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Conserved domains on  [gi|392895997|ref|NP_001254980|]
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putative ATP-dependent RNA helicase DDX55 homolog [Caenorhabditis elegans]

Protein Classification

DDX55/SPB4 family DEAD/DEAH box RNA helicase( domain architecture ID 13028873)

DDX55/SPB4 family DEAD/DEAH box containing ATP-dependent RNA helicase catalyzes the unwinding of RNA, similar to ATP-dependent rRNA helicase SPB4 that is involved in the biogenesis of 60S ribosomal subunits

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
21-219 6.77e-90

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: 275.61  E-value: 6.77e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  21 LLEVFDK-SYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAK--LQPADIGALILSPSRELCSQIV 97
Cdd:cd17960    1 ILDVVAElGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKanLKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  98 SVIQPFAEK--LNLTVETVTGGQKVDKNIKMFKNKNVNILVATPGRLFQIIQHEKTliARKMRTLQLLVIDEADRFNEIQ 175
Cdd:cd17960   81 EVLQSFLEHhlPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKAD--KVKVKSLEVLVLDEADRLLDLG 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392895997 176 FEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVK 219
Cdd:cd17960  159 FEADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
232-363 1.01e-40

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: 143.80  E-value: 1.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 232 LKNYYVECRADEKTSVCL-EFIRQRTDKKILIFFPSCNSVRYFYKIFERClgKRPLFAVHGKCSNPHRASQIKAFSDSTN 310
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEEL--GIKVAALHGDLSQEERERALKKFRSGKV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392895997 311 GVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTARCGREGNALILI 363
Cdd:cd18787   79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
399-457 9.50e-14

Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many helicase proteins.


:

Pssm-ID: 464056 [Multi-domain]  Cd Length: 59  Bit Score: 65.88  E-value: 9.50e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392895997  399 RQKMIKIQVSDRAILEAGTRAFVSHVESYAKHDCHLICSLDDLNVVGLANSYALLRLPK 457
Cdd:pfam13959   1 QLQLEKLVLKDRELKELAQKAFVSYVRAYSKHLAKSIFNVKKLDLGHLAKSFGLLRAPK 59
PTZ00121 super family cl31754
MAEBL; Provisional
378-576 8.28e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 8.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  378 EKVKLDEIKVPTNNSRKSEELRQKM----IKIQVSDRAILEAGTRAFVSHVESYAKHDchlicslddlnvvGLANSYALL 453
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAeeakKKADAAKKKAEEAKKAAEAAKAEAEAAAD-------------EAEAAEEKA 1366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  454 RLPKMRELSQRKDLDMFDRSAIETSEIKYADVKLEANRETV--MKEKHEKKVETLAAKDKKRREKEARKLKKMGGRFRNG 531
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392895997  532 GGTGRKAEEKKA---LKRKAEEEDDAQNDIRLLKRIKRGKLSKKEIKD 576
Cdd:PTZ00121 1447 DEAKKKAEEAKKaeeAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
 
Name Accession Description Interval E-value
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
21-219 6.77e-90

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: 275.61  E-value: 6.77e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  21 LLEVFDK-SYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAK--LQPADIGALILSPSRELCSQIV 97
Cdd:cd17960    1 ILDVVAElGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKanLKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  98 SVIQPFAEK--LNLTVETVTGGQKVDKNIKMFKNKNVNILVATPGRLFQIIQHEKTliARKMRTLQLLVIDEADRFNEIQ 175
Cdd:cd17960   81 EVLQSFLEHhlPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKAD--KVKVKSLEVLVLDEADRLLDLG 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392895997 176 FEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVK 219
Cdd:cd17960  159 FEADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
12-406 2.03e-85

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 272.02  E-value: 2.03e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  12 TFRE-KLGPELLE-VFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKlqPADIGALILSPS 89
Cdd:COG0513    3 SFADlGLSPPLLKaLAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR--PRAPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  90 RELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLFQIIQHeKTLiarKMRTLQLLVIDEAD 169
Cdd:COG0513   81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALK-RGVDIVVATPGRLLDLIER-GAL---DLSGVETLVLDEAD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 170 RFNEIQFEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVKVAQErnSAAPSTLKNYYVECRADEKTSVCL 249
Cdd:COG0513  156 RMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPE--NATAETIEQRYYLVDKRDKLELLR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 250 EFIRQRTDKKILIFfpsCNSVRYFYKIFERcLGKRPLFAV--HGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISD 327
Cdd:COG0513  234 RLLRDEDPERAIVF---CNTKRGADRLAEK-LQKRGISAAalHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDD 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392895997 328 IDWVIQFDLPKHSSWFVHRAGRTARCGREGNALILIASEQLAYVNFLDNHEKVKLDEIKVPTNNSRKSEELRQKMIKIQ 406
Cdd:COG0513  310 VSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIK 388
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
33-207 9.99e-47

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: 161.26  E-value: 9.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   33 TDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMmrmIQNAKLQPADIGALILSPSRELCSQIVSVIQPFAEKLNLTVE 112
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPA---LEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  113 TVTGGQKVDKNIKmfKNKNVNILVATPGRLFQIIQHEKTLiarkmRTLQLLVIDEADRFNEIQFEDHMREILSCIPKQRR 192
Cdd:pfam00270  78 SLLGGDSRKEQLE--KLKGPDILVGTPGRLLDLLQERKLL-----KNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQ 150
                         170
                  ....*....|....*
gi 392895997  193 TGLFSATQVKEEDDL 207
Cdd:pfam00270 151 ILLLSATLPRNLEDL 165
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
17-408 2.95e-46

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 168.83  E-value: 2.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  17 LGPELLEVFDK-SYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMrmiqnAKLQPA--DIGALILSPSRELC 93
Cdd:PRK11776  11 LPPALLANLNElGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLL-----QKLDVKrfRVQALVLCPTRELA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  94 SQIVSVIQPFAEKL-NLTVETVTGGQKVDKNIKMFKNkNVNILVATPGRlfqIIQHEK--TLiarKMRTLQLLVIDEADR 170
Cdd:PRK11776  86 DQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEH-GAHIIVGTPGR---ILDHLRkgTL---DLDALNTLVLDEADR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 171 FNEIQFEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVKVAQErnsAAPSTLKNYYVECRADEKTSVCLE 250
Cdd:PRK11776 159 MLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVEST---HDLPAIEQRFYEVSPDERLPALQR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 251 FIRQRTDKKILIFfpsCNSVRYFYKIFERCLGKRplF---AVHGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISD 327
Cdd:PRK11776 236 LLLHHQPESCVVF---CNTKKECQEVADALNAQG--FsalALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKA 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 328 IDWVIQFDLPKHSSWFVHRAGRTARCGREGNALILIASEQLAYVNFLDNHEKVKLDEIKVPTNNSRKSEELRQKMIKIQV 407
Cdd:PRK11776 311 LEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTLCI 390

                 .
gi 392895997 408 S 408
Cdd:PRK11776 391 D 391
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
232-363 1.01e-40

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: 143.80  E-value: 1.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 232 LKNYYVECRADEKTSVCL-EFIRQRTDKKILIFFPSCNSVRYFYKIFERClgKRPLFAVHGKCSNPHRASQIKAFSDSTN 310
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEEL--GIKVAALHGDLSQEERERALKKFRSGKV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392895997 311 GVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTARCGREGNALILI 363
Cdd:cd18787   79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
24-220 3.06e-35

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 131.46  E-value: 3.06e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997    24 VFDKSYKSFTDVQVLSGTHLL-NLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPAdigaLILSPSRELCSQIVSVIQP 102
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLsGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV----LVLVPTRELAEQWAEELKK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   103 FAEKLNLTVETVTGGQKVDKNIKMFKNKNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEADRFNEIQFEDHMRE 182
Cdd:smart00487  77 LGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKL----SLSNVDLVILDEAHRLLDGGFGDQLEK 152
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 392895997   183 ILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVKV 220
Cdd:smart00487 153 LLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV 190
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
243-354 9.20e-23

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: 93.04  E-value: 9.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  243 EKTSVCLEFIRQRTDKKILIFFPSCNSVRYfyKIFERCLGKRPLfAVHGKCSNPHRASQIKAFSDSTNGVMISTDVMARG 322
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEA--ELLLEKEGIKVA-RLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 392895997  323 IDISDIDWVIQFDLPKHSSWFVHRAGRTARCG 354
Cdd:pfam00271  78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
275-354 1.39e-16

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 74.56  E-value: 1.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   275 KIFERCLGKRPL--FAVHGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTAR 352
Cdd:smart00490   1 EELAELLKELGIkvARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 392895997   353 CG 354
Cdd:smart00490  81 AG 82
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
399-457 9.50e-14

Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many helicase proteins.


Pssm-ID: 464056 [Multi-domain]  Cd Length: 59  Bit Score: 65.88  E-value: 9.50e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392895997  399 RQKMIKIQVSDRAILEAGTRAFVSHVESYAKHDCHLICSLDDLNVVGLANSYALLRLPK 457
Cdd:pfam13959   1 QLQLEKLVLKDRELKELAQKAFVSYVRAYSKHLAKSIFNVKKLDLGHLAKSFGLLRAPK 59
DEXH_lig_assoc TIGR04121
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ...
54-167 4.18e-05

DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.


