value: 5.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 172 EDIPEVHPDLQKQLRANGITSYF-----PVQAAVIPALLESADHGfligrggyqPSDLCVSAPTGSGKTLAFVipvvqAL 246
Cdd:COG1061  55 EEDTERELAEAEALEAGDEASGTsfelrPYQQEALEALLAALERG---------GGRGLVVAPTGTGKTVLAL-----AL 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 247 LHRVVCHIRALVVLPTKELAQQVSKVFniytdttpLRVALVTGQKSLAKEQEslvqktadgfrclADIVVATPGRLV--D 324
Cdd:COG1061 121 AAELLRGKRVLVLVPRRELLEQWAEEL--------RRFLGDPLAGGGKKDSD-------------APITVATYQSLArrA 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 325 HIDQTPG-FSLqqlrfLIIDEAdrmidsmHQswlprvVAAAFYSEgptgscaLLQRTQPQ---ALTAasTcvP-----QM 395
Cdd:COG1061 180 HLDELGDrFGL-----VIIDEA-------HH------AGAPSYRR-------ILEAFPAAyrlGLTA--T--PfrsdgRE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 396 PLQKLLFSATLTQDPEKLQRLGLYQPRLFSTRLGQQSPKdTAEVDENSGKytfpvgLTHHYVPCRlSSKPLIVLHLVLRM 475
Cdd:COG1061 231 ILLFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRVDLTDE-RAEYDALSER------LREALAADA-ERKDKILRELLREH 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 476 -SCSRALCFTNSRENSHRlylLAQAFG--GVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVIN 552
Cdd:COG1061 303 pDDRKTLVFCSSVDHAEA---LAELLNeaGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL 379
                       410       420       430
                ....*....|....*....|....*....|
gi 40538825 553 YDAPQYLRTYVHRVGRTARAGKTGQAFTLL 582
Cdd:COG1061 380 LRPTGSPREFIQRLGRGLRPAPGKEDALVY 409
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
226-345 8.65e-15

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: 73.00  E-value: 8.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 226 VSAPTGSGKTLAFVIPVVQALLHRVvcHIRALVVLPTKELAQ-QVSKVFNIYTDT-TPLRVALVTGQKSLAKEQESLvqk 303
Cdd:cd17923  20 VTTGTASGKSLCYQLPILEALLRDP--GSRALYLYPTKALAQdQLRSLRELLEQLgLGIRVATYDGDTPREERRAII--- 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 40538825 304 tadgfRCLADIVVATPGRL---VDHIDQTPGFSLQQLRFLIIDEA 345
Cdd:cd17923  95 -----RNPPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA 134
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
194-351 1.81e-14

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: 71.91  E-value: 1.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 194 FPVQAAVIPALLESaDHGFLigrggyqpsdlcVSAPTGSGKTLAFVIPVVQALLHrvvCHIRALVVLPTKELAQQVSKVF 273
Cdd:cd17921   3 NPIQREALRALYLS-GDSVL------------VSAPTSSGKTLIAELAILRALAT---SGGKAVYIAPTRALVNQKEADL 66
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40538825 274 NIYTDTTPLRVALVTGQKSLAKEQESlvqktadgfrcLADIVVATPGRLVDHIDQTPGFSLQQLRFLIIDEADRMIDS 351
Cdd:cd17921  67 RERFGPLGKNVGLLTGDPSVNKLLLA-----------EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIGDG 133
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
223-352 2.05e-14

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


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 72.38  E-value: 2.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 223 DLCVSAPTGSGKTLAFVIPVVQALLHrVVCHIRALVVLPTKELAQQVSKVFNIYTDTTP-LRVALVTGQKSLAKEQESLV 301
Cdd:cd17950  41 DVLCQAKSGMGKTAVFVLSTLQQLEP-VDGQVSVLVICHTRELAFQISNEYERFSKYMPnVKTAVFFGGVPIKKDIEVLK 119
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 40538825 302 QKTADgfrcladIVVATPGRLVDHIDQTpGFSLQQLRFLIIDEADRMIDSM 352
Cdd:cd17950 120 NKCPH-------IVVGTPGRILALVREK-KLKLSHVKHFVLDECDKMLEQL 162
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
195-416 2.49e-14

DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350809 [Multi-domain]  Cd Length: 249  Bit Score: 73.15  E-value: 2.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 195 PVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLH---------------RVVCHIRALVV 259
Cdd:cd18051  46 PVQKHAIPIIKS--------KR------DLMACAQTGSGKTAAFLLPILSQIYEqgpgeslpsesgyygRRKQYPLALVL 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 260 LPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQKtadgfrClaDIVVATPGRLVDHIDQTPgFSLQQLRF 339
Cdd:cd18051 112 APTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERG------C--HLLVATPGRLVDMLERGK-IGLDYCKY 182
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40538825 340 LIIDEADRMIDSMHQSWLPRVVaaafysegptgscalLQRTQPqaltaastcvPQMPLQKLLFSATLtqdPEKLQRL 416
Cdd:cd18051 183 LVLDEADRMLDMGFEPQIRRIV---------------EQDTMP----------PTGERQTLMFSATF---PKEIQML 231
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
223-400 3.13e-14

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 71.71  E-value: 3.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 223 DLCVSAPTGSGKTLAFVIPVVQALLHRVVcHIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLvq 302
Cdd:cd18046  38 DVIAQAQSGTGKTATFSISILQQIDTSLK-ATQALVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKL-- 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 303 ktadgfRCLADIVVATPGRLVDHIDQTpGFSLQQLRFLIIDEADRMIDSMHQSWLPRVvaaaFYSEGPTGSCALLQRTQP 382
Cdd:cd18046 115 ------QAGPHIVVGTPGRVFDMINRR-YLRTDYIKMFVLDEADEMLSRGFKDQIYDI----FQKLPPDTQVVLLSATMP 183
                       170
                ....*....|....*...
gi 40538825 383 QALTAASTCVPQMPLQKL 400
Cdd:cd18046 184 NDVLEVTTKFMRDPIRIL 201
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
181-350 3.39e-14

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: 71.73  E-value: 3.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRANGITSYFPVQAAVIPALLesadhgfligrggyQPSDLCVSAPTGSGKTLAFVIPVVQALLHRVVCHIR----- 255
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIIL--------------QGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQrngpg 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 256 ALVVLPTKELAQQVSKVFNIYTDTTpLRVALVTGQKSLAKEQESLVQKtadgfrclADIVVATPGRLVDhIDQTPGFSLQ 335
Cdd:cd17958  67 VLVLTPTRELALQIEAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKG--------VDIIIATPGRLND-LQMNNVINLK 136
                       170
                ....*....|....*
gi 40538825 336 QLRFLIIDEADRMID 350
Cdd:cd17958 137 SITYLVLDEADRMLD 151
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
223-361 1.39e-13

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: 70.81  E-value: 1.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 223 DLCVSAPTGSGKTLAFVIPVV-----QALLHR---VVChiraLVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLA 294
Cdd:cd18049  63 DMVGVAQTGSGKTLSYLLPAIvhinhQPFLERgdgPIC----LVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKG 138
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40538825 295 KEQESLVQKTadgfrclaDIVVATPGRLVDHIDQTPGfSLQQLRFLIIDEADRMIDSMHQSWLPRVV 361
Cdd:cd18049 139 PQIRDLERGV--------EICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIV 196
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
223-361 2.97e-13

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: 70.42  E-value: 2.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 223 DLCVSAPTGSGKTLAFVIPVV-----QALLHR---VVChiraLVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLA 294
Cdd:cd18050 101 DMVGIAQTGSGKTLAYLLPAIvhinhQPYLERgdgPIC----LVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKG 176
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40538825 295 KEQESLVQKTadgfrclaDIVVATPGRLVDHIdQTPGFSLQQLRFLIIDEADRMIDSMHQSWLPRVV 361
Cdd:cd18050 177 PQIRDLERGV--------EICIATPGRLIDFL-EAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIV 234
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
181-349 4.92e-13

