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Conserved domains on  [gi|154759257|ref|NP_778236|]
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ATP-dependent RNA helicase DDX51 [Homo sapiens]

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

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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 ...
209-453 5.40e-121

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: 359.25  E-value: 5.40e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAHGISSYFPVQAAVIPALLESAACGflvgrGGYRPSDLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIRALVVL 288
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKST-----PPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 289 PTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKTADGYRCLADIVVATPGRLVDHIDQTPGFSLQQLRFL 368
Cdd:cd17956   76 PTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 369 IIDEADRMIDSMHQSWLPRVVAAAFQSEDPadpcallqrRQAQAVTAASTCCPQMPLQKLLFSATLTQNPEKLQQLGLHQ 448
Cdd:cd17956  156 VIDEADRLLNQSFQDWLETVMKALGRPTAP---------DLGSFGDANLLERSVRPLQKLLFSATLTRDPEKLSSLKLHR 226

                 ....*
gi 154759257 449 PRLFS 453
Cdd:cd17956  227 PRLFT 231
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
479-609 9.58e-42

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


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 147.65  E-value: 9.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 479 LTHHYVPCSLSSKPLVVLHLVLEMG-FSRVLCFTNSRENSHRLFLLVQAFGgVDVAEFSSRYGPGQRRMILKQFEQGKIQ 557
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLkPGKAIIFVNTKKRVDRLAELLEELG-IKVAALHGDLSQEERERALKKFRSGKVR 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154759257 558 LLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAGKTGQAFTLL 609
Cdd:cd18787   80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
LGT super family cl00478
Prolipoprotein diacylglyceryl transferase;
78-149 1.16e-04

Prolipoprotein diacylglyceryl transferase;


The actual alignment was detected with superfamily member PRK13108:

Pssm-ID: 469786 [Multi-domain]  Cd Length: 460  Bit Score: 44.97  E-value: 1.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154759257  78 DAEPGSPEAPQGKRRKADGEDAGAES--NEEAPGEPSAGSSEEAPGEP--SAGSSEEAPGERSTSASAEAAPDGPA 149
Cdd:PRK13108 370 DIEREQPGDLAGQAPAAHQVDAEAASaaPEEPAALASEAHDETEPEVPekAAPIPDPAKPDELAVAGPGDDPAEPD 445
 
Name Accession Description Interval E-value
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
209-453 5.40e-121

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: 359.25  E-value: 5.40e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAHGISSYFPVQAAVIPALLESAACGflvgrGGYRPSDLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIRALVVL 288
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKST-----PPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 289 PTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKTADGYRCLADIVVATPGRLVDHIDQTPGFSLQQLRFL 368
Cdd:cd17956   76 PTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 369 IIDEADRMIDSMHQSWLPRVVAAAFQSEDPadpcallqrRQAQAVTAASTCCPQMPLQKLLFSATLTQNPEKLQQLGLHQ 448
Cdd:cd17956  156 VIDEADRLLNQSFQDWLETVMKALGRPTAP---------DLGSFGDANLLERSVRPLQKLLFSATLTRDPEKLSSLKLHR 226

                 ....*
gi 154759257 449 PRLFS 453
Cdd:cd17956  227 PRLFT 231
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
204-666 1.92e-90

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 287.43  E-value: 1.92e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 204 DVHPDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIR 283
Cdd:COG0513    8 GLSPPLLKALAELGYTTPTPIQAQAIPLILA--------GR------DVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 284 ALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKtadgyrclADIVVATPGRLVDHIDQtpG-FSL 362
Cdd:COG0513   74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRG--------VDIVVATPGRLLDLIER--GaLDL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 363 QQLRFLIIDEADRMID--SMHQswLPRVVAaafqsedpadpcALLQRRqaqavtaastccpqmplQKLLFSATLtqnPEK 440
Cdd:COG0513  144 SGVETLVLDEADRMLDmgFIED--IERILK------------LLPKER-----------------QTLLFSATM---PPE 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 441 LQQLG---LHQPRLFSTGLAHRGLEDtdgdgdsgkyafpvgLTHHYVPCSLSSKPLVVLHLVLEMGFSRVLCFTNSRENS 517
Cdd:COG0513  190 IRKLAkryLKNPVRIEVAPENATAET---------------IEQRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGA 254
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 518 HRLF-LLVQAfgGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRT 596
Cdd:COG0513  255 DRLAeKLQKR--GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRT 332
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 597 ARAGKTGQAFTLLLKvQERRFLRMLteagaPELQRHELSSKLLQPLVPRYEEALSQLEESVKEERKQRAA 666
Cdd:COG0513  333 GRAGAEGTAISLVTP-DERRLLRAI-----EKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKA 396
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
204-608 6.76e-43

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 160.49  E-value: 6.76e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 204 DVHPDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLS---RVVC 280
Cdd:PRK11192   7 ELDESLLEALQDKGYTRPTAIQAEAIPPALD--------GR------DVLGSAPTGTGKTAAFLLPALQHLLDfprRKSG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 281 HIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAkEQESLVQKTadgyrclADIVVATPGRLVDHIDQTpGF 360
Cdd:PRK11192  73 PPRILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYM-NHAEVFSEN-------QDIVVATPGRLLQYIKEE-NF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 361 SLQQLRFLIIDEADRMIDSMHQSWLPRVVAAAfqsedpadpcallQRRQaqavtaastccpqmplQKLLFSATLtqNPEK 440
Cdd:PRK11192 144 DCRAVETLILDEADRMLDMGFAQDIETIAAET-------------RWRK----------------QTLLFSATL--EGDA 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 441 LQqlglhqprlfstGLAHRGLEDtdgdgdsgkyafPVGLT-----------H--HYVPCSLSSKPLVVLHLVLEMGFSRV 507
Cdd:PRK11192 193 VQ------------DFAERLLND------------PVEVEaepsrrerkkiHqwYYRADDLEHKTALLCHLLKQPEVTRS 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 508 LCFTNSRENSHRLFLLVQAfggvdvAEFSSRYGPG-----QRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDA 582
Cdd:PRK11192 249 IVFVRTRERVHELAGWLRK------AGINCCYLEGemvqaKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDM 322
                        410       420
                 ....*....|....*....|....*.
gi 154759257 583 PQYLRTYVHRVGRTARAGKTGQAFTL 608
Cdd:PRK11192 323 PRSADTYLHRIGRTGRAGRKGTAISL 348
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
479-609 9.58e-42

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 147.65  E-value: 9.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 479 LTHHYVPCSLSSKPLVVLHLVLEMG-FSRVLCFTNSRENSHRLFLLVQAFGgVDVAEFSSRYGPGQRRMILKQFEQGKIQ 557
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLkPGKAIIFVNTKKRVDRLAELLEELG-IKVAALHGDLSQEERERALKKFRSGKVR 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154759257 558 LLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAGKTGQAFTLL 609
Cdd:cd18787   80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
223-441 1.70e-41

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: 148.16  E-value: 1.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  223 PVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVcHIRALVVLPTKELAQQVSKVFN 302
Cdd:pfam00270   2 PIQAEAIPAILE--------GR------DVLVQAPTGSGKTLAFLLPALEALDKLDN-GPQALVLAPTRELAEQIYEELK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  303 IYTDATPLRVSLVTGQKSLAKEQESLVQktadgyrclADIVVATPGRLVDHIDQTPgfSLQQLRFLIIDEADRMIDSMHQ 382
Cdd:pfam00270  67 KLGKGLGLKVASLLGGDSRKEQLEKLKG---------PDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFG 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 154759257  383 SWLPRVVAAAFQSedpadpcallqrrqaqavtaastccpqmpLQKLLFSATLTQNPEKL 441
Cdd:pfam00270 136 PDLEEILRRLPKK-----------------------------RQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
213-455 2.71e-34

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 129.53  E-value: 2.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257   213 LRAHGISSYFPVQAAVIPALLEsaacgflvgrggyRPSDLCVSAPTGSGKTLAFVIPVVQALLSRVvcHIRALVVLPTKE 292
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLS-------------GLRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTRE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257   293 LAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKTadgyrclADIVVATPGRLVDHIDQTPgFSLQQLRFLIIDE 372
Cdd:smart00487  66 LAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGK-------TDILVTTPGRLLDLLENDK-LSLSNVDLVILDE 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257   373 ADRMIDSMHQSWLPRVVAAAFQSedpadpcallqrrqaqavtaastccpqmpLQKLLFSATLTQNPEKLQQLGLHQPRLF 452
Cdd:smart00487 138 AHRLLDGGFGDQLEKLLKLLPKN-----------------------------VQLLLLSATPPEEIENLLELFLNDPVFI 188

                   ...
gi 154759257   453 STG 455
Cdd:smart00487 189 DVG 191
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
490-600 1.08e-24

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: 98.82  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  490 SKPLVVLHLVLEMGFSRVLCFTNSRENSHRLFLLVQAfgGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGI 569
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEAELLLEKE--GIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 154759257  570 DVQGVELVVNYDAPQYLRTYVHRVGRTARAG 600
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
529-600 2.66e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.64  E-value: 2.66e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 154759257   529 GVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAG 600
Cdd:smart00490  11 GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
488-611 3.07e-10

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 63.21  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 488 LSSKPLVVLHLVLEM----GFSRVLCFTNSRENSHrlfLLVQAFG--GVDVAEF---SSRYGPG-----QRRMILKQFEQ 553
Cdd:COG1111  333 EHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAE---MIVEFLSepGIKAGRFvgqASKEGDKgltqkEQIEILERFRA 409
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 154759257 554 GKIQLLISTDATARGIDVQGVELVVNYDA-PQYLRtYVHRVGRTARAGKtGQAFTLLLK 611
Cdd:COG1111  410 GEFNVLVATSVAEEGLDIPEVDLVIFYEPvPSEIR-SIQRKGRTGRKRE-GRVVVLIAK 466
PRK13766 PRK13766
Hef nuclease; Provisional
505-611 9.65e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 48.72  E-value: 9.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 505 SRVLCFTNSRENSHRL--FLLVQafgGVDVAEF---SSRY---GPGQRRMI--LKQFEQGKIQLLISTDATARGIDVQGV 574
Cdd:PRK13766 366 SRIIVFTQYRDTAEKIvdLLEKE---GIKAVRFvgqASKDgdkGMSQKEQIeiLDKFRAGEFNVLVSTSVAEEGLDIPSV 442
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 154759257 575 ELVVNYDA-PQYLRTyVHRVGRTARaGKTGQAFTLLLK 611
Cdd:PRK13766 443 DLVIFYEPvPSEIRS-IQRKGRTGR-QEEGRVVVLIAK 478
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
78-149 1.16e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 44.97  E-value: 1.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154759257  78 DAEPGSPEAPQGKRRKADGEDAGAES--NEEAPGEPSAGSSEEAPGEP--SAGSSEEAPGERSTSASAEAAPDGPA 149
Cdd:PRK13108 370 DIEREQPGDLAGQAPAAHQVDAEAASaaPEEPAALASEAHDETEPEVPekAAPIPDPAKPDELAVAGPGDDPAEPD 445
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
50-181 2.11e-04

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 43.99  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  50 EPAQTEAAASTEPATRRRRRPRRRRRVNDAEPGSPEAPQGKRRKADGEDAGAESNEEAPGEPSAGSSEEAPGEPSAGSSE 129
Cdd:NF040712 213 RPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAA 292
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154759257 130 EAPgerstsASAEAAPDGPALEEAAGPLVPGLVLGGFGKRKAPKvqPFLPRW 181
Cdd:NF040712 293 EPP------APAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRR--ASVPSW 336
AIF-MLS pfam14962
Mitochondria localization Sequence; This family contains a protein found in eukaryotes. ...
76-148 2.92e-03

Mitochondria localization Sequence; This family contains a protein found in eukaryotes. Proteins in this family are typically between 240 and 613 amino acids in length. The family is found in association with pfam07992. This protein family is an N-terminal domain for the mitochondrial localization sequence for an apoptosis-inducing factor. The protein is also known as Corneal endothelium-specific protein 1 or as Ovary-specific acidic protein. It is thought to be important for membrane function and is expressed in the ovary and corneal endothelium.