Pssm-ID: 274994 [Multi-domain]  Cd Length: 804  Bit Score: 46.39  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   54 PTGSGKTLAFVLP-MMRMIQNAKLQPADIGALILSPSRELCSQIVSVIQPFAEKLNL--TVETVTGGQKVDKNIKMFKNK 130
Cdd:TIGR04121  36 PTGSGKTLAGFLPsLIDLAGPEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGLpiRVETRTGDTSSSERARQRKKP 115
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392895997  131 nVNILVATPGRLFQIIQHEKTliARKMRTLQLLVIDE 167
Cdd:TIGR04121 116 -PDILLTTPESLALLLSYPDA--ARLFKDLRCVVVDE 149
PTZ00121 PTZ00121
MAEBL; Provisional
378-576 8.28e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 8.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  378 EKVKLDEIKVPTNNSRKSEELRQKM----IKIQVSDRAILEAGTRAFVSHVESYAKHDchlicslddlnvvGLANSYALL 453
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAeeakKKADAAKKKAEEAKKAAEAAKAEAEAAAD-------------EAEAAEEKA 1366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  454 RLPKMRELSQRKDLDMFDRSAIETSEIKYADVKLEANRETV--MKEKHEKKVETLAAKDKKRREKEARKLKKMGGRFRNG 531
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392895997  532 GGTGRKAEEKKA---LKRKAEEEDDAQNDIRLLKRIKRGKLSKKEIKD 576
Cdd:PTZ00121 1447 DEAKKKAEEAKKaeeAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
302-573 1.14e-03

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 42.02  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 302 IKAFSDSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTARcGREGNALILIA----------------- 364
Cdd:COG1111  404 LERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVVVLIAkgtrdeayywssrrkek 482
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 365 ---------SEQLAYVNFLDNHEKVK--LDEIKVPTN------NSRKSEELRQKMIKIQVSDRAILEAGTRafVSHvESY 427
Cdd:COG1111  483 kmksilkklKKLLDKQEKEKLKESAQatLDEFESIKElaedeiNEKDLDEIESSENGAHVDWREPVLLQVI--VST-LAE 559
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 428 AKHDCHLICSLDDLNVVGLA-----NSYALLRLPKMRELSQRKDLDMFDRSAIETSEIKYADVKLEAnrETVMKEKHEKK 502
Cdd:COG1111  560 SLELRELGEKVDDEVNLILEidrvdVVDDGSVLRVSRLLVEIGELDGKTRVIIASYGDEYFDAILRL--TSKIKLPSLVS 637
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392895997 503 VETLAAKDKKRREKEARKLKKMGGRFRnGGGTGRKAEEKKALKRKAEEEDDAQNDIRLLKRIKRGKLSKKE 573
Cdd:COG1111  638 DISVDIPDLPIVEIVGEAVLCKKEDGS-REARFIKKERDLKGIRLAEGETLNDPLIELLRQQLYGEALREE 707
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
253-329 3.39e-03

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 40.24  E-value: 3.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392895997 253 RQRTDKKILIFFPSCNSVRYFYKIFERCLGKRPLFAVHgkCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISDID 329
Cdd:COG4098  315 RLKEGRQLLIFVPTIELLEQLVALLQKLFPEERIAGVH--AEDPERKEKVQAFRDGEIPILVTTTILERGVTFPNVD 389
 
Name Accession Description Interval E-value
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
21-219 6.77e-90

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: 275.61  E-value: 6.77e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  21 LLEVFDK-SYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAK--LQPADIGALILSPSRELCSQIV 97
Cdd:cd17960    1 ILDVVAElGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKanLKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  98 SVIQPFAEK--LNLTVETVTGGQKVDKNIKMFKNKNVNILVATPGRLFQIIQHEKTliARKMRTLQLLVIDEADRFNEIQ 175
Cdd:cd17960   81 EVLQSFLEHhlPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKAD--KVKVKSLEVLVLDEADRLLDLG 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392895997 176 FEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVK 219
Cdd:cd17960  159 FEADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
12-406 2.03e-85

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 272.02  E-value: 2.03e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  12 TFRE-KLGPELLE-VFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKlqPADIGALILSPS 89
Cdd:COG0513    3 SFADlGLSPPLLKaLAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR--PRAPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  90 RELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLFQIIQHeKTLiarKMRTLQLLVIDEAD 169
Cdd:COG0513   81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALK-RGVDIVVATPGRLLDLIER-GAL---DLSGVETLVLDEAD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 170 RFNEIQFEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVKVAQErnSAAPSTLKNYYVECRADEKTSVCL 249
Cdd:COG0513  156 RMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPE--NATAETIEQRYYLVDKRDKLELLR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 250 EFIRQRTDKKILIFfpsCNSVRYFYKIFERcLGKRPLFAV--HGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISD 327
Cdd:COG0513  234 RLLRDEDPERAIVF---CNTKRGADRLAEK-LQKRGISAAalHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDD 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392895997 328 IDWVIQFDLPKHSSWFVHRAGRTARCGREGNALILIASEQLAYVNFLDNHEKVKLDEIKVPTNNSRKSEELRQKMIKIQ 406
Cdd:COG0513  310 VSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIK 388
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
21-199 1.83e-52

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: 177.63  E-value: 1.83e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  21 LLEVFDKS-YKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPM-MRMIQNAKLQPADIGALILSPSRELCSQIVS 98
Cdd:cd00268    1 LLKALKKLgFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPIlEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  99 VIQPFAEKLNLTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLFQIIQhEKTLiarKMRTLQLLVIDEADRFNEIQFED 178
Cdd:cd00268   81 VARKLGKGTGLKVAAIYGGAPIKKQIEALK-KGPDIVVGTPGRLLDLIE-RGKL---DLSNVKYLVLDEADRMLDMGFEE 155
                        170       180
                 ....*....|....*....|.
gi 392895997 179 HMREILSCIPKQRRTGLFSAT 199
Cdd:cd00268  156 DVEKILSALPKDRQTLLFSAT 176
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
33-207 9.99e-47

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: 161.26  E-value: 9.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   33 TDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMmrmIQNAKLQPADIGALILSPSRELCSQIVSVIQPFAEKLNLTVE 112
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPA---LEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  113 TVTGGQKVDKNIKmfKNKNVNILVATPGRLFQIIQHEKTLiarkmRTLQLLVIDEADRFNEIQFEDHMREILSCIPKQRR 192
Cdd:pfam00270  78 SLLGGDSRKEQLE--KLKGPDILVGTPGRLLDLLQERKLL-----KNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQ 150
                         170
                  ....*....|....*
gi 392895997  193 TGLFSATQVKEEDDL 207
Cdd:pfam00270 151 ILLLSATLPRNLEDL 165
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
17-408 2.95e-46

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 168.83  E-value: 2.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  17 LGPELLEVFDK-SYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMrmiqnAKLQPA--DIGALILSPSRELC 93
Cdd:PRK11776  11 LPPALLANLNElGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLL-----QKLDVKrfRVQALVLCPTRELA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  94 SQIVSVIQPFAEKL-NLTVETVTGGQKVDKNIKMFKNkNVNILVATPGRlfqIIQHEK--TLiarKMRTLQLLVIDEADR 170
Cdd:PRK11776  86 DQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEH-GAHIIVGTPGR---ILDHLRkgTL---DLDALNTLVLDEADR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 171 FNEIQFEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVKVAQErnsAAPSTLKNYYVECRADEKTSVCLE 250
Cdd:PRK11776 159 MLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVEST---HDLPAIEQRFYEVSPDERLPALQR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 251 FIRQRTDKKILIFfpsCNSVRYFYKIFERCLGKRplF---AVHGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISD 327
Cdd:PRK11776 236 LLLHHQPESCVVF---CNTKKECQEVADALNAQG--FsalALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKA 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 328 IDWVIQFDLPKHSSWFVHRAGRTARCGREGNALILIASEQLAYVNFLDNHEKVKLDEIKVPTNNSRKSEELRQKMIKIQV 407
Cdd:PRK11776 311 LEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTLCI 390

                 .
gi 392895997 408 S 408
Cdd:PRK11776 391 D 391
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
11-363 5.56e-45

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 164.73  E-value: 5.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  11 KTFRE-KLGPELLEVF-DKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQN---AKLQPADIgaLI 85
Cdd:PRK11192   1 TTFSElELDESLLEALqDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDfprRKSGPPRI--LI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  86 LSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFkNKNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVI 165
Cdd:PRK11192  79 LTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVF-SENQDIVVATPGRLLQYIKEENF----DCRAVETLIL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 166 DEADRFNEIQFEDHMREILSCIPKQRRTGLFSATQvkEEDDLMVFGLRNAKQ-VKVaqernSAAPST------LKNYYve 238
Cdd:PRK11192 154 DEADRMLDMGFAQDIETIAAETRWRKQTLLFSATL--EGDAVQDFAERLLNDpVEV-----EAEPSRrerkkiHQWYY-- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 239 cRADE---KTSVCLEFIRQRTDKKILIFFPSCNSVRYFYKIFERClGKRPLFaVHGKCSNPHRASQIKAFSDSTNGVMIS 315
Cdd:PRK11192 225 -RADDlehKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKA-GINCCY-LEGEMVQAKRNEAIKRLTDGRVNVLVA 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 392895997 316 TDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTARCGREGNALILI 363
Cdd:PRK11192 302 TDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLV 349
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
29-214 5.61e-43

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: 152.51  E-value: 5.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  29 YKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPAD-IGALILSPSRELCSQIVSVIQPFAEKL 107
Cdd:cd17942   10 FTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNgTGVIIISPTRELALQIYGVAKELLKYH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 108 NLTVETVTGGQKvdKNIKMFK-NKNVNILVATPGRLFQIIQHEKTLIarkMRTLQLLVIDEADRFNEIQFEDHMREILSC 186
Cdd:cd17942   90 SQTFGIVIGGAN--RKAEAEKlGKGVNILVATPGRLLDHLQNTKGFL---YKNLQCLIIDEADRILEIGFEEEMRQIIKL 164
                        170       180
                 ....*....|....*....|....*...
gi 392895997 187 IPKQRRTGLFSATQVKEEDDLMVFGLRN 214
Cdd:cd17942  165 LPKRRQTMLFSATQTRKVEDLARISLKK 192
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
232-363 1.01e-40

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: 143.80  E-value: 1.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 232 LKNYYVECRADEKTSVCL-EFIRQRTDKKILIFFPSCNSVRYFYKIFERClgKRPLFAVHGKCSNPHRASQIKAFSDSTN 310
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEEL--GIKVAALHGDLSQEERERALKKFRSGKV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392895997 311 GVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTARCGREGNALILI 363
Cdd:cd18787   79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
17-363 2.54e-39

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 149.57  E-value: 2.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  17 LGPELLE-VFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPAD---IGALILSPSREL 92
Cdd:PRK10590   8 LSPDILRaVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGrrpVRALILTPTREL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  93 CSQIVSVIQPFAEKLNLTVETVTGGqkVDKNIKMFKNKN-VNILVATPGRLFQIiQHEKtliARKMRTLQLLVIDEADRF 171
Cdd:PRK10590  88 AAQIGENVRDYSKYLNIRSLVVFGG--VSINPQMMKLRGgVDVLVATPGRLLDL-EHQN---AVKLDQVEILVLDEADRM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 172 NEIQFEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVKVAQeRNSAAPSTLKN-YYVECRadEKTSVCLE 250
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVAR-RNTASEQVTQHvHFVDKK--RKRELLSQ 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 251 FIRQRTDKKILIFFPSCNSVRYFYKIFERClGKRPLfAVHGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISDIDW 330
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKD-GIRSA-AIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPH 316
                        330       340       350
                 ....*....|....*....|....*....|...
gi 392895997 331 VIQFDLPKHSSWFVHRAGRTARCGREGNALILI 363
Cdd:PRK10590 317 VVNYELPNVPEDYVHRIGRTGRAAATGEALSLV 349
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
5-370 4.47e-39