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: 67.96  E-value: 4.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 181 LQKQLRANGITSYFPVQAAVIPALLesadhgflIGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVCHIrALVVL 260
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGL--------LGR------DILASADTGSGKTAAFLLPVIIRCLTEHRNPS-ALILT 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 261 PTKELAQQVSK-VFNIYTDTTPLRVALVTGQKSLAKEQESLVQKTadgfrclaDIVVATPGRLVDHIDQTpGFSLQQLRF 339
Cdd:cd17962  66 PTRELAVQIEDqAKELMKGLPPMKTALLVGGLPLPPQLYRLQQGV--------KVIIATPGRLLDILKQS-SVELDNIKI 136
                       170
                ....*....|
gi 40538825 340 LIIDEADRMI 349
Cdd:cd17962 137 VVVDEADTML 146
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
171-351 9.20e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 71.08  E-value: 9.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 171 IEDIPEVHpdLQKQLRANGITSYFPVQAAVIPALLESADHgfligrggyqpsdLCVSAPTGSGKTLAFVIPVVQALLHrv 250
Cdd:COG1204   3 VAELPLEK--VIEFLKERGIEELYPPQAEALEAGLLEGKN-------------LVVSAPTASGKTLIAELAILKALLN-- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 251 vcHIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGqkslakEQESLVQKTADgfrclADIVVATPGRLVDHIDQTP 330
Cdd:COG1204  66 --GGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTG------DYDSDDEWLGR-----YDILVATPEKLDSLLRNGP 132
                       170       180
                ....*....|....*....|.
gi 40538825 331 GFsLQQLRFLIIDEAdRMIDS 351
Cdd:COG1204 133 SW-LRDVDLVVVDEA-HLIDD 151
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
478-584 6.51e-11

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 65.52  E-value: 6.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 478 SRALCFTNSRENSHRLY-LLAQAfgGVSVAEF---SSRYGPG-----QRKKILKQFEQGKIQLLISTDATARGIDVQGVE 548
Cdd:COG1111 354 SRIIVFTQYRDTAEMIVeFLSEP--GIKAGRFvgqASKEGDKgltqkEQIEILERFRAGEFNVLVATSVAEEGLDIPEVD 431
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 40538825 549 LVINYDA-PQYLRtYVHRVGRTARAGKtGQAFTLLLK 584
Cdd:COG1111 432 LVIFYEPvPSEIR-SIQRKGRTGRKRE-GRVVVLIAK 466
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
220-349 3.39e-10

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: 60.17  E-value: 3.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 220 QPSDLCVSAPTGSGKTLAFVIPVVQALlHRVVCHIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEqes 299
Cdd:cd18045  35 KGRDVIAQSQSGTGKTATFSISVLQCL-DIQVRETQALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDD--- 110
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 40538825 300 lVQKTADGFRcladIVVATPGRLVDHIdQTPGFSLQQLRFLIIDEADRMI 349
Cdd:cd18045 111 -IRKLDYGQH----IVSGTPGRVFDMI-RRRSLRTRHIKMLVLDEADEML 154
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
478-582 2.64e-09

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 55.82  E-value: 2.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 478 SRALCFTNSRENSHRLY-LLAQAFGGVSVAEF----SSRYGPG----QRKKILKQFEQGKIQLLISTDATARGIDVQGVE 548
Cdd:cd18801  31 TRVIIFSEFRDSAEEIVnFLSKIRPGIRATRFigqaSGKSSKGmsqkEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVD 110
                        90       100       110
                ....*....|....*....|....*....|....*
gi 40538825 549 LVINYDA-PQYLRTyVHRVGRTARaGKTGQAFTLL 582
Cdd:cd18801 111 LIICYDAsPSPIRM-IQRMGRTGR-KRQGRVVVLL 143
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
478-572 1.86e-08

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: 53.36  E-value: 1.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 478 SRALCFTNSR------------ENSHRLYLLAQAF--GGVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGID 543
Cdd:cd18802  26 FRGIIFVERRatavvlsrllkeHPSTLAFIRCGFLigRGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGID 105
                        90       100
                ....*....|....*....|....*....
gi 40538825 544 VQGVELVINYDAPQYLRTYVHRVGRtARA 572
Cdd:cd18802 106 VPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
ResIII pfam04851
Type III restriction enzyme, res subunit;
194-354 5.68e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 52.67  E-value: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825   194 FPVQAAVIPALLESADHGFLIGrggyqpsdlCVSAPTGSGKTL--AFVIpvvqALLHRVVCHIRALVVLPTKELAQQVSK 271
Cdd:pfam04851   5 RPYQIEAIENLLESIKNGQKRG---------LIVMATGSGKTLtaAKLI----ARLFKKGPIKKVLFLVPRKDLLEQALE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825   272 VFNIYTDTTPLRVALVTGQKSLAKEQESlvqktadgfrclaDIVVATPGRL-VDHIDQTPGFSLQQLRFLIIDEADRMID 350
Cdd:pfam04851  72 EFKKFLPNYVEIGEIISGDKKDESVDDN-------------KIVVTTIQSLyKALELASLELLPDFFDVIIIDEAHRSGA 138