Pssm-ID: 464407 [Multi-domain]  Cd Length: 192  Bit Score: 39.43  E-value: 2.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154759257   76 VNDAEPGSPEAPQGKRRKADGEDAgaesnEEAPGEPsAGSSEEAPgePSAGSSEEAPGErSTSASAEAAPDGP 148
Cdd:pfam14962  99 VAEAEKASSEAPEVSVVEAEVVDA-----EEIPDAT-AAVIEEAS--ACPGDVEAAPVE-TTAVGAETGPEVT 162
 
Name Accession Description Interval E-value
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
209-453 5.40e-121

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: 359.25  E-value: 5.40e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAHGISSYFPVQAAVIPALLESAACGflvgrGGYRPSDLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIRALVVL 288
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKST-----PPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 289 PTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKTADGYRCLADIVVATPGRLVDHIDQTPGFSLQQLRFL 368
Cdd:cd17956   76 PTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 369 IIDEADRMIDSMHQSWLPRVVAAAFQSEDPadpcallqrRQAQAVTAASTCCPQMPLQKLLFSATLTQNPEKLQQLGLHQ 448
Cdd:cd17956  156 VIDEADRLLNQSFQDWLETVMKALGRPTAP---------DLGSFGDANLLERSVRPLQKLLFSATLTRDPEKLSSLKLHR 226

                 ....*
gi 154759257 449 PRLFS 453
Cdd:cd17956  227 PRLFT 231
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
204-666 1.92e-90

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 287.43  E-value: 1.92e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 204 DVHPDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIR 283
Cdd:COG0513    8 GLSPPLLKALAELGYTTPTPIQAQAIPLILA--------GR------DVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 284 ALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKtadgyrclADIVVATPGRLVDHIDQtpG-FSL 362
Cdd:COG0513   74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRG--------VDIVVATPGRLLDLIER--GaLDL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 363 QQLRFLIIDEADRMID--SMHQswLPRVVAaafqsedpadpcALLQRRqaqavtaastccpqmplQKLLFSATLtqnPEK 440
Cdd:COG0513  144 SGVETLVLDEADRMLDmgFIED--IERILK------------LLPKER-----------------QTLLFSATM---PPE 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 441 LQQLG---LHQPRLFSTGLAHRGLEDtdgdgdsgkyafpvgLTHHYVPCSLSSKPLVVLHLVLEMGFSRVLCFTNSRENS 517
Cdd:COG0513  190 IRKLAkryLKNPVRIEVAPENATAET---------------IEQRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGA 254
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 518 HRLF-LLVQAfgGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRT 596
Cdd:COG0513  255 DRLAeKLQKR--GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRT 332
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 597 ARAGKTGQAFTLLLKvQERRFLRMLteagaPELQRHELSSKLLQPLVPRYEEALSQLEESVKEERKQRAA 666
Cdd:COG0513  333 GRAGAEGTAISLVTP-DERRLLRAI-----EKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKA 396
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
209-449 2.93e-51

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 176.09  E-value: 2.93e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVC---HIRAL 285
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILS--------GR------DVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrGPQAL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 286 VVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKtadgyrclADIVVATPGRLVDHIDQTPgFSLQQL 365
Cdd:cd00268   67 VLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKG--------PDIVVGTPGRLLDLIERGK-LDLSNV 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 366 RFLIIDEADRMIDSMHQSWLPRVVAAAfqsedPADpcallqrrqaqavtaastccpqmpLQKLLFSATLTQNPEKLQQLG 445
Cdd:cd00268  138 KYLVLDEADRMLDMGFEEDVEKILSAL-----PKD------------------------RQTLLFSATLPEEVKELAKKF 188

                 ....
gi 154759257 446 LHQP 449
Cdd:cd00268  189 LKNP 192
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
204-608 6.76e-43

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 160.49  E-value: 6.76e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 204 DVHPDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLS---RVVC 280
Cdd:PRK11192   7 ELDESLLEALQDKGYTRPTAIQAEAIPPALD--------GR------DVLGSAPTGTGKTAAFLLPALQHLLDfprRKSG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 281 HIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAkEQESLVQKTadgyrclADIVVATPGRLVDHIDQTpGF 360
Cdd:PRK11192  73 PPRILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYM-NHAEVFSEN-------QDIVVATPGRLLQYIKEE-NF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 361 SLQQLRFLIIDEADRMIDSMHQSWLPRVVAAAfqsedpadpcallQRRQaqavtaastccpqmplQKLLFSATLtqNPEK 440
Cdd:PRK11192 144 DCRAVETLILDEADRMLDMGFAQDIETIAAET-------------RWRK----------------QTLLFSATL--EGDA 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 441 LQqlglhqprlfstGLAHRGLEDtdgdgdsgkyafPVGLT-----------H--HYVPCSLSSKPLVVLHLVLEMGFSRV 507
Cdd:PRK11192 193 VQ------------DFAERLLND------------PVEVEaepsrrerkkiHqwYYRADDLEHKTALLCHLLKQPEVTRS 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 508 LCFTNSRENSHRLFLLVQAfggvdvAEFSSRYGPG-----QRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDA 582
Cdd:PRK11192 249 IVFVRTRERVHELAGWLRK------AGINCCYLEGemvqaKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDM 322
                        410       420
                 ....*....|....*....|....*.
gi 154759257 583 PQYLRTYVHRVGRTARAGKTGQAFTL 608
Cdd:PRK11192 323 PRSADTYLHRIGRTGRAGRKGTAISL 348
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
479-609 9.58e-42

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 147.65  E-value: 9.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 479 LTHHYVPCSLSSKPLVVLHLVLEMG-FSRVLCFTNSRENSHRLFLLVQAFGgVDVAEFSSRYGPGQRRMILKQFEQGKIQ 557
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLkPGKAIIFVNTKKRVDRLAELLEELG-IKVAALHGDLSQEERERALKKFRSGKVR 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154759257 558 LLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAGKTGQAFTLL 609
Cdd:cd18787   80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
223-441 1.70e-41

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: 148.16  E-value: 1.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  223 PVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVcHIRALVVLPTKELAQQVSKVFN 302
Cdd:pfam00270   2 PIQAEAIPAILE--------GR------DVLVQAPTGSGKTLAFLLPALEALDKLDN-GPQALVLAPTRELAEQIYEELK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  303 IYTDATPLRVSLVTGQKSLAKEQESLVQktadgyrclADIVVATPGRLVDHIDQTPgfSLQQLRFLIIDEADRMIDSMHQ 382
Cdd:pfam00270  67 KLGKGLGLKVASLLGGDSRKEQLEKLKG---------PDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFG 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 154759257  383 SWLPRVVAAAFQSedpadpcallqrrqaqavtaastccpqmpLQKLLFSATLTQNPEKL 441
Cdd:pfam00270 136 PDLEEILRRLPKK-----------------------------RQILLLSATLPRNLEDL 165
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
109-609 1.96e-41

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 157.38  E-value: 1.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 109 GEPSAGSSEEAPGEPSAGSSEEAPGERSTSASAEAAPDG-PALEEAAGPLVPglvlggfgkRKAPKVQPfLPRWLAEPNC 187
Cdd:PRK01297  10 GKGEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAaAPRAEKPKKDKP---------RRERKPKP-ASLWKLEDFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 188 VRRNvtEDLVPIEDIpDVHPDLQKQLRAHGISSYFPVQAAVIPALLesaacgflvgrggyRPSDLCVSAPTGSGKTLAFV 267
Cdd:PRK01297  80 VEPQ--EGKTRFHDF-NLAPELMHAIHDLGFPYCTPIQAQVLGYTL--------------AGHDAIGRAQTGTGKTAAFL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 268 IPVVQALLS------RVVCHIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKtadgyrcLAD 341
Cdd:PRK01297 143 ISIINQLLQtpppkeRYMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEAR-------FCD 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 342 IVVATPGRLVDhIDQTPGFSLQQLRFLIIDEADRMIDsmhQSWLPRVVAAAFQSEdpadpcallqrrqaqavtaastccP 421
Cdd:PRK01297 216 ILVATPGRLLD-FNQRGEVHLDMVEVMVLDEADRMLD---MGFIPQVRQIIRQTP------------------------R 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 422 QMPLQKLLFSATLTQNPEKLQQLGLHQPRLFSTGLAHRGLEDTDgdgdsgkyafpvgltHHYVPCSLSSKPLVVLHLVLE 501
Cdd:PRK01297 268 KEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVE---------------QHVYAVAGSDKYKLLYNLVTQ 332
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 502 MGFSRVLCFTNSRENSHRLF-LLVQafGGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNY 580
Cdd:PRK01297 333 NPWERVMVFANRKDEVRRIEeRLVK--DGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINF 410
                        490       500
                 ....*....|....*....|....*....
gi 154759257 581 DAPQYLRTYVHRVGRTARAGKTGQAFTLL 609
Cdd:PRK01297 411 TLPEDPDDYVHRIGRTGRAGASGVSISFA 439
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
209-452 7.53e-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: 144.71  E-value: 7.53e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSR--VVCHIRALV 286
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALL--------GK------DICASAVTGSGKTAAFLLPILERLLYRpkKKAATRVLV 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 287 VLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLaKEQESLVqktadgyRCLADIVVATPGRLVDHIDQTPGFSLQQLR 366
Cdd:cd17947   67 LVPTRELAMQCFSVLQQLAQFTDITFALAVGGLSL-KAQEAAL-------RARPDIVIATPGRLIDHLRNSPSFDLDSIE 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 367 FLIIDEADRMIDsmhqswlprvvaAAFQSEdpadpcallqrrqaqaVTAASTCCPQmPLQKLLFSATLTQNPEKLQQLGL 446
Cdd:cd17947  139 ILVLDEADRMLE------------EGFADE----------------LKEILRLCPR-TRQTMLFSATMTDEVKDLAKLSL 189

                 ....*..
gi 154759257 447 HQP-RLF 452
Cdd:cd17947  190 NKPvRVF 196
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
205-453 1.06e-38

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: 141.98  E-value: 1.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 205 VHPDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALlSRVVCHIRA 284
Cdd:cd17955    6 LSSWLVKQCASLGIKEPTPIQKLCIPEILA--------GR------DVIGGAKTGSGKTAAFALPILQRL-SEDPYGIFA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 285 LVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKtadgyrclADIVVATPGRLVDHIDQTPG--FSL 362
Cdd:cd17955   71 LVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKR--------PHIVVATPGRLADHLRSSDDttKVL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 363 QQLRFLIIDEADRMIDSMHQSWLPRVVAaafqsedpadpcallqrrqaqavtaastCCPQMPlQKLLFSATLTQNPEKLQ 442
Cdd:cd17955  143 SRVKFLVLDEADRLLTGSFEDDLATILS----------------------------ALPPKR-QTLLFSATLTDALKALK 193
                        250
                 ....*....|.
gi 154759257 443 QLGLHQPRLFS 453
Cdd:cd17955  194 ELFGNKPFFWE 204
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
209-449 1.36e-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: 141.57  E-value: 1.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALL-SRVVCHIRALVV 287
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLH--------GR------DLLACAPTGSGKTLAFLIPILQKLGkPRKKKGLRALIL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 288 LPTKELAQQVSKVFNIYTDATPLRVSLVtgQKSLAKEQESLVQKTADgyrclADIVVATPGRLVDHIDQTPgFSLQQLRF 367
Cdd:cd17957   67 APTRELASQIYRELLKLSKGTGLRIVLL--SKSLEAKAKDGPKSITK-----YDILVSTPLRLVFLLKQGP-IDLSSVEY 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 368 LIIDEADRMIDSmhqswlprvvaaAFqsedpadpcallqRRQAQAVTAAstcCPQMPLQKLLFSATLTQNPEKLQQLGLH 447
Cdd:cd17957  139 LVLDEADKLFEP------------GF-------------REQTDEILAA---CTNPNLQRSLFSATIPSEVEELARSVMK 190

                 ..
gi 154759257 448 QP 449
Cdd:cd17957  191 DP 192
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
206-644 1.13e-37