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 149.29  E-value: 4.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   5 VGPVALKT-FRE-KLGPELLE-VFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQP--- 78
Cdd:PRK01297  80 VEPQEGKTrFHDfNLAPELMHaIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKery 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  79 -ADIGALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFKNKNVNILVATPGRLFQIIQHEKTliarKM 157
Cdd:PRK01297 160 mGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARFCDILVATPGRLLDFNQRGEV----HL 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 158 RTLQLLVIDEADRFNEIQFEDHMREILSCIPK--QRRTGLFSATQVkeeDDLMVFglrnAKQ-------VKVAQErNSAA 228
Cdd:PRK01297 236 DMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFT---DDVMNL----AKQwttdpaiVEIEPE-NVAS 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 229 PSTLKNYYVECRADeKTSVCLEFIRQRTDKKILIFFPSCNSVRyfyKIFERcLGKRPLFA--VHGKCSNPHRASQIKAFS 306
Cdd:PRK01297 308 DTVEQHVYAVAGSD-KYKLLYNLVTQNPWERVMVFANRKDEVR---RIEER-LVKDGINAaqLSGDVPQHKRIKTLEGFR 382
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392895997 307 DSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTARCGREGNAlILIASEQLAY 370
Cdd:PRK01297 383 EGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVS-ISFAGEDDAF 445
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
26-220 1.45e-38

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: 140.50  E-value: 1.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  26 DKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPAD-IGALILSPSRELCSQIVSVIQPFA 104
Cdd:cd17941    7 EAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDgLGALIISPTRELAMQIFEVLRKVG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 105 EKLNLTVETVTGGqkvdKNIKMFKNK--NVNILVATPGRLFQIIQHEKTLIARkmrTLQLLVIDEADRFNEIQFEDHMRE 182
Cdd:cd17941   87 KYHSFSAGLIIGG----KDVKEEKERinRMNILVCTPGRLLQHMDETPGFDTS---NLQMLVLDEADRILDMGFKETLDA 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895997 183 ILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVKV 220
Cdd:cd17941  160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
17-219 4.55e-38

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: 139.36  E-value: 4.55e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  17 LGPELLE-VFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMmrmIQNAKLQPADIG--ALILSPSRELC 93
Cdd:cd17959    8 LSPPLLRaIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPM---IEKLKAHSPTVGarALILSPTRELA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  94 SQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFKNkNVNILVATPGRLFQIIQhEKTLiarKMRTLQLLVIDEADRFNE 173
Cdd:cd17959   85 LQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALAS-NPDIIIATPGRLLHLLV-EMNL---KLSSVEYVVFDEADRLFE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 392895997 174 IQFEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVK 219
Cdd:cd17959  160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
PTZ00110 PTZ00110
helicase; Provisional
33-360 8.84e-38

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 146.84  E-value: 8.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  33 TDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIqNAK--LQPADiG--ALILSPSRELCSQIVSVIQPFAEKLN 108
Cdd:PTZ00110 154 TPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI-NAQplLRYGD-GpiVLVLAPTRELAEQIREQCNKFGASSK 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 109 LTVETVTGGqkVDKNIKMFKNKN-VNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEADRFNEIQFEDHMREILSCI 187
Cdd:PTZ00110 232 IRNTVAYGG--VPKRGQIYALRRgVEILIACPGRLIDFLESNVT----NLRRVTYLVLDEADRMLDMGFEPQIRKIVSQI 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 188 PKQRRTGLFSATQVKEEDDLMVFGLRNAK-QVKVAQERNSAAPSTLKNYYVeCRADEKTSVCLEFIRQ--RTDKKILIFF 264
Cdd:PTZ00110 306 RPDRQTLMWSATWPKEVQSLARDLCKEEPvHVNVGSLDLTACHNIKQEVFV-VEEHEKRGKLKMLLQRimRDGDKILIFV 384
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 265 PSCNSVRYFYKifERCLGKRPLFAVHGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFV 344
Cdd:PTZ00110 385 ETKKGADFLTK--ELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYV 462
                        330
                 ....*....|....*.
gi 392895997 345 HRAGRTARCGREGNAL 360
Cdd:PTZ00110 463 HRIGRTGRAGAKGASY 478
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
33-369 1.20e-37

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 147.02  E-value: 1.20e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  33 TDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMM-RMIQNAKL---QPADIGALILSPSRELCSQIVSVIQPFAEKLN 108
Cdd:PRK04537  33 TPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMnRLLSRPALadrKPEDPRALILAPTRELAIQIHKDAVKFGADLG 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 109 LTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLFQIIQHEKTLiarKMRTLQLLVIDEADRFNEIQFEDHMREILSCIP 188
Cdd:PRK04537 113 LRFALVYGGVDYDKQRELLQ-QGVDVIIATPGRLIDYVKQHKVV---SLHACEICVLDEADRMFDLGFIKDIRFLLRRMP 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 189 KQ--RRTGLFSATQVKEEDDLMVFGLRNAKQVKVAQERNSAAPSTLKNYYVEcrADEKTSVCLEFIRQRTDKKILIFFPS 266
Cdd:PRK04537 189 ERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPA--DEEKQTLLLGLLSRSEGARTMVFVNT 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 267 CNSVRYFYKIFERClGKRpLFAVHGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHR 346
Cdd:PRK04537 267 KAFVERVARTLERH-GYR-VGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHR 344
                        330       340
                 ....*....|....*....|...
gi 392895997 347 AGRTARCGREGNAlILIASEQLA 369
Cdd:PRK04537 345 IGRTARLGEEGDA-ISFACERYA 366
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
29-199 4.51e-37

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: 136.94  E-value: 4.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  29 YKSFTDVQVLSGTHLLNL-SDVVVESPTGSGKTLAFVLPMM-RMIQ-NAKLQPADIGALILSPSRELCSQIVSVIQPFAE 105
Cdd:cd17964   14 FETMTPVQQKTLKPILSTgDDVLARAKTGTGKTLAFLLPAIqSLLNtKPAGRRSGVSALIISPTRELALQIAAEAKKLLQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 106 KL-NLTVETVTGGQKVDKNIKMFKNKNVNILVATPGRLFQIIqhEKTLIARKMRTLQLLVIDEADRFNEIQFEDHMREIL 184
Cdd:cd17964   94 GLrKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHL--ENPGVAKAFTDLDYLVLDEADRLLDMGFRPDLEQIL 171
                        170
                 ....*....|....*....
gi 392895997 185 SCIPK----QRRTGLFSAT 199
Cdd:cd17964  172 RHLPEknadPRQTLLFSAT 190
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
29-199 1.69e-35

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: 132.35  E-value: 1.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  29 YKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMmrmIQNAKLQPADIGALILSPSRELCSQIVSVIQPFAEKLN 108
Cdd:cd17955   19 IKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPI---LQRLSEDPYGIFALVLTPTRELAYQIAEQFRALGAPLG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 109 LTVETVTGGQKVDKNIKMFKNKNvNILVATPGRLFQIIQHEKTLIARKMRtLQLLVIDEADRFNEIQFEDHMREILSCIP 188
Cdd:cd17955   96 LRCCVIVGGMDMVKQALELSKRP-HIVVATPGRLADHLRSSDDTTKVLSR-VKFLVLDEADRLLTGSFEDDLATILSALP 173
                        170
                 ....*....|.
gi 392895997 189 KQRRTGLFSAT 199
Cdd:cd17955  174 PKRQTLLFSAT 184
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
12-221 2.25e-35

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: 131.67  E-value: 2.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  12 TFREkLG--PELLEVFDK-SYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNaklQPADIGALILSP 88
Cdd:cd17954    1 TFKE-LGvcEELCEACEKlGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLE---NPQRFFALVLAP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  89 SRELCSQIVSVIQPFAEKLNLTVETVTGG-QKVDKNIKMFKNKNVniLVATPGRLFQIIQHEKTLiarKMRTLQLLVIDE 167
Cdd:cd17954   77 TRELAQQISEQFEALGSSIGLKSAVLVGGmDMMAQAIALAKKPHV--IVATPGRLVDHLENTKGF---SLKSLKFLVMDE 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392895997 168 ADRFNEIQFEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAkqVKVA 221
Cdd:cd17954  152 ADRLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP--VKIE 203
DEXDc smart00487
DEAD-like helicases superfamily;
24-220 3.06e-35

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 131.46  E-value: 3.06e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997    24 VFDKSYKSFTDVQVLSGTHLL-NLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPAdigaLILSPSRELCSQIVSVIQP 102
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLsGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV----LVLVPTRELAEQWAEELKK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   103 FAEKLNLTVETVTGGQKVDKNIKMFKNKNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEADRFNEIQFEDHMRE 182
Cdd:smart00487  77 LGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKL----SLSNVDLVILDEAHRLLDGGFGDQLEK 152
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 392895997   183 ILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVKV 220
Cdd:smart00487 153 LLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV 190
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
19-389 3.37e-35

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 140.37  E-value: 3.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  19 PELLEVFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIqNAKLQPADIgaLILSPSRELCSQIVS 98
Cdd:PRK11634  16 PILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL-DPELKAPQI--LVLAPTRELAVQVAE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  99 VIQPFAEKLN-LTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLfqiIQHEK--TLiarKMRTLQLLVIDEADRFNEIQ 175
Cdd:PRK11634  93 AMTDFSKHMRgVNVVALYGGQRYDVQLRALR-QGPQIVVGTPGRL---LDHLKrgTL---DLSKLSGLVLDEADEMLRMG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 176 FEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVKVaQERNSAAPSTLKNYYVeCRADEKTSVCLEFIRQR 255
Cdd:PRK11634 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRI-QSSVTTRPDISQSYWT-VWGMRKNEALVRFLEAE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 256 TDKKILIFFPSCNSVRYFYKIFERClGKRPLfAVHGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISDIDWVIQFD 335
Cdd:PRK11634 244 DFDAAIIFVRTKNATLEVAEALERN-GYNSA-ALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYD 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392895997 336 LPKHSSWFVHRAGRTARCGREGNALILIASEQLAYVNFLDNHEKVKLDEIKVPT 389
Cdd:PRK11634 322 IPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPN 375
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
28-219 5.90e-34

