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Conserved domains on  [gi|351064569|emb|CCD73030|]
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Probable ATP-dependent RNA helicase DHX35 homolog [Caenorhabditis elegans]

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];
95-703 9.09e-175

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: 521.56  E-value: 9.09e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  95 TIIIVGETGCGKSTQVPQFLLEAGWAADGRqIVITQPRRVAVVTLATRVAEEKDCILGHDVGYTVRFDDVSDKDTKVKFM 174
Cdd:COG1643   28 VVVLAAPPGAGKTTQLPLALLELGWGAGGR-IGMLEPRRLAARAAAERMAEELGEPVGETVGYRVRFEDKVSAATRIEVV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 175 TDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQ-IRNDLRIIVSSATLDAELFKDFFemnetgnsdkD 253
Cdd:COG1643  107 TEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPaLRPDLKLLVMSATLDAERFARLL----------G 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 254 TAGIISVEGRTHPVAVHHT--KTSVPDYCQSAVDTVINIHKhENPGDILVFLTGQDEVEDVCEKLRELAgnLKNCDrlwV 331
Cdd:COG1643  177 DAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREALA-EEPGDILVFLPGEREIRRTAEALRGRL--PPDTE---I 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 332 VPCYGALPAREQMKAFDSTPHGTRKVVVATNIAEASITIPGICYVIDTGYVKlRAQ-HAANGVETLMRVTVSKASAEQRA 410
Cdd:COG1643  251 LPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLAR-IPRyDPRSGVTRLPTERISQASANQRA 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 411 GRAGRIRPGKCYRLYPESEFERFAEGTVPEIQRCQMASTILQLKALGVQNVHRFHYLSPPPSwAMIN-GLELLYALGAID 489
Cdd:COG1643  330 GRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPA-RAIAdARALLQELGALD 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 490 ETSQLTsPLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQDvfitPYRQRHQADVirkkfaveegdhMTMLN 569
Cdd:COG1643  409 ADGRLT-PLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERD----PRRGAAGSDL------------LARLN 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 570 VFTKFVENGRskkwcsdHFVNYRGLMRADNVRSQLVRLLKrfeiEKVSSRGLIncSENIRQCLVTGFFSQAAQY-----H 644
Cdd:COG1643  472 LWRRLREQQR-------EFLSYLRLREWRDLARQLRRLLG----EGANEEPAD--YEAIGLLLALAYPDRIARRrgeggR 538
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351064569 645 Y-----TGkymtvkesfpFNMYKGSSiMFKKdypKWVIFTEVMQDS----IRDVTVIEPEWLYELAPH 703
Cdd:COG1643  539 YllargRG----------AALFPGSP-LAKK---EWLVAAELVGGAaearIRLAAPIDPEWLEELAAH 592
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
95-703 9.09e-175

