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Conserved domains on  [gi|51010913|ref|NP_001003411|]
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ATP-dependent RNA helicase DDX18 [Danio rerio]

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 ...
172-369 6.18e-146

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: 421.38  E-value: 6.18e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 172 TLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRNGTGVIVLSPTRELAMQTYG 251
Cdd:cd17942   1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 252 VLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADRILEVGFEEELKQ 331
Cdd:cd17942  81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 51010913 332 IIKLLPKKRQSMLFSATQTRKVEDLARISLKKEPLYVG 369
Cdd:cd17942 161 IIKLLPKRRQTMLFSATQTRKVEDLARISLKKKPLYVG 198
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
382-512 1.24e-51

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: 174.23  E-value: 1.24e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 382 LEQGYVVCPS-EKRFLLLFTFLKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGI 460
Cdd:cd18787   1 IKQLYVVVEEeEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 51010913 461 LLCTDVAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTARGinGR-GHALLIL 512
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRA--GRkGTAITFV 131
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
544-601 2.84e-21

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: 87.45  E-value: 2.84e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 51010913   544 QSQLDKLIEKNYYLHKSAQEAYKSYVRAYDSHSLKQIYNVETLDLPKVAMSFGFKVPP 601
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 ...
172-369 6.18e-146

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: 421.38  E-value: 6.18e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 172 TLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRNGTGVIVLSPTRELAMQTYG 251
Cdd:cd17942   1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 252 VLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADRILEVGFEEELKQ 331
Cdd:cd17942  81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 51010913 332 IIKLLPKKRQSMLFSATQTRKVEDLARISLKKEPLYVG 369
Cdd:cd17942 161 IIKLLPKRRQTMLFSATQTRKVEDLARISLKKKPLYVG 198
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
160-534 2.91e-117

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 356.38  E-value: 2.91e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 160 SFASLSevVSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPsieLIYKLKFMPRNGTGVIVL 239
Cdd:COG0513   3 SFADLG--LSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP---LLQRLDPSRPRAPQALIL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 240 SPTRELAMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHL-QNTpgFMFKNLQCLIIDEAD 318
Cdd:COG0513  78 APTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIeRGA--LDLSGVETLVLDEAD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 319 RILEVGFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARISLKkEPLYVGVDdnKDTATVEGLEQGYVVCPSEKRFLLL 398
Cdd:COG0513 156 RMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVA--PENATAETIEQRYYLVDKRDKLELL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 399 FTFLKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDW 478
Cdd:COG0513 233 RRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSH 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51010913 479 IVQFDPPDDPKEYIHRVGRTARGinGR-GHALLILRPEELGFLRFL-KQAKVPLSEFE 534
Cdd:COG0513 313 VINYDLPEDPEDYVHRIGRTGRA--GAeGTAISLVTPDERRLLRAIeKLIGQKIEEEE 368
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
160-518 9.65e-69

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 231.23  E-value: 9.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  160 SFASLSevVSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFlipSIELIYKLKfMPRNGTGVIVL 239
Cdd:PRK11776   5 AFSTLP--LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAF---GLGLLQKLD-VKRFRVQALVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  240 SPTRELAMQtygVLKEL-----MTHHVHTYGLImGGSNRSAEAQKLANGVNILVATPGRLLDHLQntpgfmfK------N 308
Cdd:PRK11776  79 CPTRELADQ---VAKEIrrlarFIPNIKVLTLC-GGVPMGPQIDSLEHGAHIIVGTPGRILDHLR-------KgtldldA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  309 LQCLIIDEADRILEVGFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARiSLKKEPLYVGVDDNKDTATVEgleQGYVV 388
Cdd:PRK11776 148 LNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQ-RFQRDPVEVKVESTHDLPAIE---QRFYE 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  389 CPSEKRFLLLFTFLKKNRKKKLMVFFSS---CMSVkfhYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTD 465
Cdd:PRK11776 224 VSPDERLPALQRLLLHHQPESCVVFCNTkkeCQEV---ADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATD 300
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 51010913  466 VAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTARGINgRGHALLILRPEELG 518
Cdd:PRK11776 301 VAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGS-KGLALSLVAPEEMQ 352
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
185-356 3.49e-61

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: 201.32  E-value: 3.49e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   185 TEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKfmprNGTGVIVLSPTRELAMQTYGVLKELMTHHVHTY 264
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD----NGPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   265 GLIMGGSNRSAEAQKLAnGVNILVATPGRLLDHLQNTPGFmfKNLQCLIIDEADRILEVGFEEELKQIIKLLPKKRQSML 344
Cdd:pfam00270  77 ASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 51010913   345 FSATQTRKVEDL 356
Cdd:pfam00270 154 LSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
382-512 1.24e-51

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: 174.23  E-value: 1.24e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 382 LEQGYVVCPS-EKRFLLLFTFLKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGI 460
Cdd:cd18787   1 IKQLYVVVEEeEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 51010913 461 LLCTDVAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTARGinGR-GHALLIL 512
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRA--GRkGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
176-364 1.28e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 168.82  E-value: 1.28e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913    176 VKEMGFDTMTEIQHKTIRPLLEG-RDVLAAAKTGSGKTLAFLIPSIELIYKlkfmpRNGTGVIVLSPTRELAMQTYGVLK 254
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-----GKGGRVLVLVPTRELAEQWAEELK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913    255 ELMTHHVHTYGLIMGGSNRSAEAQKLANGV-NILVATPGRLLDHLQNTPgFMFKNLQCLIIDEADRILEVGFEEELKQII 333
Cdd:smart00487  76 KLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDK-LSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190
                   ....*....|....*....|....*....|.
gi 51010913    334 KLLPKKRQSMLFSATQTRKVEDLARISLKKE 364
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDP 185
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
393-500 6.38e-27

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: 105.37  E-value: 6.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   393 KRFLLLFTFLKKNRKKKLMVFFSSCMSVKFHYeLLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLD 472
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100
                  ....*....|....*....|....*...
gi 51010913   473 IPEVDWIVQFDPPDDPKEYIHRVGRTAR 500
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGR 107
HELICc smart00490
helicase superfamily c-terminal domain;
421-500 1.65e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.59  E-value: 1.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913    421 KFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTAR 500
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
544-601 2.84e-21

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: 87.45  E-value: 2.84e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 51010913   544 QSQLDKLIEKNYYLHKSAQEAYKSYVRAYDSHSLKQIYNVETLDLPKVAMSFGFKVPP 601
Cdd:pfam13959   1 QLQLEKLVLKDRELKELAQKAFVSYVRAYSKHLAKSIFNVKKLDLGHLAKSFGLLRAP 58
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
402-505 4.33e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 56.28  E-value: 4.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 402 LKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQ--------KQTKRTTTFFQFCNADSGILLCTDVAARGLDI 473
Cdd:COG1111 348 LGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQAskegdkglTQKEQIEILERFRAGEFNVLVATSVAEEGLDI 427
                        90       100       110
                ....*....|....*....|....*....|....
gi 51010913 474 PEVDWIVQFDPPddPKE--YIHRVGRTARGINGR 505
Cdd:COG1111 428 PEVDLVIFYEPV--PSEirSIQRKGRTGRKREGR 459
mfd TIGR00580
transcription-repair coupling factor (mfd); All proteins in this family for which functions ...
232-332 4.79e-05

transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273152 [Multi-domain]  Cd Length: 926  Bit Score: 46.58  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   232 NGTGVIVLSPTRELAMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQ---KLANG-VNILVATpGRLLdhlqnTPGFMFK 307
Cdd:TIGR00580 499 DGKQVAVLVPTTLLAQQHFETFKERFANFPVTIELLSRFRSAKEQNEilkELASGkIDILIGT-HKLL-----QKDVKFK 572
                          90       100
                  ....*....|....*....|....*
gi 51010913   308 NLQCLIIDEADRiLEVGFEEELKQI 332
Cdd:TIGR00580 573 DLGLLIIDEEQR-FGVKQKEKLKEL 596
PRK13766 PRK13766
Hef nuclease; Provisional
402-510 8.48e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 45.63  E-value: 8.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  402 LKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGK----------QKQTKRTTTffQFCNADSGILLCTDVAARGL 471
Cdd:PRK13766 360 LGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgmsQKEQIEILD--KFRAGEFNVLVSTSVAEEGL 437
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 51010913  472 DIPEVDWIVQFDPPddPKE--YIHRVGRTARGINGRGHALL 510
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 ...
172-369 6.18e-146

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: 421.38  E-value: 6.18e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 172 TLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRNGTGVIVLSPTRELAMQTYG 251
Cdd:cd17942   1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 252 VLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADRILEVGFEEELKQ 331
Cdd:cd17942  81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 51010913 332 IIKLLPKKRQSMLFSATQTRKVEDLARISLKKEPLYVG 369
Cdd:cd17942 161 IIKLLPKRRQTMLFSATQTRKVEDLARISLKKKPLYVG 198
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
160-534 2.91e-117

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 356.38  E-value: 2.91e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 160 SFASLSevVSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPsieLIYKLKFMPRNGTGVIVL 239
Cdd:COG0513   3 SFADLG--LSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP---LLQRLDPSRPRAPQALIL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 240 SPTRELAMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHL-QNTpgFMFKNLQCLIIDEAD 318
Cdd:COG0513  78 APTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIeRGA--LDLSGVETLVLDEAD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 319 RILEVGFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARISLKkEPLYVGVDdnKDTATVEGLEQGYVVCPSEKRFLLL 398
Cdd:COG0513 156 RMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVA--PENATAETIEQRYYLVDKRDKLELL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 399 FTFLKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDW 478
Cdd:COG0513 233 RRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSH 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51010913 479 IVQFDPPDDPKEYIHRVGRTARGinGR-GHALLILRPEELGFLRFL-KQAKVPLSEFE 534
Cdd:COG0513 313 VINYDLPEDPEDYVHRIGRTGRA--GAeGTAISLVTPDERRLLRAIeKLIGQKIEEEE 368
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
172-370 1.69e-92

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: 284.18  E-value: 1.69e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 172 TLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRNGTGVIVLSPTRELAMQTYG 251
Cdd:cd17941   1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 252 VLKELMTHHVHTYGLIMGGSNRSAEAQKLaNGVNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADRILEVGFEEELKQ 331
Cdd:cd17941  81 VLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 51010913 332 IIKLLPKKRQSMLFSATQTRKVEDLARISLkKEPLYVGV 370
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSL-KNPEYISV 197
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
172-368 2.12e-81

