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Conserved domains on  [gi|119596413|gb|EAW76007|]
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DEAH (Asp-Glu-Ala-His) box polypeptide 35, isoform CRA_c, partial [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 1000776)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to ATP-dependent RNA helicase that is involved in translation initiation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
54-692 3.96e-165

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG1643:

Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 495.76  E-value: 3.96e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVvGVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:COG1643   10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRI-GMLEPRRLAARAAaERMAEELGEPVGETVG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKK-RGDL 211
Cdd:COG1643   89 YRVRFEDKVSA-ATRIEVVTEGILLRELQRDPELEGV----------DTVIFDEFHERSLNADLLLALLLDLQPAlRPDL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 212 RLIVASATLDADKFRDFFNqnetsdPARdtcvILTVEGRTFPVDIFYL--QSPVPDYIKSTVETVVKIHQtEGDGDVLAF 289
Cdd:COG1643  158 KLLVMSATLDAERFARLLG------DAP----VIESSGRTYPVEVRYRplPADERDLEDAVADAVREALA-EEPGDILVF 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 290 LTGQEEvetvvsmlIEQARALARTGMKRHLRVLPMYAGLPSFEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDC 369
Cdd:COG1643  227 LPGERE--------IRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDS 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 370 GFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLKALGID 449
Cdd:COG1643  299 GLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLG 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 450 NVLRFHFMSPPPAQSMVQALELLYALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNI 529
Cdd:COG1643  379 DPEDLPFLDPPPARAIADARALLQELGALDADGRLT-PLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP 457
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 530 FvvppnqkshairvhRKFAveEGDHLTMLNIYEAFIKHnkdskwcQEHFLNYKGLVRAATVREQLKKLLvkfQVPRKSSE 609
Cdd:COG1643  458 R--------------RGAA--GSDLLARLNLWRRLREQ-------QREFLSYLRLREWRDLARQLRRLL---GEGANEEP 511
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 610 GDPDLVLRCIVSGFFAN-AARFHSTGAYRTIRdDHELHIHPASVLYAEKpprWVIYNEVIQT---SKyyMRDVTAIESAW 685
Cdd:COG1643  512 ADYEAIGLLLALAYPDRiARRRGEGGRYLLAR-GRGAALFPGSPLAKKE---WLVAAELVGGaaeAR--IRLAAPIDPEW 585

                 ....*..
gi 119596413 686 LLELAPH 692
Cdd:COG1643  586 LEELAAH 592
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
54-692 3.96e-165

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 495.76  E-value: 3.96e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVvGVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:COG1643   10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRI-GMLEPRRLAARAAaERMAEELGEPVGETVG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKK-RGDL 211
Cdd:COG1643   89 YRVRFEDKVSA-ATRIEVVTEGILLRELQRDPELEGV----------DTVIFDEFHERSLNADLLLALLLDLQPAlRPDL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 212 RLIVASATLDADKFRDFFNqnetsdPARdtcvILTVEGRTFPVDIFYL--QSPVPDYIKSTVETVVKIHQtEGDGDVLAF 289
Cdd:COG1643  158 KLLVMSATLDAERFARLLG------DAP----VIESSGRTYPVEVRYRplPADERDLEDAVADAVREALA-EEPGDILVF 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 290 LTGQEEvetvvsmlIEQARALARTGMKRHLRVLPMYAGLPSFEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDC 369
Cdd:COG1643  227 LPGERE--------IRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDS 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 370 GFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLKALGID 449
Cdd:COG1643  299 GLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLG 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 450 NVLRFHFMSPPPAQSMVQALELLYALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNI 529
Cdd:COG1643  379 DPEDLPFLDPPPARAIADARALLQELGALDADGRLT-PLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP 457
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 530 FvvppnqkshairvhRKFAveEGDHLTMLNIYEAFIKHnkdskwcQEHFLNYKGLVRAATVREQLKKLLvkfQVPRKSSE 609
Cdd:COG1643  458 R--------------RGAA--GSDLLARLNLWRRLREQ-------QREFLSYLRLREWRDLARQLRRLL---GEGANEEP 511
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 610 GDPDLVLRCIVSGFFAN-AARFHSTGAYRTIRdDHELHIHPASVLYAEKpprWVIYNEVIQT---SKyyMRDVTAIESAW 685
Cdd:COG1643  512 ADYEAIGLLLALAYPDRiARRRGEGGRYLLAR-GRGAALFPGSPLAKKE---WLVAAELVGGaaeAR--IRLAAPIDPEW 585

                 ....*..
gi 119596413 686 LLELAPH 692
Cdd:COG1643  586 LEELAAH 592
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
52-692 1.13e-145

RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273900 [Multi-domain]  Cd Length: 1283  Bit Score: 457.31  E-value: 1.13e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413    52 QKLPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGrVVGVTQPRRVAAVTV-RRVAEERGAVLGHE 130
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHG-LIGHTQPRRLAARTVaQRIAEELGTPLGEK 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   131 VGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGD 210
Cdd:TIGR01967  143 VGYKVRFHDQVSS-NTLVKLMTDGILLAETQQDRFLSRY----------DTIIIDEAHERSLNIDFLLGYLKQLLPRRPD 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   211 LRLIVASATLDADKFRDFFNQNEtsdpardtcvILTVEGRTFPVDIFY-----LQSPVP-DYIKSTVETVVKIHQtEGDG 284
Cdd:TIGR01967  212 LKIIITSATIDPERFSRHFNNAP----------IIEVSGRTYPVEVRYrplveEQEDDDlDQLEAILDAVDELFA-EGPG 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   285 DVLAFLTGQEEVEtvvsmliEQARALARTGMkRHLRVLPMYAGLPSFEQMKVFErvSRSVRKVIVATNVAETSITISGIV 364
Cdd:TIGR01967  281 DILIFLPGEREIR-------DAAEILRKRNL-RHTEILPLYARLSNKEQQRVFQ--PHSGRRIVLATNVAETSLTVPGIH 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   365 YVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLK 444
Cdd:TIGR01967  351 YVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQML 430
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   445 ALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKD---CRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIA 521
Cdd:TIGR01967  431 ALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDeaePQLT-PIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIA 509
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   522 AMMQIQNIFVVPPNQKSHAIRVHRKFAVEEGDHLTMLNIYEAF------IKHNKDSKWCQEHFLNYKGLVRAATVREQLK 595
Cdd:TIGR01967  510 SALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWRHIeeqrqaLSANQFRNACRKQYLNYLRVREWQDIYRQLT 589
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   596 KLLVKFQVPRKSSEGDPDLVLRCIVSGFFANAARFHSTGAYRTIRdDHELHIHPASVLyAEKPPRWVIYNEVIQTSKYYM 675
Cdd:TIGR01967  590 QVVKELGLKLNEEPADYDAIHKALLSGLLSQIGMKDEKHEYDGAR-GRKFHIFPGSPL-FKKPPKWVMAAELVETSKLYA 667
                          650
                   ....*....|....*..
gi 119596413   676 RDVTAIESAWLLELAPH 692
Cdd:TIGR01967  668 RLVAKIEPEWVEPVAGH 684
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
54-692 1.32e-138

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 438.72  E-value: 1.32e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGrVVGVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:PRK11131   73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKG-LIGHTQPRRLAARTVaNRIAEELETELGGCVG 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  133 YCIRFddcTDQLA--TRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGD 210
Cdd:PRK11131  152 YKVRF---NDQVSdnTMVKLMTDGILLAEIQQDRLLMQY----------DTIIIDEAHERSLNIDFILGYLKELLPRRPD 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  211 LRLIVASATLDADKFRDFFNQNEtsdpardtcvILTVEGRTFPVDIFYlqSPV--------PDYIKSTVETVVKIhQTEG 282
Cdd:PRK11131  219 LKVIITSATIDPERFSRHFNNAP----------IIEVSGRTYPVEVRY--RPIveeaddteRDQLQAIFDAVDEL-GREG 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  283 DGDVLAFLTGQEEVEtvvsmliEQARALARTGMkRHLRVLPMYAGLPSFEQMKVFErvSRSVRKVIVATNVAETSITISG 362
Cdd:PRK11131  286 PGDILIFMSGEREIR-------DTADALNKLNL-RHTEILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPG 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  363 IVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQ 442
Cdd:PRK11131  356 IKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQ 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  443 LKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKDC-----RLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEI 517
Cdd:PRK11131  436 MTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEqasayKLT-PLGRQLAQLPVDPRLARMVLEAQKHGCVREV 514
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  518 LSIAAMMQIQNIFVVPPNQKSHAIRVHRKFAVEEGDHLTMLNIYEaFIK-------HNKDSKWCQEHFLNYkglVRaatV 590
Cdd:PRK11131  515 MIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLWN-YLQeqqkalsSNQFRRLCRTDYLNY---LR---V 587
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  591 RE------QLKKLLVKFQVPRKSSEGDPDLVLRCIVSGFFA-----NAARFHSTGAyrtiRDDHeLHIHPASVLYaEKPP 659
Cdd:PRK11131  588 REwqdiytQLRQVVKELGIPVNSEPAEYREIHTALLTGLLShigmkDAEKQEYTGA----RNAR-FSIFPGSGLF-KKPP 661
                         650       660       670
                  ....*....|....*....|....*....|...
gi 119596413  660 RWVIYNEVIQTSKYYMRDVTAIESAWLLELAPH 692
Cdd:PRK11131  662 KWVMVAELVETSRLWGRIAARIEPEWIEPLAQH 694
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
54-247 1.65e-126

DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) 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: 350738 [Multi-domain]  Cd Length: 185  Bit Score: 372.96  E-value: 1.65e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVVGVTQPRRVAAVTVR-RVAEERGAVLGHEVG 132
Cdd:cd17980    1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVGCTQPRRVAAVTVAgRVAEEMGAVLGHEVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDCTDQLATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLR 212
Cdd:cd17980   81 YCIRFDDCTDPQATRIKFLTDGMLVREMMLDPLLTKY----------SVIMLDEAHERTLYTDILIGLLKKIQKKRGDLR 150
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 119596413 213 LIVASATLDADKFRDFFNQNETSDPARDTCVILTV 247
Cdd:cd17980  151 LIVASATLDAEKFRDFFNQNETNDPSKDTATILSV 185
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
468-557 1.06e-26

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 104.63  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  468 ALELLYALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFVVP----PNQKSHAIRV 543
Cdd:pfam04408   1 ALELLYYLGALDEDGELT-PLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldPRSAAKAARR 79
                          90       100
                  ....*....|....*....|....*
gi 119596413  544 HRKFAVEE-----------GDHLTM 557
Cdd:pfam04408  80 RRRAADEKarakfarldleGDHLTL 104
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
474-558 7.07e-25

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 98.49  E-value: 7.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   474 ALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFvvPPNQKSHAIRVHRKFAVEEGD 553
Cdd:smart00847   1 ELGALDDDGRLT-PLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESD 77

                   ....*
gi 119596413   554 HLTML 558
Cdd:smart00847  78 HLTLL 82
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
54-692 3.96e-165

