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Conserved domains on  [gi|187954459|gb|AAI41231|]
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DEAD (Asp-Glu-Ala-Asp) box polypeptide 18 [Mus musculus]

Protein Classification

DDX18/HAS1 family DEAD/DEAH box RNA helicase( domain architecture ID 13028608)

DDX18/HAS1 family DEAD/DEAH box containing ATP-dependent RNA helicase catalyzes the unwinding of RNA, such as fungal ATP-dependent RNA helicase HAS1 that is involved in 40S ribosomal subunit biogenesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
180-377 6.45e-143

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: 414.07  E-value: 6.45e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 180 TLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTGVLILSPTRELAMQTFG 259
Cdd:cd17942    1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 260 VLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFEEELKQ 339
Cdd:cd17942   81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 187954459 340 IIKLLPARRQTMLFSATQTRKVEDLARISLKKEPLYVG 377
Cdd:cd17942  161 IIKLLPKRRQTMLFSATQTRKVEDLARISLKKKPLYVG 198
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
390-520 5.28e-54

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: 180.78  E-value: 5.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 390 LEQGYVVCPS-EKRFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGI 468
Cdd:cd18787    1 IKQLYVVVEEeEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187954459 469 LLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARGlnGR-GHALLIL 520
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRA--GRkGTAITFV 131
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
552-609 2.80e-22

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: 90.15  E-value: 2.80e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 187954459  552 QSQLEKLIEKNYFLHKSAQEAYKSYIRAYDSHSLKQIFNVNNLNLPQVALSFGFKVPP 609
Cdd:pfam13959   1 QLQLEKLVLKDRELKELAQKAFVSYVRAYSKHLAKSIFNVKKLDLGHLAKSFGLLRAP 58
 
Name Accession Description Interval E-value
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
180-377 6.45e-143

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: 414.07  E-value: 6.45e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 180 TLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTGVLILSPTRELAMQTFG 259
Cdd:cd17942    1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 260 VLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFEEELKQ 339
Cdd:cd17942   81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 187954459 340 IIKLLPARRQTMLFSATQTRKVEDLARISLKKEPLYVG 377
Cdd:cd17942  161 IIKLLPKRRQTMLFSATQTRKVEDLARISLKKKPLYVG 198
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
167-533 1.05e-120

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 365.62  E-value: 1.05e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 167 TSFASLSnlVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIElivKLKFMPRNGTGVLI 246
Cdd:COG0513    2 MSFADLG--LSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQ---RLDPSRPRAPQALI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 247 LSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHM-QNTpgFMYKNLQCLVIDEA 325
Cdd:COG0513   77 LAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIeRGA--LDLSGVETLVLDEA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 326 DRILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARISLKkEPLYVGVDDDKevATVDGLEQGYVVCPSEKRFLL 405
Cdd:COG0513  155 DRMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPEN--ATAETIEQRYYLVDKRDKLEL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 406 LFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIPEVD 485
Cdd:COG0513  232 LRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVS 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187954459 486 WIVQYDPPDDPKEYIHRVGRTARGlnGR-GHALLILRPEELGFL----RYLKQ 533
Cdd:COG0513  312 HVINYDLPEDPEDYVHRIGRTGRA--GAeGTAISLVTPDERRLLraieKLIGQ 362
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
167-526 1.17e-70

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 236.62  E-value: 1.17e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 167 TSFASLsNLVNEnTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIE-LIVKlkfmpRNGTGVL 245
Cdd:PRK11776   4 TAFSTL-PLPPA-LLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQkLDVK-----RFRVQAL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 246 ILSPTRELAMQtfgVLKEL-----MTHHVHTYGLImGGSNRSAEVQKLLNGINIIVATPGRLLDHMQntpgfmyK----- 315
Cdd:PRK11776  77 VLCPTRELADQ---VAKEIrrlarFIPNIKVLTLC-GGVPMGPQIDSLEHGAHIIVGTPGRILDHLR-------Kgtldl 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 316 -NLQCLVIDEADRILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARiSLKKEPLYVGVDDDKEVATVdglEQGY 394
Cdd:PRK11776 146 dALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQ-RFQRDPVEVKVESTHDLPAI---EQRF 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 395 VVCPSEKRFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDV 474
Cdd:PRK11776 222 YEVSPDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDV 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 187954459 475 AARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARGLNgRGHALLILRPEELG 526
Cdd:PRK11776 302 AARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGS-KGLALSLVAPEEMQ 352
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
193-364 1.67e-60

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: 199.39  E-value: 1.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459  193 TEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKfmprNGTGVLILSPTRELAMQTFGVLKELMTHHVHTY 272
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD----NGPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459  273 GLIMGGSNRSAEVQKLlNGINIIVATPGRLLDHMQNTPGFmyKNLQCLVIDEADRILDVGFEEELKQIIKLLPARRQTML 352
Cdd:pfam00270  77 ASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 187954459  353 FSATQTRKVEDL 364
Cdd:pfam00270 154 LSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
390-520 5.28e-54

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: 180.78  E-value: 5.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 390 LEQGYVVCPS-EKRFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGI 468
Cdd:cd18787    1 IKQLYVVVEEeEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187954459 469 LLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARGlnGR-GHALLIL 520
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRA--GRkGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
184-372 2.35e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 168.44  E-value: 2.35e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459   184 IEEMGFKRMTEIQHKSIRPLLEG-RDLLAAAKTGSGKTLAFLIPVIELIvklkfMPRNGTGVLILSPTRELAMQTFGVLK 262
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-----KRGKGGRVLVLVPTRELAEQWAEELK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459   263 ELMTHHVHTYGLIMGGSNRSAEVQKLLNG-INIIVATPGRLLDHMQNTPgFMYKNLQCLVIDEADRILDVGFEEELKQII 341
Cdd:smart00487  76 KLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDK-LSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190
                   ....*....|....*....|....*....|.
gi 187954459   342 KLLPARRQTMLFSATQTRKVEDLARISLKKE 372
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDP 185
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
401-508 4.97e-29

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: 111.15  E-value: 4.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459  401 KRFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYeLLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLD 480
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100
                  ....*....|....*....|....*...
gi 187954459  481 IPEVDWIVQYDPPDDPKEYIHRVGRTAR 508
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGR 107
HELICc smart00490
helicase superfamily c-terminal domain;
429-508 3.42e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 96.51  E-value: 3.42e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459   429 KYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTAR 508
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
552-609 2.80e-22

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: 90.15  E-value: 2.80e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 187954459  552 QSQLEKLIEKNYFLHKSAQEAYKSYIRAYDSHSLKQIFNVNNLNLPQVALSFGFKVPP 609
Cdd:pfam13959   1 QLQLEKLVLKDRELKELAQKAFVSYVRAYSKHLAKSIFNVKKLDLGHLAKSFGLLRAP 58
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
410-513 2.06e-09

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 60.51  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 410 LKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQ--------KQNKRTTTFFQFCNADSGILLCTDVAARGLDI 481
Cdd:COG1111  348 LGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQAskegdkglTQKEQIEILERFRAGEFNVLVATSVAEEGLDI 427
                         90       100       110
                 ....*....|....*....|....*....|....
gi 187954459 482 PEVDWIVQYDPPddPKE--YIHRVGRTARGLNGR 513
Cdd:COG1111  428 PEVDLVIFYEPV--PSEirSIQRKGRTGRKREGR 459
PRK13766 PRK13766
Hef nuclease; Provisional
410-518 1.89e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 51.03  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 410 LKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGK----------QKQNKRTTTffQFCNADSGILLCTDVAARGL 479
Cdd:PRK13766 360 LGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgmsQKEQIEILD--KFRAGEFNVLVSTSVAEEGL 437
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 187954459 480 DIPEVDWIVQYDPPddPKE--YIHRVGRTARGLNGRGHALL 518
Cdd:PRK13766 438 DIPSVDLVIFYEPV--PSEirSIQRKGRTGRQEEGRVVVLI 476
 
Name Accession Description Interval E-value
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
180-377 6.45e-143

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: 414.07  E-value: 6.45e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 180 TLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTGVLILSPTRELAMQTFG 259
Cdd:cd17942    1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 260 VLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFEEELKQ 339
Cdd:cd17942   81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 187954459 340 IIKLLPARRQTMLFSATQTRKVEDLARISLKKEPLYVG 377
Cdd:cd17942  161 IIKLLPKRRQTMLFSATQTRKVEDLARISLKKKPLYVG 198
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
167-533 1.05e-120

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 365.62  E-value: 1.05e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 167 TSFASLSnlVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIElivKLKFMPRNGTGVLI 246
Cdd:COG0513    2 MSFADLG--LSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQ---RLDPSRPRAPQALI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 247 LSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHM-QNTpgFMYKNLQCLVIDEA 325
Cdd:COG0513   77 LAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIeRGA--LDLSGVETLVLDEA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 326 DRILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARISLKkEPLYVGVDDDKevATVDGLEQGYVVCPSEKRFLL 405
Cdd:COG0513  155 DRMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPEN--ATAETIEQRYYLVDKRDKLEL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 406 LFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIPEVD 485
Cdd:COG0513  232 LRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVS 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187954459 486 WIVQYDPPDDPKEYIHRVGRTARGlnGR-GHALLILRPEELGFL----RYLKQ 533
Cdd:COG0513  312 HVINYDLPEDPEDYVHRIGRTGRA--GAeGTAISLVTPDERRLLraieKLIGQ 362
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
180-378 5.34e-93