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: 255.44  E-value: 2.12e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 172 TLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRNGTGVIVLSPTRELAMQTYG 251
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 252 VLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPgFMFKNLQCLIIDEADRILEVGFEEELKQ 331
Cdd:cd00268  81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGK-LDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 51010913 332 IIKLLPKKRQSMLFSATQTRKVEDLARISLkKEPLYV 368
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFL-KNPVRI 195
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
173-363 7.45e-74

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: 235.61  E-value: 7.45e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIE-LIYKLKFMPrnGTGVIVLSPTRELAMQTYG 251
Cdd:cd17947   2 LRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILErLLYRPKKKA--ATRVLVLVPTRELAMQCFS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 252 VLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADRILEVGFEEELKQ 331
Cdd:cd17947  80 VLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKE 159
                       170       180       190
                ....*....|....*....|....*....|..
gi 51010913 332 IIKLLPKKRQSMLFSATQTRKVEDLARISLKK 363
Cdd:cd17947 160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNK 191
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
168-368 1.86e-73

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: 235.17  E-value: 1.86e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 168 VSENTLKGVKEMGFDTMTEIQHKTIRPLLE-GRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRNGT-GVIVLSPTREL 245
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGvSALIISPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 246 AMQTYGVLKELMTHH----VHTyglIMGGSNRSAEAQKLAN-GVNILVATPGRLLDHLQNtPGF--MFKNLQCLIIDEAD 318
Cdd:cd17964  81 ALQIAAEAKKLLQGLrklrVQS---AVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEN-PGVakAFTDLDYLVLDEAD 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 51010913 319 RILEVGFEEELKQIIKLLPKK----RQSMLFSATQTRKVEDLARISLKKEPLYV 368
Cdd:cd17964 157 RLLDMGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
160-518 9.65e-69

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 231.23  E-value: 9.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  160 SFASLSevVSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFlipSIELIYKLKfMPRNGTGVIVL 239
Cdd:PRK11776   5 AFSTLP--LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAF---GLGLLQKLD-VKRFRVQALVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  240 SPTRELAMQtygVLKEL-----MTHHVHTYGLImGGSNRSAEAQKLANGVNILVATPGRLLDHLQntpgfmfK------N 308
Cdd:PRK11776  79 CPTRELADQ---VAKEIrrlarFIPNIKVLTLC-GGVPMGPQIDSLEHGAHIIVGTPGRILDHLR-------KgtldldA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  309 LQCLIIDEADRILEVGFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARiSLKKEPLYVGVDDNKDTATVEgleQGYVV 388
Cdd:PRK11776 148 LNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQ-RFQRDPVEVKVESTHDLPAIE---QRFYE 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  389 CPSEKRFLLLFTFLKKNRKKKLMVFFSS---CMSVkfhYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTD 465
Cdd:PRK11776 224 VSPDERLPALQRLLLHHQPESCVVFCNTkkeCQEV---ADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATD 300
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 51010913  466 VAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTARGINgRGHALLILRPEELG 518
Cdd:PRK11776 301 VAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGS-KGLALSLVAPEEMQ 352
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
179-369 1.79e-65

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: 214.37  E-value: 1.79e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 179 MGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFM-PRN-GTGVIVLSPTRELAMQTYGVLKEL 256
Cdd:cd17949   9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvDRSdGTLALVLVPTRELALQIYEVLEKL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 257 M--THHVHTyGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADRILEVGFEEELKQIIK 334
Cdd:cd17949  89 LkpFHWIVP-GYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILE 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 51010913 335 LL-------------PKKRQSMLFSATQTRKVEDLARISLKKePLYVG 369
Cdd:cd17949 168 LLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKD-PVYID 214
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
172-361 3.81e-64

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: 210.51  E-value: 3.81e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 172 TLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLK-FMPRNGTGVIVLSPTRELAMQTY 250
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKaNLKKGQVGALIISPTRELATQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 251 GVLKELMTHH--VHTYGLIMGGSNRSAEAQKL-ANGVNILVATPGRLLDHLQN-TPGFMFKNLQCLIIDEADRILEVGFE 326
Cdd:cd17960  81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRkADKVKVKSLEVLVLDEADRLLDLGFE 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 51010913 327 EELKQIIKLLPKKRQSMLFSATQTRKVEDLARISL 361
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGL 195
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
169-501 1.35e-62

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 214.04  E-value: 1.35e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  169 SENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIEliYKLKFmPRNGTG---VIVLSPTREL 245
Cdd:PRK11192   9 DESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQ--HLLDF-PRRKSGpprILILTPTREL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  246 AMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTpGFMFKNLQCLIIDEADRILEVGF 325
Cdd:PRK11192  86 AMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEE-NFDCRAVETLILDEADRMLDMGF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  326 EEELKQIIKLLPKKRQSMLFSAT-QTRKVEDLARiSLKKEPLYVGVD-DNKDTATVEgleQGYVVCPS-EKRFLLLFTFL 402
Cdd:PRK11192 165 AQDIETIAAETRWRKQTLLFSATlEGDAVQDFAE-RLLNDPVEVEAEpSRRERKKIH---QWYYRADDlEHKTALLCHLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  403 KKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQF 482
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
                        330
                 ....*....|....*....
gi 51010913  483 DPPDDPKEYIHRVGRTARG 501
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRA 339
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
185-356 3.49e-61

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: 201.32  E-value: 3.49e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   185 TEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKfmprNGTGVIVLSPTRELAMQTYGVLKELMTHHVHTY 264
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD----NGPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   265 GLIMGGSNRSAEAQKLAnGVNILVATPGRLLDHLQNTPGFmfKNLQCLIIDEADRILEVGFEEELKQIIKLLPKKRQSML 344
Cdd:pfam00270  77 ASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 51010913   345 FSATQTRKVEDL 356
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 ...
160-363 1.03e-58

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: 196.00  E-value: 1.03e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 160 SFASLSevVSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPsieLIYKLKFMPRnGTGVIVL 239
Cdd:cd17954   1 TFKELG--VCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALP---ILQALLENPQ-RFFALVL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 240 SPTRELAMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADR 319
Cdd:cd17954  75 APTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADR 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 51010913 320 ILEVGFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARISLKK 363
Cdd:cd17954 155 LLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKN 198
PTZ00110 PTZ00110
helicase; Provisional
173-531 1.92e-58

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 205.78  E-value: 1.92e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFM-PRNGTGVIVLSPTRELAMQ--- 248
Cdd:PTZ00110 142 LKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLrYGDGPIVLVLAPTRELAEQire 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  249 ---TYGVLKELmtHHVHTYGlimgGSNRSAEAQKLANGVNILVATPGRLLDHL-QNTPGFMfkNLQCLIIDEADRILEVG 324
Cdd:PTZ00110 222 qcnKFGASSKI--RNTVAYG----GVPKRGQIYALRRGVEILIACPGRLIDFLeSNVTNLR--RVTYLVLDEADRMLDMG 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  325 FEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARISLKKEPLYVGVDdNKDTATVEGLEQG-YVVCPSEKRfLLLFTFLK 403
Cdd:PTZ00110 294 FEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVG-SLDLTACHNIKQEvFVVEEHEKR-GKLKMLLQ 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  404 K--NRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQ 481
Cdd:PTZ00110 372 RimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVIN 451
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 51010913  482 FDPPDDPKEYIHRVGRTARGiNGRGHALLILRPEEL----GFLRFLKQAKVPLS 531
Cdd:PTZ00110 452 FDFPNQIEDYVHRIGRTGRA-GAKGASYTFLTPDKYrlarDLVKVLREAKQPVP 504
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
160-521 7.95e-58

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 201.96  E-value: 7.95e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  160 SFASLSevVSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMP--RNGTGVI 237
Cdd:PRK10590   2 SFDSLG--LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAkgRRPVRAL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  238 VLSPTRELAMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDhLQNTPGFMFKNLQCLIIDEA 317
Cdd:PRK10590  80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  318 DRILEVGFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARiSLKKEPLYVGVDdNKDTATVEGLEQGYVVCPSEKRFLL 397
Cdd:PRK10590 159 DRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAE-KLLHNPLEIEVA-RRNTASEQVTQHVHFVDKKRKRELL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  398 LFTFLKKNRKKKLmVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVD 477
Cdd:PRK10590 237 SQMIGKGNWQQVL-VFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELP 315
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 51010913  478 WIVQFDPPDDPKEYIHRVGRTARGiNGRGHALLILRPEELGFLR 521
Cdd:PRK10590 316 HVVNYELPNVPEDYVHRIGRTGRA-AATGEALSLVCVDEHKLLR 358
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
160-368 7.53e-56

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: 188.67  E-value: 7.53e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 160 SFASLSevVSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIEliyKLK-FMPRNGTGVIV 238
Cdd:cd17959   2 GFQSMG--LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIE---KLKaHSPTVGARALI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 239 LSPTRELAMQTYGVLKELMTHHVHTYGLIMGGSnrSAEAQ--KLANGVNILVATPGRLLDHLQNTpGFMFKNLQCLIIDE 316
Cdd:cd17959  77 LSPTRELALQTLKVTKELGKFTDLRTALLVGGD--SLEEQfeALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDE 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 51010913 317 ADRILEVGFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARISLkKEPLYV 368
Cdd:cd17959 154 ADRLFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGL-NEPVLI 204
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
173-500 1.96e-54

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 191.72  E-value: 1.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLI---------PSIELiyKLKFMPRngtgVIVLSPTR 243
Cdd:PRK04837  20 VEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTatfhyllshPAPED--RKVNQPR----ALIMAPTR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  244 ELAMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHL-QNTpgFMFKNLQCLIIDEADRILE 322
Cdd:PRK04837  94 ELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAkQNH--INLGAIQVVVLDEADRMFD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  323 VGFeeeLKQIIKLL-----PKKRQSMLFSATQTRKVEDLARISLKkEPLYVGVDDNKDTATVEGLEQGYvvcPS-EKRFL 396
Cdd:PRK04837 172 LGF---IKDIRWLFrrmppANQRLNMLFSATLSYRVRELAFEHMN-NPEYVEVEPEQKTGHRIKEELFY---PSnEEKMR 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  397 LLFTFLKKNRKKKLMVFFS---SCMSVKFHYE-------LLNyidlpvmaihGKQKQTKRTTTFFQFCNADSGILLCTDV 466
Cdd:PRK04837 245 LLQTLIEEEWPDRAIIFANtkhRCEEIWGHLAadghrvgLLT----------GDVAQKKRLRILEEFTRGDLDILVATDV 314
                        330       340       350
                 ....*....|....*....|....*....|....
gi 51010913  467 AARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTAR 500
Cdd:PRK04837 315 AARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGR 348
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
173-500 3.07e-52