                  ....
gi 40538825   351 SMHQ 354
Cdd:pfam04851 139 SSYR 142
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
528-581 7.91e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 50.01  E-value: 7.91e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 40538825 528 KIQLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTARAGKT-GQAFTL 581
Cdd:cd18785  22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDeGEVILF 76
PRK13766 PRK13766
Hef nuclease; Provisional
478-584 6.27e-07

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 52.57  E-value: 6.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  478 SRALCFTNSRENSHRLY-LLAQAfgGVSVAEF---SSRYGP-G----QRKKILKQFEQGKIQLLISTDATARGIDVQGVE 548
Cdd:PRK13766 366 SRIIVFTQYRDTAEKIVdLLEKE--GIKAVRFvgqASKDGDkGmsqkEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVD 443
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 40538825  549 LVINYDA-PQYLRTyVHRVGRTARaGKTGQAFTLLLK 584
Cdd:PRK13766 444 LVIFYEPvPSEIRS-IQRKGRTGR-QEEGRVVVLIAK 478
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
226-347 6.59e-07

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 50.51  E-value: 6.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 226 VSAPTGSGKTLAFVIpVVQALLHRVVCHIRALVVL--PTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQK 303
Cdd:cd17927  22 ICLPTGSGKTFVAVL-ICEHHLKKFPAGRKGKVVFlaNKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENVSVEQIVES 100
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 40538825 304 tadgfrclADIVVATPGRLVDHIDQTPGFSLQQLRFLIIDEADR 347
Cdd:cd17927 101 --------SDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
226-351 8.02e-07

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 50.02  E-value: 8.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 226 VSAPTGSGKT-LAFVIPVVQALLHRvvchiRALVVLPTKELAQQVSKVFNIYTDTTPLRV-ALVTGQKSLAKEQESLVQK 303
Cdd:cd17924  37 IIAPTGVGKTtFGLATSLYLASKGK-----RSYLIFPTKSLVKQAYERLSKYAEKAGVEVkILVYHSRLKKKEKEELLEK 111
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 40538825 304 TADG-FrclaDIVVATPGRLVDHIDQTPGFSLQqlrFLIIDEADRMIDS 351
Cdd:cd17924 112 IEKGdF----DILVTTNQFLSKNFDLLSNKKFD---FVFVDDVDAVLKS 153
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
194-353 1.39e-06

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: 48.87  E-value: 1.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 194 FPVQAAVIPALLESADhgfligrggyqpsDLCVSAPTGSGKTLAFVIpvvqALLHRVVCHIRALVVLPTKELAQQVSKVF 273
Cdd:cd18028   3 YPPQAEAVRAGLLKGE-------------NLLISIPTASGKTLIAEM----AMVNTLLEGGKALYLVPLRALASEKYEEF 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 274 NIYTDTTpLRVALVTGqkslakEQESLVQKTADgfrclADIVVATPGRLVDHIDQTPGFsLQQLRFLIIDEAdRMIDSMH 353
Cdd:cd18028  66 KKLEEIG-LKVGISTG------DYDEDDEWLGD-----YDIIVATYEKFDSLLRHSPSW-LRDVGVVVVDEI-HLISDEE 131
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
513-574 1.61e-06

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


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 47.59  E-value: 1.61e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40538825 513 GPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTARAGK 574
Cdd:cd18794  65 EPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGL 126
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
226-345 1.86e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 48.80  E-value: 1.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 226 VSAPTGSGKTLAFVIpVVQALLHRVVC----HIRALVVLPTKELAQQVSKVFNIYtdtTPLRVALVTGQKSLAKEQESLV 301
Cdd:cd18034  21 VVLPTGSGKTLIAVM-LIKEMGELNRKeknpKKRAVFLVPTVPLVAQQAEAIRSH---TDLKVGEYSGEMGVDKWTKERW 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 40538825 302 QKTADGFrclaDIVVATPGRLVDHIDQtpGF-SLQQLRFLIIDEA 345
Cdd:cd18034  97 KEELEKY----DVLVMTAQILLDALRH--GFlSLSDINLLIFDEC 135
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
479-574 4.81e-06