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: 285.72  E-value: 5.34e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 180 TLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTGVLILSPTRELAMQTFG 259
Cdd:cd17941    1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 260 VLKELMTHHVHTYGLIMGGSNRSAEvQKLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFEEELKQ 339
Cdd:cd17941   81 VLRKVGKYHSFSAGLIIGGKDVKEE-KERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 187954459 340 IIKLLPARRQTMLFSATQTRKVEDLARISLkKEPLYVGV 378
Cdd:cd17941  160 IVENLPKSRQTLLFSATQTKSVKDLARLSL-KNPEYISV 197
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
180-376 2.86e-83

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: 260.45  E-value: 2.86e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 180 TLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTGVLILSPTRELAMQTFG 259
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 260 VLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPgFMYKNLQCLVIDEADRILDVGFEEELKQ 339
Cdd:cd00268   81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGK-LDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 187954459 340 IIKLLPARRQTMLFSATQTRKVEDLARISLkKEPLYV 376
Cdd:cd00268  160 ILSALPKDRQTLLFSATLPEEVKELAKKFL-KNPVRI 195
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
181-371 6.24e-75

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: 238.69  E-value: 6.24e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIElivKLKFMPRN--GTGVLILSPTRELAMQTF 258
Cdd:cd17947    2 LRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILE---RLLYRPKKkaATRVLVLVPTRELAMQCF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 259 GVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFEEELK 338
Cdd:cd17947   79 SVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELK 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 187954459 339 QIIKLLPARRQTMLFSATQTRKVEDLARISLKK 371
Cdd:cd17947  159 EILRLCPRTRQTMLFSATMTDEVKDLAKLSLNK 191
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
176-376 3.69e-72

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: 232.09  E-value: 3.69e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 176 VNENTLKAIEEMGFKRMTEIQHKSIRPLLE-GRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGT-GVLILSPTREL 253
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGvSALIISPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 254 AMQTFGVLKELMTHH----VHTyglIMGGSNRSAEVQKL-LNGINIIVATPGRLLDHMQNtPGF--MYKNLQCLVIDEAD 326
Cdd:cd17964   81 ALQIAAEAKKLLQGLrklrVQS---AVGGTSRRAELNRLrRGRPDILVATPGRLIDHLEN-PGVakAFTDLDYLVLDEAD 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 187954459 327 RILDVGFEEELKQIIKLLPAR----RQTMLFSATQTRKVEDLARISLKKEPLYV 376
Cdd:cd17964  157 RLLDMGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
167-526 1.17e-70

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 236.62  E-value: 1.17e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 167 TSFASLsNLVNEnTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIE-LIVKlkfmpRNGTGVL 245
Cdd:PRK11776   4 TAFSTL-PLPPA-LLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQkLDVK-----RFRVQAL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 246 ILSPTRELAMQtfgVLKEL-----MTHHVHTYGLImGGSNRSAEVQKLLNGINIIVATPGRLLDHMQntpgfmyK----- 315
Cdd:PRK11776  77 VLCPTRELADQ---VAKEIrrlarFIPNIKVLTLC-GGVPMGPQIDSLEHGAHIIVGTPGRILDHLR-------Kgtldl 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 316 -NLQCLVIDEADRILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARiSLKKEPLYVGVDDDKEVATVdglEQGY 394
Cdd:PRK11776 146 dALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQ-RFQRDPVEVKVESTHDLPAI---EQRF 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 395 VVCPSEKRFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDV 474
Cdd:PRK11776 222 YEVSPDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDV 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 187954459 475 AARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARGLNgRGHALLILRPEELG 526
Cdd:PRK11776 302 AARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGS-KGLALSLVAPEEMQ 352
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
185-377 9.89e-67

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: 217.84  E-value: 9.89e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 185 EEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFM-PRN-GTGVLILSPTRELAMQTFGVLK 262
Cdd:cd17949    7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvDRSdGTLALVLVPTRELALQIYEVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 263 ELM--THHVHTyGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFEEELKQI 340
Cdd:cd17949   87 KLLkpFHWIVP-GYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKI 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 187954459 341 IKLL-------------PARRQTMLFSATQTRKVEDLARISLKKePLYVG 377
Cdd:cd17949  166 LELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKD-PVYID 214
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
177-509 1.07e-63

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 217.12  E-value: 1.07e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 177 NENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIvkLKFmPRNGTG---VLILSPTREL 253
Cdd:PRK11192   9 DESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL--LDF-PRRKSGpprILILTPTREL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 254 AMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTpGFMYKNLQCLVIDEADRILDVGF 333
Cdd:PRK11192  86 AMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEE-NFDCRAVETLILDEADRMLDMGF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 334 EEELKQIIKLLPARRQTMLFSAT-QTRKVEDLARiSLKKEPLYVGVDDD-KEVATVdglEQGYVVCPS-EKRFLLLFTFL 410
Cdd:PRK11192 165 AQDIETIAAETRWRKQTLLFSATlEGDAVQDFAE-RLLNDPVEVEAEPSrRERKKI---HQWYYRADDlEHKTALLCHLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 411 KKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQY 490
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
                        330
                 ....*....|....*....
gi 187954459 491 DPPDDPKEYIHRVGRTARG 509
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRA 339
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
180-369 2.05e-63

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: 208.58  E-value: 2.05e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 180 TLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLK-FMPRNGTGVLILSPTRELAMQTF 258
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKaNLKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 259 GVLKELMTHH--VHTYGLIMGGSNRSAEVQKLL-NGINIIVATPGRLLDHMQN-TPGFMYKNLQCLVIDEADRILDVGFE 334
Cdd:cd17960   81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRkADKVKVKSLEVLVLDEADRLLDLGFE 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 187954459 335 EELKQIIKLLPARRQTMLFSATQTRKVEDLARISL 369
Cdd:cd17960  161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGL 195
PTZ00110 PTZ00110
helicase; Provisional
164-558 7.39e-62

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 215.41  E-value: 7.39e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 164 FEDTSFASLsnlvnenTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIP-VIELIVKLKFMPRNGT 242
Cdd:PTZ00110 132 FEYTSFPDY-------ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaIVHINAQPLLRYGDGP 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 243 GVLILSPTRELAMQ------TFGVLKELmtHHVHTYGlimgGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTpgfmYKN 316
Cdd:PTZ00110 205 IVLVLAPTRELAEQireqcnKFGASSKI--RNTVAYG----GVPKRGQIYALRRGVEILIACPGRLIDFLESN----VTN 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 317 LQ---CLVIDEADRILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARISLKKEPLYVGVDDdKEVATVDGLEQG 393
Cdd:PTZ00110 275 LRrvtYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGS-LDLTACHNIKQE 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 394 -YVVCPSEKRfLLLFTFLKK--NRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILL 470
Cdd:PTZ00110 354 vFVVEEHEKR-GKLKMLLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMI 432
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 471 CTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARGlNGRGHALLILRPEELGFLRYLKQSKVPLNQfdfswskvsD 550
Cdd:PTZ00110 433 ATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRA-GAKGASYTFLTPDKYRLARDLVKVLREAKQ---------P 502

                 ....*...
gi 187954459 551 IQSQLEKL 558
Cdd:PTZ00110 503 VPPELEKL 510
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
168-529 3.19e-61

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 211.21  E-value: 3.19e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 168 SFASLSnlVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMP--RNGTGVL 245
Cdd:PRK10590   2 SFDSLG--LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAkgRRPVRAL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 246 ILSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDhMQNTPGFMYKNLQCLVIDEA 325
Cdd:PRK10590  80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 326 DRILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARiSLKKEPLYVGVDDdKEVATVDGLEQGYVVCPSEKRFLL 405
Cdd:PRK10590 159 DRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAE-KLLHNPLEIEVAR-RNTASEQVTQHVHFVDKKRKRELL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 406 LFtFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIPEVD 485
Cdd:PRK10590 237 SQ-MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELP 315
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 187954459 486 WIVQYDPPDDPKEYIHRVGRTARGlNGRGHALLILRPEELGFLR 529
Cdd:PRK10590 316 HVVNYELPNVPEDYVHRIGRTGRA-AATGEALSLVCVDEHKLLR 358
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
193-364 1.67e-60

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: 199.39  E-value: 1.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459  193 TEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKfmprNGTGVLILSPTRELAMQTFGVLKELMTHHVHTY 272
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD----NGPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459  273 GLIMGGSNRSAEVQKLlNGINIIVATPGRLLDHMQNTPGFmyKNLQCLVIDEADRILDVGFEEELKQIIKLLPARRQTML 352
Cdd:pfam00270  77 ASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 187954459  353 FSATQTRKVEDL 364
Cdd:pfam00270 154 LSATLPRNLEDL 165
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
168-371 3.96e-60