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 187.04  E-value: 3.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIY-----KLKFM--PRngtgVIVLSPTREL 245
Cdd:PRK01297  99 MHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLqtpppKERYMgePR----ALIIAPTREL 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  246 AMQTYGVLKELMTH---HVHTYgliMGGSNRSAEAQKL-ANGVNILVATPGRLLDHLQNTPGFMfKNLQCLIIDEADRIL 321
Cdd:PRK01297 175 VVQIAKDAAALTKYtglNVMTF---VGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHL-DMVEVMVLDEADRML 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  322 EVGFEEELKQIIKLLPKK--RQSMLFSATQTRKVEDLARiSLKKEPLYVGVD-DNKDTATVEglEQGYVVCPSEKrFLLL 398
Cdd:PRK01297 251 DMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAK-QWTTDPAIVEIEpENVASDTVE--QHVYAVAGSDK-YKLL 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  399 FTFLKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDW 478
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
                        330       340
                 ....*....|....*....|..
gi 51010913  479 IVQFDPPDDPKEYIHRVGRTAR 500
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGR 428
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
382-512 1.24e-51

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: 174.23  E-value: 1.24e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 382 LEQGYVVCPS-EKRFLLLFTFLKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGI 460
Cdd:cd18787   1 IKQLYVVVEEeEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 51010913 461 LLCTDVAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTARGinGR-GHALLIL 512
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRA--GRkGTAITFV 131
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
161-368 5.72e-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: 172.79  E-value: 5.72e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 161 FASLSevVSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPsieLIYKLKfmpRNGTGV--IV 238
Cdd:cd17955   1 FEDLG--LSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP---ILQRLS---EDPYGIfaLV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 239 LSPTRELAMQ------TYGVLkelmtHHVHTyGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPG--FMFKNLQ 310
Cdd:cd17955  73 LTPTRELAYQiaeqfrALGAP-----LGLRC-CVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVK 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51010913 311 CLIIDEADRILEVGFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARISLKKEPLYV 368
Cdd:cd17955 147 FLVLDEADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
173-356 5.88e-50

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: 172.77  E-value: 5.88e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFM--PRNGTGVIVLSPTRELAMQTY 250
Cdd:cd17961   6 LKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAEsgEEQGTRALILVPTRELAQQVS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 251 GVLKELMTH---HVHTYGLimgGSNRSAEAQK--LANGVNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADRILEVGF 325
Cdd:cd17961  86 KVLEQLTAYcrkDVRVVNL---SASSSDSVQRalLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSYGY 162
                       170       180       190
                ....*....|....*....|....*....|.
gi 51010913 326 EEELKQIIKLLPKKRQSMLFSATQTRKVEDL 356
Cdd:cd17961 163 EEDLKSLLSYLPKNYQTFLMSATLSEDVEAL 193
DEXDc smart00487
DEAD-like helicases superfamily;
176-364 1.28e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 168.82  E-value: 1.28e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913    176 VKEMGFDTMTEIQHKTIRPLLEG-RDVLAAAKTGSGKTLAFLIPSIELIYKlkfmpRNGTGVIVLSPTRELAMQTYGVLK 254
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-----GKGGRVLVLVPTRELAEQWAEELK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913    255 ELMTHHVHTYGLIMGGSNRSAEAQKLANGV-NILVATPGRLLDHLQNTPgFMFKNLQCLIIDEADRILEVGFEEELKQII 333
Cdd:smart00487  76 KLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDK-LSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190
                   ....*....|....*....|....*....|.
gi 51010913    334 KLLPKKRQSMLFSATQTRKVEDLARISLKKE 364
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDP 185
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
173-500 2.84e-48

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 178.22  E-value: 2.84e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSI-ELIYKLKFMPRNGTG--VIVLSPTRELAMQT 249
Cdd:PRK04537  21 LAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMnRLLSRPALADRKPEDprALILAPTRELAIQI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  250 YGVLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADRILEVGFEEEL 329
Cdd:PRK04537 101 HKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDEADRMFDLGFIKDI 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  330 KQIIKLLPKK--RQSMLFSATQTRKVEDLARISLKkEPLYVGVDdnKDTATVEGLEQGYVVCPSEKRFLLLFTFLKKNRK 407
Cdd:PRK04537 181 RFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMN-EPEKLVVE--TETITAARVRQRIYFPADEEKQTLLLGLLSRSEG 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  408 KKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQFDPPDD 487
Cdd:PRK04537 258 ARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFD 337
                        330
                 ....*....|...
gi 51010913  488 PKEYIHRVGRTAR 500
Cdd:PRK04537 338 AEDYVHRIGRTAR 350
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
160-601 3.49e-48

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 178.89  E-value: 3.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  160 SFASLSevVSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRngtgVIVL 239
Cdd:PRK11634   7 TFADLG--LKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQ----ILVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  240 SPTRELAMQTYGVLKELmTHHVHTYGLIM--GGSNRSAEAQKLANGVNILVATPGRLLDHLQNtpGFM-FKNLQCLIIDE 316
Cdd:PRK11634  81 APTRELAVQVAEAMTDF-SKHMRGVNVVAlyGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKR--GTLdLSKLSGLVLDE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  317 ADRILEVGFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARiSLKKEPLYVGVDDNkdTATVEGLEQGYVVCPSEKRFL 396
Cdd:PRK11634 158 ADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITR-RFMKEPQEVRIQSS--VTTRPDISQSYWTVWGMRKNE 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  397 LLFTFLKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEV 476
Cdd:PRK11634 235 ALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  477 DWIVQFDPPDDPKEYIHRVGRTARGinGR-GHALLILRPEELGFLRFLKQA-KVPLSEFEFSWTKISDiQSQLDKLIEK- 553
Cdd:PRK11634 315 SLVVNYDIPMDSESYVHRIGRTGRA--GRaGRALLFVENRERRLLRNIERTmKLTIPEVELPNAELLG-KRRLEKFAAKv 391
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 51010913  554 NYYLHKSAQEAYKSYVRAYDSHSLKQIYNVETLDLPKVAMSFGFK---VPP 601
Cdd:PRK11634 392 QQQLESSDLDQYRALLAKIQPTAEGEELDLETLAAALLKMAQGERpliLPP 442
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
160-358 2.85e-47

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: 165.74  E-value: 2.85e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 160 SFAS--LSEVVSENtlkgVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRNGTG-- 235
Cdd:cd17967   1 SFEEagLRELLLEN----IKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRrk 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 236 ----VIVLSPTRELAMQTYGVLKELmthhvhTYGLIM------GGSNRSAEAQKLANGVNILVATPGRLLDHLQNtpGF- 304
Cdd:cd17967  77 aypsALILAPTRELAIQIYEEARKF------SYRSGVrsvvvyGGADVVHQQLQLLRGCDILVATPGRLVDFIER--GRi 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51010913 305 MFKNLQCLIIDEADRILEVGFEEELKQII--KLLPKK--RQSMLFSATQTRKVEDLAR 358
Cdd:cd17967 149 SLSSIKFLVLDEADRMLDMGFEPQIRKIVehPDMPPKgeRQTLMFSATFPREIQRLAA 206
PTZ00424 PTZ00424
helicase 45; Provisional
139-521 5.03e-47

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 170.78  E-value: 5.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  139 EDSDEDGPQLPSGLTGAFEDR------SFASLSevVSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKT 212
Cdd:PTZ00424   2 ATSEQKNQSEQVASTGTIESNydeivdSFDALK--LNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  213 LAFLIPSIELI-YKLkfmprNGTGVIVLSPTRELAMQTYGVLKELMTH-HVHTYGLImGGSNRSAEAQKLANGVNILVAT 290
Cdd:PTZ00424  80 ATFVIAALQLIdYDL-----NACQALILAPTRELAQQIQKVVLALGDYlKVRCHACV-GGTVVRDDINKLKAGVHMVVGT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  291 PGRLLDHLqNTPGFMFKNLQCLIIDEADRILEVGFEEELKQIIKLLPKKRQSMLFSATQ--------TRKVEDLARISLK 362
Cdd:PTZ00424 154 PGRVYDMI-DKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMpneileltTKFMRDPKRILVK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  363 KEPLyvgvddnkdtaTVEGLEQGYVVCPSEK-RFLLLFTFLKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQ 441
Cdd:PTZ00424 233 KDEL-----------TLEGIRQFYVAVEKEEwKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDM 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  442 KQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTARgINGRGHALLILRPEELGFLR 521
Cdd:PTZ00424 302 DQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGR-FGRKGVAINFVTPDDIEQLK 380
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
173-368 1.98e-45

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: 160.95  E-value: 1.98e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPR----NGTGVIVLSPTRELAMQ 248
Cdd:cd17945   2 LRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEetkdDGPYALILAPTRELAQQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 249 TYGVLKELMTHhvhtYGL----IMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTpgfMFKNLQC--LIIDEADRILE 322
Cdd:cd17945  82 IEEETQKFAKP----LGIrvvsIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERR---LLVLNQCtyVVLDEADRMID 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51010913 323 VGFEEELKQIIKLLP--------------------KKRQSMLFSATQTRKVEDLARISLKKePLYV 368
Cdd:cd17945 155 MGFEPQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRR-PVVV 219
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
173-358 2.02e-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: 151.97  E-value: 2.02e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKlkfmPRNGTGV--IVLSPTRELAMQTY 250
Cdd:cd17957   2 LNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK----PRKKKGLraLILAPTRELASQIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 251 GVLKELMTHH-VHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPgFMFKNLQCLIIDEADRILEVGFEEEL 329
Cdd:cd17957  78 RELLKLSKGTgLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEPGFREQT 156
                       170       180       190
                ....*....|....*....|....*....|
gi 51010913 330 KQIIKLLP-KKRQSMLFSATQTRKVEDLAR 358
Cdd:cd17957 157 DEILAACTnPNLQRSLFSATIPSEVEELAR 186
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
169-348 4.73e-42