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 46.48  E-value: 4.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 479 RALCFTNSRENSHRLYLLAQAfGGVSVAEFSSR-------YGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVI 551
Cdd:cd18797  37 KTIVFCRSRKLAELLLRYLKA-RLVEEGPLASKvasyragYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVV 115
                        90       100
                ....*....|....*....|...
gi 40538825 552 NYDAPQYLRTYVHRVGRTARAGK 574
Cdd:cd18797 116 LAGYPGSLASLWQQAGRAGRRGK 138
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
225-345 7.36e-06

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 46.14  E-value: 7.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 225 CVSAPTGSGKTL-AFVIPvvqALLHRVvchiRALVVLPTKELAQQVSKVFNIYTDTTPLrvalvtgqkslaKEQESLVQK 303
Cdd:cd17926  22 ILVLPTGSGKTLtALALI---AYLKEL----RTLIVVPTDALLDQWKERFEDFLGDSSI------------GLIGGGKKK 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 40538825 304 TADGfrclADIVVATPgRLVDHIDQTPGFSLQQLRFLIIDEA 345
Cdd:cd17926  83 DFDD----ANVVVATY-QSLSNLAEEEKDLFDQFGLLIVDEA 119
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
171-344 1.01e-05

N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 46.98  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 171 IEDIPEvhpdlQKQLRANGITSYFPVQAAVIPALLESADHgfligrggyqpsdLCVSAPTGSGKTLAFVIPVVQAL-LHR 249
Cdd:cd18019   1 IEELPD-----WAQPAFEGFKSLNRIQSKLFPAAFETDEN-------------LLLCAPTGAGKTNVALLTILREIgKHR 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 250 V------VCHIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQESLVQktadgfrcladIVVATPGRLv 323
Cdd:cd18019  63 NpdgtinLDAFKIVYIAPMKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQ-----------IIVTTPEKW- 130
                       170       180
                ....*....|....*....|...
gi 40538825 324 DHIDQTPGF-SLQQL-RFLIIDE 344
Cdd:cd18019 131 DIITRKSGDrTYTQLvRLIIIDE 153
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
223-344 1.40e-05

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: 45.65  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 223 DLCVSAPTGSGKTLAFVIPVVQALLHRVVCHIRALVVLPTKELAQQVSKVFNIYTD--TTPLRVALVTGQKSLAKEQESL 300
Cdd:cd17922   3 NVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDeiDLEIPVAVRHGDTSQSEKAKQL 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 40538825 301 VQktadgfrcLADIVVATPGRLVDHIDQTPGFS-LQQLRFLIIDE 344
Cdd:cd17922  83 KN--------PPGILITTPESLELLLVNKKLRElFAGLRYVVVDE 119
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
196-344 1.77e-05

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 46.20  E-value: 1.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 196 VQAAVIPALLESADhgfligrggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRVVC---HIRALVVLPTKELAQQVskv 272
Cdd:cd18023   5 IQSEVFPDLLYSDK-------------NFVVSAPTGSGKTVLFELAILRLLKERNPLpwgNRKVVYIAPIKALCSEK--- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 273 fniYTDTTP------LRVALVTGQKSLAKEQEslVQKtadgfrclADIVVATPGR--LVDHIDQTPGFSLQQLRFLIIDE 344
Cdd:cd18023  69 ---YDDWKEkfgplgLSCAELTGDTEMDDTFE--IQD--------ADIILTTPEKwdSMTRRWRDNGNLVQLVALVLIDE 135
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
177-360 2.97e-05