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: 199.85  E-value: 3.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 168 SFASLSnlVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIE--LIVKLKFMprngtgVL 245
Cdd:cd17954    1 TFKELG--VCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQalLENPQRFF------AL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 246 ILSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEA 325
Cdd:cd17954   73 VLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEA 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 187954459 326 DRILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARISLKK 371
Cdd:cd17954  153 DRLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKN 198
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
93-508 1.99e-57

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 201.68  E-value: 1.99e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459  93 LANGEAAPTPPPDSEVKKKKKKKRKmANDAGPDTKKAKTEESAEACEEPEDDVKKADDSEVPSLPLGLtgafED------ 166
Cdd:PRK01297   9 FGKGEAEQPAPAPPSPAAAPAPPPP-AKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKPKPASLWKL----EDfvvepq 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 167 ---TSFASLsNLVNEnTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIV-----KLKFM- 237
Cdd:PRK01297  84 egkTRFHDF-NLAPE-LMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLqtpppKERYMg 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 238 -PRngtgVLILSPTRELAMQTFGVLKELMTH---HVHTYgliMGGSNRSAEVQKL-LNGINIIVATPGRLLDHMQNTPGF 312
Cdd:PRK01297 162 ePR----ALIIAPTRELVVQIAKDAAALTKYtglNVMTF---VGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVH 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 313 MyKNLQCLVIDEADRILDVGFEEELKQIIKLLP--ARRQTMLFSATQTRKVEDLARiSLKKEPLYVGVDddKEVATVDGL 390
Cdd:PRK01297 235 L-DMVEVMVLDEADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAK-QWTTDPAIVEIE--PENVASDTV 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 391 EQG-YVVCPSEKrFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGIL 469
Cdd:PRK01297 311 EQHvYAVAGSDK-YKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVL 389
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 187954459 470 LCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTAR 508
Cdd:PRK01297 390 VATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGR 428
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
168-376 2.80e-55

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: 187.13  E-value: 2.80e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 168 SFASLSnlVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIElivKLK-FMPRNGTGVLI 246
Cdd:cd17959    2 GFQSMG--LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIE---KLKaHSPTVGARALI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 247 LSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTpGFMYKNLQCLVIDEAD 326
Cdd:cd17959   77 LSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDEAD 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 187954459 327 RILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARISLkKEPLYV 376
Cdd:cd17959  156 RLFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGL-NEPVLI 204
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
166-508 9.65e-55

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 192.88  E-value: 9.65e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 166 DTSFASLSnlVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLI---------PVIELivKLKF 236
Cdd:PRK04837   7 EQKFSDFA--LHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTatfhyllshPAPED--RKVN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 237 MPRngtgVLILSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHM-QNTpgFMYK 315
Cdd:PRK04837  83 QPR----ALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAkQNH--INLG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 316 NLQCLVIDEADRILDVGFeeeLKQIIKLL-----PARRQTMLFSATQTRKVEDLARISLKkEPLYVGVDDDKEVATVDGL 390
Cdd:PRK04837 157 AIQVVVLDEADRMFDLGF---IKDIRWLFrrmppANQRLNMLFSATLSYRVRELAFEHMN-NPEYVEVEPEQKTGHRIKE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 391 EQGYvvcPS-EKRFLLLFTFLKKNRKKKVMVFFS---SCMSVKYHYE-------LLNyidlpvlaihGKQKQNKRTTTFF 459
Cdd:PRK04837 233 ELFY---PSnEEKMRLLQTLIEEEWPDRAIIFANtkhRCEEIWGHLAadghrvgLLT----------GDVAQKKRLRILE 299
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 187954459 460 QFCNADSGILLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTAR 508
Cdd:PRK04837 300 EFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGR 348
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
390-520 5.28e-54

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: 180.78  E-value: 5.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 390 LEQGYVVCPS-EKRFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGI 468
Cdd:cd18787    1 IKQLYVVVEEeEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187954459 469 LLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARGlnGR-GHALLIL 520
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRA--GRkGTAITFV 131
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
166-517 3.96e-52

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 189.39  E-value: 3.96e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 166 DTSFASLSnlVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVI-ELIVKLKFMPRNGTG- 243
Cdd:PRK04537   8 DLTFSSFD--LHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMnRLLSRPALADRKPEDp 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 244 -VLILSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVI 322
Cdd:PRK04537  86 rALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 323 DEADRILDVGFEEELKQIIKLLPAR--RQTMLFSATQTRKVEDLARISLKK-EPLYVgvddDKEVATVDGLEQGYVVCPS 399
Cdd:PRK04537 166 DEADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEpEKLVV----ETETITAARVRQRIYFPAD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 400 EKRFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGL 479
Cdd:PRK04537 242 EEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGL 321
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 187954459 480 DIPEVDWIVQYDPPDDPKEYIHRVGRTARgLNGRGHAL 517
Cdd:PRK04537 322 HIDGVKYVYNYDLPFDAEDYVHRIGRTAR-LGEEGDAI 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
166-529 8.45e-52

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 189.29  E-value: 8.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 166 DTSFASLSnlVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRngtgVL 245
Cdd:PRK11634   5 ETTFADLG--LKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQ----IL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 246 ILSPTRELAMQTFGVLKELmTHHVHTYGLIM--GGSNRSAEVQKLLNGINIIVATPGRLLDHMQNtpGFM-YKNLQCLVI 322
Cdd:PRK11634  79 VLAPTRELAVQVAEAMTDF-SKHMRGVNVVAlyGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKR--GTLdLSKLSGLVL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 323 DEADRILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARiSLKKEPLYVGVDddKEVATVDGLEQGYVVCPSEKR 402
Cdd:PRK11634 156 DEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITR-RFMKEPQEVRIQ--SSVTTRPDISQSYWTVWGMRK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 403 FLLLFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIP 482
Cdd:PRK11634 233 NEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVE 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 187954459 483 EVDWIVQYDPPDDPKEYIHRVGRTARGlnGR-GHALLILRPEELGFLR 529
Cdd:PRK11634 313 RISLVVNYDIPMDSESYVHRIGRTGRA--GRaGRALLFVENRERRLLR 358
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
181-364 1.74e-51

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: 177.01  E-value: 1.74e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFM--PRNGTGVLILSPTRELAMQTF 258
Cdd:cd17961    6 LKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAEsgEEQGTRALILVPTRELAQQVS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 259 GVLKELMTH---HVHTYGLimgGSNRSAEVQK-LLNGI-NIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGF 333
Cdd:cd17961   86 KVLEQLTAYcrkDVRVVNL---SASSSDSVQRaLLAEKpDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSYGY 162
                        170       180       190
                 ....*....|....*....|....*....|.
gi 187954459 334 EEELKQIIKLLPARRQTMLFSATQTRKVEDL 364
Cdd:cd17961  163 EEDLKSLLSYLPKNYQTFLMSATLSEDVEAL 193
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
168-366 3.06e-51

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


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 176.91  E-value: 3.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 168 SFAS--LSNLVNENtlkaIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTG-- 243
Cdd:cd17967    1 SFEEagLRELLLEN----IKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRrk 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 244 ----VLILSPTRELAMQTFGVLKELmthhvhTYGLIM------GGSNRSAEVQKLLNGINIIVATPGRLLDHMQNtpGF- 312
Cdd:cd17967   77 aypsALILAPTRELAIQIYEEARKF------SYRSGVrsvvvyGGADVVHQQLQLLRGCDILVATPGRLVDFIER--GRi 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 187954459 313 MYKNLQCLVIDEADRILDVGFEEELKQII--KLLPAR--RQTMLFSATQTRKVEDLAR 366
Cdd:cd17967  149 SLSSIKFLVLDEADRMLDMGFEPQIRKIVehPDMPPKgeRQTLMFSATFPREIQRLAA 206
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
169-376 3.44e-50

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: 173.18  E-value: 3.44e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 169 FASLSnlVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKlkfmprNGTGV--LI 246
Cdd:cd17955    1 FEDLG--LSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSE------DPYGIfaLV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 247 LSPTRELAMQ---TFGVLKELMthHVHTyGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPG--FMYKNLQCLV 321
Cdd:cd17955   73 LTPTRELAYQiaeQFRALGAPL--GLRC-CVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVKFLV 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 187954459 322 IDEADRILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARISLKKEPLYV 376
Cdd:cd17955  150 LDEADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
PTZ00424 PTZ00424
helicase 45; Provisional
168-529 6.19e-49