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 521.56  E-value: 9.09e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  95 TIIIVGETGCGKSTQVPQFLLEAGWAADGRqIVITQPRRVAVVTLATRVAEEKDCILGHDVGYTVRFDDVSDKDTKVKFM 174
Cdd:COG1643   28 VVVLAAPPGAGKTTQLPLALLELGWGAGGR-IGMLEPRRLAARAAAERMAEELGEPVGETVGYRVRFEDKVSAATRIEVV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 175 TDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQ-IRNDLRIIVSSATLDAELFKDFFemnetgnsdkD 253
Cdd:COG1643  107 TEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPaLRPDLKLLVMSATLDAERFARLL----------G 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 254 TAGIISVEGRTHPVAVHHT--KTSVPDYCQSAVDTVINIHKhENPGDILVFLTGQDEVEDVCEKLRELAgnLKNCDrlwV 331
Cdd:COG1643  177 DAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREALA-EEPGDILVFLPGEREIRRTAEALRGRL--PPDTE---I 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 332 VPCYGALPAREQMKAFDSTPHGTRKVVVATNIAEASITIPGICYVIDTGYVKlRAQ-HAANGVETLMRVTVSKASAEQRA 410
Cdd:COG1643  251 LPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLAR-IPRyDPRSGVTRLPTERISQASANQRA 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 411 GRAGRIRPGKCYRLYPESEFERFAEGTVPEIQRCQMASTILQLKALGVQNVHRFHYLSPPPSwAMIN-GLELLYALGAID 489
Cdd:COG1643  330 GRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPA-RAIAdARALLQELGALD 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 490 ETSQLTsPLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQDvfitPYRQRHQADVirkkfaveegdhMTMLN 569
Cdd:COG1643  409 ADGRLT-PLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERD----PRRGAAGSDL------------LARLN 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 570 VFTKFVENGRskkwcsdHFVNYRGLMRADNVRSQLVRLLKrfeiEKVSSRGLIncSENIRQCLVTGFFSQAAQY-----H 644
Cdd:COG1643  472 LWRRLREQQR-------EFLSYLRLREWRDLARQLRRLLG----EGANEEPAD--YEAIGLLLALAYPDRIARRrgeggR 538
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351064569 645 Y-----TGkymtvkesfpFNMYKGSSiMFKKdypKWVIFTEVMQDS----IRDVTVIEPEWLYELAPH 703
Cdd:COG1643  539 YllargRG----------AALFPGSP-LAKK---EWLVAAELVGGAaearIRLAAPIDPEWLEELAAH 592
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
77-703 6.87e-136

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: 432.27  E-value: 6.87e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569    77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGrQIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:TIGR01967   66 LPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHG-LIGHTQPRRLAARTVAQRIAEELGTPLGEKVG 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   157 YTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATLDAE 236
Cdd:TIGR01967  145 YKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPE 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   237 LFKDFFemnetgnsdkDTAGIISVEGRTHPVAVHHTKTSVP------DYCQSAVDTVINIHKHEnPGDILVFLTGQDEVE 310
Cdd:TIGR01967  225 RFSRHF----------NNAPIIEVSGRTYPVEVRYRPLVEEqedddlDQLEAILDAVDELFAEG-PGDILIFLPGEREIR 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   311 DVCEKLRELagNLKNCDrlwVVPCYGALPAREQMKAFDstPHGTRKVVVATNIAEASITIPGICYVIDTGYVKLRAQHAA 390
Cdd:TIGR01967  294 DAAEILRKR--NLRHTE---ILPLYARLSNKEQQRVFQ--PHSGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYR 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   391 NGVETLMRVTVSKASAEQRAGRAGRIRPGKCYRLYPESEFERFAEGTVPEIQRCQMASTILQLKALGVQNVHRFHYLSPP 470
Cdd:TIGR01967  367 TKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAFPFIEAP 446
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   471 PSWAMINGLELLYALGAIDE---TSQLTsPLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQDVFITPYRQR 547
Cdd:TIGR01967  447 DPRAIRDGFRLLEELGALDDdeaEPQLT-PIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQ 525
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   548 HQADVIRKKFAVEEGDHMTMLNVFTKFVE--NGRSK----KWCSDHFVNYRGLMRADNVRSQLVRLLKRFEIEKVSSRGl 621
Cdd:TIGR01967  526 QAADQAHARFKDPRSDFLSRVNLWRHIEEqrQALSAnqfrNACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPA- 604
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   622 inCSENIRQCLVTGFFSQAAQYHYTGKYMTVKESfPFNMYKGSSiMFKKDyPKWVIFTEVMQDS---IRDVTVIEPEWLY 698
Cdd:TIGR01967  605 --DYDAIHKALLSGLLSQIGMKDEKHEYDGARGR-KFHIFPGSP-LFKKP-PKWVMAAELVETSklyARLVAKIEPEWVE 679

                   ....*
gi 351064569   699 ELAPH 703
Cdd:TIGR01967  680 PVAGH 684
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
77-703 3.29e-133