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 45.48  E-value: 2.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 177 VHPDLQKQLRANGITSYFPVQAAVIPALLESAdhgfligrggyqPSDLCVSAPTGSGKTLAFVIpvvqALLHRV--VCH- 253
Cdd:cd18047   8 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEP------------PQNLIAQSQSGTGKTAAFVL----AMLSQVepANKy 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 254 IRALVVLPTKELAQQVSKVFNIYTDTTPlRVALVTGQKSLAKEQeslvqktadGFRCLADIVVATPGRLVDHIDQTPGFS 333
Cdd:cd18047  72 PQCLCLSPTYELALQTGKVIEQMGKFYP-ELKLAYAVRGNKLER---------GQKISEQIVIGTPGTVLDWCSKLKFID 141
                       170       180
                ....*....|....*....|....*...
gi 40538825 334 LQQLRFLIIDEADRMIDSM-HQSWLPRV 360
Cdd:cd18047 142 PKKIKVFVLDEADVMIATQgHQDQSIRI 169
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
468-574 3.75e-05

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: 44.18  E-value: 3.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 468 VLHLVLRMSCSraLCFTNSRENSHRLY-LLAQAFGGVSVAEFS----SRYGPGQRKKILKQFEQGKIQLLISTDATARGI 542
Cdd:cd18796  31 VIFLLERHKST--LVFTNTRSQAERLAqRLRELCPDRVPPDFIalhhGSLSRELREEVEAALKRGDLKVVVATSSLELGI 108
                        90       100       110
                ....*....|....*....|....*....|..
gi 40538825 543 DVQGVELVINYDAPQYLRTYVHRVGRTARAGK 574
Cdd:cd18796 109 DIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
221-304 1.14e-04

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: 43.17  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 221 PSDLCVSAPTGSGKTLAFVIPVVQALLHrvvcHIRALVVLPTKELAQQVSKVFNIYtdTTPLRVALVT-GQKSLAKEQES 299
Cdd:cd17918  36 PMDRLLSGDVGSGKTLVALGAALLAYKN----GKQVAILVPTEILAHQHYEEARKF--LPFINVELVTgGTKAQILSGIS 109

                ....*
gi 40538825 300 LVQKT 304
Cdd:cd17918 110 LLVGT 114
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
502-571 1.38e-04

C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 43.06  E-value: 1.38e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40538825 502 GVSVAEFSSRygpgqRKKILKQFEQGKIQLLISTdATARGIDVQGVEL------VINYDAPqyLRTYVHRVGRTAR 571
Cdd:cd18798  51 GIKAELALSS-----TEKNLEKFEEGEIDVLIGV-ASYYGVLVRGIDLperikyAIFYGVP--VTTYIQASGRTSR 118
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
189-345 2.55e-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: 42.52  E-value: 2.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 189 GITSYFPVQAAVIPALLEsadhgfliGRggyqpsDLCVSAPTGSGKTLAFVIPvvqALLHRVVChiraLVVLPTKELAQ- 267
Cdd:cd17920   9 GYDEFRPGQLEAINAVLA--------GR------DVLVVMPTGGGKSLCYQLP---ALLLDGVT----LVVSPLISLMQd 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 268 QVSKVfniytDTTPLRVALVTGQKSlAKEQESLVQKTADGfrcLADIVVATPGRLvdhidQTPGF--SLQQLR------F 339
Cdd:cd17920  68 QVDRL-----QQLGIRAAALNSTLS-PEEKREVLLRIKNG---QYKLLYVTPERL-----LSPDFleLLQRLPerkrlaL 133

                ....*.
gi 40538825 340 LIIDEA 345
Cdd:cd17920 134 IVVDEA 139
PRK00254 PRK00254
ski2-like helicase; Provisional
181-289 2.62e-04

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 44.04  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  181 LQKQLRANGITSYFPVQAavipallESADHGFLIGRggyqpsDLCVSAPTGSGKTLAFVIPVVQALLHRvvcHIRALVVL 260
Cdd:PRK00254  12 IKRVLKERGIEELYPPQA-------EALKSGVLEGK------NLVLAIPTASGKTLVAEIVMVNKLLRE---GGKAVYLV 75
                         90       100
                 ....*....|....*....|....*....
gi 40538825  261 PTKELAQQVSKVFNIYtDTTPLRVALVTG 289
Cdd:PRK00254  76 PLKALAEEKYREFKDW-EKLGLRVAMTTG 103
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
461-567 9.73e-04