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 495.76  E-value: 3.96e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVvGVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:COG1643   10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRI-GMLEPRRLAARAAaERMAEELGEPVGETVG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKK-RGDL 211
Cdd:COG1643   89 YRVRFEDKVSA-ATRIEVVTEGILLRELQRDPELEGV----------DTVIFDEFHERSLNADLLLALLLDLQPAlRPDL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 212 RLIVASATLDADKFRDFFNqnetsdPARdtcvILTVEGRTFPVDIFYL--QSPVPDYIKSTVETVVKIHQtEGDGDVLAF 289
Cdd:COG1643  158 KLLVMSATLDAERFARLLG------DAP----VIESSGRTYPVEVRYRplPADERDLEDAVADAVREALA-EEPGDILVF 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 290 LTGQEEvetvvsmlIEQARALARTGMKRHLRVLPMYAGLPSFEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDC 369
Cdd:COG1643  227 LPGERE--------IRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDS 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 370 GFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLKALGID 449
Cdd:COG1643  299 GLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLG 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 450 NVLRFHFMSPPPAQSMVQALELLYALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNI 529
Cdd:COG1643  379 DPEDLPFLDPPPARAIADARALLQELGALDADGRLT-PLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP 457
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 530 FvvppnqkshairvhRKFAveEGDHLTMLNIYEAFIKHnkdskwcQEHFLNYKGLVRAATVREQLKKLLvkfQVPRKSSE 609
Cdd:COG1643  458 R--------------RGAA--GSDLLARLNLWRRLREQ-------QREFLSYLRLREWRDLARQLRRLL---GEGANEEP 511
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 610 GDPDLVLRCIVSGFFAN-AARFHSTGAYRTIRdDHELHIHPASVLYAEKpprWVIYNEVIQT---SKyyMRDVTAIESAW 685
Cdd:COG1643  512 ADYEAIGLLLALAYPDRiARRRGEGGRYLLAR-GRGAALFPGSPLAKKE---WLVAAELVGGaaeAR--IRLAAPIDPEW 585

                 ....*..
gi 119596413 686 LLELAPH 692
Cdd:COG1643  586 LEELAAH 592
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
52-692 1.13e-145

RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273900 [Multi-domain]  Cd Length: 1283  Bit Score: 457.31  E-value: 1.13e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413    52 QKLPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGrVVGVTQPRRVAAVTV-RRVAEERGAVLGHE 130
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHG-LIGHTQPRRLAARTVaQRIAEELGTPLGEK 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   131 VGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGD 210
Cdd:TIGR01967  143 VGYKVRFHDQVSS-NTLVKLMTDGILLAETQQDRFLSRY----------DTIIIDEAHERSLNIDFLLGYLKQLLPRRPD 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   211 LRLIVASATLDADKFRDFFNQNEtsdpardtcvILTVEGRTFPVDIFY-----LQSPVP-DYIKSTVETVVKIHQtEGDG 284
Cdd:TIGR01967  212 LKIIITSATIDPERFSRHFNNAP----------IIEVSGRTYPVEVRYrplveEQEDDDlDQLEAILDAVDELFA-EGPG 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   285 DVLAFLTGQEEVEtvvsmliEQARALARTGMkRHLRVLPMYAGLPSFEQMKVFErvSRSVRKVIVATNVAETSITISGIV 364
Cdd:TIGR01967  281 DILIFLPGEREIR-------DAAEILRKRNL-RHTEILPLYARLSNKEQQRVFQ--PHSGRRIVLATNVAETSLTVPGIH 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   365 YVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLK 444
Cdd:TIGR01967  351 YVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQML 430
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   445 ALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKD---CRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIA 521
Cdd:TIGR01967  431 ALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDeaePQLT-PIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIA 509
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   522 AMMQIQNIFVVPPNQKSHAIRVHRKFAVEEGDHLTMLNIYEAF------IKHNKDSKWCQEHFLNYKGLVRAATVREQLK 595
Cdd:TIGR01967  510 SALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWRHIeeqrqaLSANQFRNACRKQYLNYLRVREWQDIYRQLT 589
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   596 KLLVKFQVPRKSSEGDPDLVLRCIVSGFFANAARFHSTGAYRTIRdDHELHIHPASVLyAEKPPRWVIYNEVIQTSKYYM 675
Cdd:TIGR01967  590 QVVKELGLKLNEEPADYDAIHKALLSGLLSQIGMKDEKHEYDGAR-GRKFHIFPGSPL-FKKPPKWVMAAELVETSKLYA 667
                          650
                   ....*....|....*..
gi 119596413   676 RDVTAIESAWLLELAPH 692
Cdd:TIGR01967  668 RLVAKIEPEWVEPVAGH 684
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
54-692 1.32e-138

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 438.72  E-value: 1.32e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGrVVGVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:PRK11131   73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKG-LIGHTQPRRLAARTVaNRIAEELETELGGCVG 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  133 YCIRFddcTDQLA--TRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGD 210
Cdd:PRK11131  152 YKVRF---NDQVSdnTMVKLMTDGILLAEIQQDRLLMQY----------DTIIIDEAHERSLNIDFILGYLKELLPRRPD 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  211 LRLIVASATLDADKFRDFFNQNEtsdpardtcvILTVEGRTFPVDIFYlqSPV--------PDYIKSTVETVVKIhQTEG 282
Cdd:PRK11131  219 LKVIITSATIDPERFSRHFNNAP----------IIEVSGRTYPVEVRY--RPIveeaddteRDQLQAIFDAVDEL-GREG 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  283 DGDVLAFLTGQEEVEtvvsmliEQARALARTGMkRHLRVLPMYAGLPSFEQMKVFErvSRSVRKVIVATNVAETSITISG 362
Cdd:PRK11131  286 PGDILIFMSGEREIR-------DTADALNKLNL-RHTEILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPG 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  363 IVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQ 442
Cdd:PRK11131  356 IKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQ 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  443 LKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKDC-----RLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEI 517
Cdd:PRK11131  436 MTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEqasayKLT-PLGRQLAQLPVDPRLARMVLEAQKHGCVREV 514
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  518 LSIAAMMQIQNIFVVPPNQKSHAIRVHRKFAVEEGDHLTMLNIYEaFIK-------HNKDSKWCQEHFLNYkglVRaatV 590
Cdd:PRK11131  515 MIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLWN-YLQeqqkalsSNQFRRLCRTDYLNY---LR---V 587
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  591 RE------QLKKLLVKFQVPRKSSEGDPDLVLRCIVSGFFA-----NAARFHSTGAyrtiRDDHeLHIHPASVLYaEKPP 659
Cdd:PRK11131  588 REwqdiytQLRQVVKELGIPVNSEPAEYREIHTALLTGLLShigmkDAEKQEYTGA----RNAR-FSIFPGSGLF-KKPP 661
                         650       660       670
                  ....*....|....*....|....*....|...
gi 119596413  660 RWVIYNEVIQTSKYYMRDVTAIESAWLLELAPH 692
Cdd:PRK11131  662 KWVMVAELVETSRLWGRIAARIEPEWIEPLAQH 694
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
54-247 1.65e-126

DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) 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: 350738 [Multi-domain]  Cd Length: 185  Bit Score: 372.96  E-value: 1.65e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVVGVTQPRRVAAVTVR-RVAEERGAVLGHEVG 132
Cdd:cd17980    1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVGCTQPRRVAAVTVAgRVAEEMGAVLGHEVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDCTDQLATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLR 212
Cdd:cd17980   81 YCIRFDDCTDPQATRIKFLTDGMLVREMMLDPLLTKY----------SVIMLDEAHERTLYTDILIGLLKKIQKKRGDLR 150
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 119596413 213 LIVASATLDADKFRDFFNQNETSDPARDTCVILTV 247
Cdd:cd17980  151 LIVASATLDAEKFRDFFNQNETNDPSKDTATILSV 185
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
54-230 5.27e-79

DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 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: 438710 [Multi-domain]  Cd Length: 178  Bit Score: 249.58  E-value: 5.27e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGwTAEGRVVGVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:cd17978    1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAG-FARGGMIGITQPRRVAAVSVaKRVAEEMGVELGQLVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGD-- 210
Cdd:cd17978   80 YSVRFDDVTSE-ETRIKYMTDGMLLREAIGDPLLSKY----------SVIILDEAHERTVHTDVLFGLVKSAQRRRKEqk 148
                        170       180
                 ....*....|....*....|...
gi 119596413 211 ---LRLIVASATLDADKFRDFFN 230
Cdd:cd17978  149 lspLKVIIMSATLDADLFSEYFN 171
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
71-231 2.08e-77

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: 244.68  E-value: 2.08e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  71 QTVVIVGETGCGKSTQIPQYLAEAGWTAEGRV-VGVTQPRRVAAVTV-RRVAEERGAVLGHEVGYCIRFDDCTDQlATRI 148
Cdd:cd17917    2 QVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGrIVCTQPRRIAAISVaERVAEERGEKLGEEVGYQIRFESKTSS-KTRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 149 KFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDF 228
Cdd:cd17917   81 KFCTDGILLRELLSDPLLSGY----------SHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSY 150

                 ...
gi 119596413 229 FNQ 231
Cdd:cd17917  151 FGG 153
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
252-415 2.45e-75

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; 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 members 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: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 239.74  E-value: 2.45e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 252 FPVDIFYLQSPV-----------PDYIKSTVETVVKIHQTEGDGDVLAFLTGQEEVETVVSMLieqaRALARTGMKRHLR 320
Cdd:cd18791    1 FPVEVYYLEDILellgissekedPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELL----REELLSPDLGKLL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 321 VLPMYAGLPSFEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRA 400
Cdd:cd18791   77 VLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRA 156
                        170
                 ....*....|....*
gi 119596413 401 GRGGRSRSGKCYRLY 415
Cdd:cd18791  157 GRAGRTRPGKCYRLY 171
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
54-523 2.90e-74

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 256.00  E-value: 2.90e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIP-QYLAEAGWTaeGRVVgVTQPRRVAAVTV-RRVAEERGAVLGHEV 131
Cdd:PRK11664   4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGIN--GKII-MLEPRRLAARNVaQRLAEQLGEKPGETV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 132 GYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKyrltesfsliLSVIMLDEAHERTLYTDIAIGLLKKIQKK-RGD 210
Cdd:PRK11664  81 GYRMRAESKVGP-NTRLEVVTEGILTRMIQRDPELSG----------VGLVILDEFHERSLQADLALALLLDVQQGlRDD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 211 LRLIVASATLDADKFRDFFnqnetsdParDTCVILTvEGRTFPVDIFYLQSPVPDYIKSTVETVVKIHQTEGDGDVLAFL 290
Cdd:PRK11664 150 LKLLIMSATLDNDRLQQLL-------P--DAPVIVS-EGRSFPVERRYQPLPAHQRFDEAVARATAELLRQESGSLLLFL 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 291 TGQEEVETVVSMLIEQaralartgMKRHLRVLPMYAGLPSFEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDCG 370
Cdd:PRK11664 220 PGVGEIQRVQEQLASR--------VASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSG 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 371 FVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLKALGIDN 450
Cdd:PRK11664 292 LERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLELLQWGCHD 371
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119596413 451 VLRFHFMSPPPAQSMVQALELLYALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFgcSQEILSIAAM 523
Cdd:PRK11664 372 PAQLSWLDQPPAAALAAAKRLLQQLGALDGQGRLT-ARGRKMAALGNDPRLAAMLVAAKED--DEAALATAAK 441
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
49-229 1.00e-72

DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 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: 350729 [Multi-domain]  Cd Length: 179  Bit Score: 233.14  E-value: 1.00e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  49 QQRQKLPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVvGVTQPRRVAAVTV-RRVAEERGAVL 127
Cdd:cd17971    1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKI-GCTQPRRVAAMSVaKRVAEEFGCCL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 128 GHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKK 207
Cdd:cd17971   80 GQEVGYTIRFEDCTSP-ETVIKYMTDGMLLRECLIDPDLSQY----------SVIMLDEAHERTIHTDVLFGLLKKTVQK 148
                        170       180
                 ....*....|....*....|..
gi 119596413 208 RGDLRLIVASATLDADKFRDFF 229
Cdd:cd17971  149 RPDLKLIVTSATLDAVKFSQYF 170
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
45-230 3.42e-69

DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. DHX15 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: 438709 [Multi-domain]  Cd Length: 187  Bit Score: 224.22  E-value: 3.42e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  45 LSIEQQRQKLPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWT-AEGRVVGVTQPRRVAAVTV-RRVAEE 122
Cdd:cd17973    4 FEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPhQPKKLVACTQPRRVAAMSVaQRVAEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 123 RGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLK 202
Cdd:cd17973   84 MDVKLGEEVGYSIRFEDCSSA-KTILKYMTDGMLLREAMSDPLLSRY----------SVIILDEAHERTLATDILMGLLK 152
                        170       180
                 ....*....|....*....|....*...
gi 119596413 203 KIQKKRGDLRLIVASATLDADKFRDFFN 230
Cdd:cd17973  153 EVVRRRPDLKLIVMSATLDAGKFQKYFD 180
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
54-231 5.51e-68

DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 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: 350732 [Multi-domain]  Cd Length: 174  Bit Score: 220.45  E-value: 5.51e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVVGVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:cd17974    1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGKIGCTQPRRVAAMSVaARVAEEMGVKLGNEVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLR 212
Cdd:cd17974   81 YSIRFEDCTSE-KTVLKYMTDGMLLREFLTEPDLASY----------SVMIIDEAHERTLHTDILFGLVKDIARFRPDLK 149
                        170
                 ....*....|....*....
gi 119596413 213 LIVASATLDADKFRDFFNQ 231
Cdd:cd17974  150 LLISSATMDAEKFSAFFDD 168
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
54-229 6.25e-63

DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as PRP16) is involved in pre-mRNA splicing. DHX38 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: 350741 [Multi-domain]  Cd Length: 173  Bit Score: 206.93  E-value: 6.25e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGrVVGVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:cd17983    1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYG-MIGCTQPRRVAAMSVaKRVSEEMGVELGEEVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLR 212
Cdd:cd17983   80 YAIRFEDCTSE-NTVIKYMTDGILLRESLRDPDLDKY----------SAIIMDEAHERSLNTDVLFGLLREVVARRRDLK 148
                        170
                 ....*....|....*..
gi 119596413 213 LIVASATLDADKFRDFF 229
Cdd:cd17983  149 LIVTSATMDADKFADFF 165
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
54-227 1.66e-56

DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) 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: 350740 [Multi-domain]  Cd Length: 191  Bit Score: 190.64  E-value: 1.66e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAE----GRVVGVTQPRRVAAV-TVRRVAEERGaVLG 128
Cdd:cd17982    1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPesdnPGMIGITQPRRVAAVsMAKRVAEELN-VFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 129 HEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKR 208
Cdd:cd17982   80 KEVSYQIRYDSTVSE-NTKIKFMTDGVLLKEIQTDFLLRKY----------SVIIIDEAHERSVNTDILIGMLSRIVPLR 148
                        170       180
                 ....*....|....*....|....*....
gi 119596413 209 GD----------LRLIVASATLDADKFRD 227
Cdd:cd17982  149 AKlylqdqtvkpLKLVIMSATLRVEDFTE 177
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
54-229 2.15e-52

DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) 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: 350742 [Multi-domain]  Cd Length: 178  Bit Score: 178.89  E-value: 2.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVvGVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:cd17984    1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMI-GVTQPRRVAAISVaQRVAEEMKCTLGSKVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKI--QKKRG- 209
Cdd:cd17984   80 YQVRFDDCSSK-ETAIKYMTDGCLLRHILADPNLTKY----------SVIILDEAHERSLTTDILFGLLKKLfqEKSPNr 148
                        170       180
                 ....*....|....*....|..
gi 119596413 210 --DLRLIVASATLDADKFRDFF 229
Cdd:cd17984  149 keHLKVVVMSATLELAKLSAFF 170
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
54-231 1.97e-46

DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 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: 350737 [Multi-domain]  Cd Length: 170  Bit Score: 162.61  E-value: 1.97e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAegrvVGVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:cd17979    1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH----IACTQPRRIACISLaKRVAFESLNQYGSKVA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDcTDQLATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLR 212
Cdd:cd17979   77 YQIRFER-TRTLATKLLFLTEGLLLRQIQRDASLPQY----------NVLILDEVHERHLHGDFLLGVLRCLLRLRPDLK 145
                        170
                 ....*....|....*....
gi 119596413 213 LIVASATLDADKFRDFFNQ 231
Cdd:cd17979  146 LILMSATINIELFSGYFEG 164
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
54-230 1.30e-44

DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpA 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: 350747 [Multi-domain]  Cd Length: 173  Bit Score: 157.62  E-value: 1.30e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGrVVGVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:cd17989    1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRG-LIGHTQPRRLAARSVaERIAEELKTELGGAVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLR 212
Cdd:cd17989   80 YKVRFTDQTSD-ETCVKLMTDGILLAETQTDRYLRAY----------DTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLK 148
                        170
                 ....*....|....*...
gi 119596413 213 LIVASATLDADKFRDFFN 230
Cdd:cd17989  149 VIITSATIDAERFSRHFN 166
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
54-230 3.15e-41

DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 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: 350739 [Multi-domain]  Cd Length: 180  Bit Score: 148.45  E-value: 3.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYL----AEAGWTAEGRVVgVTQPRRVAAVTV-RRVAEERG--AV 126
Cdd:cd17981    1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFIlddaIERGKGSSCRIV-CTQPRRISAISVaERVAAERAesCG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 127 LGHEVGYCIRFDDCTDQLATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQK 206
Cdd:cd17981   80 LGNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNV----------SHLVLDEIHERNLQSDVLMGIVKDLLP 149
                        170       180
                 ....*....|....*....|....
gi 119596413 207 KRGDLRLIVASATLDADKFRDFFN 230
Cdd:cd17981  150 FRSDLKVILMSATLNAEKFSDYFN 173
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
54-231 9.95e-39

DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of the 43S pre-initiation complex involved in translation initiation of mRNAs with structured 5'-UTRs. DHX29 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: 350733 [Multi-domain]  Cd Length: 183  Bit Score: 141.59  E-value: 9.95e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAE----AGWTAEGRVVGVTQPRRVAAVTVR-RVAEERGAVLG 128
Cdd:cd17975    1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEdlllNGGTAQKCNIVCTQPRRISAMSLAtRVCEELGCESG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 129 -----HEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKyrltesfsliLSVIMLDEAHERTLYTDIAIGLLKK 203
Cdd:cd17975   81 pggknSLCGYQIRMESRTGE-ATRLLYCTTGVLLRKLQEDGLLSS----------ISHIIVDEVHERSVQSDFLLIILKE 149
                        170       180
                 ....*....|....*....|....*...
gi 119596413 204 IQKKRGDLRLIVASATLDADKFRDFFNQ 231
Cdd:cd17975  150 ILHKRSDLHLILMSATVDCEKFSSYFTH 177
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
54-230 3.57e-38

DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) 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: 350743 [Multi-domain]  Cd Length: 177  Bit Score: 139.59  E-value: 3.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGW-TAEGRVVGV--TQPRRVAAVTV-RRVAEERGAVLGH 129
Cdd:cd17985    1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLqGPPLPVANIicTQPRRISAISVaERVAQERAERVGQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 130 EVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKyrltesfsliLSVIMLDEAHERTLYTDIAIGLLKKIQKKRG 209
Cdd:cd17985   81 SVGYQIRLESVKSS-ATRLLYCTTGVLLRRLEGDPTLQG----------VTHVIVDEVHERTEESDFLLLVLKDLMVQRP 149
                        170       180
                 ....*....|....*....|.
gi 119596413 210 DLRLIVASATLDADKFRDFFN 230
Cdd:cd17985  150 DLKVILMSATLNAELFSDYFN 170
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
7-229 1.82e-37

DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 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: 350730 [Multi-domain]  Cd Length: 234  Bit Score: 139.58  E-value: 1.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   7 PVKFWRPGT-----EGPGVSISEERQSLA-ENSGTTVVYNPYAALSIEQQRQKLPVFKLRNHILYLIENYQTVVIVGETG 80
Cdd:cd17972    6 PQSNWNPWTssnidEGPLAFATPEQISMDlKNELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  81 CGKSTQIPQYLAE----AGWTAEGRVVgVTQPRRVAAVTV-RRVAEERGAVLGHEVGYCIRFDDCTDQLATRIKFLTDGM 155
Cdd:cd17972   86 CGKTTQVPQYILDdfiqNDRAAECNIV-VTQPRRISAVSVaERVAFERGEEVGKSCGYSVRFESVLPRPHASILFCTVGV 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119596413 156 LVREMmvdplltkyrltESFSLILSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFF 229
Cdd:cd17972  165 LLRKL------------EAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYF 226
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
54-225 1.14e-36

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB 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: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 135.54  E-value: 1.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVVgVTQPRRVAAVTV-RRVAEERGAVLGHEVG 132
Cdd:cd17990    1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKII-VLEPRRVAARAAaRRLATLLGEAPGETVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 133 YCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKyrltesfsliLSVIMLDEAHERTLYTDIAIGLLKKIQK-KRGDL 211
Cdd:cd17990   80 YRVRGESRVGR-RTRVEVVTEGVLLRRLQRDPELSG----------VGAVILDEFHERSLDADLALALLLEVQQlLRDDL 148
                        170
                 ....*....|....
gi 119596413 212 RLIVASATLDADKF 225
Cdd:cd17990  149 RLLAMSATLDGDGL 162
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
54-229 1.22e-33

DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 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: 350734 [Multi-domain]  Cd Length: 178  Bit Score: 126.83  E-value: 1.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAE----AGWTAEGRVVgVTQPRRVAAVTV-RRVAEERGAVLG 128
Cdd:cd17976    1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEdyvlRGRGARCNVV-ITQPRRISAVSVaQRVAHELGPNLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 129 HEVGYCIRFDDCTDQLATRIKFLTDGMLVREMMVDPLLTKyrltesfsliLSVIMLDEAHERTLYTDIAIGLLKKIQKKR 208
Cdd:cd17976   80 RNVGYQVRLESRPPPRGGALLFCTVGVLLKKLQSNPRLEG----------VSHVIVDEVHERDVNTDFLLILLKGVLQLN 149
                        170       180
                 ....*....|....*....|.
gi 119596413 209 GDLRLIVASATLDADKFRDFF 229
Cdd:cd17976  150 PELRVVLMSATGDNQRLSRYF 170
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
54-218 4.34e-33

DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) 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: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 125.32  E-value: 4.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGR--VVGVTQPRRVAAVTVR-RVAEERGAVLGHE 130
Cdd:cd17977    1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAHYQhgVVVCTQVHKQTAVWLAlRVADEMDVNIGHE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 131 VGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKRGD 210
Cdd:cd17977   81 VGYVIPFENCCTN-ETILRYCTDDMLLREMMSDPLLESY----------GVIILDDAHERTVSTDVLLGLLKDVLLSRPE 149