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: 127.76  E-value: 5.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  28 SYKSFTDVQ------VLSGThllnlsDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPADIGALILSPSRELCSQIVSVIQ 101
Cdd:cd17947    9 GFTKPTPIQaaaiplALLGK------DICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFSVLQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 102 PFAEKLNLTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLfqiIQHEKTLIARKMRTLQLLVIDEADRFNEIQFEDHMR 181
Cdd:cd17947   83 QLAQFTDITFALAVGGLSLKAQEAALR-ARPDIVIATPGRL---IDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELK 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895997 182 EILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVK 219
Cdd:cd17947  159 EILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
PTZ00424 PTZ00424
helicase 45; Provisional
43-385 3.32e-33

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 131.10  E-value: 3.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  43 LLNLSDVVVESPTGSGKTLAFVLPMMRMIqNAKLQPADigALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDK 122
Cdd:PTZ00424  62 ILDGYDTIGQAQSGTGKTATFVIAALQLI-DYDLNACQ--ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRD 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 123 NIKMFKNkNVNILVATPGRLFQIIQHEKTLIARkmrtLQLLVIDEADRFNEIQFEDHMREILSCIPKQRRTGLFSATQVK 202
Cdd:PTZ00424 139 DINKLKA-GVHMVVGTPGRVYDMIDKRHLRVDD----LKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPN 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 203 EEDDLMVFGLRNAKQVKVAQERNSAapSTLKNYYVECRADE-KTSVCLEFIRQRTDKKILIFfpsCNSVRYFYKIFERCL 281
Cdd:PTZ00424 214 EILELTTKFMRDPKRILVKKDELTL--EGIRQFYVAVEKEEwKFDTLCDLYETLTITQAIIY---CNTRRKVDYLTKKMH 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 282 GKrpLFAV---HGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTARCGREGN 358
Cdd:PTZ00424 289 ER--DFTVscmHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGV 366
                        330       340
                 ....*....|....*....|....*..
gi 392895997 359 ALILIASEQLAYVNFLDNHEKVKLDEI 385
Cdd:PTZ00424 367 AINFVTPDDIEQLKEIERHYNTQIEEM 393
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
48-199 2.70e-31

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: 120.95  E-value: 2.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKTLAFVLPMMRMIQNAKLQPADIG--ALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIK 125
Cdd:cd17953   51 DVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEGpiGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIA 130
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392895997 126 MFKnKNVNILVATPGRLFQIIqhekTLIARKMRTLQ---LLVIDEADRFNEIQFEDHMREILSCIPKQRRTGLFSAT 199
Cdd:cd17953  131 ELK-RGAEIVVCTPGRMIDIL----TANNGRVTNLRrvtYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSAT 202
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
16-199 5.13e-31

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: 119.71  E-value: 5.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  16 KLGPELLE-VFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQpadIGALILSPSRELCS 94
Cdd:cd17940    5 GLKRELLMgIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV---IQALILVPTRELAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  95 QIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFKNKnVNILVATPGRLFQIIQheKTLIarKMRTLQLLVIDEADRFNEI 174
Cdd:cd17940   82 QTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQT-VHVLVGTPGRILDLAK--KGVA--DLSHCKTLVLDEADKLLSQ 156
                        170       180
                 ....*....|....*....|....*
gi 392895997 175 QFEDHMREILSCIPKQRRTGLFSAT 199
Cdd:cd17940  157 DFQPIIEKILNFLPKERQILLFSAT 181
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
29-219 5.70e-31

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: 120.00  E-value: 5.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  29 YKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNakLQPA---DIG--ALILSPSRELCSQIVSVIQ-- 101
Cdd:cd17949   11 IEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLS--LEPRvdrSDGtlALVLVPTRELALQIYEVLEkl 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 102 --PFaekLNLTVETVTGGQKVDKNiKMFKNKNVNILVATPGRLFQIIQHEKTLiarKMRTLQLLVIDEADRFNEIQFEDH 179
Cdd:cd17949   89 lkPF---HWIVPGYLIGGEKRKSE-KARLRKGVNILIATPGRLLDHLKNTQSF---DVSNLRWLVLDEADRLLDMGFEKD 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392895997 180 MREILSCI-------------PKQRRTGLFSATQVKEEDDLMVFGLRNAKQVK 219
Cdd:cd17949  162 ITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
24-199 1.69e-29

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: 115.38  E-value: 1.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  24 VFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKlQPADIGALILSPSRELCSQIVSVIQPF 103
Cdd:cd17957    5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPR-KKKGLRALILAPTRELASQIYRELLKL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 104 AEKLNLTVETVTGGQKVDKNIKMFKNKNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEADRFNEIQFEDHMREI 183
Cdd:cd17957   84 SKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPI----DLSSVEYLVLDEADKLFEPGFREQTDEI 159
                        170
                 ....*....|....*..
gi 392895997 184 L-SCIPKQRRTGLFSAT 199
Cdd:cd17957  160 LaACTNPNLQRSLFSAT 176
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
17-370 3.65e-29

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 120.08  E-value: 3.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  17 LGPELLEVFDKSYKSF-TDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLP----MMRMIQNAKLQPADIGALILSPSRE 91
Cdd:PRK04837  15 LHPQVVEALEKKGFHNcTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKVNQPRALIMAPTRE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  92 LCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFkNKNVNILVATPGRlfqIIQHEKTLIARkMRTLQLLVIDEADRF 171
Cdd:PRK04837  95 LAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVL-ESGVDILIGTTGR---LIDYAKQNHIN-LGAIQVVVLDEADRM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 172 NEIQFEDHMREILSCIP--KQRRTGLFSAT---QVKEeddlmvfglrnakqvkVAQER-NSAApstlknyYVECRADEKT 245
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPpaNQRLNMLFSATlsyRVRE----------------LAFEHmNNPE-------YVEVEPEQKT 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 246 SVcleFIRQRtdkkilIFFPSC-NSVRYFYKIFE-----RCLgkrpLFA--VHgKCSNPH-------------------- 297
Cdd:PRK04837 227 GH---RIKEE------LFYPSNeEKMRLLQTLIEeewpdRAI----IFAntKH-RCEEIWghlaadghrvglltgdvaqk 292
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392895997 298 -RASQIKAFSDSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTARCGREGNAlILIASEQLAY 370
Cdd:PRK04837 293 kRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHS-ISLACEEYAL 365
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
23-218 3.85e-28

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: 111.31  E-value: 3.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  23 EVFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQN-AKLQPADiG--ALILSPSRELCSQIVSV 99
Cdd:cd17966    4 ELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAqPPLERGD-GpiVLVLAPTRELAQQIQQE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 100 IQPFAEKLNLTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEADRFNEIQFEDH 179
Cdd:cd17966   83 ANKFGGSSRLRNTCVYGGAPKGPQIRDLR-RGVEICIATPGRLIDFLDQGKT----NLRRVTYLVLDEADRMLDMGFEPQ 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392895997 180 MREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQV 218
Cdd:cd17966  158 IRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
48-199 1.78e-27

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: 110.79  E-value: 1.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKTLAFVLPMMRMIQNAKLQPADIG------ALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVD 121
Cdd:cd17946   30 DVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGkqkplrALILTPTRELAVQVKDHLKAIAKYTNIKIASIVGGLAVQ 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 122 KNIKMFKNKNvNILVATPGRLFQIIQHEKTLIARkMRTLQLLVIDEADRFNEIQFEDHMREILSCIP-------KQRRTG 194
Cdd:cd17946  110 KQERLLKKRP-EIVVATPGRLWELIQEGNEHLAN-LKSLRFLVLDEADRMLEKGHFAELEKILELLNkdragkkRKRQTF 187

                 ....*
gi 392895997 195 LFSAT 199
Cdd:cd17946  188 VFSAT 192
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
12-199 4.54e-27

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: 109.11  E-value: 4.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  12 TFRE-KLGPELLEVFDKS-YKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMM-RMIQNAKLQPADIG------ 82
Cdd:cd17967    1 SFEEaGLRELLLENIKRAgYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIIsKLLEDGPPSVGRGRrkayps 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  83 ALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLFQIIQHEKTliarKMRTLQL 162
Cdd:cd17967   81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLL-RGCDILVATPGRLVDFIERGRI----SLSSIKF 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895997 163 LVIDEADRFNEIQFEDHMREILSC--IPK--QRRTGLFSAT 199
Cdd:cd17967  156 LVLDEADRMLDMGFEPQIRKIVEHpdMPPkgERQTLMFSAT 196
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
21-199 7.91e-27

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: 7.91e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  21 LLEVFDK-SYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPADIG-----ALILSPSRELCS 94
Cdd:cd17945    1 LLRVIRKlGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKddgpyALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  95 QIVSVIQPFAEKLNLTVETVTGGQKVDKnIKMFKNKNVNILVATPGRLFQIIqhEKTLIArkMRTLQLLVIDEADRFNEI 174
Cdd:cd17945   81 QIEEETQKFAKPLGIRVVSIVGGHSIEE-QAFSLRNGCEILIATPGRLLDCL--ERRLLV--LNQCTYVVLDEADRMIDM 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 392895997 175 QFEDHMREILSCIP--------------------KQRRTGLFSAT 199
Cdd:cd17945  156 GFEPQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTAT 200
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
37-202 4.95e-26

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: 105.88  E-value: 4.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  37 VLSGthllnlSDVVVESPTGSGKTLAFVLPM-MRMIQNAKLQPADIG----ALILSPSRELCSQIVSVIQPFAEKLN--- 108
Cdd:cd17951   24 ILSG------RDMIGIAFTGSGKTLVFTLPLiMFALEQEKKLPFIKGegpyGLIVCPSRELARQTHEVIEYYCKALQegg 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 109 ---LTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLfqiiqheKTLIARKMRTLQL---LVIDEADRFNEIQFEDHMRE 182
Cdd:cd17951   98 ypqLRCLLCIGGMSVKEQLEVIR-KGVHIVVATPGRL-------MDMLNKKKINLDIcryLCLDEADRMIDMGFEEDIRT 169
                        170       180
                 ....*....|....*....|
gi 392895997 183 ILSCIPKQRRTGLFSATQVK 202
Cdd:cd17951  170 IFSYFKGQRQTLLFSATMPK 189
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
48-220 6.50e-26