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 425.24  E-value: 3.29e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGrQIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:PRK11131   73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKG-LIGHTQPRRLAARTVANRIAEELETELGGCVG 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  157 YTVRFDD-VSDkDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATLDA 235
Cdd:PRK11131  152 YKVRFNDqVSD-NTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  236 ELFKDFFemnetgnsdkDTAGIISVEGRTHPVAVHH------TKTSVPDYCQSAVDTVINIhKHENPGDILVFLTGQDEV 309
Cdd:PRK11131  231 ERFSRHF----------NNAPIIEVSGRTYPVEVRYrpiveeADDTERDQLQAIFDAVDEL-GREGPGDILIFMSGEREI 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  310 EDVCEKLRELagNLKNCDrlwVVPCYGALPAREQMKAFDstPHGTRKVVVATNIAEASITIPGICYVIDTGYVKLRAQHA 389
Cdd:PRK11131  300 RDTADALNKL--NLRHTE---ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSY 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  390 ANGVETLMRVTVSKASAEQRAGRAGRIRPGKCYRLYPESEFERFAEGTVPEIQRCQMASTILQLKALGVQNVHRFHYLSP 469
Cdd:PRK11131  373 RTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEA 452
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  470 PPSWAMINGLELLYALGAIDETS-----QLTsPLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQDVFITPY 544
Cdd:PRK11131  453 PDKRNIQDGVRLLEELGAITTDEqasayKLT-PLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPM 531
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  545 RQRHQADVIRKKFAVEEGDHMTMLNVFTKFVENGRS------KKWCSDHFVNYRGLMRADNVRSQLVRLLKRFEI----E 614
Cdd:PRK11131  532 DKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKAlssnqfRRLCRTDYLNYLRVREWQDIYTQLRQVVKELGIpvnsE 611
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  615 KVSSRGlINCSenirqcLVTGFFSQAAQ-----YHYTGkymtvKESFPFNMYKGSSImFKKDyPKWVIFTEVMQDSI--- 686
Cdd:PRK11131  612 PAEYRE-IHTA------LLTGLLSHIGMkdaekQEYTG-----ARNARFSIFPGSGL-FKKP-PKWVMVAELVETSRlwg 677
                         650
                  ....*....|....*..
gi 351064569  687 RDVTVIEPEWLYELAPH 703
Cdd:PRK11131  678 RIAARIEPEWIEPLAQH 694
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
77-260 1.26e-119

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: 356.01  E-value: 1.26e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGRQIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:cd17980    1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 157 YTVRFDDVSDKD-TKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATLDA 235
Cdd:cd17980   81 YCIRFDDCTDPQaTRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160
                        170       180
                 ....*....|....*....|....*
gi 351064569 236 ELFKDFFEMNETGNSDKDTAGIISV 260
Cdd:cd17980  161 EKFRDFFNQNETNDPSKDTATILSV 185
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
484-568 1.23e-27

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: 106.58  E-value: 1.23e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   484 ALGAIDETSQLTsPLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQDVFitPYRQRHQADVIRKKFAVEEGD 563
Cdd:smart00847   1 ELGALDDDGRLT-PLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESD 77

                   ....*
gi 351064569   564 HMTML 568
Cdd:smart00847  78 HLTLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
479-567 1.68e-27

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: 106.94  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  479 LELLYALGAIDETSQLTsPLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQDVFITPY-------------R 545
Cdd:pfam04408   2 LELLYYLGALDEDGELT-PLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNfldprsaakaarrR 80
                          90       100
                  ....*....|....*....|....
gi 351064569  546 QRHQADVIRKKFAVE--EGDHMTM 567
Cdd:pfam04408  81 RRAADEKARAKFARLdlEGDHLTL 104
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
95-703 9.09e-175