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 146.10  E-value: 1.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 206 HPDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQAL-LSRVVChiRA 284
Cdd:PRK11776  12 PPALLANLNELGYTEMTPIQAQSLPAILA--------GK------DVIAQAKTGSGKTAAFGLGLLQKLdVKRFRV--QA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 285 LVVLPTKELAQQVSKVFNIYTDATP-LRVSLVTGQKSLAKEQESLVQKtadgyrclADIVVATPGRLVDHIDQTpGFSLQ 363
Cdd:PRK11776  76 LVLCPTRELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHG--------AHIIVGTPGRILDHLRKG-TLDLD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 364 QLRFLIIDEADRMIDSMHQSWLPRVVAAAfqsedPAdpcallqRRQAqavtaastccpqmplqkLLFSATLTQNPEKLQQ 443
Cdd:PRK11776 147 ALNTLVLDEADRMLDMGFQDAIDAIIRQA-----PA-------RRQT-----------------LLFSATYPEGIAAISQ 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 444 LGLHQPRLFStglahrgLEDTDGD----------GDSGKYAFPVGLTHHYVPCSlsskplvvlhlvlemgfsrVLCFTNS 513
Cdd:PRK11776 198 RFQRDPVEVK-------VESTHDLpaieqrfyevSPDERLPALQRLLLHHQPES-------------------CVVFCNT 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 514 RENSHRLFLLVQAFGGVDVA---EFSSRygpgQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYV 590
Cdd:PRK11776 252 KKECQEVADALNAQGFSALAlhgDLEQR----DRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHV 327
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 154759257 591 HRVGRTARAGKTGQAFTlLLKVQERRFLRMLTEAGAPELQRH---ELSSKLLQPLVP 644
Cdd:PRK11776 328 HRIGRTGRAGSKGLALS-LVAPEEMQRANAIEDYLGRKLNWEplpSLSPLSGVPLLP 383
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
207-664 2.04e-37

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 145.34  E-value: 2.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 207 PDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVcH----- 281
Cdd:PRK10590  10 PDILRAVAEQGYREPTPIQQQAIPAVLE--------GR------DLMASAQTGTGKTAGFTLPLLQHLITRQP-Hakgrr 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 282 -IRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLvqktadgyRCLADIVVATPGRLVDhIDQTPGF 360
Cdd:PRK10590  75 pVRALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKL--------RGGVDVLVATPGRLLD-LEHQNAV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 361 SLQQLRFLIIDEADRMIDSMHQSWLPRVVAaafqsedpadpcALLQRRqaqavtaastccpqmplQKLLFSATLTQNPEK 440
Cdd:PRK10590 146 KLDQVEILVLDEADRMLDMGFIHDIRRVLA------------KLPAKR-----------------QNLLFSATFSDDIKA 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 441 LQQLGLHQPrlFSTGLAHRGLEDTDgdgdsgkyafpvgLTHHYVPCSLSSKPLVVLHLVLEMGFSRVLCFTNSRENSHRL 520
Cdd:PRK10590 197 LAEKLLHNP--LEIEVARRNTASEQ-------------VTQHVHFVDKKRKRELLSQMIGKGNWQQVLVFTRTKHGANHL 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 521 FLLVQAfGGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAG 600
Cdd:PRK10590 262 AEQLNK-DGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAA 340
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154759257 601 KTGQAFTLLLkVQERRFLRMLteagapelqrhelsSKLLQPLVPR-----YEEALSQLEESVKEERKQR 664
Cdd:PRK10590 341 ATGEALSLVC-VDEHKLLRDI--------------EKLLKKEIPRiaipgYEPDPSIKAEPIQNGRQQR 394
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
204-666 1.26e-36

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 145.09  E-value: 1.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 204 DVHPDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVC--- 280
Cdd:PRK04537  15 DLHPALLAGLESAGFTRCTPIQALTLPVALP--------GG------DVAGQAQTGTGKTLAFLVAVMNRLLSRPALadr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 281 ---HIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKtadgyrclADIVVATPGRLVDHIDQT 357
Cdd:PRK04537  81 kpeDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQG--------VDVIIATPGRLIDYVKQH 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 358 PGFSLQQLRFLIIDEADRMIDsmhqswLPRVVAAAFqsedpadpcalLQRRQAQAVTAastccpqmplQKLLFSATLTQN 437
Cdd:PRK04537 153 KVVSLHACEICVLDEADRMFD------LGFIKDIRF-----------LLRRMPERGTR----------QTLLFSATLSHR 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 438 PEKLQQLGLHQPRLF----STGLAHRGLEDTdgdgdsgkyafpvglthhYVPCSLSSKPLVVLHLVLEMGfSRVLCFTNS 513
Cdd:PRK04537 206 VLELAYEHMNEPEKLvvetETITAARVRQRI------------------YFPADEEKQTLLLGLLSRSEG-ARTMVFVNT 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 514 RENSHRLFLLVQAfGGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRV 593
Cdd:PRK04537 267 KAFVERVARTLER-HGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRI 345
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 594 GRTARAGKTGQAFTLLLKvqerRFLRMLTEAGAPELQR---HELSSKLLQPLvPRYEEALSQLEES-----------VKE 659
Cdd:PRK04537 346 GRTARLGEEGDAISFACE----RYAMSLPDIEAYIEQKipvEPVTAELLTPL-PRPPRVPVEGEEAddeagdsvgtiFRE 420

                 ....*..
gi 154759257 660 ERKQRAA 666
Cdd:PRK04537 421 AREQRAA 427
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
223-449 1.74e-36

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: 135.52  E-value: 1.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 223 PVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVcHIRALVVLPTKELAQQVSKVFN 302
Cdd:cd17954   25 KIQEEAIPVALQ--------GR------DIIGLAETGSGKTAAFALPILQALLENPQ-RFFALVLAPTRELAQQISEQFE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 303 IYTDATPLRVSLVTGQKSLAKEQESLVQKtadgyrclADIVVATPGRLVDHIDQTPGFSLQQLRFLIIDEADRMIDsmhq 382
Cdd:cd17954   90 ALGSSIGLKSAVLVGGMDMMAQAIALAKK--------PHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLN---- 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 383 swlprvvaAAFQSE-DpadpcALLQrrqaqavtaastccpQMPLQK--LLFSATLTQNPEKLQQLGLHQP 449
Cdd:cd17954  158 --------MDFEPEiD-----KILK---------------VIPRERttYLFSATMTTKVAKLQRASLKNP 199
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
210-450 6.74e-35

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: 130.87  E-value: 6.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 210 QKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVCH---IRALV 286
Cdd:cd17941    2 LKGLKEAGFIKMTEIQRDSIPHALQ--------GR------DILGAAKTGSGKTLAFLVPLLEKLYRERWTPedgLGALI 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 287 VLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQktadgyrclADIVVATPGRLVDHIDQTPGFSLQQLR 366
Cdd:cd17941   68 ISPTRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINR---------MNILVCTPGRLLQHMDETPGFDTSNLQ 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 367 FLIIDEADRMIDSMHQSWLPRVVAaafqsedpadpcALLQRRQAqavtaastccpqmplqkLLFSATLTQNPEKLQQLGL 446
Cdd:cd17941  139 MLVLDEADRILDMGFKETLDAIVE------------NLPKSRQT-----------------LLFSATQTKSVKDLARLSL 189

                 ....
gi 154759257 447 HQPR 450
Cdd:cd17941  190 KNPE 193
DEXDc smart00487
DEAD-like helicases superfamily;
213-455 2.71e-34

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 129.53  E-value: 2.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257   213 LRAHGISSYFPVQAAVIPALLEsaacgflvgrggyRPSDLCVSAPTGSGKTLAFVIPVVQALLSRVvcHIRALVVLPTKE 292
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLS-------------GLRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTRE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257   293 LAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKTadgyrclADIVVATPGRLVDHIDQTPgFSLQQLRFLIIDE 372
Cdd:smart00487  66 LAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGK-------TDILVTTPGRLLDLLENDK-LSLSNVDLVILDE 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257   373 ADRMIDSMHQSWLPRVVAAAFQSedpadpcallqrrqaqavtaastccpqmpLQKLLFSATLTQNPEKLQQLGLHQPRLF 452
Cdd:smart00487 138 AHRLLDGGFGDQLEKLLKLLPKN-----------------------------VQLLLLSATPPEEIENLLELFLNDPVFI 188

                   ...
gi 154759257   453 STG 455
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, ...
223-449 3.09e-33

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: 126.54  E-value: 3.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 223 PVQAAVIPALLESaacgflvgrggyrpSDLCVSAPTGSGKTLAFVIPVVQALLSRVVC----HIRALVVLPTKELAQQVS 298
Cdd:cd17960   15 PVQAATIPLFLSN--------------KDVVVEAVTGSGKTLAFLIPVLEILLKRKANlkkgQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 299 KVFNIYTDA--TPLRVSLVTGQKSLAKEQESLVQKTadgyrclADIVVATPGRLVDHID-QTPGFSLQQLRFLIIDEADR 375
Cdd:cd17960   81 EVLQSFLEHhlPKLKCQLLIGGTNVEEDVKKFKRNG-------PNILVGTPGRLEELLSrKADKVKVKSLEVLVLDEADR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 376 MID-----SMHQ--SWLPRvvaaafqsedpadpcallQRRQAqavtaastccpqmplqklLFSATLTQNPEKLQQLGLHQ 448
Cdd:cd17960  154 LLDlgfeaDLNRilSKLPK------------------QRRTG------------------LFSATQTDAVEELIKAGLRN 197

                 .
gi 154759257 449 P 449
Cdd:cd17960  198 P 198
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
205-444 1.59e-32

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: 124.62  E-value: 1.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 205 VHPDLQKQLRAHGISSYFPVQAAVIPALLESAacgflvgrggyrpSDLCVSAPTGSGKTLAFVIPVVQALLSR----VVC 280
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTG-------------DDVLARAKTGTGKTLAFLLPAIQSLLNTkpagRRS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 281 HIRALVVLPTKELAQQVSKVFN-IYTDATPLRVSLVTGQKSLAKEQESLVQKtadgyRClaDIVVATPGRLVDHI-DQTP 358
Cdd:cd17964   68 GVSALIISPTRELALQIAAEAKkLLQGLRKLRVQSAVGGTSRRAELNRLRRG-----RP--DILVATPGRLIDHLeNPGV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 359 GFSLQQLRFLIIDEADRMIDSMHQSWLPRVVAAafqsedpadpcalLQRRQAQavtaastccpqmPLQKLLFSATLtqnP 438
Cdd:cd17964  141 AKAFTDLDYLVLDEADRLLDMGFRPDLEQILRH-------------LPEKNAD------------PRQTLLFSATV---P 192

                 ....*.
gi 154759257 439 EKLQQL 444
Cdd:cd17964  193 DEVQQI 198
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
209-449 2.12e-32

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: 124.62  E-value: 2.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAH-GISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIR---- 283
Cdd:cd17949    1 LVSHLKSKmGIEKPTAIQKLAIPVLLQ--------GR------DVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRsdgt 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 284 -ALVVLPTKELAQQVSKVFNIYTDATP-LRVSLVTGQKSLAKEQESLvqktadgyRCLADIVVATPGRLVDHIDQTPGFS 361
Cdd:cd17949   67 lALVLVPTRELALQIYEVLEKLLKPFHwIVPGYLIGGEKRKSEKARL--------RKGVNILIATPGRLLDHLKNTQSFD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 362 LQQLRFLIIDEADRMIDsMhqswlprvvaaAFQsEDPADPCALLQRRQAQAVTAAStcCPQMpLQKLLFSATLTQNPEKL 441
Cdd:cd17949  139 VSNLRWLVLDEADRLLD-M-----------GFE-KDITKILELLDDKRSKAGGEKS--KPSR-RQTVLVSATLTDGVKRL 202

                 ....*...
gi 154759257 442 QQLGLHQP 449
Cdd:cd17949  203 AGLSLKDP 210
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
206-608 2.31e-32