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: 39.77  E-value: 9.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 461 LSSKPLIVLHLV--LRMSCSRALCFTNSRENshrLYLLAQAFG--GVSVAEFSSRYGPGQRKKILKQF--EQGKIQLLIS 534
Cdd:cd18793   9 VSGKLEALLELLeeLREPGEKVLIFSQFTDT---LDILEEALRerGIKYLRLDGSTSSKERQKLVDRFneDPDIRVFLLS 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 40538825 535 TDATARGIDVQGVELVINYDA---PQYL-----RtyVHRVG 567
Cdd:cd18793  86 TKAGGVGLNLTAANRVILYDPwwnPAVEeqaidR--AHRIG 124
DEXHc_TRCF cd17991
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ...
221-347 1.30e-03

DEXH/Q-box 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 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: 350749 [Multi-domain]  Cd Length: 193  Bit Score: 40.25  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 221 PSDLCVSAPTGSGKT-LAfvipvVQALLHRVVCHIRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSlAKEQES 299
Cdd:cd17991  36 PMDRLICGDVGFGKTeVA-----MRAAFKAVLSGKQVAVLVPTTLLAQQHYETFKERFANFPVNVELLSRFTT-AAEQRE 109
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 40538825 300 LVQKTADGfrcLADIVVATpGRLVdhidqTPGFSLQQLRFLIIDEADR 347
Cdd:cd17991 110 ILEGLKEG---KVDIVIGT-HRLL-----SKDVEFKNLGLLIIDEEQR 148
PRK02362 PRK02362
ATP-dependent DNA helicase;
171-318 1.42e-03

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 41.87  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  171 IEDIPeVHPDLQKQLRANGITSYFPVQAAVIPAllesadhGFLIGRggyqpsDLCVSAPTGSGKTLafvipVVQ-ALLHR 249
Cdd:PRK02362   3 IAELP-LPEGVIEFYEAEGIEELYPPQAEAVEA-------GLLDGK------NLLAAIPTASGKTL-----IAElAMLKA 63
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40538825  250 VVCHIRALVVLPTKELAQQVSKVFNIYTDTTpLRVALVTGqkSLAKEQESLVQKtadgfrclaDIVVAT 318
Cdd:PRK02362  64 IARGGKALYIVPLRALASEKFEEFERFEELG-VRVGISTG--DYDSRDEWLGDN---------DIIVAT 120
PRK13766 PRK13766
Hef nuclease; Provisional
224-347 1.92e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 41.40  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  224 LCVsAPTGSGKTlAFVIPVVQALLHRVVChiRALVVLPTKELAQQVSKVFNIYTDTTPLRVALVTGQKSLAKEQEsLVQK 303
Cdd:PRK13766  33 LVV-LPTGLGKT-AIALLVIAERLHKKGG--KVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKRAE-LWEK 107
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 40538825  304 tadgfrclADIVVATP---------GRLvdhidqtpgfSLQQLRFLIIDEADR 347
Cdd:PRK13766 108 --------AKVIVATPqviendliaGRI----------SLEDVSLLIFDEAHR 142
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
496-579 2.03e-03

C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350191 [Multi-domain]  Cd Length: 238  Bit Score: 40.31  E-value: 2.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 496 LAQAFGGVSVAEFSSR--YGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELV--INYDAPQYL-------RTY-- 562
Cdd:cd18804 110 LKTLFPEARIARIDRDttRKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADSGLNSpdfraseRAFql 189
                        90
                ....*....|....*...
gi 40538825 563 VHRV-GRTARAGKTGQAF 579
Cdd:cd18804 190 LTQVsGRAGRGDKPGKVI 207
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
502-581 5.15e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 40.08  E-value: 5.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825  502 GVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYLRTYVHRVGRTARAGKTGQAFTL 581
Cdd:PRK11057 260 GISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
484-617 6.09e-03

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 39.35  E-value: 6.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 484 TNSRENSHRLY-LLAQAfgGVSVAEFSSRYGPGQRKKILKQFEQGKIQLLISTDATARGIDVQGVELVINYDAPQYLRTY 562
Cdd:COG0514 237 CLSRKKVEELAeWLREA--GIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAY 314
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538825 563 VHRVGRTARAGKtgQAFTLLL-----KVQERKFLqmvsEAGVPELTHHEIPRKLLQPLVA 617
Cdd:COG0514 315 YQEIGRAGRDGL--PAEALLLygpedVAIQRFFI----EQSPPDEERKRVERAKLDAMLA 368
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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