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: 105.36  E-value: 6.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKTLAFVLPMMRMIQNAKLQPAD---IGALILSPSRELCSQIVSVIQPFAEKLNLTVETVT-GGQKVDKN 123
Cdd:cd17961   33 DILARARTGSGKTAAYALPIIQKILKAKAESGEeqgTRALILVPTRELAQQVSKVLEQLTAYCRKDVRVVNlSASSSDSV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 124 IKMFKNKNVNILVATPGRLFQIIQhEKTLIARKmrTLQLLVIDEADRFNEIQFEDHMREILSCIPKQRRTGLFSATQVKE 203
Cdd:cd17961  113 QRALLAEKPDIVVSTPARLLSHLE-SGSLLLLS--TLKYLVIDEADLVLSYGYEEDLKSLLSYLPKNYQTFLMSATLSED 189
                        170
                 ....*....|....*..
gi 392895997 204 EDDLMVFGLRNAKQVKV 220
Cdd:cd17961  190 VEALKKLVLHNPAILKL 206
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
37-199 7.20e-26

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: 105.19  E-value: 7.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  37 VLSGthllnlSDVVVESPTGSGKTLAFVLPMMRMIQNAK-LQPADiG--ALILSPSRELCSQIVSVIQPFAEKLNLTVET 113
Cdd:cd17952   24 ALSG------RDMIGIAKTGSGKTAAFIWPMLVHIMDQReLEKGE-GpiAVIVAPTRELAQQIYLEAKKFGKAYNLRVVA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 114 VTGGQKVDKNIKMFKnKNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEADRFNEIQFEDHMREILSCIPKQRRT 193
Cdd:cd17952   97 VYGGGSKWEQAKALQ-EGAEIVVATPGRLIDMVKKKAT----NLQRVTYLVLDEADRMFDMGFEYQVRSIVGHVRPDRQT 171

                 ....*.
gi 392895997 194 GLFSAT 199
Cdd:cd17952  172 LLFSAT 177
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
33-201 2.32e-25

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: 104.76  E-value: 2.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  33 TDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPA----DIGALILSPSRELCSQIVSVIQPFAEKLN 108
Cdd:cd17948   14 TTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEgpfnAPRGLVITPSRELAEQIGSVAQSLTEGLG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 109 LTVETVTGGQKVdKNIKMFKNKNVNILVATPGRLFQIIqheKTLIARkMRTLQLLVIDEADRFNEIQFEDHMREILSCIP 188
Cdd:cd17948   94 LKVKVITGGRTK-RQIRNPHFEEVDILVATPGALSKLL---TSRIYS-LEQLRHLVLDEADTLLDDSFNEKLSHFLRRFP 168
                        170
                 ....*....|....*...
gi 392895997 189 -----KQRRTGLFSATQV 201
Cdd:cd17948  169 lasrrSENTDGLDPGTQL 186
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
48-204 4.30e-24

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: 100.09  E-value: 4.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKTLAFVLPMMrmiQNAKLQPADIGALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMF 127
Cdd:cd17939   36 DVIAQAQSGTGKTATFSIGAL---QRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKL 112
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392895997 128 KnKNVNILVATPGRLFQIIQhEKTLIARKMRtlqLLVIDEADRFNEIQFEDHMREILSCIPKQRRTGLFSATQVKEE 204
Cdd:cd17939  113 Q-YGPHIVVGTPGRVFDMLQ-RRSLRTDKIK---MFVLDEADEMLSRGFKDQIYDIFQFLPPETQVVLFSATMPHEV 184
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
48-199 1.40e-23

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: 98.49  E-value: 1.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKTLAFVLPMMRMIqnaKLQPADIGALILSPSRELCSQIVSVIQPFAEKL-NLTVETVTGGQKVDKNIKm 126
Cdd:cd17943   29 DLIVQAKSGTGKTLVFVVIALESL---DLERRHPQVLILAPTREIAVQIHDVFKKIGKKLeGLKCEVFIGGTPVKEDKK- 104
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392895997 127 fKNKNVNILVATPGRLFQIIQhektLIARKMRTLQLLVIDEADRFNEIQFEDHMREILSCIPKQRRTGLFSAT 199
Cdd:cd17943  105 -KLKGCHIAVGTPGRIKQLIE----LGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLPKNKQVIAFSAT 172
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
7-199 1.85e-23

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: 100.04  E-value: 1.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   7 PVALKTFRE-KLGPELLEVFDKS-YKSFTDVQ------VLSGthllnlSDVVVESPTGSGKTLAFVLPMM-RMIQNAKLQ 77
Cdd:cd18052   39 PPAILTFEEaNLCETLLKNIRKAgYEKPTPVQkyaipiILAG------RDLMACAQTGSGKTAAFLLPVLtGMMKEGLTA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  78 PADIG-----ALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLFQIIQHEKTL 152
Cdd:cd18052  113 SSFSEvqepqALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIE-KGCHILVATPGRLLDFIGRGKIS 191
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392895997 153 IARkmrtLQLLVIDEADRFNEIQFEDHMREILSCI---PKQRR-TGLFSAT 199
Cdd:cd18052  192 LSK----LKYLILDEADRMLDMGFGPEIRKLVSEPgmpSKEDRqTLMFSAT 238
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
48-199 7.44e-23

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: 97.32  E-value: 7.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKTLAFVLPMMRMIQNAKLqpADIGALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMF 127
Cdd:cd17956   38 DLCVSAPTGSGKTLAYVLPIVQALSKRVV--PRLRALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 128 K-------NKNVNILVATPGRLfqiIQHEKTLIARKMRTLQLLVIDEADRFNEIQFED----HMREI------------- 183
Cdd:cd17956  116 LvdtsgryLSRVDILVATPGRL---VDHLNSTPGFTLKHLRFLVIDEADRLLNQSFQDwletVMKALgrptapdlgsfgd 192
                        170
                 ....*....|....*....
gi 392895997 184 ---LSCIPKQRRTGLFSAT 199
Cdd:cd17956  193 anlLERSVRPLQKLLFSAT 211
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
243-354 9.20e-23

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: 93.04  E-value: 9.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  243 EKTSVCLEFIRQRTDKKILIFFPSCNSVRYfyKIFERCLGKRPLfAVHGKCSNPHRASQIKAFSDSTNGVMISTDVMARG 322
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEA--ELLLEKEGIKVA-RLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 392895997  323 IDISDIDWVIQFDLPKHSSWFVHRAGRTARCG 354
Cdd:pfam00271  78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
15-210 2.29e-22

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: 95.08  E-value: 2.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  15 EKLG--PELLE-VFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQnaklqpadigALILSPSRE 91
Cdd:cd17938    2 EELGvmPELIKaVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV----------ALILEPSRE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  92 LCSQIVSVIQPFAEKL-NLTVET--VTGGQKVDKNIKMFKNkNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEA 168
Cdd:cd17938   72 LAEQTYNCIENFKKYLdNPKLRValLIGGVKAREQLKRLES-GVDIVVGTPGRLEDLIKTGKL----DLSSVRFFVLDEA 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392895997 169 DRFNEIQFEDHMREILSCIPKQRRTG------LFSAT----QVKE-EDDLMVF 210
Cdd:cd17938  147 DRLLSQGNLETINRIYNRIPKITSDGkrlqviVCSATlhsfEVKKlADKIMHF 199
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
16-366 9.03e-22

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 98.71  E-value: 9.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  16 KLGPELLEVFDKS-YKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPADIG----ALILSPSR 90
Cdd:PLN00206 127 GLPPKLLLNLETAgYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEQrnplAMVLTPTR 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  91 ELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLFQII-QHEKTLiarkmRTLQLLVIDEAD 169
Cdd:PLN00206 207 ELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQ-QGVELIVGTPGRLIDLLsKHDIEL-----DNVSVLVLDEVD 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 170 RFNEIQFEDHMREILSCIPkQRRTGLFSATQVKEEDDlmvFGLRNAKQVKVAQERNSAAPS-TLKNYYVECRADEKTSVC 248
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEK---FASSLAKDIILISIGNPNRPNkAVKQLAIWVETKQKKQKL 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 249 LEFI--RQRTDKKILIFFPS-------CNSVRYFYKIfeRCLgkrplfAVHGKCSNPHRASQIKAFSDSTNGVMISTDVM 319
Cdd:PLN00206 357 FDILksKQHFKPPAVVFVSSrlgadllANAITVVTGL--KAL------SIHGEKSMKERREVMKSFLVGEVPVIVATGVL 428
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 392895997 320 ARGIDISDIDWVIQFDLPKHSSWFVHRAGRTARCGREGNALILIASE 366
Cdd:PLN00206 429 GRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE 475
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
24-221 1.14e-21

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: 95.08  E-value: 1.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  24 VFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPADIG--ALILSPSRELCSQIVSVIQ 101
Cdd:cd18050   77 LLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGpiCLVLAPTRELAQQVQQVAD 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 102 PFAEKLNLTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEADRFNEIQFEDHMR 181
Cdd:cd18050  157 DYGKSSRLKSTCIYGGAPKGPQIRDLE-RGVEICIATPGRLIDFLEAGKT----NLRRCTYLVLDEADRMLDMGFEPQIR 231
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392895997 182 EILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVKVA 221
Cdd:cd18050  232 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
6-221 8.82e-21

DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 91.61  E-value: 8.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   6 GPVALKTFREKLGPE-LLEVFDKsyKSFTD---VQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPADI 81
Cdd:cd18049   19 CPKPVLNFYEANFPAnVMDVIAR--QNFTEptaIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  82 G--ALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLFQIIQHEKTliarKMRT 159
Cdd:cd18049   97 GpiCLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLE-RGVEICIATPGRLIDFLEAGKT----NLRR 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392895997 160 LQLLVIDEADRFNEIQFEDHMREILSCIPKQRRTGLFSATQVKEEDDLMVFGLRNAKQVKVA 221
Cdd:cd18049  172 CTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
28-203 6.25e-20

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: 89.33  E-value: 6.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  28 SYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQN---AKLQPADIG----------ALILSPSRELCS 94
Cdd:cd18051   40 RYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEqgpGESLPSESGyygrrkqyplALVLAPTRELAS 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  95 QIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFkNKNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEADRFNEI 174
Cdd:cd18051  120 QIYDEARKFAYRSRVRPCVVYGGADIGQQMRDL-ERGCHLLVATPGRLVDMLERGKI----GLDYCKYLVLDEADRMLDM 194
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895997 175 QFEDHMREILS--CIPK--QRRTGLFSATQVKE 203
Cdd:cd18051  195 GFEPQIRRIVEqdTMPPtgERQTLMFSATFPKE 227
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
50-199 8.07e-20

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: 87.63  E-value: 8.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  50 VVESPTGSGKTLAFVLPMMRMIQNAKLQPAdigALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNikmfKN 129
Cdd:cd17963   37 IAQSQSGTGKTAAFVLAMLSRVDPTLKSPQ---ALCLAPTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRG----KK 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392895997 130 KNVNILVATPGRLFQIIQHeKTLIARKMRtlqLLVIDEADRFNEIQ-FEDHMREILSCIPKQRRTGLFSAT 199
Cdd:cd17963  110 ITAQIVIGTPGTVLDWLKK-RQLDLKKIK---ILVLDEADVMLDTQgHGDQSIRIKRMLPRNCQILLFSAT 176
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
17-203 3.28e-19