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: 150.94  E-value: 4.73e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 169 SENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYklkfMPRNGTGVIVLSPTRELAMQ 248
Cdd:cd17939   5 SEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRID----TTVRETQALVLAPTRELAQQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 249 TYGVLKEL---MTHHVHtygLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTpGFMFKNLQCLIIDEADRILEVGF 325
Cdd:cd17939  81 IQKVVKALgdyMGVKVH---ACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRR-SLRTDKIKMFVLDEADEMLSRGF 156
                       170       180
                ....*....|....*....|...
gi 51010913 326 EEELKQIIKLLPKKRQSMLFSAT 348
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSAT 179
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
173-368 5.15e-42

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: 150.95  E-value: 5.15e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIP----SIELIYKLKFMPRNGTGVIVLSPTRELAMQ 248
Cdd:cd17951   2 LKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlimfALEQEKKLPFIKGEGPYGLIVCPSRELARQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 249 TYGVLkELMTHHVHTYG-------LIMGGSNRSAEAQKLANGVNILVATPGRLLDHLqNTPGFMFKNLQCLIIDEADRIL 321
Cdd:cd17951  82 THEVI-EYYCKALQEGGypqlrclLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADRMI 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 51010913 322 EVGFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARISLKKePLYV 368
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVK-PVTV 205
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
173-363 1.55e-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: 1.55e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYklkfMPRNGTGVIVLSPTRELAMQTYGV 252
Cdd:cd17940  11 LMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKID----PKKDVIQALILVPTRELALQTSQV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 253 LKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFMfKNLQCLIIDEADRILEVGFEEELKQI 332
Cdd:cd17940  87 CKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADL-SHCKTLVLDEADKLLSQDFQPIIEKI 165
                       170       180       190
                ....*....|....*....|....*....|.
gi 51010913 333 IKLLPKKRQSMLFSATQTRKVEDLARISLKK 363
Cdd:cd17940 166 LNFLPKERQILLFSATFPLTVKNFMDRHMHN 196
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
173-364 5.77e-41

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: 149.31  E-value: 5.77e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRP-LLEGRDVLAAAKTGSGKTLAFLIPSIE-LIYKLKFMPRNG--TGVI--VLSPTRELA 246
Cdd:cd17946   2 LRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILErLLSQKSSNGVGGkqKPLRalILTPTRELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 247 MQTYGVLKELMTHHVHTYGLIMGGsnRSAEAQK--LANGVNILVATPGRLLDHLQNTPGFM--FKNLQCLIIDEADRILE 322
Cdd:cd17946  82 VQVKDHLKAIAKYTNIKIASIVGG--LAVQKQErlLKKRPEIVVATPGRLWELIQEGNEHLanLKSLRFLVLDEADRMLE 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 51010913 323 VGFEEELKQIIKLLP-------KKRQSMLFSATQTRKVEDLARISLKKE 364
Cdd:cd17946 160 KGHFAELEKILELLNkdragkkRKRQTFVFSATLTLDHQLPLKLNSKKK 208
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
173-368 7.00e-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: 148.93  E-value: 7.00e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEG---------RDVLAAAKTGSGKTLAFLIPSIELIYKlKFMPRngTGVIVLSPTR 243
Cdd:cd17956   2 LKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSK-RVVPR--LRALIVVPTK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 244 ELAMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQKLANG--------VNILVATPGRLLDHLQNTPGFMFKNLQCLIID 315
Cdd:cd17956  79 ELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGFTLKHLRFLVID 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51010913 316 EADRILEVGFEEELKQIIKLL--------------------PKKRQSMLFSATQTRKVEDLARISLKKEPLYV 368
Cdd:cd17956 159 EADRLLNQSFQDWLETVMKALgrptapdlgsfgdanllersVRPLQKLLFSATLTRDPEKLSSLKLHRPRLFT 231
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
173-362 9.99e-40

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: 144.43  E-value: 9.99e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPR-NGTGVIVLSPTRELAMQTYG 251
Cdd:cd17966   2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERgDGPIVLVLAPTRELAQQIQQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 252 VLKELmthhVHTYGL----IMGGSNRSAEAQKLANGVNILVATPGRLLDHLQN--TPgfmFKNLQCLIIDEADRILEVGF 325
Cdd:cd17966  82 EANKF----GGSSRLrntcVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQgkTN---LRRVTYLVLDEADRMLDMGF 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 51010913 326 EEELKQIIKLLPKKRQSMLFSATQTRKVEDLARISLK 362
Cdd:cd17966 155 EPQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLK 191
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
180-500 1.44e-39

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 152.63  E-value: 1.44e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  180 GFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIE---LIYKLKFMPRNGTGVIVLSPTRELAMQTYGVLKEL 256
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTIRSGHPSEQRNPLAMVLTPTRELCVQVEDQAKVL 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  257 MTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTpGFMFKNLQCLIIDEADRILEVGFEEELKQIIKLL 336
Cdd:PLN00206 220 GKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKH-DIELDNVSVLVLDEVDCMLERGFRDQVMQIFQAL 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  337 PKKrQSMLFSATQTRKVEDLARiSLKKEPLYVGV-DDNKDTATVeglEQGYVVCPSEKRFLLLFTFLK-KNR-KKKLMVF 413
Cdd:PLN00206 299 SQP-QVLLFSATVSPEVEKFAS-SLAKDIILISIgNPNRPNKAV---KQLAIWVETKQKKQKLFDILKsKQHfKPPAVVF 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  414 FSSCMSVKFHYELLNYID-LPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQFDPPDDPKEYI 492
Cdd:PLN00206 374 VSSRLGADLLANAITVVTgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYI 453

                 ....*...
gi 51010913  493 HRVGRTAR 500
Cdd:PLN00206 454 HQIGRASR 461
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
168-363 1.73e-39

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: 144.44  E-value: 1.73e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 168 VSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIyKLKFMPRNGTGVI--VLSPTREL 245
Cdd:cd17953  19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI-KDQRPVKPGEGPIglIMAPTREL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 246 AMQTYGVLKELMThhvhTYGLIM----GGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFM--FKNLQCLIIDEADR 319
Cdd:cd17953  98 ALQIYVECKKFSK----ALGLRVvcvyGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVtnLRRVTYVVLDEADR 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 51010913 320 ILEVGFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLARISLKK 363
Cdd:cd17953 174 MFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHK 217
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
173-358 5.86e-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: 139.47  E-value: 5.86e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFM-PRNGTGVIVLSPTRELAMQTYG 251
Cdd:cd17952   2 LNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELeKGEGPIAVIVAPTRELAQQIYL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 252 VLKELmthhVHTYGL----IMGGSNRSAEAQKLANGVNILVATPGRLLDHLQnTPGFMFKNLQCLIIDEADRILEVGFEE 327
Cdd:cd17952  82 EAKKF----GKAYNLrvvaVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVK-KKATNLQRVTYLVLDEADRMFDMGFEY 156
                       170       180       190
                ....*....|....*....|....*....|.
gi 51010913 328 ELKQIIKLLPKKRQSMLFSATQTRKVEDLAR 358
Cdd:cd17952 157 QVRSIVGHVRPDRQTLLFSATFKKKIEQLAR 187
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
173-368 1.89e-36

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: 135.28  E-value: 1.89e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPS-IELIYKL-KFMPRNGTGVIVLSPTRELAMQTY 250
Cdd:cd17958   2 MKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGfIHLDLQPiPREQRNGPGVLVLTPTRELALQIE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 251 GVLKELMTHHVHTYgLIMGGSNRSAEAQKLANGVNILVATPGRLLDhLQNTPGFMFKNLQCLIIDEADRILEVGFEEELK 330
Cdd:cd17958  82 AECSKYSYKGLKSV-CVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 51010913 331 QIIKLLPKKRQSMLFSATQTRKVEDLARiSLKKEPLYV 368
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQ-SYLKDPMIV 196
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
145-370 4.57e-36

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: 136.25  E-value: 4.57e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 145 GPQLPSGLTgAFEDrsfASLSEVVSENtlkgVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIEliy 224
Cdd:cd18052  35 GRNPPPAIL-TFEE---ANLCETLLKN----IRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLT--- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 225 klKFMPRNGTG----------VIVLSPTRELAMQTYgvlKEL-------MTHHVHTYglimGGSNRSAEAQKLANGVNIL 287
Cdd:cd18052 104 --GMMKEGLTAssfsevqepqALIVAPTRELANQIF---LEArkfsygtCIRPVVVY----GGVSVGHQIRQIEKGCHIL 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 288 VATPGRLLDHLqNTPGFMFKNLQCLIIDEADRILEVGFEEELKQIIKLL--PKK--RQSMLFSATQTRKVEDLARISLKK 363
Cdd:cd18052 175 VATPGRLLDFI-GRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmPSKedRQTLMFSATFPEEIQRLAAEFLKE 253

                ....*..
gi 51010913 364 EPLYVGV 370
Cdd:cd18052 254 DYLFLTV 260
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
176-368 7.63e-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: 130.75  E-value: 7.63e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 176 VKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPsieLIYKLKFMPRNGTGVIvLSPTRELAMQTYGVLKE 255
Cdd:cd17962   5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLP---VIIRCLTEHRNPSALI-LTPTRELAVQIEDQAKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 256 LMTHHVH-TYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLqNTPGFMFKNLQCLIIDEADRILEVGFEEELKQIIK 334
Cdd:cd17962  81 LMKGLPPmKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILE 159
                       170       180       190
                ....*....|....*....|....*....|....
gi 51010913 335 LLPKKRQSMLFSATQTRKVEDLARiSLKKEPLYV 368
Cdd:cd17962 160 NISHDHQTILVSATIPRGIEQLAG-QLLQNPVRI 192
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
145-358 1.11e-34