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 521.56  E-value: 9.09e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  95 TIIIVGETGCGKSTQVPQFLLEAGWAADGRqIVITQPRRVAVVTLATRVAEEKDCILGHDVGYTVRFDDVSDKDTKVKFM 174
Cdd:COG1643   28 VVVLAAPPGAGKTTQLPLALLELGWGAGGR-IGMLEPRRLAARAAAERMAEELGEPVGETVGYRVRFEDKVSAATRIEVV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 175 TDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQ-IRNDLRIIVSSATLDAELFKDFFemnetgnsdkD 253
Cdd:COG1643  107 TEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPaLRPDLKLLVMSATLDAERFARLL----------G 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 254 TAGIISVEGRTHPVAVHHT--KTSVPDYCQSAVDTVINIHKhENPGDILVFLTGQDEVEDVCEKLRELAgnLKNCDrlwV 331
Cdd:COG1643  177 DAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREALA-EEPGDILVFLPGEREIRRTAEALRGRL--PPDTE---I 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 332 VPCYGALPAREQMKAFDSTPHGTRKVVVATNIAEASITIPGICYVIDTGYVKlRAQ-HAANGVETLMRVTVSKASAEQRA 410
Cdd:COG1643  251 LPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLAR-IPRyDPRSGVTRLPTERISQASANQRA 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 411 GRAGRIRPGKCYRLYPESEFERFAEGTVPEIQRCQMASTILQLKALGVQNVHRFHYLSPPPSwAMIN-GLELLYALGAID 489
Cdd:COG1643  330 GRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPA-RAIAdARALLQELGALD 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 490 ETSQLTsPLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQDvfitPYRQRHQADVirkkfaveegdhMTMLN 569
Cdd:COG1643  409 ADGRLT-PLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERD----PRRGAAGSDL------------LARLN 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 570 VFTKFVENGRskkwcsdHFVNYRGLMRADNVRSQLVRLLKrfeiEKVSSRGLIncSENIRQCLVTGFFSQAAQY-----H 644
Cdd:COG1643  472 LWRRLREQQR-------EFLSYLRLREWRDLARQLRRLLG----EGANEEPAD--YEAIGLLLALAYPDRIARRrgeggR 538
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351064569 645 Y-----TGkymtvkesfpFNMYKGSSiMFKKdypKWVIFTEVMQDS----IRDVTVIEPEWLYELAPH 703
Cdd:COG1643  539 YllargRG----------AALFPGSP-LAKK---EWLVAAELVGGAaearIRLAAPIDPEWLEELAAH 592
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
77-703 6.87e-136

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: 432.27  E-value: 6.87e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569    77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGrQIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:TIGR01967   66 LPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHG-LIGHTQPRRLAARTVAQRIAEELGTPLGEKVG 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   157 YTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATLDAE 236
Cdd:TIGR01967  145 YKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPE 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   237 LFKDFFemnetgnsdkDTAGIISVEGRTHPVAVHHTKTSVP------DYCQSAVDTVINIHKHEnPGDILVFLTGQDEVE 310
Cdd:TIGR01967  225 RFSRHF----------NNAPIIEVSGRTYPVEVRYRPLVEEqedddlDQLEAILDAVDELFAEG-PGDILIFLPGEREIR 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   311 DVCEKLRELagNLKNCDrlwVVPCYGALPAREQMKAFDstPHGTRKVVVATNIAEASITIPGICYVIDTGYVKLRAQHAA 390
Cdd:TIGR01967  294 DAAEILRKR--NLRHTE---ILPLYARLSNKEQQRVFQ--PHSGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYR 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   391 NGVETLMRVTVSKASAEQRAGRAGRIRPGKCYRLYPESEFERFAEGTVPEIQRCQMASTILQLKALGVQNVHRFHYLSPP 470
Cdd:TIGR01967  367 TKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAFPFIEAP 446
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   471 PSWAMINGLELLYALGAIDE---TSQLTsPLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQDVFITPYRQR 547
Cdd:TIGR01967  447 DPRAIRDGFRLLEELGALDDdeaEPQLT-PIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQ 525
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   548 HQADVIRKKFAVEEGDHMTMLNVFTKFVE--NGRSK----KWCSDHFVNYRGLMRADNVRSQLVRLLKRFEIEKVSSRGl 621
Cdd:TIGR01967  526 QAADQAHARFKDPRSDFLSRVNLWRHIEEqrQALSAnqfrNACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPA- 604
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   622 inCSENIRQCLVTGFFSQAAQYHYTGKYMTVKESfPFNMYKGSSiMFKKDyPKWVIFTEVMQDS---IRDVTVIEPEWLY 698
Cdd:TIGR01967  605 --DYDAIHKALLSGLLSQIGMKDEKHEYDGARGR-KFHIFPGSP-LFKKP-PKWVMAAELVETSklyARLVAKIEPEWVE 679