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 176.17  E-value: 6.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 168 SFASLSnlVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELI-VKLkfmprNGTGVLI 246
Cdd:PTZ00424  29 SFDALK--LNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIdYDL-----NACQALI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 247 LSPTRELAMQTFGVLKELMTH-HVHTYGLImGGSNRSAEVQKLLNGINIIVATPGRLLDhMQNTPGFMYKNLQCLVIDEA 325
Cdd:PTZ00424 102 LAPTRELAQQIQKVVLALGDYlKVRCHACV-GGTVVRDDINKLKAGVHMVVGTPGRVYD-MIDKRHLRVDDLKLFILDEA 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 326 DRILDVGFEEELKQIIKLLPARRQTMLFSATQ--------TRKVEDLARISLKKEPLyvgvdddkevaTVDGLEQGYVVC 397
Cdd:PTZ00424 180 DEMLSRGFKGQIYDVFKKLPPDVQVALFSATMpneileltTKFMRDPKRILVKKDEL-----------TLEGIRQFYVAV 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 398 PSEK-RFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAA 476
Cdd:PTZ00424 249 EKEEwKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLA 328
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187954459 477 RGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARgLNGRGHALLILRPEELGFLR 529
Cdd:PTZ00424 329 RGIDVQQVSLVINYDLPASPENYIHRIGRSGR-FGRKGVAINFVTPDDIEQLK 380
DEXDc smart00487
DEAD-like helicases superfamily;
184-372 2.35e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 168.44  E-value: 2.35e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459   184 IEEMGFKRMTEIQHKSIRPLLEG-RDLLAAAKTGSGKTLAFLIPVIELIvklkfMPRNGTGVLILSPTRELAMQTFGVLK 262
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-----KRGKGGRVLVLVPTRELAEQWAEELK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459   263 ELMTHHVHTYGLIMGGSNRSAEVQKLLNG-INIIVATPGRLLDHMQNTPgFMYKNLQCLVIDEADRILDVGFEEELKQII 341
Cdd:smart00487  76 KLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDK-LSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190
                   ....*....|....*....|....*....|.
gi 187954459   342 KLLPARRQTMLFSATQTRKVEDLARISLKKE 372
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDP 185
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
181-376 4.42e-48

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: 168.27  E-value: 4.42e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPR----NGTGVLILSPTRELAMQ 256
Cdd:cd17945    2 LRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEetkdDGPYALILAPTRELAQQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 257 TFGVLKELMTHhvhtYGL----IMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTpgfmYKNL-QC--LVIDEADRIL 329
Cdd:cd17945   82 IEEETQKFAKP----LGIrvvsIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERR----LLVLnQCtyVVLDEADRMI 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187954459 330 DVGFEEELKQIIKLLP--------------------ARRQTMLFSATQTRKVEDLARISLKKePLYV 376
Cdd:cd17945  154 DMGFEPQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRR-PVVV 219
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
181-376 2.05e-44

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: 157.89  E-value: 2.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVI----ELIVKLKFMPRNGTGVLILSPTRELAMQ 256
Cdd:cd17951    2 LKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfalEQEKKLPFIKGEGPYGLIVCPSRELARQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 257 TFGVLkELMTHHVHTYG-------LIMGGSNRSAEVQKLLNGINIIVATPGRLLDhMQNTPGFMYKNLQCLVIDEADRIL 329
Cdd:cd17951   82 THEVI-EYYCKALQEGGypqlrclLCIGGMSVKEQLEVIRKGVHIVVATPGRLMD-MLNKKKINLDICRYLCLDEADRMI 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 187954459 330 DVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARISLKKePLYV 376
Cdd:cd17951  160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVK-PVTV 205
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
181-366 1.36e-42

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: 152.36  E-value: 1.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKlkfmPRNGTGV--LILSPTRELAMQTF 258
Cdd:cd17957    2 LNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK----PRKKKGLraLILAPTRELASQIY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 259 GVLKELMTHH-VHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMyKNLQCLVIDEADRILDVGFEEEL 337
Cdd:cd17957   78 RELLKLSKGTgLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDL-SSVEYLVLDEADKLFEPGFREQT 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 187954459 338 KQIIKLLPARR-QTMLFSATQTRKVEDLAR 366
Cdd:cd17957  157 DEILAACTNPNlQRSLFSATIPSEVEELAR 186
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
181-372 1.50e-42

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: 153.55  E-value: 1.50e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRP-LLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTGV-----LILSPTRELA 254
Cdd:cd17946    2 LRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQkplraLILTPTRELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 255 MQTFGVLKELMTHHVHTYGLIMGGsnRSAEVQK--LLNGINIIVATPGRLLDHMQNTPGFM--YKNLQCLVIDEADRILD 330
Cdd:cd17946   82 VQVKDHLKAIAKYTNIKIASIVGG--LAVQKQErlLKKRPEIVVATPGRLWELIQEGNEHLanLKSLRFLVLDEADRMLE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 187954459 331 VGFEEELKQIIKLLPA-------RRQTMLFSATQTRKVEDLARISLKKE 372
Cdd:cd17946  160 KGHFAELEKILELLNKdragkkrKRQTFVFSATLTLDHQLPLKLNSKKK 208
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
181-370 8.15e-42

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: 150.21  E-value: 8.15e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPR-NGTGVLILSPTRELAMQtfg 259
Cdd:cd17966    2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERgDGPIVLVLAPTRELAQQ--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 260 vLKELMTHHVHTYGL----IMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMyKNLQCLVIDEADRILDVGFEE 335
Cdd:cd17966   79 -IQQEANKFGGSSRLrntcVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNL-RRVTYLVLDEADRMLDMGFEP 156
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 187954459 336 ELKQIIKLLPARRQTMLFSATQTRKVEDLARISLK 370
Cdd:cd17966  157 QIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLK 191
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
181-376 1.16e-41

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: 150.86  E-value: 1.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLEG---------RDLLAAAKTGSGKTLAFLIPVIELIVKlKFMPRngTGVLILSPTR 251
Cdd:cd17956    2 LKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSK-RVVPR--LRALIVVPTK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 252 ELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAE--------VQKLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVID 323
Cdd:cd17956   79 ELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEqklllvdtSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFLVID 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187954459 324 EADRILDVGFEEELKQIIKLLPARR--------------------QTMLFSATQTRKVEDLARISLKKEPLYV 376
Cdd:cd17956  159 EADRLLNQSFQDWLETVMKALGRPTapdlgsfgdanllersvrplQKLLFSATLTRDPEKLSSLKLHRPRLFT 231
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
176-371 1.17e-41

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: 150.61  E-value: 1.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 176 VNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIV-KLKFMPRNGTGVLILSPTRELA 254
Cdd:cd17953   19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKdQRPVKPGEGPIGLIMAPTRELA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 255 MQTFGVLKELMThhvhTYGL----IMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMyKNLQ---CLVIDEADR 327
Cdd:cd17953   99 LQIYVECKKFSK----ALGLrvvcVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRV-TNLRrvtYVVLDEADR 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 187954459 328 ILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARISLKK 371
Cdd:cd17953  174 MFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHK 217
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
181-371 1.74e-41

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: 149.37  E-value: 1.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIvklkFMPRNGTGVLILSPTRELAMQTFGV 260
Cdd:cd17940   11 LMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI----DPKKDVIQALILVPTRELALQTSQV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 261 LKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMyKNLQCLVIDEADRILDVGFEEELKQI 340
Cdd:cd17940   87 CKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADL-SHCKTLVLDEADKLLSQDFQPIIEKI 165
                        170       180       190
                 ....*....|....*....|....*....|.
gi 187954459 341 IKLLPARRQTMLFSATQTRKVEDLARISLKK 371
Cdd:cd17940  166 LNFLPKERQILLFSATFPLTVKNFMDRHMHN 196
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
177-356 6.45e-40

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: 145.16  E-value: 6.45e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 177 NENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVklkfMPRNGTGVLILSPTRELAMQ 256
Cdd:cd17939    5 SEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRID----TTVRETQALVLAPTRELAQQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 257 TFGVLKEL---MTHHVHtygLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTpGFMYKNLQCLVIDEADRILDVGF 333
Cdd:cd17939   81 IQKVVKALgdyMGVKVH---ACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRR-SLRTDKIKMFVLDEADEMLSRGF 156
                        170       180
                 ....*....|....*....|...
gi 187954459 334 EEELKQIIKLLPARRQTMLFSAT 356
Cdd:cd17939  157 KDQIYDIFQFLPPETQVVLFSAT 179
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
167-378 5.80e-39

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: 144.72  E-value: 5.80e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 167 TSF--ASLSNLVNENTLKAieemGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIElivklKFMPRNGTG- 243
Cdd:cd18052   43 LTFeeANLCETLLKNIRKA----GYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLT-----GMMKEGLTAs 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 244 ---------VLILSPTRELAMQTFgvlKEL-------MTHHVHTYglimGGSNRSAEVQKLLNGINIIVATPGRLLDHMq 307
Cdd:cd18052  114 sfsevqepqALIVAPTRELANQIF---LEArkfsygtCIRPVVVY----GGVSVGHQIRQIEKGCHILVATPGRLLDFI- 185
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187954459 308 nTPGFMY-KNLQCLVIDEADRILDVGFEEELKQIIKLL--PA--RRQTMLFSATQTRKVEDLARISLKKEPLYVGV 378
Cdd:cd18052  186 -GRGKISlSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmPSkeDRQTLMFSATFPEEIQRLAAEFLKEDYLFLTV 260
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
181-376 7.79e-39