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: 132.09  E-value: 1.11e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 145 GPQLPSGLTgAFEDrsfASLSEVVSENtlkgVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIY 224
Cdd:cd18051  13 GENCPPHIE-TFSD---LDLGEIIRNN----IELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 225 KL---KFMPRNGTG---------VIVLSPTRELAMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPG 292
Cdd:cd18051  85 EQgpgESLPSESGYygrrkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPG 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51010913 293 RLLDHLQNtpGFM-FKNLQCLIIDEADRILEVGFEEELKQIIK--LLPKK--RQSMLFSATQTRKVEDLAR 358
Cdd:cd18051 165 RLVDMLER--GKIgLDYCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPKEIQMLAR 233
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
168-358 9.90e-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: 127.95  E-value: 9.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 168 VSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELI-YKLKfmprnGTGVIVLSPTRELA 246
Cdd:cd18046   6 LKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIdTSLK-----ATQALVLAPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 247 MQTYGV---LKELMTHHVHTyglIMGGSNRSAEAQKLANGVNILVATPGRLLDHLqNTPGFMFKNLQCLIIDEADRILEV 323
Cdd:cd18046  81 QQIQKVvmaLGDYMGIKCHA---CIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSR 156
                       170       180       190
                ....*....|....*....|....*....|....*
gi 51010913 324 GFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLAR 358
Cdd:cd18046 157 GFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTT 191
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
174-348 4.59e-33

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: 125.90  E-value: 4.59e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 174 KGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYklkfmprngtgVIVLSPTRELAMQTYGVL 253
Cdd:cd17938  12 KAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV-----------ALILEPSRELAEQTYNCI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 254 ---KELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDhLQNTPGFMFKNLQCLIIDEADRILEVGFEEELK 330
Cdd:cd17938  81 enfKKYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLED-LIKTGKLDLSSVRFFVLDEADRLLSQGNLETIN 159
                       170       180
                ....*....|....*....|....
gi 51010913 331 QIIKLLPK-----KR-QSMLFSAT 348
Cdd:cd17938 160 RIYNRIPKitsdgKRlQVIVCSAT 183
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
171-362 1.10e-31

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: 123.20  E-value: 1.10e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 171 NTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPR-NGTGVIVLSPTRELAMQT 249
Cdd:cd18049  34 NVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERgDGPICLVLAPTRELAQQV 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 250 YGVLKELMTHHVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFMfKNLQCLIIDEADRILEVGFEEEL 329
Cdd:cd18049 114 QQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNL-RRCTYLVLDEADRMLDMGFEPQI 192
                       170       180       190
                ....*....|....*....|....*....|...
gi 51010913 330 KQIIKLLPKKRQSMLFSATQTRKVEDLARISLK 362
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, ...
172-348 1.84e-31

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: 121.22  E-value: 1.84e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 172 TLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLkfmpRNGTGVIVLSPTRELAMQTYG 251
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE----RRHPQVLILAPTREIAVQIHD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 252 VLKELMTH----HVHTYgliMGGSNRSAEAQKLaNGVNILVATPGRLLdHLQNTPGFMFKNLQCLIIDEADRILEVGFEE 327
Cdd:cd17943  77 VFKKIGKKleglKCEVF---IGGTPVKEDKKKL-KGCHIAVGTPGRIK-QLIELGALNVSHVRLFVLDEADKLMEGSFQK 151
                       170       180
                ....*....|....*....|.
gi 51010913 328 ELKQIIKLLPKKRQSMLFSAT 348
Cdd:cd17943 152 DVNWIFSSLPKNKQVIAFSAT 172
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
170-356 2.12e-31

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: 121.42  E-value: 2.12e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 170 ENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFlipSIELIYKLKFMPRNgTGVIVLSPTRELAMQT 249
Cdd:cd18045   8 EDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATF---SISVLQCLDIQVRE-TQALILSPTRELAVQI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 250 YGVLKELMTH-HVHTYGLImGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTpGFMFKNLQCLIIDEADRILEVGFEEE 328
Cdd:cd18045  84 QKVLLALGDYmNVQCHACI-GGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRR-SLRTRHIKMLVLDEADEMLNKGFKEQ 161
                       170       180
                ....*....|....*....|....*...
gi 51010913 329 LKQIIKLLPKKRQSMLFSATQTRKVEDL 356
Cdd:cd18045 162 IYDVYRYLPPATQVVLVSATLPQDILEM 189
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
181-357 7.56e-30

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: 118.96  E-value: 7.56e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 181 FDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPR-NGTGVIVLSPTRELAMQTYGVLKELMTH 259
Cdd:cd18050  82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERgDGPICLVLAPTRELAQQVQQVADDYGKS 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 260 HVHTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFMfKNLQCLIIDEADRILEVGFEEELKQIIKLLPKK 339
Cdd:cd18050 162 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNL-RRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 240
                       170
                ....*....|....*...
gi 51010913 340 RQSMLFSATQTRKVEDLA 357
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 ...
172-371 9.14e-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: 116.49  E-value: 9.14e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 172 TLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRNGTG--VIVLSPTRELAMQT 249
Cdd:cd17944   1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRApkVLVLAPTRELANQV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 250 YGVLKELmTHHVhTYGLIMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPgFMFKNLQCLIIDEADRILEVGFEEEL 329
Cdd:cd17944  81 TKDFKDI-TRKL-SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLDMGFAEQV 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 51010913 330 KQIIKLLPKKR-----QSMLFSATQTRKVEDLARISLKKEplYVGVD 371
Cdd:cd17944 158 EEILSVSYKKDsednpQTLLFSATCPDWVYNVAKKYMKSQ--YEQVD 202
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
169-358 1.15e-27

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: 110.36  E-value: 1.15e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 169 SENTLKGVKEMGFDTMTEIQHKTIrPLLEG---RDVLAAAKTGSGKTLAFLIPSIELI-YKLKFmprngTGVIVLSPTRE 244
Cdd:cd17963   2 KPELLKGLYAMGFNKPSKIQETAL-PLILSdppENLIAQSQSGTGKTAAFVLAMLSRVdPTLKS-----PQALCLAPTRE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 245 LAMQTYGVLKELMTHHVHTYGLIMGGS----NRSAEAQklangvnILVATPGRLLDHLQnTPGFMFKNLQCLIIDEADRI 320
Cdd:cd17963  76 LARQIGEVVEKMGKFTGVKVALAVPGNdvprGKKITAQ-------IVIGTPGTVLDWLK-KRQLDLKKIKILVLDEADVM 147
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 51010913 321 LEV-GFEEELKQIIKLLPKKRQSMLFSATQTRKVEDLAR 358
Cdd:cd17963 148 LDTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAE 186
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
393-500 6.38e-27

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: 105.37  E-value: 6.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   393 KRFLLLFTFLKKNRKKKLMVFFSSCMSVKFHYeLLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLD 472
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100
                  ....*....|....*....|....*...
gi 51010913   473 IPEVDWIVQFDPPDDPKEYIHRVGRTAR 500
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 ...
173-363 4.01e-25

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: 103.58  E-value: 4.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKlkfmPRNGTGVIVLSPTRELAMQT--- 249
Cdd:cd17950  14 LRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEP----VDGQVSVLVICHTRELAFQIsne 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 250 YGVLKELMtHHVHTyGLIMGGSNRSAEAQKLANGV-NILVATPGRLLDHLQNTpGFMFKNLQCLIIDEADRILE-VGFEE 327
Cdd:cd17950  90 YERFSKYM-PNVKT-AVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREK-KLKLSHVKHFVLDECDKMLEqLDMRR 166
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 51010913 328 ELKQIIKLLPKKRQSMLFSATQTRKvedlARISLKK 363
Cdd:cd17950 167 DVQEIFRATPHDKQVMMFSATLSKE----IRPVCKK 198
HELICc smart00490
helicase superfamily c-terminal domain;
421-500 1.65e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.59  E-value: 1.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913    421 KFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTAR 500
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
544-601 2.84e-21

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: 87.45  E-value: 2.84e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 51010913   544 QSQLDKLIEKNYYLHKSAQEAYKSYVRAYDSHSLKQIYNVETLDLPKVAMSFGFKVPP 601
Cdd:pfam13959   1 QLQLEKLVLKDRELKELAQKAFVSYVRAYSKHLAKSIFNVKKLDLGHLAKSFGLLRAP 58
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
197-511 1.56e-20

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 95.86  E-value: 1.56e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 197 EGRDVLAAAKTGSGKTLAFLipsiELIYKLKFMPRngtgVIVLSPTRELAMQTYGVLKElmthhvHTYGLIMGGSNRSAE 276
Cdd:COG1061  99 GGGRGLVVAPTGTGKTVLAL----ALAAELLRGKR----VLVLVPRRELLEQWAEELRR------FLGDPLAGGGKKDSD 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 277 AqklangvNILVATPGRL-----LDHLQNTPGFmfknlqcLIIDEADRIlevgFEEELKQIIKLLPKKRqsML-FSAT-- 348
Cdd:COG1061 165 A-------PITVATYQSLarrahLDELGDRFGL-------VIIDEAHHA----GAPSYRRILEAFPAAY--RLgLTATpf 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 349 ----QTRKVEDLA----RISLK--------KEPLYVGVDD------NKDTATVEGLEQGYVVCPSEKRfLLLFTFLKKNR 406
Cdd:COG1061 225 rsdgREILLFLFDgivyEYSLKeaiedgylAPPEYYGIRVdltderAEYDALSERLREALAADAERKD-KILRELLREHP 303
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 407 K-KKLMVFfssCMSVKfH----YELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQ 481
Cdd:COG1061 304 DdRKTLVF---CSSVD-HaealAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL 379
                       330       340       350
                ....*....|....*....|....*....|
gi 51010913 482 FDPPDDPKEYIHRVGRTARGINGRGHALLI 511
Cdd:COG1061 380 LRPTGSPREFIQRLGRGLRPAPGKEDALVY 409
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
198-348 2.16e-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: 87.84  E-value: 2.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 198 GRDVLAAAKTGSGKTLAFLIPSIELIYKlkfmprNGTGVIVLSPTRELAMQTYGVLKELMTHHVHTYglIMGGSNRSAEA 277
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLK------KGKKVLVLVPTKALALQTAERLRELFGPGIRVA--VLVGGSSAEER 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51010913 278 QKLANGVN-ILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADRIL--EVGFEEELKQIIKLLPKKRQSMLFSAT 348
Cdd:cd00046  73 EKNKLGDAdIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLidSRGALILDLAVRKAGLKNAQVILLSAT 146
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
156-366 2.49e-20