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 130.09  E-value: 2.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 206 HPDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLS------RVV 279
Cdd:PRK04837  16 HPQVVEALEKKGFHNCTPIQALALPLTLA--------GR------DVAGQAQTGTGKTMAFLTATFHYLLShpapedRKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 280 CHIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLvqktADGyrclADIVVATPGRLVDHIDQTPg 359
Cdd:PRK04837  82 NQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVL----ESG----VDILIGTTGRLIDYAKQNH- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 360 FSLQQLRFLIIDEADRMIDsmhqswlprvvaAAFQSedpaDPCALLQRrqaqavtaastcCPQmPLQKL--LFSATLT-- 435
Cdd:PRK04837 153 INLGAIQVVVLDEADRMFD------------LGFIK----DIRWLFRR------------MPP-ANQRLnmLFSATLSyr 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 436 ---------QNPEKLQQlglhQPrLFSTGlaHRGLEDTdgdgdsgkyafpvglthhYVPcSLSSKPLVVLHLVLEMGFSR 506
Cdd:PRK04837 204 vrelafehmNNPEYVEV----EP-EQKTG--HRIKEEL------------------FYP-SNEEKMRLLQTLIEEEWPDR 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 507 VLCFTNSRE-----------NSHRLFLLVQafggvDVAEfssrygpGQRRMILKQFEQGKIQLLISTDATARGIDVQGVE 575
Cdd:PRK04837 258 AIIFANTKHrceeiwghlaaDGHRVGLLTG-----DVAQ-------KKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
                        410       420       430
                 ....*....|....*....|....*....|...
gi 154759257 576 LVVNYDAPQYLRTYVHRVGRTARAGKTGQAFTL 608
Cdd:PRK04837 326 HVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
223-443 1.25e-31

DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 123.12  E-value: 1.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 223 PVQAAVIPALLesaacgflvgRGGYrpsDLCVSAPTGSGKTLAFVIPVVQALLSRV--------VCHIRALVVLPTKELA 294
Cdd:cd17946   15 PIQALALPAAI----------RDGK---DVIGAAETGSGKTLAFGIPILERLLSQKssngvggkQKPLRALILTPTRELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 295 QQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKtadgyrclADIVVATPGRLVDHIDQTPGF--SLQQLRFLIIDE 372
Cdd:cd17946   82 VQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKR--------PEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDE 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154759257 373 ADRMIDSMH----QSWLPRVvaaafqSEDPADPCallQRRQAqavtaastccpqmplqkLLFSATLT---QNPEKLQQ 443
Cdd:cd17946  154 ADRMLEKGHfaelEKILELL------NKDRAGKK---RKRQT-----------------FVFSATLTldhQLPLKLNS 205
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
207-449 6.42e-30

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: 117.30  E-value: 6.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 207 PDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSR--VVCH--- 281
Cdd:cd17961    3 PRLLKAIAKLGWEKPTLIQSKAIPLALE--------GK------DILARARTGSGKTAAYALPIIQKILKAkaESGEeqg 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 282 IRALVVLPTKELAQQVSKVFNIYTDATPLRVSLV--TGQKSlAKEQESLVqktadgyRCLADIVVATPGRLVDHIDQTPG 359
Cdd:cd17961   69 TRALILVPTRELAQQVSKVLEQLTAYCRKDVRVVnlSASSS-DSVQRALL-------AEKPDIVVSTPARLLSHLESGSL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 360 FSLQQLRFLIIDEADRMIdsmhqswlprvvaaAFQSEDpaDPCALLQrrqaqavtaastccpQMP--LQKLLFSATLTQN 437
Cdd:cd17961  141 LLLSTLKYLVIDEADLVL--------------SYGYEE--DLKSLLS---------------YLPknYQTFLMSATLSED 189
                        250
                 ....*....|..
gi 154759257 438 PEKLQQLGLHQP 449
Cdd:cd17961  190 VEALKKLVLHNP 201
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
223-444 4.60e-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: 115.28  E-value: 4.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 223 PVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLS---------RVVCHIRALVVLPTKEL 293
Cdd:cd17967   25 PVQKYAIPIILA--------GR------DLMACAQTGSGKTAAFLLPIISKLLEdgppsvgrgRRKAYPSALILAPTREL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 294 AQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQktadGyrclADIVVATPGRLVDHIDQtpGF-SLQQLRFLIIDE 372
Cdd:cd17967   91 AIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLR----G----CDILVATPGRLVDFIER--GRiSLSSIKFLVLDE 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154759257 373 ADRMIDsmhQSWLPRVvaaafqsedpadpcallqRRQAQavtaastcCPQMPL----QKLLFSATLtqnPEKLQQL 444
Cdd:cd17967  161 ADRMLD---MGFEPQI------------------RKIVE--------HPDMPPkgerQTLMFSATF---PREIQRL 204
PTZ00110 PTZ00110
helicase; Provisional
190-631 5.25e-28

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 118.72  E-value: 5.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 190 RNVTEDLVPIEDI--PDVhpdLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFV 267
Cdd:PTZ00110 123 ENVPKPVVSFEYTsfPDY---ILKSLKNAGFTEPTPIQVQGWPIALS--------GR------DMIGIAETGSGKTLAFL 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 268 IPVVqallsrvvCHIRA------------LVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKtadg 335
Cdd:PTZ00110 186 LPAI--------VHINAqpllrygdgpivLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRG---- 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 336 yrclADIVVATPGRLVDHIDQTPGfSLQQLRFLIIDEADRMIDSMHQSWLPRVVAaafqsedpadpcallQRRQAQavta 415
Cdd:PTZ00110 254 ----VEILIACPGRLIDFLESNVT-NLRRVTYLVLDEADRMLDMGFEPQIRKIVS---------------QIRPDR---- 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 416 astccpqmplQKLLFSATLTQNPEKL-QQLGLHQPRLFSTG----LAHRGLEdtdgdgdsgKYAFPVglTHHYVPCSLSS 490
Cdd:PTZ00110 310 ----------QTLMWSATWPKEVQSLaRDLCKEEPVHVNVGsldlTACHNIK---------QEVFVV--EEHEKRGKLKM 368
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 491 kplvVLHLVLEMGfSRVLCFTNSRENSHRLFLLVQaFGGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGID 570
Cdd:PTZ00110 369 ----LLQRIMRDG-DKILIFVETKKGADFLTKELR-LDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLD 442
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154759257 571 VQGVELVVNYDAPQYLRTYVHRVGRTARAGKTGQAFTLLLKVQ---ERRFLRMLTEAG---APELQR 631
Cdd:PTZ00110 443 VKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKyrlARDLVKVLREAKqpvPPELEK 509
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
210-452 7.43e-27

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: 108.22  E-value: 7.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 210 QKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQaLLSRVVCHIR----AL 285
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLE--------GR------DVLGAAKTGSGKTLAFLIPAIE-LLYKLKFKPRngtgVI 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 286 VVLPTKELAQQ---VSKVFNIYTDATplrVSLVTGQKSLAKEQESLVQKTadgyrclaDIVVATPGRLVDHIDQTPGFSL 362
Cdd:cd17942   67 IISPTRELALQiygVAKELLKYHSQT---FGIVIGGANRKAEAEKLGKGV--------NILVATPGRLLDHLQNTKGFLY 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 363 QQLRFLIIDEADRMI-----DSMHQ--SWLPRvvaaafqsedpadpcallqRRQAqavtaastccpqmplqkLLFSATLT 435
Cdd:cd17942  136 KNLQCLIIDEADRILeigfeEEMRQiiKLLPK-------------------RRQT-----------------MLFSATQT 179
                        250
                 ....*....|....*..
gi 154759257 436 QNPEKLQQLGLHQPRLF 452
Cdd:cd17942  180 RKVEDLARISLKKKPLY 196
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
223-449 1.04e-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: 108.56  E-value: 1.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 223 PVQAAVIPALLEsaacgflvgrggyrPSDLCVSAPTGSGKTLAFVIPVVQAL-----LSRVVCHI--RALVVLPTKELAQ 295
Cdd:cd17945   15 PIQRQAIPIGLQ--------------NRDIIGIAETGSGKTAAFLIPLLVYIsrlppLDEETKDDgpYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 296 QVSKVFNIYTDATPLR-VSLVTGQKslAKEQESLVQKTadgyrclADIVVATPGRLVDHIDQTPgFSLQQLRFLIIDEAD 374
Cdd:cd17945   81 QIEEETQKFAKPLGIRvVSIVGGHS--IEEQAFSLRNG-------CEILIATPGRLLDCLERRL-LVLNQCTYVVLDEAD 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 154759257 375 RMIDSMHQSWLPRVVAAAFQSEDPADPCALLQRRQAQAvtaastccpQMPLQKLLFSATLTQNPEKLQQLGLHQP 449
Cdd:cd17945  151 RMIDMGFEPQVTKILDAMPVSNKKPDTEEAEKLAASGK---------HRYRQTMMFTATMPPAVEKIAKGYLRRP 216
PTZ00424 PTZ00424
helicase 45; Provisional
256-609 2.10e-26

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 111.84  E-value: 2.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 256 APTGSGKTLAFVIPVVQaLLSRVVCHIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKTadg 335
Cdd:PTZ00424  72 AQSGTGKTATFVIAALQ-LIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGV--- 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 336 yrclaDIVVATPGRLVDHIDQTpGFSLQQLRFLIIDEADRMIDSMHQSWLPRVVaaafqsedpadpcallqRRQAQAVTA 415
Cdd:PTZ00424 148 -----HMVVGTPGRVYDMIDKR-HLRVDDLKLFILDEADEMLSRGFKGQIYDVF-----------------KKLPPDVQV 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 416 AstccpqmplqklLFSATLTQNPEKLQQLGLHQPRlfstglahRGLEDTDGDGDSGKYAFPVGLTHHyvpcSLSSKPLVV 495
Cdd:PTZ00424 205 A------------LFSATMPNEILELTTKFMRDPK--------RILVKKDELTLEGIRQFYVAVEKE----EWKFDTLCD 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 496 LHLVLEMGFSRVLCFTNSR------ENSHRLFLLVQAFGGVDVAEfssrygpgqRRMILKQFEQGKIQLLISTDATARGI 569
Cdd:PTZ00424 261 LYETLTITQAIIYCNTRRKvdyltkKMHERDFTVSCMHGDMDQKD---------RDLIMREFRSGSTRVLITTDLLARGI 331
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 154759257 570 DVQGVELVVNYDAPQYLRTYVHRVGRTARAGKTGQAFTLL 609
Cdd:PTZ00424 332 DVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFV 371
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
206-451 1.38e-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: 104.69  E-value: 1.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 206 HPDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRV-VCHIRA 284
Cdd:cd17959    9 SPPLLRAIKKKGYKVPTPIQRKTIPLILD--------GR------DVVAMARTGSGKTAAFLIPMIEKLKAHSpTVGARA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 285 LVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKtadgyrclADIVVATPGRLVDHIDQTpGFSLQQ 364
Cdd:cd17959   75 LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASN--------PDIIIATPGRLLHLLVEM-NLKLSS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 365 LRFLIIDEADRMIDSMHQSWLPRVVAaafqsedpadpcALLQRRQAqavtaastccpqmplqkLLFSATLtqnPEKLQQL 444
Cdd:cd17959  146 VEYVVFDEADRLFEMGFAEQLHEILS------------RLPENRQT-----------------LLFSATL---PKLLVEF 193
                        250
                 ....*....|
gi 154759257 445 ---GLHQPRL 451
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 ...
223-434 5.48e-25

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


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 103.17  E-value: 5.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 223 PVQAAVIPALLesaacgflvgrGGyrpSDLCVSAPTGSGKTLAFVIPVVQAllsrvvchIRALVVLPTKELAQQVS---K 299
Cdd:cd17938   24 DIQAEAIPLIL-----------GG---GDVLMAAETGSGKTGAFCLPVLQI--------VVALILEPSRELAEQTYnciE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 300 VFNIYTDATPLRVSLVTGQKSlAKEQESLVQKTADgyrcladIVVATPGRLVDHIdQTPGFSLQQLRFLIIDEADRMIDS 379
Cdd:cd17938   82 NFKKYLDNPKLRVALLIGGVK-AREQLKRLESGVD-------IVVGTPGRLEDLI-KTGKLDLSSVRFFVLDEADRLLSQ 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 154759257 380 MHQswlprvvaaafqsedpaDPCALLQRRQAQAVTAASTccpqmpLQKLLFSATL 434
Cdd:cd17938  153 GNL-----------------ETINRIYNRIPKITSDGKR------LQVIVCSATL 184
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
223-619 9.93e-25