                 ....*...
gi 119596413 211 LRLIVASA 218
Cdd:cd17977  150 LKLVIITC 157
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
54-228 5.75e-33

DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 (DQX1) 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: 350744 [Multi-domain]  Cd Length: 177  Bit Score: 125.01  E-value: 5.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIV-GETGCGKSTQIPQYLAEAGWT---AEGRVVgVTQPRRVAAVTVR-RVAEERGAVLG 128
Cdd:cd17986    1 LPIWAAKFTFLEQLESPSGIVLVsGEPGSGKSTQVPQWCAEFALSrgfQKGQVT-VTQPHPLAARSLAlRVADEMDLNLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 129 HEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKIQKKR 208
Cdd:cd17986   80 HEVGYSIPQEDCTGP-NTILRFCWDRLLLQEMTSTPLLGAW----------GVVVLDEAQERSVASDSLLGLLKDVRLQR 148
                        170       180
                 ....*....|....*....|
gi 119596413 209 GDLRLIVASATLDADKFRDF 228
Cdd:cd17986  149 PELRVVVVTSPALEPKLRAF 168
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
54-230 6.09e-32

DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 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: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 122.25  E-value: 6.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGW-TAEGRVVGVTQPRRVAAVTV-RRVAEERGAVLGHEV 131
Cdd:cd17987    1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYaNGIPCRIFCTQPRRLAAIAVaERVAAERGEKIGQTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 132 GYCIRFDDCTDQlATRIKFLTDGMLVREMMVDplltkyrlTESFSLILSVImLDEAHERTLYTDIAIGLLKKIQKKRGDL 211
Cdd:cd17987   81 GYQIRLESRVSP-KTLLTFCTNGVLLRTLMAG--------DSALSTVTHVI-VDEVHERDRFSDFLLTKLRDILQKHPNL 150
                        170
                 ....*....|....*....
gi 119596413 212 RLIVASATLDADKFRDFFN 230
Cdd:cd17987  151 KLILSSAALDVNLFIRYFG 169
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
54-229 8.82e-28

DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 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: 350746 [Multi-domain]  Cd Length: 180  Bit Score: 110.28  E-value: 8.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  54 LPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQY-LAEAGWTAEGRVVGVTQPRRVAAVTV-RRVAEERGAVLGHEV 131
Cdd:cd17988    1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFiLDHYYKRGKYCNIVVTQPRRIAAISIaRRVSQEREWTLGSLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 132 GYCIRFDDcTDQLATRIKFLTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKK-IQKKRGD 210
Cdd:cd17988   81 GYQVGLER-PASEETRLIYCTTGVLLQKLINNKTLTEY----------THIILDEVHERDQELDFLLLVVRRlLRTNSRH 149
                        170
                 ....*....|....*....
gi 119596413 211 LRLIVASATLDADKFRDFF 229
Cdd:cd17988  150 VKIILMSATISCKEFADYF 168
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
468-557 1.06e-26

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 104.63  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  468 ALELLYALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFVVP----PNQKSHAIRV 543
Cdd:pfam04408   1 ALELLYYLGALDEDGELT-PLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldPRSAAKAARR 79
                          90       100
                  ....*....|....*....|....*
gi 119596413  544 HRKFAVEE-----------GDHLTM 557
Cdd:pfam04408  80 RRRAADEKarakfarldleGDHLTL 104
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
474-558 7.07e-25

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 98.49  E-value: 7.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   474 ALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFvvPPNQKSHAIRVHRKFAVEEGD 553
Cdd:smart00847   1 ELGALDDDGRLT-PLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESD 77

                   ....*
gi 119596413   554 HLTML 558
Cdd:smart00847  78 HLTLL 82
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
615-692 1.93e-21

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 88.85  E-value: 1.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  615 VLRCIVSGFFANAARF-HSTGAYRTIRDDHELHIHPASVLY--AEKPPRWVIYNEVIQTSKYYMRDVTAIESAWLLELAP 691
Cdd:pfam07717   1 LRAALAAGLYPNVARRdPKGKGYTTLSDNQRVFIHPSSVLFneKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80

                  .
gi 119596413  692 H 692
Cdd:pfam07717  81 H 81
DEXDc smart00487
DEAD-like helicases superfamily;
53-233 1.77e-17

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 81.38  E-value: 1.77e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413    53 KLPVFKLRNH----ILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVVGVTQPRRVAAVTVRRVAEERGAVLG 128
Cdd:smart00487   3 KFGFEPLRPYqkeaIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   129 HEVGYCIRFDDCTDQLA------TRIKFLTDGMLVREMMVDPLLTKYrltesfsliLSVIMLDEAHERT--LYTDIAIGL 200
Cdd:smart00487  83 LKVVGLYGGDSKREQLRklesgkTDILVTTPGRLLDLLENDKLSLSN---------VDLVILDEAHRLLdgGFGDQLEKL 153
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 119596413   201 LKKIQKKRgdlRLIVASATL--DADKFRDFFNQNE 233
Cdd:smart00487 154 LKLLPKNV---QLLLLSATPpeEIENLLELFLNDP 185
HELICc smart00490
helicase superfamily c-terminal domain;
310-405 8.82e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 66.85  E-value: 8.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413   310 LARTGMKRHLRVLPMYAGLPSFEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDCGFvklraynprtaieclvvv 389
Cdd:smart00490   3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL------------------ 64
                           90
                   ....*....|....*.
gi 119596413   390 PVSQASANQRAGRGGR 405
Cdd:smart00490  65 PWSPASYIQRIGRAGR 80
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
271-405 1.79e-12