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: 141.83  E-value: 7.79e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIP-VIELIVKL-KFMPRNGTGVLILSPTRELAMQTF 258
Cdd:cd17958    2 MKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQPiPREQRNGPGVLVLTPTRELALQIE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 259 GVLKELMTHHVHTYgLIMGGSNRSAEVQKLLNGINIIVATPGRLLDhMQNTPGFMYKNLQCLVIDEADRILDVGFEEELK 338
Cdd:cd17958   82 AECSKYSYKGLKSV-CVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 187954459 339 QIIKLLPARRQTMLFSATQTRKVEDLARiSLKKEPLYV 376
Cdd:cd17958  160 KILLDIRPDRQTIMTSATWPDGVRRLAQ-SYLKDPMIV 196
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
181-366 2.91e-38

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: 140.24  E-value: 2.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFM-PRNGTGVLILSPTRELAMQTFG 259
Cdd:cd17952    2 LNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELeKGEGPIAVIVAPTRELAQQIYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 260 VLKELmthhVHTYGL----IMGGSNRSAEVQKLLNGINIIVATPGRLLDH--MQNTpgfmykNLQ---CLVIDEADRILD 330
Cdd:cd17952   82 EAKKF----GKAYNLrvvaVYGGGSKWEQAKALQEGAEIVVATPGRLIDMvkKKAT------NLQrvtYLVLDEADRMFD 151
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 187954459 331 VGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLAR 366
Cdd:cd17952  152 MGFEYQVRSIVGHVRPDRQTLLFSATFKKKIEQLAR 187
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
178-523 2.91e-38

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 148.78  E-value: 2.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 178 ENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKF---MPRNGTGVLILSPTRELA 254
Cdd:PLN00206 130 PKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSghpSEQRNPLAMVLTPTRELC 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 255 MQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLD----HMQNTPGFMyknlqCLVIDEADRILD 330
Cdd:PLN00206 210 VQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDllskHDIELDNVS-----VLVLDEVDCMLE 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 331 VGFEEELKQIIKLLPaRRQTMLFSATQTRKVEDLARiSLKKEPLYVGVDDDKevATVDGLEQGYVVCPSEKRFLLLFTFL 410
Cdd:PLN00206 285 RGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFAS-SLAKDIILISIGNPN--RPNKAVKQLAIWVETKQKKQKLFDIL 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 411 K-KNR-KKKVMVFFSSCMSVkyhyELL-NYID----LPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIPE 483
Cdd:PLN00206 361 KsKQHfKPPAVVFVSSRLGA----DLLaNAITvvtgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 187954459 484 VDWIVQYDPPDDPKEYIHRVGRTARgLNGRGHALLILRPE 523
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASR-MGEKGTAIVFVNEE 475
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
164-366 4.67e-36

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: 135.94  E-value: 4.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 164 FEDtsfASLSNLVNENtlkaIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKL---KFMPRN 240
Cdd:cd18051   23 FSD---LDLGEIIRNN----IELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgESLPSE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 241 GTG---------VLILSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPG 311
Cdd:cd18051   96 SGYygrrkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKI 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 187954459 312 FMyKNLQCLVIDEADRILDVGFEEELKQIIK--LLPAR--RQTMLFSATQTRKVEDLAR 366
Cdd:cd18051  176 GL-DYCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPKEIQMLAR 233
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
182-356 7.22e-36

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: 133.99  E-value: 7.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 182 KAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVklkfmprngtgVLILSPTRELAMQT---F 258
Cdd:cd17938   12 KAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV-----------ALILEPSRELAEQTyncI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 259 GVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDhMQNTPGFMYKNLQCLVIDEADRILDVGFEEELK 338
Cdd:cd17938   81 ENFKKYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLED-LIKTGKLDLSSVRFFVLDEADRLLSQGNLETIN 159
                        170       180
                 ....*....|....*....|....
gi 187954459 339 QIIKLLPA------RRQTMLFSAT 356
Cdd:cd17938  160 RIYNRIPKitsdgkRLQVIVCSAT 183
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
184-376 5.66e-35

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: 131.13  E-value: 5.66e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 184 IEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVielIVKLKFMPRNGTGvLILSPTRELAMQTFGVLKE 263
Cdd:cd17962    5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPV---IIRCLTEHRNPSA-LILTPTRELAVQIEDQAKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 264 LMTHHVH-TYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDhMQNTPGFMYKNLQCLVIDEADRILDVGFEEELKQIIK 342
Cdd:cd17962   81 LMKGLPPmKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLD-ILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILE 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 187954459 343 LLPARRQTMLFSATQTRKVEDLARiSLKKEPLYV 376
Cdd:cd17962  160 NISHDHQTILVSATIPRGIEQLAG-QLLQNPVRI 192
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
178-366 2.56e-34

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: 129.49  E-value: 2.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 178 ENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELI-VKLKfmprnGTGVLILSPTRELAMQ 256
Cdd:cd18046    8 ESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIdTSLK-----ATQALVLAPTRELAQQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 257 TFGV---LKELMTHHVHTyglIMGGSNRSAEVQKLLNGINIIVATPGRLLDhMQNTPGFMYKNLQCLVIDEADRILDVGF 333
Cdd:cd18046   83 IQKVvmaLGDYMGIKCHA---CIGGTSVRDDAQKLQAGPHIVVGTPGRVFD-MINRRYLRTDYIKMFVLDEADEMLSRGF 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 187954459 334 EEELKQIIKLLPARRQTMLFSATQTRKVEDLAR 366
Cdd:cd18046  159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTT 191
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
179-370 6.80e-33

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: 126.66  E-value: 6.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 179 NTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPR-NGTGVLILSPTRELAMQT 257
Cdd:cd18049   34 NVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERgDGPICLVLAPTRELAQQV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 258 FGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMyKNLQCLVIDEADRILDVGFEEEL 337
Cdd:cd18049  114 QQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNL-RRCTYLVLDEADRMLDMGFEPQI 192
                        170       180       190
                 ....*....|....*....|....*....|...
gi 187954459 338 KQIIKLLPARRQTMLFSATQTRKVEDLARISLK 370
Cdd:cd18049  193 RKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLK 225
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
180-356 1.47e-32

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: 124.30  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 180 TLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLkfmpRNGTGVLILSPTRELAMQTFG 259
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE----RRHPQVLILAPTREIAVQIHD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 260 VLKELMTH----HVHTYgliMGGSNRSAEVQKlLNGINIIVATPGRLLdHMQNTPGFMYKNLQCLVIDEADRILDVGFEE 335
Cdd:cd17943   77 VFKKIGKKleglKCEVF---IGGTPVKEDKKK-LKGCHIAVGTPGRIK-QLIELGALNVSHVRLFVLDEADKLMEGSFQK 151
                        170       180
                 ....*....|....*....|.
gi 187954459 336 ELKQIIKLLPARRQTMLFSAT 356
Cdd:cd17943  152 DVNWIFSSLPKNKQVIAFSAT 172
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
178-364 8.63e-32

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: 122.19  E-value: 8.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 178 ENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPV---IELIVKlkfmprnGTGVLILSPTRELA 254
Cdd:cd18045    8 EDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVlqcLDIQVR-------ETQALILSPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 255 MQTFGVLKELMTH-HVHTYGLImGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTpGFMYKNLQCLVIDEADRILDVGF 333
Cdd:cd18045   81 VQIQKVLLALGDYmNVQCHACI-GGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRR-SLRTRHIKMLVLDEADEMLNKGF 158
                        170       180       190
                 ....*....|....*....|....*....|.
gi 187954459 334 EEELKQIIKLLPARRQTMLFSATQTRKVEDL 364
Cdd:cd18045  159 KEQIYDVYRYLPPATQVVLVSATLPQDILEM 189
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
177-366 2.35e-31

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: 120.76  E-value: 2.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 177 NENTLKAIEEMGFKRMTEIQHKSIrPLLEG---RDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRngtgVLILSPTREL 253
Cdd:cd17963    2 KPELLKGLYAMGFNKPSKIQETAL-PLILSdppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQ----ALCLAPTREL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 254 AMQTFGVLKELMTHHVHTYGLIMGGSNRSAEvqkllNGIN--IIVATPGRLLDHMQnTPGFMYKNLQCLVIDEADRILDV 331
Cdd:cd17963   77 ARQIGEVVEKMGKFTGVKVALAVPGNDVPRG-----KKITaqIVIGTPGTVLDWLK-KRQLDLKKIKILVLDEADVMLDT 150
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 187954459 332 -GFEEELKQIIKLLPARRQTMLFSATQTRKVEDLAR 366
Cdd:cd17963  151 qGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAE 186
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
189-365 3.20e-31

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: 122.81  E-value: 3.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 189 FKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPR-NGTGVLILSPTRELAMQTFGVLKELMTH 267
Cdd:cd18050   82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERgDGPICLVLAPTRELAQQVQQVADDYGKS 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 268 HVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMyKNLQCLVIDEADRILDVGFEEELKQIIKLLPAR 347
Cdd:cd18050  162 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNL-RRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 240
                        170
                 ....*....|....*...
gi 187954459 348 RQTMLFSATQTRKVEDLA 365
Cdd:cd18050  241 RQTLMWSATWPKEVRQLA 258
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
180-379 6.92e-30