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 109.17  E-value: 9.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 223 PVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPvvqaLLSRVVCHIRA---LVVLPTKELAQQVSK 299
Cdd:PRK11634  31 PIQAECIPHLLN--------GR------DVLGMAQTGSGKTAAFSLP----LLHNLDPELKApqiLVLAPTRELAVQVAE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 300 VFNIYTDATPlRVSLVtgqkSLAKEQESLVQKTAdgYRCLADIVVATPGRLVDHIDQTPgFSLQQLRFLIIDEADRMIds 379
Cdd:PRK11634  93 AMTDFSKHMR-GVNVV----ALYGGQRYDVQLRA--LRQGPQIVVGTPGRLLDHLKRGT-LDLSKLSGLVLDEADEML-- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 380 mhqswlprvvaaafqsedpadpcallqrrQAQAVTAASTCCPQMPL--QKLLFSATLTQNPEKLQQLGLHQP---RLFST 454
Cdd:PRK11634 163 -----------------------------RMGFIEDVETIMAQIPEghQTALFSATMPEAIRRITRRFMKEPqevRIQSS 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 455 glahrglEDTDGDgdsgkyafpvgLTHHYVPCSLSSKPLVVLHLVLEMGFSRVLCFTNSRENShrlfllvqafggVDVAE 534
Cdd:PRK11634 214 -------VTTRPD-----------ISQSYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNAT------------LEVAE 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 535 FSSRYG-----------PGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAGKTG 603
Cdd:PRK11634 264 ALERNGynsaalngdmnQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAG 343
                        410
                 ....*....|....*.
gi 154759257 604 QAFtLLLKVQERRFLR 619
Cdd:PRK11634 344 RAL-LFVENRERRLLR 358
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
490-600 1.08e-24

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: 98.82  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  490 SKPLVVLHLVLEMGFSRVLCFTNSRENSHRLFLLVQAfgGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGI 569
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEAELLLEKE--GIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 154759257  570 DVQGVELVVNYDAPQYLRTYVHRVGRTARAG 600
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
207-605 2.53e-24

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 107.18  E-value: 2.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 207 PDLQKQLRAHGISSYFPVQAAVIPALLesaacgflVGRggyrpsDLCVSAPTGSGKTLAFVIPVVqallSRVvCHIR--- 283
Cdd:PLN00206 130 PKLLLNLETAGYEFPTPIQMQAIPAAL--------SGR------SLLVSADTGSGKTASFLVPII----SRC-CTIRsgh 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 284 --------ALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKTadgyrclaDIVVATPGRLVDHID 355
Cdd:PLN00206 191 pseqrnplAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGV--------ELIVGTPGRLIDLLS 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 356 QTpGFSLQQLRFLIIDEADRMIDSmhqswlprvvaaAFqsedpadpcallqRRQA-QAVTAASTccPQMplqkLLFSATL 434
Cdd:PLN00206 263 KH-DIELDNVSVLVLDEVDCMLER------------GF-------------RDQVmQIFQALSQ--PQV----LLFSATV 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 435 TQNPEKLQQLGLHQPRLFSTGLAHRgledtdgdgdsgkyafPVGLTHHYVPCSLSSKPLVVLHLVLEmgfSR------VL 508
Cdd:PLN00206 311 SPEVEKFASSLAKDIILISIGNPNR----------------PNKAVKQLAIWVETKQKKQKLFDILK---SKqhfkppAV 371
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 509 CFTNSRENSHRLFLLVQAFGGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRT 588
Cdd:PLN00206 372 VFVSSRLGADLLANAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKE 451
                        410
                 ....*....|....*..
gi 154759257 589 YVHRVGRTARAGKTGQA 605
Cdd:PLN00206 452 YIHQIGRASRMGEKGTA 468
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
223-454 2.70e-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: 2.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 223 PVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIR--------ALVVLPTKELA 294
Cdd:cd18052   68 PVQKYAIPIILA--------GR------DLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSfsevqepqALIVAPTRELA 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 295 QQvskvfnIYTDA------TPLRVSLVTGQKSLAkEQESLVQKTADgyrcladIVVATPGRLVDHIDQTPgFSLQQLRFL 368
Cdd:cd18052  134 NQ------IFLEArkfsygTCIRPVVVYGGVSVG-HQIRQIEKGCH-------ILVATPGRLLDFIGRGK-ISLSKLKYL 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 369 IIDEADRMIDSMHQSWLPRVVAaafqsedpadpcallqrrqaqavtaastcCPQMPL----QKLLFSATLtqnPEKLQQL 444
Cdd:cd18052  199 ILDEADRMLDMGFGPEIRKLVS-----------------------------EPGMPSkedrQTLMFSATF---PEEIQRL 246
                        250
                 ....*....|...
gi 154759257 445 G---LHQPRLFST 454
Cdd:cd18052  247 AaefLKEDYLFLT 259
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
213-378 5.01e-24

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 100.90  E-value: 5.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 213 LRAHGISSYFPVQAAVIPALLesaacgflvgrggyRPSDLCVSAPTGSGKTLAFVIPVVQALLSR-VVC-----HIRALV 286
Cdd:cd17948    5 LQRQGITKPTTVQKQGIPSIL--------------RGRNTLCAAETGSGKTLTYLLPIIQRLLRYkLLAegpfnAPRGLV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 287 VLPTKELAQQVSKVFNIYTDATPLRVSLVTG----QKSLAKEQESlvqktadgyrclADIVVATPGRLV----DHIdqtp 358
Cdd:cd17948   71 ITPSRELAEQIGSVAQSLTEGLGLKVKVITGgrtkRQIRNPHFEE------------VDILVATPGALSklltSRI---- 134
                        170       180
                 ....*....|....*....|
gi 154759257 359 gFSLQQLRFLIIDEADRMID 378
Cdd:cd17948  135 -YSLEQLRHLVLDEADTLLD 153
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
213-378 2.24e-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: 95.91  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 213 LRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQallsrvvcHIR--------- 283
Cdd:cd17953   27 IKKLGYEKPTPIQAQALPAIMS--------GR------DVIGIAKTGSGKTLAFLLPMFR--------HIKdqrpvkpge 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 284 ---ALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLaKEQESLVQKTadgyrclADIVVATPGRLVDHIDQTPG- 359
Cdd:cd17953   85 gpiGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGI-SEQIAELKRG-------AEIVVCTPGRMIDILTANNGr 156
                        170       180
                 ....*....|....*....|
gi 154759257 360 -FSLQQLRFLIIDEADRMID 378
Cdd:cd17953  157 vTNLRRVTYVVLDEADRMFD 176
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
211-442 5.40e-22

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: 94.33  E-value: 5.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 211 KQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVV-QALLSRVVCHIR------ 283
Cdd:cd17951    3 KGLKKKGIKKPTPIQMQGLPTILS--------GR------DMIGIAFTGSGKTLVFTLPLImFALEQEKKLPFIkgegpy 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 284 ALVVLPTKELAQQVSKVFNIYTDA------TPLRVSLVTGQKSLaKEQESLVQKTADgyrcladIVVATPGRLVDHIdQT 357
Cdd:cd17951   69 GLIVCPSRELARQTHEVIEYYCKAlqeggyPQLRCLLCIGGMSV-KEQLEVIRKGVH-------IVVATPGRLMDML-NK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 358 PGFSLQQLRFLIIDEADRMIDSMHQSWLpRVVAAAFQSedpadpcallQRrqaqavtaastccpqmplQKLLFSATLtqn 437
Cdd:cd17951  140 KKINLDICRYLCLDEADRMIDMGFEEDI-RTIFSYFKG----------QR------------------QTLLFSATM--- 187

                 ....*
gi 154759257 438 PEKLQ 442
Cdd:cd17951  188 PKKIQ 192
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
209-449 8.69e-21

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


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 90.55  E-value: 8.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVV-----QALLSRVVCHIr 283
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALS--------GR------DMIGIAKTGSGKTAAFIWPMLvhimdQRELEKGEGPI- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 284 ALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLvqktadgyRCLADIVVATPGRLVDHIdQTPGFSLQ 363
Cdd:cd17952   66 AVIVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKAL--------QEGAEIVVATPGRLIDMV-KKKATNLQ 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 364 QLRFLIIDEADRMIDSMHQSWLPRVVAaafqsedpadpcallQRRQAQavtaastccpqmplQKLLFSATLTQNPEKLQQ 443
Cdd:cd17952  137 RVTYLVLDEADRMFDMGFEYQVRSIVG---------------HVRPDR--------------QTLLFSATFKKKIEQLAR 187

                 ....*.
gi 154759257 444 LGLHQP 449
Cdd:cd17952  188 DILSDP 193
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
200-609 1.67e-20

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: 96.44  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 200 EDIPD-VHPDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRV 278
Cdd:COG1205   35 APWPDwLPPELRAALKKRGIERLYSHQAEAIEAARA--------GK------NVVIATPTASGKSLAYLLPVLEALLEDP 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 279 VChiRALVVLPTKELAQ-QVSKvFNIYTDATPLRVSLVT-------GQKSLAKEQeslvqktadgyrclADIVVATP--- 347
Cdd:COG1205  101 GA--TALYLYPTKALARdQLRR-LRELAEALGLGVRVATydgdtppEERRWIREH--------------PDIVLTNPdml 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 348 --GRLVDHidqtPGFS--LQQLRFLIIDEAD--RMIDSMHQSWlprvvaaafqsedpadpcaLLQR--RQAQAVTAAstc 419
Cdd:COG1205  164 hyGLLPHH----TRWArfFRNLRYVVIDEAHtyRGVFGSHVAN-------------------VLRRlrRICRHYGSD--- 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 420 cPQMplqkLLFSATLtQNPEKLQQlglhqpRLFstglahrGLEDT--DGDGdsgkyaFPVGLTHH--YVPCSLSSKP--- 492
Cdd:COG1205  218 -PQF----ILASATI-GNPAEHAE------RLT-------GRPVTvvDEDG------SPRGERTFvlWNPPLVDDGIrrs 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 493 ------LVVLHLVLEmGFsRVLCFTNSRENSHRLFL-----LVQAFGGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLIS 561
Cdd:COG1205  273 alaeaaRLLADLVRE-GL-RTLVFTRSRRGAELLARyarraLREPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVS 350
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 154759257 562 TDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAGKTGQAFTLL 609
Cdd:COG1205  351 TNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVA 398
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
209-378 1.38e-19