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: 86.24  E-value: 3.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  17 LGPELLE-VFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIqnaKLQPADIGALILSPSRELCSQ 95
Cdd:cd17950    9 LKPELLRaIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL---EPVDGQVSVLVICHTRELAFQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  96 IVSVIQPFAEKL-NLTVETVTGGQKVDKNIKMFKNKNVNILVATPGRLFQIIQhEKTLiarKMRTLQLLVIDEADRfnei 174
Cdd:cd17950   86 ISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKCPHIVVGTPGRILALVR-EKKL---KLSHVKHFVLDECDK---- 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895997 175 QFED-HMR----EILSCIPKQRRTGLFSATQVKE 203
Cdd:cd17950  158 MLEQlDMRrdvqEIFRATPHDKQVMMFSATLSKE 191
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
48-199 1.00e-18

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: 84.52  E-value: 1.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKTLAFVLPMMRMIQNAKLQPAdigALILSPSRELCSQIVSVIQPFAEKL-NLTVETVTGGQKVDKNIKM 126
Cdd:cd17962   29 DILASADTGSGKTAAFLLPVIIRCLTEHRNPS---ALILTPTRELAVQIEDQAKELMKGLpPMKTALLVGGLPLPPQLYR 105
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392895997 127 FKnKNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEADRFNEIQFEDHMREILSCIPKQRRTGLFSAT 199
Cdd:cd17962  106 LQ-QGVKVIIATPGRLLDILKQSSV----ELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQTILVSAT 173
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
16-199 1.04e-18

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: 84.44  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  16 KLGPELLE-VFDKSYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQnakLQPADIGALILSPSRELCS 94
Cdd:cd18045    5 GLREDLLRgIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLD---IQVRETQALILSPTRELAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  95 QIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMFKnKNVNILVATPGRLFQIIQHektliaRKMRT--LQLLVIDEADRFN 172
Cdd:cd18045   82 QIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLD-YGQHIVSGTPGRVFDMIRR------RSLRTrhIKMLVLDEADEML 154
                        170       180
                 ....*....|....*....|....*..
gi 392895997 173 EIQFEDHMREILSCIPKQRRTGLFSAT 199
Cdd:cd18045  155 NKGFKEQIYDVYRYLPPATQVVLVSAT 181
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
43-199 1.46e-18

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: 84.05  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  43 LLNLSDVVVESPTGSGKTLAFVLPMMRMIQnakLQPA------DIGALILSPSRELCSQIVSVIQPFAEKlNLTVETVTG 116
Cdd:cd17958   24 ILQGIDLIGVAQTGTGKTLAYLLPGFIHLD---LQPIpreqrnGPGVLVLTPTRELALQIEAECSKYSYK-GLKSVCVYG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 117 GQKVDKNIKMFKnKNVNILVATPGRLFQIIQHEktliARKMRTLQLLVIDEADRFNEIQFEDHMREILSCIPKQRRTGLF 196
Cdd:cd17958  100 GGNRNEQIEDLS-KGVDIIIATPGRLNDLQMNN----VINLKSITYLVLDEADRMLDMGFEPQIRKILLDIRPDRQTIMT 174

                 ...
gi 392895997 197 SAT 199
Cdd:cd17958  175 SAT 177
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
48-199 8.34e-18

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: 82.11  E-value: 8.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKTLAFVLPMMRMIQNAKLQPAdigALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNIKMF 127
Cdd:cd18046   38 DVIAQAQSGTGKTATFSISILQQIDTSLKATQ---ALVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKL 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392895997 128 KNkNVNILVATPGRLFQIIQHektliaRKMRT--LQLLVIDEADRFNEIQFEDHMREILSCIPKQRRTGLFSAT 199
Cdd:cd18046  115 QA-GPHIVVGTPGRVFDMINR------RYLRTdyIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDTQVVLLSAT 181
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
34-199 3.59e-17

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: 80.28  E-value: 3.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  34 DVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQnAKLQPADIG----ALILSPSRELCSQIVSVIQPFAEKLNl 109
Cdd:cd17944   15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQ-EDQQPRKRGrapkVLVLAPTRELANQVTKDFKDITRKLS- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 110 tVETVTGGQKVDKNIKMFKNkNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEADRFNEIQFEDHMREILSCIPK 189
Cdd:cd17944   93 -VACFYGGTPYQQQIFAIRN-GIDILVGTPGRIKDHLQNGRL----DLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYK 166
                        170
                 ....*....|....*
gi 392895997 190 QR-----RTGLFSAT 199
Cdd:cd17944  167 KDsednpQTLLFSAT 181
HELICc smart00490
helicase superfamily c-terminal domain;
275-354 1.39e-16

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 74.56  E-value: 1.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   275 KIFERCLGKRPL--FAVHGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTAR 352
Cdd:smart00490   1 EELAELLKELGIkvARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 392895997   353 CG 354
Cdd:smart00490  81 AG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
48-521 9.85e-15

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 76.99  E-value: 9.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKTLAFVLPMMRMIQNAKlqpadigALILSPSRELCSQIVSVIQPFaeklnLTVETVTGGQkvdknikmf 127
Cdd:COG1061  102 RGLVVAPTGTGKTVLALALAAELLRGKR-------VLVLVPRRELLEQWAEELRRF-----LGDPLAGGGK--------- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 128 KNKNVNILVATpgrlfqiIQhekTLIARKM-RTLQ----LLVIDE-----ADRFneiqfedhmREILSCIPKQRRTGLfS 197
Cdd:COG1061  161 KDSDAPITVAT-------YQ---SLARRAHlDELGdrfgLVIIDEahhagAPSY---------RRILEAFPAAYRLGL-T 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 198 ATqVKEEDDLMV-----------FGLRNAKQ-------------VKVAQERN--SAAPSTLKNYYVECrADEKTSVCLEF 251
Cdd:COG1061  221 AT-PFRSDGREIllflfdgivyeYSLKEAIEdgylappeyygirVDLTDERAeyDALSERLREALAAD-AERKDKILREL 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 252 IRQRTD-KKILIFFPSCNSVRYFYKIFERcLGKRPLfAVHGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISDIDW 330
Cdd:COG1061  299 LREHPDdRKTLVFCSSVDHAEALAELLNE-AGIRAA-VVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDV 376
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 331 VIQFDLPKHSSWFVHRAGRTAR-CGREGNALIL--IASEQLAYVNFLDNHEKVKLDEIKVptnnsrKSEELRQKMIKIQV 407
Cdd:COG1061  377 AILLRPTGSPREFIQRLGRGLRpAPGKEDALVYdfVGNDVPVLEELAKDLRDLAGYRVEF------LDEEESEELALLIA 450
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 408 SDRAILEAGTRAFVSHVESYAKHDCHLICSLDDLNVVGLANSYALLRLPKMRELSQRKDLDMFDRSAIETSEIKYADVKL 487
Cdd:COG1061  451 VKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLL 530
                        490       500       510
                 ....*....|....*....|....*....|....
gi 392895997 488 EANRETVMKEKHEKKVETLAAKDKKRREKEARKL 521
Cdd:COG1061  531 LLLLLLELLELLAALLRLEELAALLLKELLRAAL 564
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
55-208 2.45e-14

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: 73.18  E-value: 2.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  55 TGSGKTLAFVLPMMRMIQNAKLQP--------------ADIGALILSPSRELCSQIVSVIQPFAE--KLNLTVETVTGGQ 118
Cdd:cd17965   70 TGSGKTLAYLAPLLDYLKRQEQEPfeeaeeeyesakdtGRPRSVILVPTHELVEQVYSVLKKLSHtvKLGIKTFSSGFGP 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 119 KVDKNIKMFKNKnVNILVATPGRLFQIIQHEKTLIARkmrtLQLLVIDEADRFNEIQFEDHMREILSCIPKQRRTGLFSA 198
Cdd:cd17965  150 SYQRLQLAFKGR-IDILVTTPGKLASLAKSRPKILSR----VTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSA 224
                        170
                 ....*....|
gi 392895997 199 TQVKEEDDLM 208
Cdd:cd17965  225 TIPKEFDKTL 234
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
399-457 9.50e-14

Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many helicase proteins.


Pssm-ID: 464056 [Multi-domain]  Cd Length: 59  Bit Score: 65.88  E-value: 9.50e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392895997  399 RQKMIKIQVSDRAILEAGTRAFVSHVESYAKHDCHLICSLDDLNVVGLANSYALLRLPK 457
Cdd:pfam13959   1 QLQLEKLVLKDRELKELAQKAFVSYVRAYSKHLAKSIFNVKKLDLGHLAKSFGLLRAPK 59
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
54-192 3.44e-13

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: 68.45  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  54 PTGSGKTLAFVLPMMRMI-QNAKLQPADIGALILSPSRELCSQIVSVIQpfaEKLNLTVETVTGGQKVDKNIKMFKN--- 129
Cdd:cd18034   24 PTGSGKTLIAVMLIKEMGeLNRKEKNPKKRAVFLVPTVPLVAQQAEAIR---SHTDLKVGEYSGEMGVDKWTKERWKeel 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392895997 130 KNVNILVATPGRLFQIIQHEKTliarKMRTLQLLVIDEADR------FNEIqfedhMREILSCIPKQRR 192
Cdd:cd18034  101 EKYDVLVMTAQILLDALRHGFL----SLSDINLLIFDECHHatgdhpYARI-----MKEFYHLEGRTSR 160
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
47-199 4.57e-12

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: 63.96  E-value: 4.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  47 SDVVVESPTGSGKTLAFvlpMMRMIQNAKLQPAdiGALILSPSRELCSQIVSVIQPFAeKLNLTVETVTGGqkVDKNIK- 125
Cdd:cd00046    2 ENVLITAPTGSGKTLAA---LLAALLLLLKKGK--KVLVLVPTKALALQTAERLRELF-GPGIRVAVLVGG--SSAEERe 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392895997 126 MFKNKNVNILVATPGRLFQIIQHEKtliARKMRTLQLLVIDEADRFNEIQFEDHMREILSC--IPKQRRTGLFSAT 199
Cdd:cd00046   74 KNKLGDADIIIATPDMLLNLLLRED---RLFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
17-168 3.29e-11