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: 116.87  E-value: 6.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 180 TLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTG--VLILSPTRELAMQT 257
Cdd:cd17944    1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRApkVLVLAPTRELANQV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 258 FGVLKELmTHHVhTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMYKnLQCLVIDEADRILDVGFEEEL 337
Cdd:cd17944   81 TKDFKDI-TRKL-SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTK-LKHVVLDEVDQMLDMGFAEQV 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 187954459 338 KQII-----KLLPARRQTMLFSATQTRKVEDLARISLKKEplYVGVD 379
Cdd:cd17944  158 EEILsvsykKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQ--YEQVD 202
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
401-508 4.97e-29

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: 111.15  E-value: 4.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459  401 KRFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYeLLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLD 480
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100
                  ....*....|....*....|....*...
gi 187954459  481 IPEVDWIVQYDPPDDPKEYIHRVGRTAR 508
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGR 107
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
175-371 1.70e-24

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: 101.65  E-value: 1.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 175 LVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKlkfmPRNGTGVLILSPTRELA 254
Cdd:cd17950    8 LLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEP----VDGQVSVLVICHTRELA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 255 MQT---FGVLKELMtHHVHTyGLIMGGSNRSAEVQKLLNGI-NIIVATPGRLLDHMQNTpGFMYKNLQCLVIDEADRIL- 329
Cdd:cd17950   84 FQIsneYERFSKYM-PNVKT-AVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREK-KLKLSHVKHFVLDECDKMLe 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 187954459 330 DVGFEEELKQIIKLLPARRQTMLFSATQTRKvedlARISLKK 371
Cdd:cd17950  161 QLDMRRDVQEIFRATPHDKQVMMFSATLSKE----IRPVCKK 198
HELICc smart00490
helicase superfamily c-terminal domain;
429-508 3.42e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 96.51  E-value: 3.42e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459   429 KYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTAR 508
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
181-364 4.56e-23

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 98.21  E-value: 4.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTG---VLILSPTRELAMQT 257
Cdd:cd17948    2 VEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNaprGLVITPSRELAEQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 258 FGVLKELmthhvhTYGL------IMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTpgfMYK--NLQCLVIDEADRIL 329
Cdd:cd17948   82 GSVAQSL------TEGLglkvkvITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSR---IYSleQLRHLVLDEADTLL 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 187954459 330 DVGFEEELKQIIKLLP-------------ARRQTMLFSATQTRKVEDL 364
Cdd:cd17948  153 DDSFNEKLSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEV 200
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
552-609 2.80e-22

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: 90.15  E-value: 2.80e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 187954459  552 QSQLEKLIEKNYFLHKSAQEAYKSYIRAYDSHSLKQIFNVNNLNLPQVALSFGFKVPP 609
Cdd:pfam13959   1 QLQLEKLVLKDRELKELAQKAFVSYVRAYSKHLAKSIFNVKKLDLGHLAKSFGLLRAP 58
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
154-374 1.76e-21

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: 93.55  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 154 PSLPLgltgaFEDTSFASLSnlVNENTLKAIEEMGFKRMTEIQHKSIRPLLEG--RDLLAAAKTGSGKTLAFLIPVIELI 231
Cdd:cd18048   10 PTSPL-----FSVKSFEELH--LKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 232 VKLKFMPRngtgVLILSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNgiNIIVATPGRLLDHMQNTPG 311
Cdd:cd18048   83 DALKLYPQ----CLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEA--QIVIGTPGTVLDWCFKLRL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187954459 312 FMYKNLQCLVIDEADRILDV-GFEEELKQIIKLLPARRQTMLFSAT--------QTRKVEDLARISLKKEPL 374
Cdd:cd18048  157 IDVTNISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATfedsvwafAERIVPDPNIIKLKKEEL 228
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
205-519 1.93e-21

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 98.56  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 205 EGRDLLAAAKTGSGKTLAFLipviELIVKLKFMPRngtgVLILSPTRELAMQTFGVLKELMTHHVHTyglimGGSNRSAE 284
Cdd:COG1061   99 GGGRGLVVAPTGTGKTVLAL----ALAAELLRGKR----VLVLVPRRELLEQWAEELRRFLGDPLAG-----GGKKDSDA 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 285 vqkllngiNIIVATPGRL-----LDHMQNTPGFmyknlqcLVIDEADRIldvgFEEELKQIIKLLPARRqTMLFSAT--- 356
Cdd:COG1061  166 --------PITVATYQSLarrahLDELGDRFGL-------VIIDEAHHA----GAPSYRRILEAFPAAY-RLGLTATpfr 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 357 ---QTRKVEDLA----RISLK--------KEPLYVGVDDD--KEVATVDGLEQGY--VVCPSEKR-FLLLFTFLKKNRK- 415
Cdd:COG1061  226 sdgREILLFLFDgivyEYSLKeaiedgylAPPEYYGIRVDltDERAEYDALSERLreALAADAERkDKILRELLREHPDd 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 416 KKVMVFfssCMSVKyH----YELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQYD 491
Cdd:COG1061  306 RKTLVF---CSSVD-HaealAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR 381
                        330       340
                 ....*....|....*....|....*...
gi 187954459 492 PPDDPKEYIHRVGRTARGLNGRGHALLI 519
Cdd:COG1061  382 PTGSPREFIQRLGRGLRPAPGKEDALVY 409
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
206-356 3.45e-20

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: 87.46  E-value: 3.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 206 GRDLLAAAKTGSGKTLAFLIPVIELIVKlkfmprNGTGVLILSPTRELAMQTFGVLKELMTHHVHTYglIMGGSNRSAEV 285
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLK------KGKKVLVLVPTKALALQTAERLRELFGPGIRVA--VLVGGSSAEER 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187954459 286 QKLLNG-INIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFE--EELKQIIKLLPARRQTMLFSAT 356
Cdd:cd00046   73 EKNKLGdADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGalILDLAVRKAGLKNAQVILLSAT 146
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
210-356 1.83e-18

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: 85.51  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 210 LAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTG-------------VLILSPTRELAMQTFGVLKELmtHHVHTYGLIM 276
Cdd:cd17965   65 LLAAETGSGKTLAYLAPLLDYLKRQEQEPFEEAEeeyesakdtgrprSVILVPTHELVEQVYSVLKKL--SHTVKLGIKT 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 277 GGSNRSAEVQKLL----NGINIIVATPGRLLDhMQNTPGFMYKNLQCLVIDEADRILDVGFEEELKQIIKLLPARRQTML 352
Cdd:cd17965  143 FSSGFGPSYQRLQlafkGRIDILVTTPGKLAS-LAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLIL 221

                 ....
gi 187954459 353 FSAT 356
Cdd:cd17965  222 CSAT 225
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
181-356 5.22e-13

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: 68.59  E-value: 5.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 181 LKAIEEMGFKRMTEIQHKSIRPLLE--GRDLLAAAKTGSGKTLAFLIPVIELI-VKLKFmprngTGVLILSPTRELAMQT 257
Cdd:cd18047   13 LQGVYAMGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAMLSQVePANKY-----PQCLCLSPTYELALQT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 258 FGVLKELMTHHVH---TYGLIMGGSNRSAEVQKllngiNIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDV-GF 333
Cdd:cd18047   88 GKVIEQMGKFYPElklAYAVRGNKLERGQKISE-----QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATqGH 162
                        170       180
                 ....*....|....*....|...
gi 187954459 334 EEELKQIIKLLPARRQTMLFSAT 356
Cdd:cd18047  163 QDQSIRIQRMLPRNCQMLLFSAT 185
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
173-393 1.39e-12

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 70.69  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 173 SNLVNENTLKAIEEMGFKRMTEIQHKSI-RPLLEGRDLLAAAKTGSGKTLaflipVIELIVkLKFMPRNGTgVLILSPTR 251
Cdd:COG1204    4 AELPLEKVIEFLKERGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTL-----IAELAI-LKALLNGGK-ALYIVPLR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 252 ELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEvqkLLNGINIIVATPGRLLDHMQNTPGFMyKNLQCLVIDEA------ 325
Cdd:COG1204   77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE---WLGRYDILVATPEKLDSLLRNGPSWL-RDVDLVVVDEAhlidde 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187954459 326 DR--ILdvgfeEELKQIIKLLPARRQTMLFSATqTRKVEDLARIsLKKE---------PLYVGVDDDKEVATVDGLEQG 393
Cdd:COG1204  153 SRgpTL-----EVLLARLRRLNPEAQIVALSAT-IGNAEEIAEW-LDAElvksdwrpvPLNEGVLYDGVLRFDDGSRRS 224
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
192-375 8.92e-11

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: 61.12  E-value: 8.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 192 MTEIQHKSIRPL-LEGRDLLAAAKTGSGKTLaflipVIEL-IVKLKFmpRNGTGVLILSPTRELAMQTFGVLKELMTHHV 269
Cdd:cd17921    2 LNPIQREALRALyLSGDSVLVSAPTSSGKTL-----IAELaILRALA--TSGGKAVYIAPTRALVNQKEADLRERFGPLG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 270 HTYGLIMGGSNRSAEvqkLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADrilDVGFEEE---LKQIIKLLPA 346
Cdd:cd17921   75 KNVGLLTGDPSVNKL---LLAEADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAH---LIGDGERgvvLELLLSRLLR 148
                        170       180       190
                 ....*....|....*....|....*....|..
gi 187954459 347 RRQTMLF---SATqTRKVEDLARIsLKKEPLY 375
Cdd:cd17921  149 INKNARFvglSAT-LPNAEDLAEW-LGVEDLI 178
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
168-325 3.47e-10