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


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 87.42  E-value: 1.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVV-----QALLSRVVCHIr 283
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALS--------GR------DMVGIAQTGSGKTLAFLLPAIvhinaQPPLERGDGPI- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 284 ALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKtadgyrclADIVVATPGRLVDHIDQ--TPgfs 361
Cdd:cd17966   66 VLVLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRG--------VEICIATPGRLIDFLDQgkTN--- 134
                        170
                 ....*....|....*..
gi 154759257 362 LQQLRFLIIDEADRMID 378
Cdd:cd17966  135 LRRVTYLVLDEADRMLD 151
HELICc smart00490
helicase superfamily c-terminal domain;
529-600 2.66e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.64  E-value: 2.66e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 154759257   529 GVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAG 600
Cdd:smart00490  11 GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
211-422 1.01e-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: 84.90  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 211 KQLRAHGISSYFPVQAAVIPALlesaacgflvgrggYRPSDLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIRA-----L 285
Cdd:cd17944    3 KLLQARGVTYLFPIQVKTFHPV--------------YSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGrapkvL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 286 VVLPTKELAQQVSKVFNIYTdaTPLRVSLVTGQKSLakeqeslvQKTADGYRCLADIVVATPGRLVDHIdQTPGFSLQQL 365
Cdd:cd17944   69 VLAPTRELANQVTKDFKDIT--RKLSVACFYGGTPY--------QQQIFAIRNGIDILVGTPGRIKDHL-QNGRLDLTKL 137
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 154759257 366 RFLIIDEADRMIDSMHQSWLPRVVAAAFQSEDPADPCALLqrrqaqavtaASTCCPQ 422
Cdd:cd17944  138 KHVVLDEVDQMLDMGFAEQVEEILSVSYKKDSEDNPQTLL----------FSATCPD 184
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
206-433 1.54e-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: 84.16  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 206 HPDLQKQLRAHGISSYFPVQAAVIPALLESAacgflvgrggyrPSDLCVSAPTGSGKTLAFVIpvvqALLSRVVCHIR-- 283
Cdd:cd17963    2 KPELLKGLYAMGFNKPSKIQETALPLILSDP------------PENLIAQSQSGTGKTAAFVL----AMLSRVDPTLKsp 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 284 -ALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQktadgyrcladIVVATPGRLVDHIdQTPGFSL 362
Cdd:cd17963   66 qALCLAPTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKITAQ-----------IVIGTPGTVLDWL-KKRQLDL 133
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154759257 363 QQLRFLIIDEADRMIDSMHQswlprvvaaafqsedpADPCALLQRrqaqAVTaastccpqMPLQKLLFSAT 433
Cdd:cd17963  134 KKIKILVLDEADVMLDTQGH----------------GDQSIRIKR----MLP--------RNCQILLFSAT 176
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
211-382 1.01e-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: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 211 KQLRAHGISSYFPVQAAVIPallesaacgflVGRGGYrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVcHIRALVVLPT 290
Cdd:cd17943    3 EGLKAAGFQRPSPIQLAAIP-----------LGLAGH---DLIVQAKSGTGKTLVFVVIALESLDLERR-HPQVLILAPT 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 291 KELAQQVSKVF-NIYTDATPLRVSLVTGQKSLAKEQESLVQktadgyrclADIVVATPGRLVdHIDQTPGFSLQQLRFLI 369
Cdd:cd17943   68 REIAVQIHDVFkKIGKKLEGLKCEVFIGGTPVKEDKKKLKG---------CHIAVGTPGRIK-QLIELGALNVSHVRLFV 137
                        170
                 ....*....|...
gi 154759257 370 IDEADRMIDSMHQ 382
Cdd:cd17943  138 LDEADKLMEGSFQ 150
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
251-379 1.38e-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: 81.60  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 251 DLCVSAPTGSGKTLAFVIPVVQALlSRVVCHIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQ 330
Cdd:cd17939   36 DVIAQAQSGTGKTATFSIGALQRI-DTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQY 114
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 154759257 331 KTadgyrclaDIVVATPGRLVDHIdQTPGFSLQQLRFLIIDEADRMIDS 379
Cdd:cd17939  115 GP--------HIVVGTPGRVFDML-QRRSLRTDKIKMFVLDEADEMLSR 154
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
254-385 1.97e-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: 79.37  E-value: 1.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 254 VSAPTGSGKTLAFVIPVVQALLSRvvcHIRALVVLPTKELAQQVSKVFNIYTDAtPLRVSLVTGQKSlAKEQESLVQKta 333
Cdd:cd00046    6 ITAPTGSGKTLAALLAALLLLLKK---GKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSS-AEEREKNKLG-- 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154759257 334 dgyrcLADIVVATPGRLVDHIDQTPGFSLQQLRFLIIDEADRMIDSMHQSWL 385
Cdd:cd00046   79 -----DADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALI 125
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
207-378 2.55e-17

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: 80.80  E-value: 2.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 207 PDLQKQLRAHGISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRVVcHIRALV 286
Cdd:cd17940    8 RELLMGIFEKGFEKPSPIQEESIPIALS--------GR------DILARAKNGTGKTGAYLIPILEKIDPKKD-VIQALI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 287 VLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKTadgyrclaDIVVATPGRLVDHIDQTPGfSLQQLR 366
Cdd:cd17940   73 LVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTV--------HVLVGTPGRILDLAKKGVA-DLSHCK 143
                        170
                 ....*....|..
gi 154759257 367 FLIIDEADRMID 378
Cdd:cd17940  144 TLVLDEADKLLS 155
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
251-437 1.49e-15

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: 75.84  E-value: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 251 DLCVSAPTGSGKTLAFVIPVVQALlSRVVCHIRALVVLPTKELAQQVSKVFNIYTDATP-LRVSLVTGQKSLAKEQESLV 329
Cdd:cd17950   41 DVLCQAKSGMGKTAVFVLSTLQQL-EPVDGQVSVLVICHTRELAFQISNEYERFSKYMPnVKTAVFFGGVPIKKDIEVLK 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 330 QKTADgyrcladIVVATPGRLVDHIDQTpGFSLQQLRFLIIDEADRMIDSmhqswlprvvaaafqsedpadpcaLLQRRQ 409
Cdd:cd17950  120 NKCPH-------IVVGTPGRILALVREK-KLKLSHVKHFVLDECDKMLEQ------------------------LDMRRD 167
                        170       180       190
                 ....*....|....*....|....*....|
gi 154759257 410 AQAVTAAStccpqmPLQK--LLFSATLTQN 437
Cdd:cd17950  168 VQEIFRAT------PHDKqvMMFSATLSKE 191
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
223-386 5.98e-15

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: 75.11  E-value: 5.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 223 PVQAAVIPALLESAACGFLVGRGGY--RPSDLCVSAPTGSGKTLAFVIPVVQAL----------------LSRVVCHIRA 284
Cdd:cd17965   33 PIQTLAIKKLLKTLMRKVTKQTSNEepKLEVFLLAAETGSGKTLAYLAPLLDYLkrqeqepfeeaeeeyeSAKDTGRPRS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 285 LVVLPTKELAQQVSKVFNIYTDATPLRVslvtgqKSLAKEQESLVQKTADGYRCLADIVVATPGRLVDhIDQTPGFSLQQ 364
Cdd:cd17965  113 VILVPTHELVEQVYSVLKKLSHTVKLGI------KTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLAS-LAKSRPKILSR 185
                        170       180
                 ....*....|....*....|..
gi 154759257 365 LRFLIIDEADRMIDsmhQSWLP 386
Cdd:cd17965  186 VTHLVVDEADTLFD---RSFLQ 204
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
204-666 6.03e-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: 6.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 204 DVHPDLQKQLRAHgissyfpvQAAVIPALLESAAcgflvgRGGYRpsdLCVSAPTGSGKTLAFVipvvqALLSRVVCHIR 283
Cdd:COG1061   72 DEASGTSFELRPY--------QQEALEALLAALE------RGGGR---GLVVAPTGTGKTVLAL-----ALAAELLRGKR 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 284 ALVVLPTKELAQQVSKVFniytdatpLRVSLVTGQKSLAKEQEslvqktadgyrclADIVVATPGRLV--DHIDQTPG-F 360
Cdd:COG1061  130 VLVLVPRRELLEQWAEEL--------RRFLGDPLAGGGKKDSD-------------APITVATYQSLArrAHLDELGDrF 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 361 SLqqlrfLIIDEAdrmidsmHqswlpRVVAAAFQsedpadpcALLQRRQAQAVtaastccpqmplqkLLFSATltqnPEK 440
Cdd:COG1061  189 GL-----VIIDEA-------H-----HAGAPSYR--------RILEAFPAAYR--------------LGLTAT----PFR 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 441 LQqlGLHQPRLFSTGLAHR-GLED----------------TDGDGDSGKY-AFPVGLTHHYVPCSlSSKPLVVLHLVLEM 502
Cdd:COG1061  226 SD--GREILLFLFDGIVYEySLKEaiedgylappeyygirVDLTDERAEYdALSERLREALAADA-ERKDKILRELLREH 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 503 G-FSRVLCFTNSRENSHRlflLVQAFG--GVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVN 579
Cdd:COG1061  303 PdDRKTLVFCSSVDHAEA---LAELLNeaGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 580 YDAPQYLRTYVHRVGRTARAGKTGQAFTLLLKVQERRFlrmLTEAGAPELQRHELSSKLLQPLVPRYEEALSQLEESVKE 659
Cdd:COG1061  380 LRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGNDVP---VLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALE 456

                 ....*..
gi 154759257 660 ERKQRAA 666
Cdd:COG1061  457 VKGELEE 463
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
254-373 8.92e-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: 8.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 254 VSAPTGSGKTLAFVIPVVQALLSRVvcHIRALVVLPTKELAQ-QVSKV--FNIYTDAtPLRVSLVTGQKSLAKEQeslvq 330
Cdd:cd17923   20 VTTGTASGKSLCYQLPILEALLRDP--GSRALYLYPTKALAQdQLRSLreLLEQLGL-GIRVATYDGDTPREERR----- 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 154759257 331 ktaDGYRCLADIVVATPGRL---VDHIDQTPGFSLQQLRFLIIDEA 373
Cdd:cd17923   92 ---AIIRNPPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA 134
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
251-389 2.25e-14

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: 73.12  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 251 DLCVSAPTGSGKTLAFVIPVV-----QALLSR---VVChiraLVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLA 322
Cdd:cd18049   63 DMVGVAQTGSGKTLSYLLPAIvhinhQPFLERgdgPIC----LVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKG 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154759257 323 KEQESLVQKTadgyrclaDIVVATPGRLVDHIDQTPGfSLQQLRFLIIDEADRMIDSMHQSWLPRVV 389
Cdd:cd18049  139 PQIRDLERGV--------EICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIV 196
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
223-378 3.62e-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: 72.77  E-value: 3.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 223 PVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPVVQAL---------------LSRVVCHIRALVV 287
Cdd:cd18051   46 PVQKHAIPIIKS--------KR------DLMACAQTGSGKTAAFLLPILSQIyeqgpgeslpsesgyYGRRKQYPLALVL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 288 LPTKELAQQvskvfnIYTDA------TPLRVSLVTGQKSLAKEQESLVQKtadgyrClaDIVVATPGRLVDHIDQTPgFS 361
Cdd:cd18051  112 APTRELASQ------IYDEArkfayrSRVRPCVVYGGADIGQQMRDLERG------C--HLLVATPGRLVDMLERGK-IG 176
                        170
                 ....*....|....*..
gi 154759257 362 LQQLRFLIIDEADRMID 378
Cdd:cd18051  177 LDYCKYLVLDEADRMLD 193
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
254-379 6.25e-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: 70.37  E-value: 6.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 254 VSAPTGSGKTLAFVIPVVQALLSrvvCHIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESlvqkta 333
Cdd:cd17921   22 VSAPTSSGKTLIAELAILRALAT---SGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVNKLLLA------ 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 154759257 334 dgyrcLADIVVATPGRLVDHIDQTPGFSLQQLRFLIIDEADRMIDS 379
Cdd:cd17921   93 -----EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIGDG 133
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
209-378 6.32e-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: 70.96  E-value: 6.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAHGISSYFPVQAAVIPALLESaacgflvgrggyrpSDLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIR----- 283
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQG--------------IDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQrngpg 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 284 ALVVLPTKELAQQVSKVFNIYTdATPLRVSLVTGQKSLAKEQESLVQKtadgyrclADIVVATPGRLVDhIDQTPGFSLQ 363
Cdd:cd17958   67 VLVLTPTRELALQIEAECSKYS-YKGLKSVCVYGGGNRNEQIEDLSKG--------VDIIIATPGRLND-LQMNNVINLK 136
                        170
                 ....*....|....*
gi 154759257 364 QLRFLIIDEADRMID 378
Cdd:cd17958  137 SITYLVLDEADRMLD 151
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
251-389 1.88e-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: 71.20  E-value: 1.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 251 DLCVSAPTGSGKTLAFVIPVV-----QALLSR---VVChiraLVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLA 322
Cdd:cd18050  101 DMVGIAQTGSGKTLAYLLPAIvhinhQPYLERgdgPIC----LVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKG 176
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154759257 323 KEQESLVQKTadgyrclaDIVVATPGRLVDHIdQTPGFSLQQLRFLIIDEADRMIDSMHQSWLPRVV 389
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 ...
209-453 2.19e-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: 69.11  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAHGISSYFPVQAAVIPALLesaacgflVGRggyrpsDLCVSAPTGSGKTLAFVIPVVqallSRVVCHIR---AL 285
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGL--------LGR------DILASADTGSGKTAAFLLPVI----IRCLTEHRnpsAL 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 286 VVLPTKELAQQVSKVFNIYTDATP-LRVSLVTGQKSLAKEQESLVQKTadgyrclaDIVVATPGRLVDHIDQTpGFSLQQ 364
Cdd:cd17962   63 ILTPTRELAVQIEDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGV--------KVIIATPGRLLDILKQS-SVELDN 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 365 LRFLIIDEADRMIDSMHQSWLPRVVAAAfqsedPADPcallqrrqaqavtaastccpqmplQKLLFSATLTQNPEKLQQL 444
Cdd:cd17962  134 IKIVVVDEADTMLKMGFQQQVLDILENI-----SHDH------------------------QTILVSATIPRGIEQLAGQ 184