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: 90.47  E-value: 2.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 156 FEDRSFASLSevVSENTLKGVKEMGFDTMTEIQHKTIRPLLEG--RDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRng 233
Cdd:cd18048  15 FSVKSFEELH--LKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQ-- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 234 tgVIVLSPTRELAMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQKLAngVNILVATPGRLLDHLQNTPGFMFKNLQCLI 313
Cdd:cd18048  91 --CLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIE--AQIVIGTPGTVLDWCFKLRLIDVTNISVFV 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51010913 314 IDEADRILEV-GFEEELKQIIKLLPKKRQSMLFSAT--------QTRKVEDLARISLKKEPL 366
Cdd:cd18048 167 LDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATfedsvwafAERIVPDPNIIKLKKEEL 228
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
177-356 3.92e-20

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: 89.73  E-value: 3.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 177 KEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRNGTG---VIVLSPTRELAMQTYGVL 253
Cdd:cd17948   6 QRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNaprGLVITPSRELAEQIGSVA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 254 KELmthhvhTYGL------IMGGSNRSAEAQKLANGVNILVATPGRLLDhLQNTPGFMFKNLQCLIIDEADRILEVGFEE 327
Cdd:cd17948  86 QSL------TEGLglkvkvITGGRTKRQIRNPHFEEVDILVATPGALSK-LLTSRIYSLEQLRHLVLDEADTLLDDSFNE 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 51010913 328 ELKQIIKLLP-------------KKRQSMLFSATQTRKVEDL 356
Cdd:cd17948 159 KLSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEV 200
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
202-348 8.56e-19

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: 86.28  E-value: 8.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 202 LAAAKTGSGKTLAFLIPSIELIYKLKFMPRNGTG-------------VIVLSPTRELAMQTYGVLKELmtHHVHTYGLIM 268
Cdd:cd17965  65 LLAAETGSGKTLAYLAPLLDYLKRQEQEPFEEAEeeyesakdtgrprSVILVPTHELVEQVYSVLKKL--SHTVKLGIKT 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 269 GGSNRSAEAQKLA----NGVNILVATPGRLLDhLQNTPGFMFKNLQCLIIDEADRILEVGFEEELKQIIKLLPKKRQSML 344
Cdd:cd17965 143 FSSGFGPSYQRLQlafkGRIDILVTTPGKLAS-LAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLIL 221

                ....
gi 51010913 345 FSAT 348
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 ...
173-348 3.59e-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: 68.98  E-value: 3.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 173 LKGVKEMGFDTMTEIQHKTIRPLLEG--RDVLAAAKTGSGKTLAFLIPSIELIYKlkfmPRNGTGVIVLSPTRELAMQTY 250
Cdd:cd18047  13 LQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEP----ANKYPQCLCLSPTYELALQTG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 251 GVLKELMTHHVHTYGLIMGGSNRSAEAQKLANgvNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADRILEV-GFEEEL 329
Cdd:cd18047  89 KVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATqGHQDQS 166
                       170
                ....*....|....*....
gi 51010913 330 KQIIKLLPKKRQSMLFSAT 348
Cdd:cd18047 167 IRIQRMLPRNCQMLLFSAT 185
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
183-367 8.82e-13

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: 66.90  E-value: 8.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 183 TMTEIQHKTIRPL-LEGRDVLAAAKTGSGKTLAFLIpsieLIYKLKFmpRNGTGVIVLSPTRELAMQTYGVLKELMTHHV 261
Cdd:cd17921   1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAEL----AILRALA--TSGGKAVYIAPTRALVNQKEADLRERFGPLG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 262 HTYGLIMGG--SNRSAEAQKlangvNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADrilEVGFEEE---LKQIIKLL 336
Cdd:cd17921  75 KNVGLLTGDpsVNKLLLAEA-----DILVATPEKLDLLLRNGGERLIQDVRLVVVDEAH---LIGDGERgvvLELLLSRL 146
                       170       180       190
                ....*....|....*....|....*....|....
gi 51010913 337 P---KKRQSMLFSATqTRKVEDLARIsLKKEPLY 367
Cdd:cd17921 147 LrinKNARFVGLSAT-LPNAEDLAEW-LGVEDLI 178
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
198-384 1.04e-11

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: 63.76  E-value: 1.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 198 GRDVLAAAKTGSGKTLAFLIPSIELIYKLkfmPRNGTGVIVLSPTRELAMQTYGVLKELMTHHVH--TYGLIMGGSNRSA 275
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADE---PEKGVQVLYISPLKALINDQERRLEEPLDEIDLeiPVAVRHGDTSQSE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 276 EAQKLANGVNILVATPGRLLDHLQNTPGF-MFKNLQCLIIDEadrilevgfeeelkqIIKLLPKKRQSMLFSAtqtrkve 354
Cdd:cd17922  78 KAKQLKNPPGILITTPESLELLLVNKKLReLFAGLRYVVVDE---------------IHALLGSKRGVQLELL------- 135
                       170       180       190
                ....*....|....*....|....*....|..
gi 51010913 355 dLARIS--LKKEPLYVGVddnkdTATVEGLEQ 384
Cdd:cd17922 136 -LERLRklTGRPLRRIGL-----SATLGNLEE 161
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
165-385 6.21e-11

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 65.30  E-value: 6.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 165 SEVVSENTLKGVKEMGFDTMTEIQHKTI-RPLLEGRDVLAAAKTGSGKTLaflipsIELIYKLKFMPRNGTgVIVLSPTR 243
Cdd:COG1204   4 AELPLEKVIEFLKERGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTL------IAELAILKALLNGGK-ALYIVPLR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 244 ELAMQTYGVLKELMTHHVHTYGLIMGgsNRSAEAQKLANgVNILVATPGRLLDHLQNTPGFMfKNLQCLIIDEA------ 317
Cdd:COG1204  77 ALASEKYREFKRDFEELGIKVGVSTG--DYDSDDEWLGR-YDILVATPEKLDSLLRNGPSWL-RDVDLVVVDEAhlidde 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51010913 318 DR--ILEVgfeeeLKQIIKLLPKKRQSMLFSATqTRKVEDLARIsLKKE---------PLYVGVDDNKDTATVEGLEQG 385
Cdd:COG1204 153 SRgpTLEV-----LLARLRRLNPEAQIVALSAT-IGNAEEIAEW-LDAElvksdwrpvPLNEGVLYDGVLRFDDGSRRS 224
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
188-317 8.14e-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: 58.37  E-value: 8.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 188 QHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKlkfmpRNGTGVIVLSPTRELAMQTYGVLKELM--THHVHTYG 265
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLR-----DPGSRALYLYPTKALAQDQLRSLRELLeqLGLGIRVA 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 51010913 266 LIMGGSNRSAEAQKLANGVNILVATPGRL----LDHLQNTPGFmFKNLQCLIIDEA 317
Cdd:cd17923  80 TYDGDTPREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARF-LRNLRYVVLDEA 134
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
207-348 1.11e-09

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: 57.32  E-value: 1.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 207 TGSGKTL-AFLIpsIELIYKLKfmprngtgVIVLSPTRELAMQTYGVLKELMTHHVhtYGLIMGGSNrsaeaqKLANGVN 285
Cdd:cd17926  27 TGSGKTLtALAL--IAYLKELR--------TLIVVPTDALLDQWKERFEDFLGDSS--IGLIGGGKK------KDFDDAN 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51010913 286 ILVATPgRLLDHLQNTPGFMFKNLQCLIIDEADRILEVGFEEelkqIIKLLPKKRQsMLFSAT 348
Cdd:cd17926  89 VVVATY-QSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSE----ILKELNAKYR-LGLTAT 145
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
440-505 3.10e-09

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 55.82  E-value: 3.10e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51010913 440 KQKQTKRTTTffQFCNADSGILLCTDVAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTARGINGR 505
Cdd:cd18801  75 SQKEQKEVIE--QFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQGR 138
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
160-317 3.41e-09

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: 59.85  E-value: 3.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 160 SFASLSEVVSENTLKGVKEMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKlkfmPRNGTgVIVL 239
Cdd:COG1205  33 RYAPWPDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE----DPGAT-ALYL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 240 SPTRELAMQTYGVLKELMTH-----HVHTYglimGGSNRSAEAQKLANGVNILVATP-----GrLLDHLQNTPGFmFKNL 309
Cdd:COG1205 108 YPTKALARDQLRRLRELAEAlglgvRVATY----DGDTPPEERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARF-FRNL 181

                ....*...
gi 51010913 310 QCLIIDEA 317
Cdd:COG1205 182 RYVVIDEA 189
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
170-355 6.61e-09

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: 56.39  E-value: 6.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 170 ENTLKGVkeMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSieLIyklkfmpRNGTgVIVLSPTREL---- 245
Cdd:cd17920   1 EQILKEV--FGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPA--LL-------LDGV-TLVVSPLISLmqdq 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 246 --AMQTYGVLKELMTHHVHTyglimggSNRSAEAQKLANG-VNILVATPGRL-----LDHLQNTPgfMFKNLQCLIIDEA 317
Cdd:cd17920  69 vdRLQQLGIRAAALNSTLSP-------EEKREVLLRIKNGqYKLLYVTPERLlspdfLELLQRLP--ERKRLALIVVDEA 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 51010913 318 DRILEVGFE-----EELKQIIKLLPKKrQSMLFSATQTRKVED 355
Cdd:cd17920 140 HCVSQWGHDfrpdyLRLGRLRRALPGV-PILALTATATPEVRE 181
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
402-505 4.33e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 56.28  E-value: 4.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 402 LKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQ--------KQTKRTTTFFQFCNADSGILLCTDVAARGLDI 473
Cdd:COG1111 348 LGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQAskegdkglTQKEQIEILERFRAGEFNVLVATSVAEEGLDI 427
                        90       100       110
                ....*....|....*....|....*....|....
gi 51010913 474 PEVDWIVQFDPPddPKE--YIHRVGRTARGINGR 505
Cdd:COG1111 428 PEVDLVIFYEPV--PSEirSIQRKGRTGRKREGR 459
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
460-501 4.41e-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: 50.40  E-value: 4.41e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 51010913 460 ILLCTDVAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTARG 501
Cdd:cd18785  25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRG 66
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
181-316 1.18e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 55.11  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 181 FDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLA-FLIPSIELI-YKLKFMPRNGTGVIVLSPTRELA------------ 246
Cdd:COG1201  22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAaFLPALDELArRPRPGELPDGLRVLYISPLKALAndiernlraple 101
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51010913 247 --MQTYGVLKELMTHHVHTyglimgGSNRSAEAQK-LANGVNILVATPGRL-LdhLQNTPGF--MFKNLQCLIIDE 316
Cdd:COG1201 102 eiGEAAGLPLPEIRVGVRT------GDTPASERQRqRRRPPHILITTPESLaL--LLTSPDAreLLRGVRTVIVDE 169
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
184-319 2.41e-07