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 65.69  E-value: 3.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  17 LGPELLEVFDK-SYKSFTDVQ---VLSGthLLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLqpadigALILSPSREL 92
Cdd:COG1204    7 PLEKVIEFLKErGIEELYPPQaeaLEAG--LLEGKNLVVSAPTASGKTLIAELAILKALLNGGK------ALYIVPLRAL 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392895997  93 CSQIVS-VIQPFaEKLNLTVETVTGGqkVDKNIKMFKNKnvNILVATPGRLFQIIQHEKTLIARkmrtLQLLVIDEA 168
Cdd:COG1204   79 ASEKYReFKRDF-EELGIKVGVSTGD--YDSDDEWLGRY--DILVATPEKLDSLLRNGPSWLRD----VDLVVVDEA 146
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
9-213 2.30e-10

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 60.81  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   9 ALKTFRE-KLGPELLE-VFDKSYKSFTDVQVLSGTHLLN--LSDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPAdigAL 84
Cdd:cd18048   16 SVKSFEElHLKEELLRgIYAMGFNRPSKIQENALPMMLAdpPQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQ---CL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  85 ILSPSRELCSQIVSVIQPFAEKLN-LTVETVTGGQKVDKNIKMFKnknvNILVATPGRLFQIIQHEKTLIARKMRtlqLL 163
Cdd:cd18048   93 CLSPTFELALQTGKVVEEMGKFCVgIQVIYAIRGNRPGKGTDIEA----QIVIGTPGTVLDWCFKLRLIDVTNIS---VF 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392895997 164 VIDEADRFNEIQ-FEDHMREILSCIPKQRRTGLFSATQvkeEDDLMVFGLR 213
Cdd:cd18048  166 VLDEADVMINVQgHSDHSVRVKRSMPKECQMLLFSATF---EDSVWAFAER 213
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
36-168 1.38e-09

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: 57.59  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  36 QVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMrmiqNAKLQPADIGALILSPSRELCSQIVSVIQPFAEKL--NLTVET 113
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPIL----EALLRDPGSRALYLYPTKALAQDQLRSLRELLEQLglGIRVAT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392895997 114 VTGGQKVDKNIKMFKNkNVNILVATPGRLFQIIQHEKTLIARKMRTLQLLVIDEA 168
Cdd:cd17923   81 YDGDTPREERRAIIRN-PPRILLTNPDMLHYALLPHHDRWARFLRNLRYVVLDEA 134
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
31-167 4.06e-09

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: 56.60  E-value: 4.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  31 SFTDVQVLSGTHLLNlSD--VVVESPTGSGKTLAFVLPMMRMIQNAKLQP-ADIGALILSPSRELCSQIVSVIQPFAEKL 107
Cdd:cd18023    1 YFNRIQSEVFPDLLY-SDknFVVSAPTGSGKTVLFELAILRLLKERNPLPwGNRKVVYIAPIKALCSEKYDDWKEKFGPL 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 108 NLTVETVTGGQKVDkniKMFKNKNVNILVATPGRLFQIIQHEKTLiARKMRTLQLLVIDE 167
Cdd:cd18023   80 GLSCAELTGDTEMD---DTFEIQDADIILTTPEKWDSMTRRWRDN-GNLVQLVALVLIDE 135
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
49-168 1.23e-08

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 54.96  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  49 VVVESPTGSGKTLAFVLPMMRMI-QNAKLqpadigALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDKNikmf 127
Cdd:cd17921   20 VLVSAPTSSGKTLIAELAILRALaTSGGK------AVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVNKL---- 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 392895997 128 KNKNVNILVATPGRLFQIIqheKTLIARKMRTLQLLVIDEA 168
Cdd:cd17921   90 LLAEADILVATPEKLDLLL---RNGGERLIQDVRLVVVDEA 127
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
48-167 1.64e-08

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: 54.13  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKTLAFVLPMMRMIqnAKLQPADIGALILSPSRELCSQIVSVIQPFAE--KLNLTVETVTGGQKVDKNIK 125
Cdd:cd17922    3 NVLIAAPTGSGKTEAAFLPALSSL--ADEPEKGVQVLYISPLKALINDQERRLEEPLDeiDLEIPVAVRHGDTSQSEKAK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 392895997 126 MFKNKNvNILVATPGRLFQIIQHEKTliARKMRTLQLLVIDE 167
Cdd:cd17922   81 QLKNPP-GILITTPESLELLLVNKKL--RELFAGLRYVVVDE 119
ResIII pfam04851
Type III restriction enzyme, res subunit;
49-199 1.90e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 53.83  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   49 VVVESPTGSGKTLAfvlpMMRMIQNAKLQPADIGALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGgqkvdkNIKMFK 128
Cdd:pfam04851  26 GLIVMATGSGKTLT----AAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISG------DKKDES 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392895997  129 NKNVNILVATPGRLFQIIQHEKTLIARKmrTLQLLVIDEADRFNeiqfEDHMREILSCIPKQRRTGlFSAT 199
Cdd:pfam04851  96 VDDNKIVVTTIQSLYKALELASLELLPD--FFDVIIIDEAHRSG----ASSYRNILEYFKPAFLLG-LTAT 159
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
11-213 3.03e-08

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: 54.34  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  11 KTFRE-KLGPELLE-VFDKSYKSFTDVQVLSGTHLLNL--SDVVVESPTGSGKTLAFVLPMMRMIQNAKLQPAdigALIL 86
Cdd:cd18047    1 KSFEElRLKPQLLQgVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ---CLCL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  87 SPSRELCSQIVSVIQPFAEKL-NLTVETVTGGQKVDKNIKMfKNKnvnILVATPGRLFQIIQHEKTLIARKMRtlqLLVI 165
Cdd:cd18047   78 SPTYELALQTGKVIEQMGKFYpELKLAYAVRGNKLERGQKI-SEQ---IVIGTPGTVLDWCSKLKFIDPKKIK---VFVL 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392895997 166 DEADRFNEIQ-FEDHMREILSCIPKQRRTGLFSATQvkeEDDLMVFGLR 213
Cdd:cd18047  151 DEADVMIATQgHQDQSIRIQRMLPRNCQMLLFSATF---EDSVWKFAQK 196
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
13-168 3.84e-08

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 56.38  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  13 FREKLGPELLEVFDKSY-KSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIqnakLQPADIGALILSPSRE 91
Cdd:COG1205   37 WPDWLPPELRAALKKRGiERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL----LEDPGATALYLYPTKA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  92 LCSQIVSVIQPFAEKL--NLTVETVTGGQKVD--KNIKmfknKNVNILVATPGRLFQIIQHEKTLIARKMRTLQLLVIDE 167
Cdd:COG1205  113 LARDQLRRLRELAEALglGVRVATYDGDTPPEerRWIR----EHPDIVLTNPDMLHYGLLPHHTRWARFFRNLRYVVIDE 188

                 .
gi 392895997 168 A 168
Cdd:COG1205  189 A 189
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
50-199 2.52e-07

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: 50.38  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  50 VVESPTGSGKTLAfvlpMMRMIQNAKLQPadigALILSPSRELCSQIVSVIQPFAEKlnLTVETVTGGQKVDKNIKmfkn 129
Cdd:cd17926   22 ILVLPTGSGKTLT----ALALIAYLKELR----TLIVVPTDALLDQWKERFEDFLGD--SSIGLIGGGKKKDFDDA---- 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 130 knvNILVATPGRLFQIIQHEKTLIARKMrtlqLLVIDEADRFNEIQFedhmREILSCIPKQRRTGlFSAT 199
Cdd:cd17926   88 ---NVVVATYQSLSNLAEEEKDLFDQFG----LLIVDEAHHLPAKTF----SEILKELNAKYRLG-LTAT 145
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
44-195 3.21e-05

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: 45.12  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  44 LNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKL-QPADIgaLILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVD- 121
Cdd:cd17927   15 LKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAgRKGKV--VFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENv 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 122 KNIKMFKNKNVniLVATPgrlfQIIQHE-KTLIARKMRTLQLLVIDEADR------FNEIQFEDHMREILSCIPKQRRTG 194
Cdd:cd17927   93 SVEQIVESSDV--IIVTP----QILVNDlKSGTIVSLSDFSLLVFDECHNttknhpYNEIMFRYLDQKLGSSGPLPQILG 166

                 .
gi 392895997 195 L 195
Cdd:cd17927  167 L 167
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
36-170 3.80e-05

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 44.81  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  36 QVLSGTHLLNLSDVVVeSPTGSGKTLAFVlpmmrMIQNAKLQPADIGALILSPSRELCSQIVSVIQPFAeKLNLTVETVT 115
Cdd:cd18035    7 QVLIAAVALNGNTLIV-LPTGLGKTIIAI-----LVAADRLTKKGGKVLILAPSRPLVEQHAENLKRVL-NIPDKITSLT 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392895997 116 GGQKVDKNIKMFKNKnvNILVATPgrlfQIIqhEKTLIARKM--RTLQLLVIDEADR 170
Cdd:cd18035   80 GEVKPEERAERWDAS--KIIVATP----QVI--ENDLLAGRItlDDVSLLIFDEAHH 128
DEXH_lig_assoc TIGR04121
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ...
54-167 4.18e-05

DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.


Pssm-ID: 274994 [Multi-domain]  Cd Length: 804  Bit Score: 46.39  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997   54 PTGSGKTLAFVLP-MMRMIQNAKLQPADIGALILSPSRELCSQIVSVIQPFAEKLNL--TVETVTGGQKVDKNIKMFKNK 130
Cdd:TIGR04121  36 PTGSGKTLAGFLPsLIDLAGPEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGLpiRVETRTGDTSSSERARQRKKP 115
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392895997  131 nVNILVATPGRLFQIIQHEKTliARKMRTLQLLVIDE 167
Cdd:TIGR04121 116 -PDILLTTPESLALLLSYPDA--ARLFKDLRCVVVDE 149
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
290-352 7.80e-05

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 43.02  E-value: 7.80e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392895997 290 HGKCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTAR 352
Cdd:cd18796   75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
PTZ00121 PTZ00121
MAEBL; Provisional
378-576 8.28e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 8.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  378 EKVKLDEIKVPTNNSRKSEELRQKM----IKIQVSDRAILEAGTRAFVSHVESYAKHDchlicslddlnvvGLANSYALL 453
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAeeakKKADAAKKKAEEAKKAAEAAKAEAEAAAD-------------EAEAAEEKA 1366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  454 RLPKMRELSQRKDLDMFDRSAIETSEIKYADVKLEANRETV--MKEKHEKKVETLAAKDKKRREKEARKLKKMGGRFRNG 531
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392895997  532 GGTGRKAEEKKA---LKRKAEEEDDAQNDIRLLKRIKRGKLSKKEIKD 576
Cdd:PTZ00121 1447 DEAKKKAEEAKKaeeAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
20-168 2.65e-04

DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations in RecQ2 cause Bloom syndrome.