                 ....*....
gi 154759257 445 GLHQPRLFS 453
Cdd:cd17962  185 LLQNPVRIT 193
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
251-377 6.61e-13

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: 67.86  E-value: 6.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 251 DLCVSAPTGSGKTLAFVIPVVQALLSRVVcHIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLvq 330
Cdd:cd18046   38 DVIAQAQSGTGKTATFSISILQQIDTSLK-ATQALVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKL-- 114
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 154759257 331 ktadgyRCLADIVVATPGRLVDHIDQTpGFSLQQLRFLIIDEADRMI 377
Cdd:cd18046  115 ------QAGPHIVVGTPGRVFDMINRR-YLRTDYIKMFVLDEADEML 154
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
199-379 3.69e-12

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 69.15  E-value: 3.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 199 IEDIPDVHpdLQKQLRAHGISSYFPVQAAVIPALLESAACgflvgrggyrpsdLCVSAPTGSGKTLAFVIPVVQALLSrv 278
Cdd:COG1204    3 VAELPLEK--VIEFLKERGIEELYPPQAEALEAGLLEGKN-------------LVVSAPTASGKTLIAELAILKALLN-- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 279 vcHIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGqkslakEQESLVQKTADgyrclADIVVATPGRLVDHIDQTP 358
Cdd:COG1204   66 --GGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTG------DYDSDDEWLGR-----YDILVATPEKLDSLLRNGP 132
                        170       180
                 ....*....|....*....|.
gi 154759257 359 GFsLQQLRFLIIDEAdRMIDS 379
Cdd:COG1204  133 SW-LRDVDLVVVDEA-HLIDD 151
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
251-377 1.99e-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: 60.94  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 251 DLCVSAPTGSGKTLAFVIPVVQALlSRVVCHIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEqeslVQ 330
Cdd:cd18045   38 DVIAQSQSGTGKTATFSISVLQCL-DIQVRETQALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDD----IR 112
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 154759257 331 KTADGYRcladIVVATPGRLVDHIdQTPGFSLQQLRFLIIDEADRMI 377
Cdd:cd18045  113 KLDYGQH----IVSGTPGRVFDMI-RRRSLRTRHIKMLVLDEADEML 154
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
488-611 3.07e-10

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 63.21  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 488 LSSKPLVVLHLVLEM----GFSRVLCFTNSRENSHrlfLLVQAFG--GVDVAEF---SSRYGPG-----QRRMILKQFEQ 553
Cdd:COG1111  333 EHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAE---MIVEFLSepGIKAGRFvgqASKEGDKgltqkEQIEILERFRA 409
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 154759257 554 GKIQLLISTDATARGIDVQGVELVVNYDA-PQYLRtYVHRVGRTARAGKtGQAFTLLLK 611
Cdd:COG1111  410 GEFNVLVATSVAEEGLDIPEVDLVIFYEPvPSEIR-SIQRKGRTGRKRE-GRVVVLIAK 466
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
505-609 3.08e-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: 3.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 505 SRVLCFTNSRENSHRLF-LLVQAFGGVDVAEF----SSRYGPGQRRM----ILKQFEQGKIQLLISTDATARGIDVQGVE 575
Cdd:cd18801   31 TRVIIFSEFRDSAEEIVnFLSKIRPGIRATRFigqaSGKSSKGMSQKeqkeVIEQFRKGGYNVLVATSIGEEGLDIGEVD 110
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 154759257 576 LVVNYDA-PQYLRTyVHRVGRTARaGKTGQAFTLL 609
Cdd:cd18801  111 LIICYDAsPSPIRM-IQRMGRTGR-KRQGRVVVLL 143
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
543-599 2.70e-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: 52.98  E-value: 2.70e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 154759257 543 QRRM--ILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRtARA 599
Cdd:cd18802   76 QRKQkeTLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
555-608 1.07e-07

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: 49.62  E-value: 1.07e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 154759257 555 KIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAGKT-GQAFTL 608
Cdd:cd18785   22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDeGEVILF 76
ResIII pfam04851
Type III restriction enzyme, res subunit;
222-382 5.50e-07

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 49.98  E-value: 5.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  222 FPVQAAVIPALLESaacgFLVGRGGYrpsdlCVSAPTGSGKTL--AFVIpvvqALLSRVVCHIRALVVLPTKELAQQVSK 299
Cdd:pfam04851   5 RPYQIEAIENLLES----IKNGQKRG-----LIVMATGSGKTLtaAKLI----ARLFKKGPIKKVLFLVPRKDLLEQALE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  300 VFNIYTDATPLRVSLVTGQKSLAKEQESlvqktadgyrclaDIVVATPGRL-VDHIDQTPGFSLQQLRFLIIDEADRMID 378
Cdd:pfam04851  72 EFKKFLPNYVEIGEIISGDKKDESVDDN-------------KIVVTTIQSLyKALELASLELLPDFFDVIIIDEAHRSGA 138

                  ....
gi 154759257  379 SMHQ 382
Cdd:pfam04851 139 SSYR 142
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
254-379 6.30e-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: 50.40  E-value: 6.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 254 VSAPTGSGKT-LAFVIPVVQALLSRvvchiRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSL-AKEQESLVQK 331
Cdd:cd17924   37 IIAPTGVGKTtFGLATSLYLASKGK-----RSYLIFPTKSLVKQAYERLSKYAEKAGVEVKILVYHSRLkKKEKEELLEK 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 154759257 332 TADGYrclADIVVATPGRLVDHIDQTPGFSLQqlrFLIIDEADRMIDS 379
Cdd:cd17924  112 IEKGD---FDILVTTNQFLSKNFDLLSNKKFD---FVFVDDVDAVLKS 153
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
253-373 1.50e-06

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 48.07  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 253 CVSAPTGSGKTLafvipvVQALLSRVVCHIRALVVLPTKELAQQVSKVFNIYTDATPLrvslvtgqkslaKEQESLVQKT 332
Cdd:cd17926   22 ILVLPTGSGKTL------TALALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSI------------GLIGGGKKKD 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 154759257 333 ADGyrclADIVVATPgRLVDHIDQTPGFSLQQLRFLIIDEA 373
Cdd:cd17926   84 FDD----ANVVVATY-QSLSNLAEEEKDLFDQFGLLIVDEA 119
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
254-373 1.65e-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: 49.19  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 254 VSAPTGSGKTLafvipvVQALLSRVVCHI---------RALVVLPTKELAQQVSKVFNIYtdaTPLRVSLVTGQKSLAKE 324
Cdd:cd18034   21 VVLPTGSGKTL------IAVMLIKEMGELnrkeknpkkRAVFLVPTVPLVAQQAEAIRSH---TDLKVGEYSGEMGVDKW 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 154759257 325 QESLVQKTADGYrclaDIVVATPGRLVDHIDQtpGF-SLQQLRFLIIDEA 373
Cdd:cd18034   92 TKERWKEELEKY----DVLVMTAQILLDALRH--GFlSLSDINLLIFDEC 135
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
254-375 1.67e-06

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 49.35  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 254 VSAPTGSGKTLAFVIpVVQALLSRVVCHIRALVVL--PTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQK 331
Cdd:cd17927   22 ICLPTGSGKTFVAVL-ICEHHLKKFPAGRKGKVVFlaNKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENVSVEQIVES 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 154759257 332 tadgyrclADIVVATPGRLVDHIDQTPGFSLQQLRFLIIDEADR 375
Cdd:cd17927  101 --------SDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
205-388 2.21e-06

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: 48.95  E-value: 2.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 205 VHPDLQKQLRAHGISSYFPVQAAVIPALLESAacgflvgrggyrPSDLCVSAPTGSGKTLAFVIpvvqALLSRV--VCH- 281
Cdd:cd18047    8 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEP------------PQNLIAQSQSGTGKTAAFVL----AMLSQVepANKy 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 282 IRALVVLPTKELAQQVSKVFNIYTDATPlRVSLVTGQKSLAKEQeslvqktadGYRCLADIVVATPGRLVDHIDQTPGFS 361
Cdd:cd18047   72 PQCLCLSPTYELALQTGKVIEQMGKFYP-ELKLAYAVRGNKLER---------GQKISEQIVIGTPGTVLDWCSKLKFID 141
                        170       180
                 ....*....|....*....|....*...
gi 154759257 362 LQQLRFLIIDEADRMIDSM-HQSWLPRV 388
Cdd:cd18047  142 PKKIKVFVLDEADVMIATQgHQDQSIRI 169
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
506-601 4.33e-06

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 46.87  E-value: 4.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 506 RVLCFTNSRENSHRLFLLVQAfGGVDVAEFSSR-------YGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVV 578
Cdd:cd18797   37 KTIVFCRSRKLAELLLRYLKA-RLVEEGPLASKvasyragYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVV 115
                         90       100
                 ....*....|....*....|...
gi 154759257 579 NYDAPQYLRTYVHRVGRTARAGK 601
Cdd:cd18797  116 LAGYPGSLASLWQQAGRAGRRGK 138
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
222-381 6.32e-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: 46.94  E-value: 6.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 222 FPVQAAVIPAllesaacGFLVGRggyrpsDLCVSAPTGSGKTLAFVIpvvqALLSRVVCHIRALVVLPTKELAQQVSKVF 301
Cdd:cd18028    3 YPPQAEAVRA-------GLLKGE------NLLISIPTASGKTLIAEM----AMVNTLLEGGKALYLVPLRALASEKYEEF 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 302 NIYtDATPLRVSLVTGQkslakeqeslvQKTADGYRCLADIVVATPGRLVDHIDQTPGFsLQQLRFLIIDEAdRMIDSMH 381
Cdd:cd18028   66 KKL-EEIGLKVGISTGD-----------YDEDDEWLGDYDIIVATYEKFDSLLRHSPSW-LRDVGVVVVDEI-HLISDEE 131
PRK13766 PRK13766
Hef nuclease; Provisional
505-611 9.65e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 48.72  E-value: 9.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 505 SRVLCFTNSRENSHRL--FLLVQafgGVDVAEF---SSRY---GPGQRRMI--LKQFEQGKIQLLISTDATARGIDVQGV 574
Cdd:PRK13766 366 SRIIVFTQYRDTAEKIvdLLEKE---GIKAVRFvgqASKDgdkGMSQKEQIeiLDKFRAGEFNVLVSTSVAEEGLDIPSV 442
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 154759257 575 ELVVNYDA-PQYLRTyVHRVGRTARaGKTGQAFTLLLK 611
Cdd:PRK13766 443 DLVIFYEPvPSEIRS-IQRKGRTGR-QEEGRVVVLIAK 478
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
540-601 9.65e-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: 45.66  E-value: 9.65e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 154759257 540 GPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAGK 601
Cdd:cd18794   65 EPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGL 126
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
251-372 1.95e-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: 45.27  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 251 DLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIRALVVLPTKELAQQVSKVFNIYTDA--TPLRVSLVTGQKSLAKEQESL 328
Cdd:cd17922    3 NVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEidLEIPVAVRHGDTSQSEKAKQL 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 154759257 329 VQktadgyrcLADIVVATPGRLVDHIDQTPGFS-LQQLRFLIIDE 372
Cdd:cd17922   83 KN--------PPGILITTPESLELLLVNKKLRElFAGLRYVVVDE 119
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
78-149 1.16e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 44.97  E-value: 1.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154759257  78 DAEPGSPEAPQGKRRKADGEDAGAES--NEEAPGEPSAGSSEEAPGEP--SAGSSEEAPGERSTSASAEAAPDGPA 149
Cdd:PRK13108 370 DIEREQPGDLAGQAPAAHQVDAEAASaaPEEPAALASEAHDETEPEVPekAAPIPDPAKPDELAVAGPGDDPAEPD 445
PHA03169 PHA03169
hypothetical protein; Provisional
79-156 1.34e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.96  E-value: 1.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154759257  79 AEPGSPEAPQGKRRKADGEDAGAESNEEAPGEPSAGSSEEAPGEPSAGSSEEAPGERSTSASAEAAPDGPALEEAAGP 156
Cdd:PHA03169 115 ASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGP 192
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
224-372 1.72e-04