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: 51.26  E-value: 2.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 184 MTEIQHKTIRPllEGRDVLAAAKTGSGKTLAFLIPSIeLIYKlkfmprNGTGVIVLSPTRELAMQTYGVLKELMTH-HVH 262
Cdd:cd17918  24 IKDIEKDLHSP--EPMDRLLSGDVGSGKTLVALGAAL-LAYK------NGKQVAILVPTEILAHQHYEEARKFLPFiNVE 94
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 51010913 263 tygLIMGGSNRSAEAqklanGVNILVATPGRLldHLQNtpgfMFKNLQCLIIDEADR 319
Cdd:cd17918  95 ---LVTGGTKAQILS-----GISLLVGTHALL--HLDV----KFKNLDLVIVDEQHR 137
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
194-319 2.91e-07

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 51.28  E-value: 2.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 194 PLLEGRDVLAAAKTGSGKTLAFLIPSIELIYklKFMPRNGTGVIVLSPTRELAMQTYGVLKELMTHHVHTYGLIMGGSNR 273
Cdd:cd17927  13 PALKGKNTIICLPTGSGKTFVAVLICEHHLK--KFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSE 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51010913 274 SAEAQKLANGVNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADR 319
Cdd:cd17927  91 NVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
180-357 8.72e-07

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: 49.95  E-value: 8.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 180 GFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSieliyklKFMPRNGTGV-IVLSPTRELAMQTYGVLKELMT 258
Cdd:cd18018   9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPA-------LLLRRRGPGLtLVVSPLIALMKDQVDALPRAIK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 259 hhVHTYGLIMGGSNRSAEAQKLANG-VNILVATPGRLldhlqNTPGFMF-----KNLQCLIIDEADRILEVGFE-----E 327
Cdd:cd18018  82 --AAALNSSLTREERRRILEKLRAGeVKILYVSPERL-----VNESFREllrqtPPISLLVVDEAHCISEWSHNfrpdyL 154
                       170       180       190
                ....*....|....*....|....*....|.
gi 51010913 328 ELKQIIKLLPKKRQSMLFSATQTRKV-EDLA 357
Cdd:cd18018 155 RLCRVLRELLGAPPVLALTATATKRVvEDIA 185
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
199-317 1.13e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 49.57  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 199 RDVLAAAKTGSGKTL--AFLIPsiELIYKLKFMPRNGTGVIVLSPTRELAMQTYGVLKELMTHHV-HTYGLIMGGSNRSA 275
Cdd:cd18034  17 RNTIVVLPTGSGKTLiaVMLIK--EMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTDLKVgEYSGEMGVDKWTKE 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 51010913 276 EAQKLANGVNILVATPGRLLDHLQNtpGFM-FKNLQCLIIDEA 317
Cdd:cd18034  95 RWKEELEKYDVLVMTAQILLDALRH--GFLsLSDINLLIFDEC 135
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
165-521 2.99e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 50.48  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  165 SEVVSENTLKGVkeMGFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSieliyklkfMPRNGTgVIVLSPTRE 244
Cdd:PRK11057   9 LESLAKQVLQET--FGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPA---------LVLDGL-TLVVSPLIS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  245 L------AMQTYGVLKELMThhvhtyglimggSNRSAEAQ-KLANG-----VNILVATPGRL-----LDHLQNTPGFMfk 307
Cdd:PRK11057  77 LmkdqvdQLLANGVAAACLN------------STQTREQQlEVMAGcrtgqIKLLYIAPERLmmdnfLEHLAHWNPAL-- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  308 nlqcLIIDEADRILEVG--FEEE------LKQIIKLLPkkrqSMLFSAT---QTRKveDLARISLKKEPL-YVGVDDNKD 375
Cdd:PRK11057 143 ----LAVDEAHCISQWGhdFRPEyaalgqLRQRFPTLP----FMALTATaddTTRQ--DIVRLLGLNDPLiQISSFDRPN 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  376 TAtvegleqgYVVCPSEKRFLLLFTFLKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCN 455
Cdd:PRK11057 213 IR--------YTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQR 284
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51010913  456 ADSGILLCTDVAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTAR-GINGRghALLILRPEELGFLR 521
Cdd:PRK11057 285 DDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRdGLPAE--AMLFYDPADMAWLR 349
ResIII pfam04851
Type III restriction enzyme, res subunit;
188-348 3.01e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 47.67  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   188 QHKTIRPLLEGRD-----VLAAAKTGSGKTL--AFLIpsieLIYKLKFMPRNgtgVIVLSPTRELAMQTYGVLKELMTHH 260
Cdd:pfam04851   8 QIEAIENLLESIKngqkrGLIVMATGSGKTLtaAKLI----ARLFKKGPIKK---VLFLVPRKDLLEQALEEFKKFLPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   261 VHTYGLIMGGSNRSAEAQKlangvNILVATPGRLLDHLQNTPGFMFKNLQ-CLIIDEADRILEVGFeeelKQIIKLLPKK 339
Cdd:pfam04851  81 VEIGEIISGDKKDESVDDN-----KIVVTTIQSLYKALELASLELLPDFFdVIIIDEAHRSGASSY----RNILEYFKPA 151

                  ....*....
gi 51010913   340 RQsMLFSAT 348
Cdd:pfam04851 152 FL-LGLTAT 159
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
180-529 6.50e-06

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 48.98  E-value: 6.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 180 GFDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSieLIyklkfmpRNGTGVIVlSPtreL---------AMQTY 250
Cdd:COG0514  14 GYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPA--LL-------LPGLTLVV-SP---LialmkdqvdALRAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 251 GVlkelmthHVHTYglimgGSNRSAEA-----QKLANG-VNILVATPGRLldhlqNTPGF--MFKNLQC--LIIDEADRI 320
Cdd:COG0514  81 GI-------RAAFL-----NSSLSAEErrevlRALRAGeLKLLYVAPERL-----LNPRFleLLRRLKIslFAIDEAHCI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 321 LEVG--FEEE---LKQIIKLLPkKRQSMLFSATQTRKVED--LARISLKKEPLYV-GVD-DNKDTATVEgleqgyvvCPS 391
Cdd:COG0514 144 SQWGhdFRPDyrrLGELRERLP-NVPVLALTATATPRVRAdiAEQLGLEDPRVFVgSFDrPNLRLEVVP--------KPP 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 392 EKRFLLLFTFLKKNRKKKLMVFFSS---CMSVkfhYELLNYIDLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTdVA- 467
Cdd:COG0514 215 DDKLAQLLDFLKEHPGGSGIVYCLSrkkVEEL---AEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAf 290
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51010913 468 ARGLDIPEVDWIVQFDPPDDPKEYIHRVGRTARGInGRGHALLILRPEELGFLRFLKQAKVP 529
Cdd:COG0514 291 GMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDG-LPAEALLLYGPEDVAIQRFFIEQSPP 351
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
198-317 2.25e-05

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: 45.36  E-value: 2.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 198 GRDVLAAAKTGSGKTLAFLIPSIELIYKLKfmprnGTGVIVLSPTRELAMQTYGVLKELM---------THHVHTYGLIM 268
Cdd:cd17930   1 PGLVILEAPTGSGKTEAALLWALKLAARGG-----KRRIIYALPTRATINQMYERIREILgrlddedkvLLLHSKAALEL 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51010913 269 ------GGSNRSAEAQKLANGVN-----ILVATPGRLLDHLQNTPGFMFK--NLQ--CLIIDEA 317
Cdd:cd17930  76 lesdeePDDDPVEAVDWALLLKRswlapIVVTTIDQLLESLLKYKHFERRlhGLAnsVVVLDEV 139
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
201-256 2.89e-05

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: 46.90  E-value: 2.89e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 51010913 201 VLAAAKTGSGKTLAFLIPSIELIyklkfmpRNGTGVIVLSPTRELAMQTYGVLKEL 256
Cdd:COG3505   2 VLVIGPTGSGKTVGLVIPNLTQL-------ARGESVVVTDPKGDLAELTAGFRRRA 50
mfd TIGR00580
transcription-repair coupling factor (mfd); All proteins in this family for which functions ...
232-332 4.79e-05

transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273152 [Multi-domain]  Cd Length: 926  Bit Score: 46.58  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   232 NGTGVIVLSPTRELAMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQ---KLANG-VNILVATpGRLLdhlqnTPGFMFK 307
Cdd:TIGR00580 499 DGKQVAVLVPTTLLAQQHFETFKERFANFPVTIELLSRFRSAKEQNEilkELASGkIDILIGT-HKLL-----QKDVKFK 572
                          90       100
                  ....*....|....*....|....*
gi 51010913   308 NLQCLIIDEADRiLEVGFEEELKQI 332
Cdd:TIGR00580 573 DLGLLIIDEEQR-FGVKQKEKLKEL 596
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
195-348 6.20e-05

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 44.25  E-value: 6.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 195 LLEGRDVLAAAKTGSGKTLaflipsIELIYKLKFMPRNGTGvIVLSPTRELAMQTYGVLKELmthhvHTYGLIMG---GS 271
Cdd:cd18028  14 LLKGENLLISIPTASGKTL------IAEMAMVNTLLEGGKA-LYLVPLRALASEKYEEFKKL-----EEIGLKVGistGD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 272 NRSaEAQKLANgVNILVATPGRLLDHLQNTPGFMfKNLQCLIIDE------ADR--ILEVgfeeeLKQIIKLLPKKRQSM 343
Cdd:cd18028  82 YDE-DDEWLGD-YDIIVATYEKFDSLLRHSPSWL-RDVGVVVVDEihlisdEERgpTLES-----IVARLRRLNPNTQII 153