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: 63.32  E-value: 3.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 168 SFASLSNLVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKlkfmPRNGTgVLIL 247
Cdd:COG1205   33 RYAPWPDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE----DPGAT-ALYL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 248 SPTRELAMQTFGVLKELMTH-----HVHTYglimGGSNRSAEVQKLLNGINIIVATP-----GrLLDHMQNTPGFmYKNL 317
Cdd:COG1205  108 YPTKALARDQLRRLRELAEAlglgvRVATY----DGDTPPEERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARF-FRNL 181

                 ....*...
gi 187954459 318 QCLVIDEA 325
Cdd:COG1205  182 RYVVIDEA 189
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
196-325 4.12e-10

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: 59.52  E-value: 4.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 196 QHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKlkfmpRNGTGVLILSPTRELAMQTFGVLKELM--THHVHTYG 273
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLR-----DPGSRALYLYPTKALAQDQLRSLRELLeqLGLGIRVA 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 187954459 274 LIMGGSNRSAEVQKLLNGINIIVATPGRL----LDHMQNTPGFMyKNLQCLVIDEA 325
Cdd:cd17923   80 TYDGDTPREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFL-RNLRYVVLDEA 134
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
448-513 4.56e-10

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: 58.14  E-value: 4.56e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187954459 448 KQKQNKRTTTffQFCNADSGILLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARGLNGR 513
Cdd:cd18801   75 SQKEQKEVIE--QFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQGR 138
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
410-513 2.06e-09

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 60.51  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 410 LKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQ--------KQNKRTTTFFQFCNADSGILLCTDVAARGLDI 481
Cdd:COG1111  348 LGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQAskegdkglTQKEQIEILERFRAGEFNVLVATSVAEEGLDI 427
                         90       100       110
                 ....*....|....*....|....*....|....
gi 187954459 482 PEVDWIVQYDPPddPKE--YIHRVGRTARGLNGR 513
Cdd:COG1111  428 PEVDLVIFYEPV--PSEirSIQRKGRTGRKREGR 459
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
215-356 1.57e-08

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: 53.85  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 215 TGSGKTL-AFLipvieLIVKLKFMPrngtgVLILSPTRELAMQTFGVLKELMTHHVhtYGLIMGGSNrsaevqKLLNGIN 293
Cdd:cd17926   27 TGSGKTLtALA-----LIAYLKELR-----TLIVVPTDALLDQWKERFEDFLGDSS--IGLIGGGKK------KDFDDAN 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187954459 294 IIVATPgRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFEEelkqIIKLLPARRQtMLFSAT 356
Cdd:cd17926   89 VVVATY-QSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSE----ILKELNAKYR-LGLTAT 145
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
468-509 6.79e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 50.01  E-value: 6.79e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 187954459 468 ILLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARG 509
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRG 66
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
206-324 1.14e-07

DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 51.82  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 206 GRDLLAAAKTGSGKTLAFLIPVIELIVKLkfmPRNGTGVLILSPTRELAMQTFGVLKELMThhvhtyGLIMG-------G 278
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLADE---PEKGVQVLYISPLKALINDQERRLEEPLD------EIDLEipvavrhG 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 187954459 279 SNRSAEVQKLL-NGINIIVATPgRLLDHMQNTPGF--MYKNLQCLVIDE 324
Cdd:cd17922   72 DTSQSEKAKQLkNPPGILITTP-ESLELLLVNKKLreLFAGLRYVVVDE 119
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
189-254 1.65e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 54.72  E-value: 1.65e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187954459 189 FKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLA-FLIPVIELIVK-LKFMPRNGTGVLILSPTRELA 254
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAaFLPALDELARRpRPGELPDGLRVLYISPLKALA 89
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
178-363 1.22e-06

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: 49.46  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 178 ENTLKAIeeMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPvielivklkFMPRNGTgVLILSPTREL---- 253
Cdd:cd17920    1 EQILKEV--FGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLP---------ALLLDGV-TLVVSPLISLmqdq 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 254 --AMQTFGVLKELMTHHVHTyglimggSNRSAEVQKLLNG-INIIVATPGRLLdhmqnTPGFM--------YKNLQCLVI 322
Cdd:cd17920   69 vdRLQQLGIRAAALNSTLSP-------EEKREVLLRIKNGqYKLLYVTPERLL-----SPDFLellqrlpeRKRLALIVV 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 187954459 323 DEADRILDVG--FEEELKQIIKLLPARR--QTMLFSATQTRKVED 363
Cdd:cd17920  137 DEAHCVSQWGhdFRPDYLRLGRLRRALPgvPILALTATATPEVRE 181
PRK13766 PRK13766
Hef nuclease; Provisional
410-518 1.89e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 51.03  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 410 LKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGK----------QKQNKRTTTffQFCNADSGILLCTDVAARGL 479
Cdd:PRK13766 360 LGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgmsQKEQIEILD--KFRAGEFNVLVSTSVAEEGL 437
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 187954459 480 DIPEVDWIVQYDPPddPKE--YIHRVGRTARGLNGRGHALL 518
Cdd:PRK13766 438 DIPSVDLVIFYEPV--PSEirSIQRKGRTGRQEEGRVVVLI 476
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
191-327 1.90e-06

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 48.57  E-value: 1.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 191 RMTEIQHKSIRPLL------EGRDLLAAAKTGSGKTLAFLIPVIeLIVKlkfmprNGTGVLILSPTRELAMQTFGVLKEL 264
Cdd:cd17918   15 SLTKDQAQAIKDIEkdlhspEPMDRLLSGDVGSGKTLVALGAAL-LAYK------NGKQVAILVPTEILAHQHYEEARKF 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187954459 265 MTH-HVHtygLIMGGSNrsaevQKLLNGINIIVATPGRLLDHMQntpgfmYKNLQCLVIDEADR 327
Cdd:cd17918   88 LPFiNVE---LVTGGTK-----AQILSGISLLVGTHALLHLDVK------FKNLDLVIVDEQHR 137
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
188-365 3.00e-06

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) 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 cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 48.41  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 188 GFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVielivklKFMPRNGTGV-LILSPTRELaM--QTFGvLKEL 264
Cdd:cd18018    9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPA-------LLLRRRGPGLtLVVSPLIAL-MkdQVDA-LPRA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 265 MThhVHTYGLIMGGSNRSAEVQKLLNG-INIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFE-----EELK 338
Cdd:cd18018   80 IK--AAALNSSLTREERRRILEKLRAGeVKILYVSPERLVNESFRELLRQTPPISLLVVDEAHCISEWSHNfrpdyLRLC 157
                        170       180
                 ....*....|....*....|....*...
gi 187954459 339 QIIKLLPARRQTMLFSATQTRKV-EDLA 365
Cdd:cd18018  158 RVLRELLGAPPVLALTATATKRVvEDIA 185
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
215-325 5.56e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 47.65  E-value: 5.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 215 TGSGKTL-AFLipVI-ELIVKLKFMPRNGTGVLILSPTRELAMQTFGVLKELMTHHV-HTYGLIMGGSNRSAEVQKLLNG 291
Cdd:cd18034   25 TGSGKTLiAVM--LIkEMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTDLKVgEYSGEMGVDKWTKERWKEELEK 102
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 187954459 292 INIIVATPGRLLDHMQNtpGFM-YKNLQCLVIDEA 325
Cdd:cd18034  103 YDVLVMTAQILLDALRH--GFLsLSDINLLIFDEC 135
ResIII pfam04851
Type III restriction enzyme, res subunit;
196-356 1.13e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 46.13  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459  196 QHKSIRPLLEGRD------LLAAAkTGSGKTL--AFLIpvieLIVKLKFMPRNgtgVLILSPTRELAMQTFGVLKELMTH 267
Cdd:pfam04851   8 QIEAIENLLESIKngqkrgLIVMA-TGSGKTLtaAKLI----ARLFKKGPIKK---VLFLVPRKDLLEQALEEFKKFLPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459  268 HVHTYGLIMGGSNRSAevqklLNGINIIVATPGRLLDHMQNTP-GFMYKNLQCLVIDEADRILDVGFeeelKQIIKLLPA 346
Cdd:pfam04851  80 YVEIGEIISGDKKDES-----VDDNKIVVTTIQSLYKALELASlELLPDFFDVIIIDEAHRSGASSY----RNILEYFKP 150
                         170
                  ....*....|.
gi 187954459  347 rrQTML-FSAT 356
Cdd:pfam04851 151 --AFLLgLTAT 159
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
203-356 1.35e-05