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: 64.15  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  271 VETVVKIHQTEGDGDVLAFLTGQEEVETvvSMLIEqaralartgmKRHLRVLPMYAGLPSFEQMKVFERVSRSVRKVIVA 350
Cdd:pfam00271   3 LEALLELLKKERGGKVLIFSQTKKTLEA--ELLLE----------KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVA 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119596413  351 TNVAETSITISGIVYVIDCGFVklraYNPRTAIeclvvvpvsqasanQRAGRGGR 405
Cdd:pfam00271  71 TDVAERGLDLPDVDLVINYDLP----WNPASYI--------------QRIGRAGR 107
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
41-416 6.49e-09

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 59.22  E-value: 6.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  41 PYAALSIEQQRQklpVFKLrnhilyLIENYQtVVIVGETGCGKSTQIPQ------YLAeAGWTAEGRVVGVTQPRRVAaV 114
Cdd:PHA02653 160 PLASLQPDVQLK---IFEA------WISRKP-VVLTGGTGVGKTSQVPKlllwfnYLF-GGFDNLDKIDPNFIERPIV-L 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 115 TVRRVAEER--GAVLGHEVGY--------CIRFDDCTDQLA-TRIKFltDGMLV---RemmvdplLTKYRLTESfslilS 180
Cdd:PHA02653 228 SLPRVALVRlhSITLLKSLGFdeidgspiSLKYGSIPDELInTNPKP--YGLVFsthK-------LTLNKLFDY-----G 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 181 VIMLDEAHERTLYTDIAIGLLKkiqKKRGDLR-LIVASATL--DADKFRDFFNqnetsDPArdtcvILTVEGRT-FPVDI 256
Cdd:PHA02653 294 TVIIDEVHEHDQIGDIIIAVAR---KHIDKIRsLFLMTATLedDRDRIKEFFP-----NPA-----FVHIPGGTlFPISE 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 257 FYL---QSPvPDYIKSTVETVVKIHQTEGDGDVLAFLTGQEEVETvVSMLIEQARALArtgmKRH--LRVLPMYAGLPSF 331
Cdd:PHA02653 361 VYVknkYNP-KNKRAYIEEEKKNIVTALKKYTPPKGSSGIVFVAS-VSQCEEYKKYLE----KRLpiYDFYIIHGKVPNI 434
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 332 EQM--KVF--ERVSrsvrkVIVATNVAETSITISGIVYVIDCGfvklRAYNPRtaieclvvvP-------VSQASANQRA 400
Cdd:PHA02653 435 DEIleKVYssKNPS-----IIISTPYLESSVTIRNATHVYDTG----RVYVPE---------PfggkemfISKSMRTQRK 496
                        410
                 ....*....|....*.
gi 119596413 401 GRGGRSRSGKCYRLYT 416
Cdd:PHA02653 497 GRVGRVSPGTYVYFYD 512
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
73-219 2.29e-06

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: 47.78  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  73 VVIVGETGCGKSTQIPQYLAEAGWTAEGRVVgVTQPRRVAAV-TVRRVAEERG-----AVLGHEVGYCIRFDDCTDQLat 146
Cdd:cd00046    4 VLITAPTGSGKTLAALLAALLLLLKKGKKVL-VLVPTKALALqTAERLRELFGpgirvAVLVGGSSAEEREKNKLGDA-- 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119596413 147 RIKFLTDGMLVREMMVDPLLTKYRltesfsliLSVIMLDEAHeRTLYTD--IAIGLLKKIQKKRGDLRLIVASAT 219
Cdd:cd00046   81 DIIIATPDMLLNLLLREDRLFLKD--------LKLIIVDEAH-ALLIDSrgALILDLAVRKAGLKNAQVILLSAT 146
PRK13766 PRK13766
Hef nuclease; Provisional
270-420 2.86e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 44.09  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 270 TVETVVKIHQTEGDGDVLAFLTGQEEVETVVSMLIE----------QARALARTGMKRHlrvlpmyaglpsfEQMKVFER 339
Cdd:PRK13766 352 LREIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKegikavrfvgQASKDGDKGMSQK-------------EQIEILDK 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 340 VSRSVRKVIVATNVAETSITISGIVYVIdcgFvklraYNPrtaieclvvVPvSQASANQRAGRGGRSRSGKCYRLYTE-- 417
Cdd:PRK13766 419 FRAGEFNVLVSTSVAEEGLDIPSVDLVI---F-----YEP---------VP-SEIRSIQRKGRTGRQEEGRVVVLIAKgt 480

                 ....*
gi 119596413 418 --EAF 420
Cdd:PRK13766 481 rdEAY 485
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
71-219 4.38e-04

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 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: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 41.38  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413  71 QTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVVgVTQPRRVAAvtvrrvAEERGAVLGHEVGYCIRFDDCTDQLATRIKF 150
Cdd:cd17931    2 QLTVLDLHPGAGKTTRVLPQIIREAIKKRLRTL-VLAPTRVVA------AEMYEALRGLPIRYRTGAVKEEHGGNEIVDY 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119596413 151 LTDGMLVREMMVDPLLTKYrltesfslilSVIMLDEAHERTLYTDIAIGLLKKiQKKRGDLRLIVASAT 219
Cdd:cd17931   75 MCHGTFTCRLLSPKRVPNY----------NLIIMDEAHFTDPASIAARGYIHT-RVEMGEAAVIFMTAT 132
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
338-415 1.41e-03

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 38.07  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119596413 338 ERVSRSVrKVIVATNVAETSITISGIVYVIDCGFVKlraynprtaieclvvvpvSQASANQRAGRGGR--SRSGKCYRLY 415
Cdd:cd18785   17 EEIASSL-EILVATNVLGEGIDVPSLDTVIFFDPPS------------------SAASYIQRVGRAGRggKDEGEVILFV 77
 
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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