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 43.11  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 224 VQAAVIPALLESAacgflvgrggyrpSDLCVSAPTGSGKTLAFVIPVVQALLSRVVC---HIRALVVLPTKELAQQVskv 300
Cdd:cd18023    5 IQSEVFPDLLYSD-------------KNFVVSAPTGSGKTVLFELAILRLLKERNPLpwgNRKVVYIAPIKALCSEK--- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 301 fniYTDATP------LRVSLVTGQKSLAKEQEslVQKtadgyrclADIVVATPGR--LVDHIDQTPGFSLQQLRFLIIDE 372
Cdd:cd18023   69 ---YDDWKEkfgplgLSCAELTGDTEMDDTFE--IQD--------ADIILTTPEKwdSMTRRWRDNGNLVQLVALVLIDE 135
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
249-332 1.78e-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: 42.79  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 249 PSDLCVSAPTGSGKTLAFVIPVVQALLSrvvcHIRALVVLPTKELAQQVSKVFNIYTdaTPLRVSLVT-GQKSLAKEQES 327
Cdd:cd17918   36 PMDRLLSGDVGSGKTLVALGAALLAYKN----GKQVAILVPTEILAHQHYEEARKFL--PFINVELVTgGTKAQILSGIS 109

                 ....*
gi 154759257 328 LVQKT 332
Cdd:cd17918  110 LLVGT 114
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
217-373 1.99e-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: 42.91  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 217 GISSYFPVQAAVIPALLEsaacgflvGRggyrpsDLCVSAPTGSGKTLAFVIPvvqALLSRVVChiraLVVLPTKELAQ- 295
Cdd:cd17920    9 GYDEFRPGQLEAINAVLA--------GR------DVLVVMPTGGGKSLCYQLP---ALLLDGVT----LVVSPLISLMQd 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 296 QVSKVfniytDATPLRVSLVTGQKSlAKEQESLVQKTADGyrcLADIVVATPGRLvdhidQTPGF--SLQQLR------F 367
Cdd:cd17920   68 QVDRL-----QQLGIRAAALNSTLS-PEEKREVLLRIKNG---QYKLLYVTPERL-----LSPDFleLLQRLPerkrlaL 133

                 ....*.
gi 154759257 368 LIIDEA 373
Cdd:cd17920  134 IVVDEA 139
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
50-181 2.11e-04

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 43.99  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  50 EPAQTEAAASTEPATRRRRRPRRRRRVNDAEPGSPEAPQGKRRKADGEDAGAESNEEAPGEPSAGSSEEAPGEPSAGSSE 129
Cdd:NF040712 213 RPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAA 292
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154759257 130 EAPgerstsASAEAAPDGPALEEAAGPLVPGLVLGGFGKRKAPKvqPFLPRW 181
Cdd:NF040712 293 EPP------APAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRR--ASVPSW 336
PRK00254 PRK00254
ski2-like helicase; Provisional
209-317 2.96e-04

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 44.04  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 209 LQKQLRAHGISSYFPVQAavipallESAACGFLVGRggyrpsDLCVSAPTGSGKTLAFVIPVVQALLSRvvcHIRALVVL 288
Cdd:PRK00254  12 IKRVLKERGIEELYPPQA-------EALKSGVLEGK------NLVLAIPTASGKTLVAEIVMVNKLLRE---GGKAVYLV 75
                         90       100
                 ....*....|....*....|....*....
gi 154759257 289 PTKELAQQVSKVFNIYtDATPLRVSLVTG 317
Cdd:PRK00254  76 PLKALAEEKYREFKDW-EKLGLRVAMTTG 103
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
217-372 4.95e-04

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: 41.97  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 217 GISSYFPVQAAVIPALLESaacgflvgrggyrPSDLCVSAPTGSGKTLAFVIPVVQAL-------LSRVVCHIRALVVLP 289
Cdd:cd18019   14 GFKSLNRIQSKLFPAAFET-------------DENLLLCAPTGAGKTNVALLTILREIgkhrnpdGTINLDAFKIVYIAP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 290 TKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQktadgyrcladIVVATPGRLvDHIDQTPGF-SLQQL-RF 367
Cdd:cd18019   81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQ-----------IIVTTPEKW-DIITRKSGDrTYTQLvRL 148

                 ....*
gi 154759257 368 LIIDE 372
Cdd:cd18019  149 IIIDE 153
PHA03325 PHA03325
nuclear-egress-membrane-like protein; Provisional
33-161 7.12e-04

nuclear-egress-membrane-like protein; Provisional


Pssm-ID: 223044  Cd Length: 418  Bit Score: 42.56  E-value: 7.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  33 ALLERLQSRARERQQQREPAQTEAAASTEPATR--RRRRPRRRRRVNDAEPGSPE-APQGKRRKADGEDAGAESNEEAPG 109
Cdd:PHA03325 262 FMLNSSLPTSAPKRRSRRAGAMRAAAGETADLAddDGSEHSDPEPLPASLPPPPVrRPRVKHPEAGKEEPDGARNAEAKE 341
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 154759257 110 EPSAGSSEEAPGEPSAGSSEEAPGER-STSASAEAAPDGPALEEAAGPLVPGL 161
Cdd:PHA03325 342 PAQPATSTSSKGSSSAQNKDSGSTGPgSSLAAASSFLEDDDFGSPPLDLTTSL 394
DEXHc_TRCF cd17991
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ...
206-375 1.49e-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: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 206 HPDLQKQLRAHGISSYFPVQAAVIPALLESAACGflvgrggyRPSDLCVSAPTGSGKT-LAfvipvVQALLSRVVCHIRA 284
Cdd:cd17991    1 DGEEQEEFEASFPYEETPDQLKAIEEILKDMESG--------KPMDRLICGDVGFGKTeVA-----MRAAFKAVLSGKQV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 285 LVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSlAKEQESLVQKTADGYrclADIVVATpGRLVdhidqTPGFSLQQ 364
Cdd:cd17991   68 AVLVPTTLLAQQHYETFKERFANFPVNVELLSRFTT-AAEQREILEGLKEGK---VDIVIGT-HRLL-----SKDVEFKN 137
                        170
                 ....*....|.
gi 154759257 365 LRFLIIDEADR 375
Cdd:cd17991  138 LGLLIIDEEQR 148
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
488-594 2.21e-03

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 38.61  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 488 LSSKPLVVLHLVLEMGFS--RVLCFTNSRENshrLFLLVQAFG--GVDVAEFSSRYGPGQRRMILKQF--EQGKIQLLIS 561
Cdd:cd18793    9 VSGKLEALLELLEELREPgeKVLIFSQFTDT---LDILEEALRerGIKYLRLDGSTSSKERQKLVDRFneDPDIRVFLLS 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 154759257 562 TDATARGIDVQGVELVVNYDA---PQYL-----RtyVHRVG 594
Cdd:cd18793   86 TKAGGVGLNLTAANRVILYDPwwnPAVEeqaidR--AHRIG 124
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
507-601 2.87e-03

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: 38.78  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 507 VLCFTNSRENSHRLF-LLVQAFGGVDVAEFS----SRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYD 581
Cdd:cd18796   41 TLVFTNTRSQAERLAqRLRELCPDRVPPDFIalhhGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
                         90       100
                 ....*....|....*....|
gi 154759257 582 APQYLRTYVHRVGRTARAGK 601
Cdd:cd18796  121 SPKSVARLLQRLGRSGHRPG 140
AIF-MLS pfam14962
Mitochondria localization Sequence; This family contains a protein found in eukaryotes. ...
76-148 2.92e-03

Mitochondria localization Sequence; This family contains a protein found in eukaryotes. Proteins in this family are typically between 240 and 613 amino acids in length. The family is found in association with pfam07992. This protein family is an N-terminal domain for the mitochondrial localization sequence for an apoptosis-inducing factor. The protein is also known as Corneal endothelium-specific protein 1 or as Ovary-specific acidic protein. It is thought to be important for membrane function and is expressed in the ovary and corneal endothelium.


Pssm-ID: 464407 [Multi-domain]  Cd Length: 192  Bit Score: 39.43  E-value: 2.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154759257   76 VNDAEPGSPEAPQGKRRKADGEDAgaesnEEAPGEPsAGSSEEAPgePSAGSSEEAPGErSTSASAEAAPDGP 148
Cdd:pfam14962  99 VAEAEKASSEAPEVSVVEAEVVDA-----EEIPDAT-AAVIEEAS--ACPGDVEAAPVE-TTAVGAETGPEVT 162
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
529-649 4.47e-03

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 40.12  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 529 GVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAGKTGQAfTL 608
Cdd:COG0514  254 GIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEA-LL 332
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 154759257 609 LLKVQERRFLRMLTEAGAPELQRHELSSKLLQPLVpRYEEA 649
Cdd:COG0514  333 LYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAML-AYAET 372
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
33-160 4.72e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  33 ALLERLQSRARERQQQREPAQTeAAASTEPATRRRRRPRRRRRVNDAEPGSPEAPQGKRRKADG-----EDAGAESNEEA 107
Cdd:PRK12323 432 ALAAARQASARGPGGAPAPAPA-PAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDdpppwEELPPEFASPA 510
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 154759257 108 PGEPSAGSSEEAPGEPSAGSSEEAPGERSTSASAEAAPDGPALEEAAGPLVPG 160
Cdd:PRK12323 511 PAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAP 563
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
529-634 5.11e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 40.08  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 529 GVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAGKTGQAFTL 608
Cdd:PRK11057 260 GISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
                         90       100
                 ....*....|....*....|....*....
gi 154759257 609 LLKVQERRFLRMLTEAGAPELQ---RHEL 634
Cdd:PRK11057 340 YDPADMAWLRRCLEEKPAGQQQdieRHKL 368
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
50-156 6.31e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 39.58  E-value: 6.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  50 EPAQTEAAASTEPATRRRRRPRRRRRVNDAEPGSPEAPQGKRRKADGEDAGAESNEEAPGEPSAGSSEEAP------GEP 123
Cdd:PRK13108 297 EREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSeadierEQP 376
                         90       100       110
                 ....*....|....*....|....*....|...
gi 154759257 124 SAGSSEEAPGERSTSASAEAAPDGPALEEAAGP 156
Cdd:PRK13108 377 GDLAGQAPAAHQVDAEAASAAPEEPAALASEAH 409
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
529-598 6.85e-03

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: 38.05  E-value: 6.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154759257 529 GVDVAEFSSRygpgqRRMILKQFEQGKIQLLISTdATARGIDVQGVEL------VVNYDAPqyLRTYVHRVGRTAR 598
Cdd:cd18798   51 GIKAELALSS-----TEKNLEKFEEGEIDVLIGV-ASYYGVLVRGIDLperikyAIFYGVP--VTTYIQASGRTSR 118
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
33-156 7.35e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 7.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257  33 ALLERLQSR------------ARERQQQREPAQTEAAASTEPATRRRRRPRRRrrvNDAEPGSPEAPQGKRRKADGEDAG 100
Cdd:PRK07764 376 ARLERLERRlgvaggagapaaAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAA---PQPAPAPAPAPAPPSPAGNAPAGG 452
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 154759257 101 AESNEEAPGEPSAGSSEEAPGEPSAGSSEEAPGERSTSASAEAAPDGPALEEAAGP 156
Cdd:PRK07764 453 APSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADD 508
PRK13766 PRK13766
Hef nuclease; Provisional
252-375 7.50e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 39.47  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 252 LCVsAPTGSGKTlAFVIPVVQALLSRVVChiRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQEsLVQK 331
Cdd:PRK13766  33 LVV-LPTGLGKT-AIALLVIAERLHKKGG--KVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKRAE-LWEK 107
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 154759257 332 tadgyrclADIVVATP---------GRLvdhidqtpgfSLQQLRFLIIDEADR 375
Cdd:PRK13766 108 --------AKVIVATPqviendliaGRI----------SLEDVSLLIFDEAHR 142
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
539-606 9.04e-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: 38.38  E-value: 9.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759257 539 YGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDA------PQY---LRTY--VHRV-GRTARAGKTGQAF 606
Cdd:cd18804  128 RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNAdsglnsPDFrasERAFqlLTQVsGRAGRGDKPGKVI 207
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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