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 46.17  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 203 LLEGRDLLAAAKTGSGKTLaflipvIELIVKLKFMPRNGTGVLILsPTRELAMQTFGVLKELmthhvHTYGLIMG---GS 279
Cdd:cd18028   14 LLKGENLLISIPTASGKTL------IAEMAMVNTLLEGGKALYLV-PLRALASEKYEEFKKL-----EEIGLKVGistGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 280 NRSAEvqKLLNGINIIVATPGRLLDHMQNTPGFMyKNLQCLVIDEADRILDVGFEEELKQII---KLLPARRQTMLFSAT 356
Cdd:cd18028   82 YDEDD--EWLGDYDIIVATYEKFDSLLRHSPSWL-RDVGVVVVDEIHLISDEERGPTLESIVarlRRLNPNTQIIGLSAT 158
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
202-327 3.85e-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: 3.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 202 PLLEGRDLLAAAKTGSGKTLAFLipvieLIVK---LKFMPRNGTGVLILSPTRELAMQTFGVLKELMTHHVHTYGLIMGG 278
Cdd:cd17927   13 PALKGKNTIICLPTGSGKTFVAV-----LICEhhlKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGD 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 187954459 279 SNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADR 327
Cdd:cd17927   88 TSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
213-325 2.82e-04

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 42.28  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 213 AKTGSGKTLAFLIPVielivkLKFMPRNGTGVLILS-PTRELAMQTFGVLKELM---------THHVHTYGLIM------ 276
Cdd:cd17930    8 APTGSGKTEAALLWA------LKLAARGGKRRIIYAlPTRATINQMYERIREILgrlddedkvLLLHSKAALELlesdee 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 187954459 277 GGSNRSAEVQKLLNGIN-----IIVATPGRLLDHMQNTPGFMYK--NLQ--CLVIDEA 325
Cdd:cd17930   82 PDDDPVEAVDWALLLKRswlapIVVTTIDQLLESLLKYKHFERRlhGLAnsVVVLDEV 139
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
468-508 3.15e-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: 41.42  E-value: 3.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 187954459 468 ILLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRtAR 508
Cdd:cd18802   93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-AR 132
PRK13766 PRK13766
Hef nuclease; Provisional
192-299 9.13e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 42.55  E-value: 9.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 192 MTEIQHKSIRP-LLEGR----DLLAAAK---------TGSGKTlaflipVIELIVKLKFMPRNGTGVLILSPTRELAMQT 257
Cdd:PRK13766   1 MMYIEHPLIKPnTIEARlyqqLLAATALkkntlvvlpTGLGKT------AIALLVIAERLHKKGGKVLILAPTKPLVEQH 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 187954459 258 FGVLKELMThhVHTYGLIM-GGSNRSAEVQKLLNGINIIVATP 299
Cdd:PRK13766  75 AEFFRKFLN--IPEEKIVVfTGEVSPEKRAELWEKAKVIVATP 115
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
210-264 1.25e-03

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


Pssm-ID: 442728 [Multi-domain]  Cd Length: 402  Bit Score: 41.51  E-value: 1.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 187954459 210 LAAAKTGSGKTLAFLIPVIELIvklkfmpRNGTGVLILSPTRELAMQTFGVLKEL 264
Cdd:COG3505    3 LVIGPTGSGKTVGLVIPNLTQL-------ARGESVVVTDPKGDLAELTAGFRRRA 50
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
394-496 1.48e-03

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 39.38  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 394 YVVCPsekRFLLLFTFLKKNRKK--KVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFcNADSGI--- 468
Cdd:cd18793    7 EVVSG---KLEALLELLEELREPgeKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIrvf 82
                         90       100
                 ....*....|....*....|....*...
gi 187954459 469 LLCTDVAARGLDIPEVDWIVQYDPPDDP 496
Cdd:cd18793   83 LLSTKAGGVGLNLTAANRVILYDPWWNP 110
PRK00254 PRK00254
ski2-like helicase; Provisional
176-356 1.64e-03

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 41.73  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 176 VNENTLKAIEEMGFKRMTEIQHKSIRP-LLEGRDLLAAAKTGSGKTLaflipVIELIVKLKFMPRNGTGVLILsPTRELA 254
Cdd:PRK00254   8 VDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTL-----VAEIVMVNKLLREGGKAVYLV-PLKALA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 255 MQTFGVLKELmthhvHTYGL---IMGGSNRSAEvqKLLNGINIIVATPGR---LLDHMQNtpgfMYKNLQCLVIDEADRI 328
Cdd:PRK00254  82 EEKYREFKDW-----EKLGLrvaMTTGDYDSTD--EWLGKYDIIIATAEKfdsLLRHGSS----WIKDVKLVVADEIHLI 150
                        170       180
                 ....*....|....*....|....*...
gi 187954459 329 LDVGFEEELKQIIKLLPARRQTMLFSAT 356
Cdd:PRK00254 151 GSYDRGATLEMILTHMLGRAQILGLSAT 178
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
203-251 1.66e-03

Rad3-related DNA helicase DinG [Replication, recombination and repair];


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 41.45  E-value: 1.66e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 187954459 203 LLEGRDLLAAAKTGSGKTLAFLIPVIelivklKFMPRNGTGVLILSPTR 251
Cdd:COG1199   30 LAEGRHLLIEAGTGTGKTLAYLVPAL------LAARETGKKVVISTATK 72
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
439-524 2.65e-03

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


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 38.86  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 439 DLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRV-GRTARGlNGRGHAL 517
Cdd:cd18810   51 EARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRS-KERAYAY 129

                 ....*..
gi 187954459 518 LILRPEE 524
Cdd:cd18810  130 FLYPDQK 136
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
190-344 5.58e-03

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


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 38.46  E-value: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 190 KRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTlAFLIpVIELIVKLKfmprnGTGVLILSPTRELAMQTFGVLKELMTH-- 267
Cdd:cd17924   16 FPPWGAQRTWAKRLLRGKSFAIIAPTGVGKT-TFGL-ATSLYLASK-----GKRSYLIFPTKSLVKQAYERLSKYAEKag 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 268 ---HVHTYGLIMGGSNRSAEVQKLLNG-INIIVATPGRLLDHMQNTPGFMYknlQCLVIDEADRILDVGfeeelKQIIKL 343
Cdd:cd17924   89 vevKILVYHSRLKKKEKEELLEKIEKGdFDILVTTNQFLSKNFDLLSNKKF---DFVFVDDVDAVLKSS-----KNIDRL 160

                 .
gi 187954459 344 L 344
Cdd:cd17924  161 L 161
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
196-327 5.76e-03

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 37.93  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 196 QHKSIRPLLEGRD------LLAAAkTGSGKTL--AFLIPvielivklKFMPRNGTG-VLILSPTRELAMQTFGVLKELMT 266
Cdd:cd18032    5 QQEAIEALEEAREkgqrraLLVMA-TGTGKTYtaAFLIK--------RLLEANRKKrILFLAHREELLEQAERSFKEVLP 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187954459 267 HhvHTYGLIMGGSnrsaevQKLLNGiNIIVATP---GRLLDHMQNTPGFmYKnlqCLVIDEADR 327
Cdd:cd18032   76 D--GSFGNLKGGK------KKPDDA-RVVFATVqtlNKRKRLEKFPPDY-FD---LIIIDEAHH 126
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
210-299 6.74e-03

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: 38.26  E-value: 6.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 210 LAAAKTGSGKTLaflipvIELIVKLKFMPRNGTGVLILSPTRELAMQTFGVLKELMTHHVHTYGLImgGSNRSAEVQKLL 289
Cdd:cd18035   20 LIVLPTGLGKTI------IAILVAADRLTKKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLT--GEVKPEERAERW 91
                         90
                 ....*....|
gi 187954459 290 NGINIIVATP 299
Cdd:cd18035   92 DASKIIVATP 101
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
215-326 6.97e-03

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 39.29  E-value: 6.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 215 TGSGKTLAFLIPVIELIVKLKfMPRngtGVLILsPTRELAMQTFGVLKELMT-----HH----VHTYGLIMGGSNRSAEV 285
Cdd:COG1203  156 TGGGKTEAALLFALRLAAKHG-GRR---IIYAL-PFTSIINQTYDRLRDLFGedvllHHsladLDLLEEEEEYESEARWL 230
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 187954459 286 QKLLNGIN--IIVATPGRLLDH-MQNTPGFMYK--NLQ--CLVIDEAD 326
Cdd:COG1203  231 KLLKELWDapVVVTTIDQLFESlFSNRKGQERRlhNLAnsVIILDEVQ 278
PRK02362 PRK02362
ATP-dependent DNA helicase;
203-324 9.66e-03

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 39.17  E-value: 9.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954459 203 LLEGRDLLAAAKTGSGKTLaflipVIELIVkLKFMPRNGTGVLILsPTRELAMQTFGVLKELMTHHVHTyGLIMGGSNRS 282
Cdd:PRK02362  36 LLDGKNLLAAIPTASGKTL-----IAELAM-LKAIARGGKALYIV-PLRALASEKFEEFERFEELGVRV-GISTGDYDSR 107
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 187954459 283 AEvqkLLNGINIIVATPGRLLDHMQNTPGFMyKNLQCLVIDE 324
Cdd:PRK02362 108 DE---WLGDNDIIVATSEKVDSLLRNGAPWL-DDITCVVVDE 145
 
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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