Pssm-ID: 350774 [Multi-domain]  Cd Length: 208  Bit Score: 42.51  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  20 ELLEVFDKSY--KSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLPmmrmiqnAKLQPAdiGALILSPSRELcsqIV 97
Cdd:cd18016    4 EMMKIFHKKFglHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLP-------ACVSPG--VTVVISPLRSL---IV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  98 SVIQPFAEkLNLTVETVTGGQKVDKNIKMF-----KNKNVNILVATP------GRLFQIIQ--HEKTLIARkmrtlqlLV 164
Cdd:cd18016   72 DQVQKLTS-LDIPATYLTGDKTDAEATKIYlqlskKDPIIKLLYVTPekisasNRLISTLEnlYERKLLAR-------FV 143

                 ....
gi 392895997 165 IDEA 168
Cdd:cd18016  144 IDEA 147
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
302-363 4.57e-04

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: 40.80  E-value: 4.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392895997 302 IKAFSDSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTARcGREGNALILI 363
Cdd:cd18801   83 IEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVLL 143
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
302-352 6.09e-04

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: 40.27  E-value: 6.09e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392895997 302 IKAFSDSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRtAR 352
Cdd:cd18802   83 LDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-AR 132
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
48-355 7.58e-04

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 42.03  E-value: 7.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKT---LAFVLpmmrmiQNAKLQPADIGALILsPSRELcsqivsviqpfAEKLNLTVETVTGGQKVDKNI 124
Cdd:cd09639    1 LLVIEAPTGYGKTeaaLLWAL------HSLKSQKADRVIIAL-PTRAT-----------INAMYRRAKEAFGETGLYHSS 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 125 KMFKN------------------KNVNILVATP---GRLFQII--------QHEKTLIARkmrTLQLLVIDEADrfneiQ 175
Cdd:cd09639   63 ILSSRikemgdseefehlfplyiHSNDTLFLDPitvCTIDQVLksvfgefgHYEFTLASI---ANSLLIFDEVH-----F 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 176 FEDHMRE-ILSCIPKQRRTG----LFSATQVKeeddlmvFGLRNAKQVKVAQERNSAAPSTLKNYYVECRADEKTS---- 246
Cdd:cd09639  135 YDEYTLAlILAVLEVLKDNDvpilLMSATLPK-------FLKEYAEKIGYVEENEPLDLKPNERAPFIKIESDKVGeiss 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 247 --VCLEFIRQRtdKKILIFFPSCNSVRYFYKIFERCLGKRPLFAVHGKCSNPHRASQ----IKAFSDSTNGVMISTDVMA 320
Cdd:cd09639  208 leRLLEFIKKG--GSVAIIVNTVDRAQEFYQQLKEKGPEEEIMLIHSRFTEKDRAKKeaelLLEFKKSEKFVIVATQVIE 285
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 392895997 321 RGIDIsDIDWVIQFDLPKHSswFVHRAGRTARCGR 355
Cdd:cd09639  286 ASLDI-SVDVMITELAPIDS--LIQRLGRLHRYGE 317
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
302-573 1.14e-03

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 42.02  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 302 IKAFSDSTNGVMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTARcGREGNALILIA----------------- 364
Cdd:COG1111  404 LERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVVVLIAkgtrdeayywssrrkek 482
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 365 ---------SEQLAYVNFLDNHEKVK--LDEIKVPTN------NSRKSEELRQKMIKIQVSDRAILEAGTRafVSHvESY 427
Cdd:COG1111  483 kmksilkklKKLLDKQEKEKLKESAQatLDEFESIKElaedeiNEKDLDEIESSENGAHVDWREPVLLQVI--VST-LAE 559
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997 428 AKHDCHLICSLDDLNVVGLA-----NSYALLRLPKMRELSQRKDLDMFDRSAIETSEIKYADVKLEAnrETVMKEKHEKK 502
Cdd:COG1111  560 SLELRELGEKVDDEVNLILEidrvdVVDDGSVLRVSRLLVEIGELDGKTRVIIASYGDEYFDAILRL--TSKIKLPSLVS 637
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392895997 503 VETLAAKDKKRREKEARKLKKMGGRFRnGGGTGRKAEEKKALKRKAEEEDDAQNDIRLLKRIKRGKLSKKE 573
Cdd:COG1111  638 DISVDIPDLPIVEIVGEAVLCKKEDGS-REARFIKKERDLKGIRLAEGETLNDPLIELLRQQLYGEALREE 707
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
312-352 1.64e-03

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: 37.30  E-value: 1.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 392895997 312 VMISTDVMARGIDISDIDWVIQFDLPKHSSWFVHRAGRTAR 352
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
49-168 2.06e-03

C-terminal D[D/E]X[H/Q]-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: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 39.55  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  49 VVVESPTGSGKTLAFVLPMMRMIqnakLQPADIGALILSPSRELCSQIVSVIQP-FAEKLNLTVETVTGGQKVDknIKMF 127
Cdd:cd18021   22 VFVGAPTGSGKTVCAELALLRHW----RQNPKGRAVYIAPMQELVDARYKDWRAkFGPLLGKKVVKLTGETSTD--LKLL 95
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 392895997 128 KNKNVniLVATPGRLFQIIQHEKTliaRKM-RTLQLLVIDEA 168
Cdd:cd18021   96 AKSDV--ILATPEQWDVLSRRWKQ---RKNvQSVELFIADEL 132
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
20-168 2.58e-03

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: 39.44  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  20 ELLEVFDksYKSFTDVQVLSGTHLLNLSDVVVESPTGSGKTLAFVLP--MMRMIqnaklqpadigALILSP--S------ 89
Cdd:cd17920    3 ILKEVFG--YDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV-----------TLVVSPliSlmqdqv 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  90 RELCSQIVSviqpfAEKLNLTVeTVTGGQKVDKNIKMFKnknVNILVATPGRL-----FQIIQHektliARKMRTLQLLV 164
Cdd:cd17920   70 DRLQQLGIR-----AAALNSTL-SPEEKREVLLRIKNGQ---YKLLYVTPERLlspdfLELLQR-----LPERKRLALIV 135

                 ....
gi 392895997 165 IDEA 168
Cdd:cd17920  136 VDEA 139
DEXHc_POLQ-like cd18026
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ...
35-167 2.77e-03

DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.


Pssm-ID: 350784 [Multi-domain]  Cd Length: 202  Bit Score: 39.51  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  35 VQVLSGTHLLNLSDVVVESPTGSGKTL-AFVLPMMRMIQNAKLqpadigALILSPSRELCSQIVSVIQPFAEKLNLTVET 113
Cdd:cd18026   22 KECLSLPGLLEGRNLVYSLPTSGGKTLvAEILMLKRLLERRKK------ALFVLPYVSIVQEKVDALSPLFEELGFRVEG 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392895997 114 VTGGQkvdKNIKMFKNKNVNILVATPGRLFQIIQHektLIA-RKMRTLQLLVIDE 167
Cdd:cd18026   96 YAGNK---GRSPPKRRKSLSVAVCTIEKANSLVNS---LIEeGRLDELGLVVVDE 144
PTZ00121 PTZ00121
MAEBL; Provisional
472-575 3.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  472 RSAIETSEIKYADVKLEANRETVMKEKHEKKVETLAAKDKKRREKEARK---------LKKMGGRFRNGGGTGRKAEEKK 542
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeekkkadeAKKKAEEAKKADEAKKKAEEAK 1328
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392895997  543 ----ALKRKAEEEDDAQNDIRLLKRIKRGKLSKKEIK 575
Cdd:PTZ00121 1329 kkadAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
253-329 3.39e-03

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 40.24  E-value: 3.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392895997 253 RQRTDKKILIFFPSCNSVRYFYKIFERCLGKRPLFAVHgkCSNPHRASQIKAFSDSTNGVMISTDVMARGIDISDID 329
Cdd:COG4098  315 RLKEGRQLLIFVPTIELLEQLVALLQKLFPEERIAGVH--AEDPERKEKVQAFRDGEIPILVTTTILERGVTFPNVD 389
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
27-167 3.77e-03

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: 38.89  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  27 KSYKSFTDVQV-LSGTHLLNLSDVVVESPTGSGKTLAFVLPMMRMIQN-----AKLQPADIGALILSPSRELCSQIVSVI 100
Cdd:cd18019   13 EGFKSLNRIQSkLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKhrnpdGTINLDAFKIVYIAPMKALVQEMVGNF 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392895997 101 QPFAEKLNLTVETVTGGQKVDKNikmfKNKNVNILVATPgrlfqiiqhEK-TLIARK------MRTLQLLVIDE 167
Cdd:cd18019   93 SKRLAPYGITVAELTGDQQLTKE----QISETQIIVTTP---------EKwDIITRKsgdrtyTQLVRLIIIDE 153
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
43-167 4.36e-03

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 38.47  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  43 LLNLSDVVVESPTGSGKTLAFVLPMMRMIQNAKLqpadigALILSPSRELCSQivsVIQPFA--EKLNLTVETVTGgqkv 120
Cdd:cd18028   14 LLKGENLLISIPTASGKTLIAEMAMVNTLLEGGK------ALYLVPLRALASE---KYEEFKklEEIGLKVGISTG---- 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 392895997 121 DKNIKMFKNKNVNILVATPGRLFQIIQHEKTLIarkmRTLQLLVIDE 167
Cdd:cd18028   81 DYDEDDEWLGDYDIIVATYEKFDSLLRHSPSWL----RDVGVVVVDE 123
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
48-173 5.62e-03

N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 38.57  E-value: 5.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895997  48 DVVVESPTGSGKTLAFVLPMMRMI-----QNAKLQPADIGALILSPSRELCSQIVSVIQPFAEKLNLTVETVTGGQKVDK 122
Cdd:cd18020   19 NMLICAPTGAGKTNIAMLTILHEIrqhvnQGGVIKKDDFKIVYIAPMKALAAEMVEKFSKRLAPLGIKVKELTGDMQLTK 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392895997 123 NikmfKNKNVNILVATPGRlFQIIQHEKTLIARKMRTLQLLVIDEADRFNE 173
Cdd:cd18020   99 K----EIAETQIIVTTPEK-WDVVTRKSSGDVALSQLVRLLIIDEVHLLHD 144
 
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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