                ....*
gi 51010913 344 LFSAT 348
Cdd:cd18028 154 GLSAT 158
PRK13766 PRK13766
Hef nuclease; Provisional
402-510 8.48e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 45.63  E-value: 8.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913  402 LKKNRKKKLMVFFSSCMSVKFHYELLNYIDLPVMAIHGK----------QKQTKRTTTffQFCNADSGILLCTDVAARGL 471
Cdd:PRK13766 360 LGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgmsQKEQIEILD--KFRAGEFNVLVSTSVAEEGL 437
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 51010913  472 DIPEVDWIVQFDPPddPKE--YIHRVGRTARGINGRGHALL 510
Cdd:PRK13766 438 DIPSVDLVIFYEPV--PSEirSIQRKGRTGRQEEGRVVVLI 476
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
460-500 2.06e-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: 41.81  E-value: 2.06e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 51010913 460 ILLCTDVAARGLDIPEVDWIVQFDPPDDPKEYIHRVGRtAR 500
Cdd:cd18802  93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-AR 132
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
184-336 4.51e-04

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: 41.54  E-value: 4.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 184 MTEIQHKTIRPLLEGRDVLAAAKTGSGKTlAFLipsieLIYKLKFMPRNGTGVIVLsPTRELAMQTYGVLKELMTH---- 259
Cdd:cd17924  18 PWGAQRTWAKRLLRGKSFAIIAPTGVGKT-TFG-----LATSLYLASKGKRSYLIF-PTKSLVKQAYERLSKYAEKagve 90
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51010913 260 -HVHTYGLIMGGSNRSAEAQKLANG-VNILVATPGRLLDHLQNTPGFMFknlQCLIIDEADRILEVGfeeelKQIIKLL 336
Cdd:cd17924  91 vKILVYHSRLKKKEKEELLEKIEKGdFDILVTTNQFLSKNFDLLSNKKF---DFVFVDDVDAVLKSS-----KNIDRLL 161
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
207-366 7.02e-04

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: 42.76  E-value: 7.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 207 TGSGKTLAFLIPSIELIYKlkfmpRNGTGVIVLSPTRELAMQTYGVLKELMT-----HH----VHTYGLIMGGSNRSAEA 277
Cdd:COG1203 156 TGGGKTEAALLFALRLAAK-----HGGRRIIYALPFTSIINQTYDRLRDLFGedvllHHsladLDLLEEEEEYESEARWL 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 278 QKLANGVN--ILVATPGRLLDHL-QNTPGFMFK--NLQ--CLIIDEAD-------RILEVG------------------- 324
Cdd:COG1203 231 KLLKELWDapVVVTTIDQLFESLfSNRKGQERRlhNLAnsVIILDEVQayppymlALLLRLlewlknlggsvilmtatlp 310
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 51010913 325 --FEEELKQIIKLLP-KKRQSMLFSATQTRKvedlaRISLKKEPL 366
Cdd:COG1203 311 plLREELLEAYELIPdEPEELPEYFRAFVRK-----RVELKEGPL 350
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
205-357 8.94e-04

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 42.60  E-value: 8.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   205 AKTGSGKTLAFLIPSIELIYKLKFM------PRNGTGVIVLSPT--------RELAMQTYGVLKELM----THHVHTYGL 266
Cdd:PRK09751    3 APTGSGKTLAAFLYALDRLFREGGEdtreahKRKTSRILYISPIkalgtdvqRNLQIPLKGIADERRrrgeTEVNLRVGI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913   267 IMGGSNRSAEAQKLANGVNILVATPGRLLDHLQNTPGFMFKNLQCLIIDEADRIleVGFEE------ELKQIIKLLPKKR 340
Cdd:PRK09751   83 RTGDTPAQERSKLTRNPPDILITTPESLYLMLTSRARETLRGVETVIIDEVHAV--AGSKRgahlalSLERLDALLHTSA 160
                         170
                  ....*....|....*..
gi 51010913   341 QSMLFSATqTRKVEDLA 357
Cdd:PRK09751  161 QRIGLSAT-VRSASDVA 176
DEXHc_TRCF cd17991
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ...
232-332 9.58e-04

DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350749 [Multi-domain]  Cd Length: 193  Bit Score: 40.63  E-value: 9.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 232 NGTGVIVLSPTRELAMQTYGVLKELMTHHVHTYGLIMGGSNRSAEAQ---KLANG-VNILVATpGRLLdhlqnTPGFMFK 307
Cdd:cd17991  63 SGKQVAVLVPTTLLAQQHYETFKERFANFPVNVELLSRFTTAAEQREileGLKEGkVDIVIGT-HRLL-----SKDVEFK 136
                        90       100
                ....*....|....*....|....*
gi 51010913 308 NLQCLIIDEADRiLEVGFEEELKQI 332
Cdd:cd17991 137 NLGLLIIDEEQR-FGVKQKEKLKEL 160
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
195-243 1.31e-03

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 41.83  E-value: 1.31e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 51010913 195 LLEGRDVLAAAKTGSGKTLAFLIPSIeliyklKFMPRNGTGVIVLSPTR 243
Cdd:COG1199  30 LAEGRHLLIEAGTGTGKTLAYLVPAL------LAARETGKKVVISTATK 72
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
185-316 2.53e-03

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 39.65  E-value: 2.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 185 TEIQHKTIRPLLEG-RDVLAAAKTGSGKTLAFLIPSIELIYKLKFMPRNGTGVIVLSPTRELAMQTYGVLKELMThhvhT 263
Cdd:cd18023   3 NRIQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFG----P 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51010913 264 YGLIMG---GSNRSAEAQKLANgVNILVATPGR--LLDHLQNTPGFMFKNLQCLIIDE 316
Cdd:cd18023  79 LGLSCAeltGDTEMDDTFEIQD-ADIILTTPEKwdSMTRRWRDNGNLVQLVALVLIDE 135
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
431-516 4.98e-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: 38.09  E-value: 4.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 431 DLPVMAIHGKQKQTKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQFDPPDDPKEYIHRV-GRTARGiNGRGHAL 509
Cdd:cd18810  51 EARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRS-KERAYAY 129

                ....*..
gi 51010913 510 LILRPEE 516
Cdd:cd18810 130 FLYPDQK 136
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
201-348 5.04e-03

DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to 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: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 38.21  E-value: 5.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 201 VLAAAKTGSGKT---LAFLipsieliykLKFMPRNGTG--VIVLSPTR----ELAMQtygVLKELMTHHVHTYGLIMGGS 271
Cdd:cd17917   4 VVIVGETGSGKTtqvPQFL---------LEDGLAKGGKgrIVCTQPRRiaaiSVAER---VAEERGEKLGEEVGYQIRFE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 272 NRSAEAQKlangvnILVATPGRLLDHLQNTPgfMFKNLQCLIIDEA-DRILEVGFeeeLKQIIKLLPKKRQSM---LFSA 347
Cdd:cd17917  72 SKTSSKTR------IKFCTDGILLRELLSDP--LLSGYSHVILDEAhERSLDTDF---LLGLLKDLLRKRPDLkviLMSA 140

                .
gi 51010913 348 T 348
Cdd:cd17917 141 T 141
PRK13767 PRK13767
ATP-dependent helicase; Provisional
181-246 5.57e-03

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 39.87  E-value: 5.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51010913  181 FDTMTEIQHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSIELIYKL--KFMPRNGTGVIVLSPTRELA 246
Cdd:PRK13767  30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLgrEGELEDKVYCLYVSPLRALN 97
DEXHc_RecQ5 cd18014
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ...
171-363 5.95e-03

DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) 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.


Pssm-ID: 350772 [Multi-domain]  Cd Length: 205  Bit Score: 38.61  E-value: 5.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 171 NTLKGVKEmGFDTMTEIQHKTIRPLLEGR-DVLAAAKTGSGKTLAFLIPSieLIYKlkfmprngtGV-IVLSPTRELAMQ 248
Cdd:cd18014   2 STLKKVFG-HSDFKSPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPA--LLAK---------GItIVISPLIALIQD 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 249 TYGVLKELmthHVHTYGL--IMGGSNRS---AEAQKLANGVNILVATP--------GRLLDHLQNTpgfmfKNLQCLIID 315
Cdd:cd18014  70 QVDHLKTL---KIRVDSLnsKLSAQERKriiADLESEKPQTKFLYITPemaatssfQPLLSSLVSR-----NLLSYLVVD 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 51010913 316 EADRILEVGFEE-----ELKQIIKLLPKKRQSMLfSATQTRKVED--LARISLKK 363
Cdd:cd18014 142 EAHCVSQWGHDFrpdylRLGALRSRYGHVPWVAL-TATATPQVQEdiFAQLRLKK 195
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
188-300 6.13e-03

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 38.65  E-value: 6.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 188 QHKTIRPLLEGRDVLAAAKTGSGKTLAFLIPSielIYKLKFMPRNGTGVIVLSPTR-ELAMQTYGVLKELMTHHVHTYGL 266
Cdd:cd18073   7 QLELALPAMKGKNTIICAPTGCGKTFVSLLIC---EHHLKKFPQGQKGKVVFFATKvPVYEQQKSVFSKYFERHGYRVTG 83
                        90       100       110
                ....*....|....*....|....*....|....
gi 51010913 267 IMGGSNRSAEAQKLANGVNILVATPGRLLDHLQN 300
Cdd:cd18073  84 ISGATAENVPVEQIIENNDIIILTPQILVNNLKK 117
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
188-319 9.45e-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: 37.54  E-value: 9.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 188 QHKTIRPLLEGRD-----VLAAAKTGSGKTLAFlipsIELIYKLKFMPRNGTgVIVLSPTRELAMQTYGVLKELMTHhvH 262
Cdd:cd18032   5 QQEAIEALEEAREkgqrrALLVMATGTGKTYTA----AFLIKRLLEANRKKR-ILFLAHREELLEQAERSFKEVLPD--G 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010913 263 TYGLIMGGSNRSAEAqklangvNILVATPGRL--LDHLQN-TPGFmFKnlqCLIIDEADR 319
Cdd:cd18032  78 SFGNLKGGKKKPDDA-------RVVFATVQTLnkRKRLEKfPPDY-FD---LIIIDEAHH 126
 
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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