                   ....*
gi 351064569   699 ELAPH 703
Cdd:TIGR01967  680 PVAGH 684
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
77-703 3.29e-133

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 425.24  E-value: 3.29e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGrQIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:PRK11131   73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKG-LIGHTQPRRLAARTVANRIAEELETELGGCVG 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  157 YTVRFDD-VSDkDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATLDA 235
Cdd:PRK11131  152 YKVRFNDqVSD-NTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  236 ELFKDFFemnetgnsdkDTAGIISVEGRTHPVAVHH------TKTSVPDYCQSAVDTVINIhKHENPGDILVFLTGQDEV 309
Cdd:PRK11131  231 ERFSRHF----------NNAPIIEVSGRTYPVEVRYrpiveeADDTERDQLQAIFDAVDEL-GREGPGDILIFMSGEREI 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  310 EDVCEKLRELagNLKNCDrlwVVPCYGALPAREQMKAFDstPHGTRKVVVATNIAEASITIPGICYVIDTGYVKLRAQHA 389
Cdd:PRK11131  300 RDTADALNKL--NLRHTE---ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSY 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  390 ANGVETLMRVTVSKASAEQRAGRAGRIRPGKCYRLYPESEFERFAEGTVPEIQRCQMASTILQLKALGVQNVHRFHYLSP 469
Cdd:PRK11131  373 RTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEA 452
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  470 PPSWAMINGLELLYALGAIDETS-----QLTsPLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQDVFITPY 544
Cdd:PRK11131  453 PDKRNIQDGVRLLEELGAITTDEqasayKLT-PLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPM 531
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  545 RQRHQADVIRKKFAVEEGDHMTMLNVFTKFVENGRS------KKWCSDHFVNYRGLMRADNVRSQLVRLLKRFEI----E 614
Cdd:PRK11131  532 DKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKAlssnqfRRLCRTDYLNYLRVREWQDIYTQLRQVVKELGIpvnsE 611
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  615 KVSSRGlINCSenirqcLVTGFFSQAAQ-----YHYTGkymtvKESFPFNMYKGSSImFKKDyPKWVIFTEVMQDSI--- 686
Cdd:PRK11131  612 PAEYRE-IHTA------LLTGLLSHIGMkdaekQEYTG-----ARNARFSIFPGSGL-FKKP-PKWVMVAELVETSRlwg 677
                         650
                  ....*....|....*..
gi 351064569  687 RDVTVIEPEWLYELAPH 703
Cdd:PRK11131  678 RIAARIEPEWIEPLAQH 694
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
77-260 1.26e-119

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: 356.01  E-value: 1.26e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGRQIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:cd17980    1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 157 YTVRFDDVSDKD-TKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATLDA 235
Cdd:cd17980   81 YCIRFDDCTDPQaTRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160
                        170       180
                 ....*....|....*....|....*
gi 351064569 236 ELFKDFFEMNETGNSDKDTAGIISV 260
Cdd:cd17980  161 EKFRDFFNQNETNDPSKDTATILSV 185
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
96-538 1.04e-91

ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 304.00  E-value: 1.04e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   96 IIIVGETGCGKSTQVPQFLLEAGWAadGRQIVITQPRRVAVVTLATRVAEEKDCILGHDVGYTVRFDDVSDKDTKVKFMT 175
Cdd:TIGR01970  20 VVLEAPPGAGKSTAVPLALLDAPGI--GGKIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYRVRGENKVSRRTRLEVVT 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  176 DGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKI-IQIRNDLRIIVSSATLDAELFKDFFemnetgnsdkDT 254
Cdd:TIGR01970  98 EGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVqSSLREDLKILAMSATLDGERLSSLL----------PD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  255 AGIISVEGRTHPVAVHHTKTSVPDYCQSAV-DTVINIHKHEnPGDILVFLTGQDEVEDVCEKLRELAGNlkncdRLWVVP 333
Cdd:TIGR01970 168 APVVESEGRSFPVEIRYLPLRGDQRLEDAVsRAVEHALASE-TGSILVFLPGQAEIRRVQEQLAERLDS-----DVLICP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  334 CYGALPAREQMKAFDSTPHGTRKVVVATNIAEASITIPGICYVIDTGYVKLRAQHAANGVETLMRVTVSKASAEQRAGRA 413
Cdd:TIGR01970 242 LYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  414 GRIRPGKCYRLYPESEFERFAEGTVPEIQRCQMASTILQLKALGVQNVHRFHYLSPPPSWAMINGLELLYALGAIDETSQ 493
Cdd:TIGR01970 322 GRLEPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGR 401
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 351064569  494 LTSpLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQD 538
Cdd:TIGR01970 402 LTA-HGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALLEERG 445
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
102-522 1.12e-83

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 282.20  E-value: 1.12e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 102 TGCGKSTQVP-QFLLEAGWaaDGRqIVITQPRRVAVVTLATRVAE---EKdciLGHDVGYTVRFDDVSDKDTKVKFMTDG 177
Cdd:PRK11664  29 TGAGKSTWLPlQLLQHGGI--NGK-IIMLEPRRLAARNVAQRLAEqlgEK---PGETVGYRMRAESKVGPNTRLEVVTEG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 178 LLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQ-IRNDLRIIVSSATLDAE----LFKDffemnetgnsdk 252
Cdd:PRK11664 103 ILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVQQgLRDDLKLLIMSATLDNDrlqqLLPD------------ 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 253 dtAGIISVEGRTHPVAVHHTKTSVPDYCQSAVDTVINIHKHENPGDILVFLTGQDEVEDVCEKLRE-LAGNLKNCdrlwv 331
Cdd:PRK11664 171 --APVIVSEGRSFPVERRYQPLPAHQRFDEAVARATAELLRQESGSLLLFLPGVGEIQRVQEQLASrVASDVLLC----- 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 332 vPCYGALPAREQMKAFDSTPHGTRKVVVATNIAEASITIPGICYVIDTGYVKLRAQHAANGVETLMRVTVSKASAEQRAG 411
Cdd:PRK11664 244 -PLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAG 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 412 RAGRIRPGKCYRLYPESEFERFAEGTVPEIQRCQMASTILQLKALGVQNVHRFHYLSPPPSWAMINGLELLYALGAIDET 491
Cdd:PRK11664 323 RAGRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQ 402
                        410       420       430
                 ....*....|....*....|....*....|.
gi 351064569 492 SQLTSpLGLQMAEFPLPPMHSKCLLKSAEFG 522
Cdd:PRK11664 403 GRLTA-RGRKMAALGNDPRLAAMLVAAKEDD 432
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
94-260 1.23e-83

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: 261.63  E-value: 1.23e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  94 RTIIIVGETGCGKSTQVPQFLLEAGWAADGR-QIVITQPRRVAVVTLATRVAEEKDCILGHDVGYTVRFDDVSDKDTKVK 172
Cdd:cd17917    2 QVVVIVGETGSGKTTQVPQFLLEDGLAKGGKgRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRIK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 173 FMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATLDAELFKDFFemnetgnsdk 252
Cdd:cd17917   82 FCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYF---------- 151

                 ....*...
gi 351064569 253 DTAGIISV 260
Cdd:cd17917  152 GGAPVIHI 159
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
77-242 1.02e-75

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: 241.88  E-value: 1.02e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAaDGRQIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:cd17978    1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFA-RGGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 157 YTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIR-----NDLRIIVSSA 231
Cdd:cd17978   80 YSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVIIMSA 159
                        170
                 ....*....|.
gi 351064569 232 TLDAELFKDFF 242
Cdd:cd17978  160 TLDADLFSEYF 170
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
265-425 2.43e-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: 240.51  E-value: 2.43e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 265 HPVAVHHTKT-----------SVPDYCQSAVDTVINIHKHENPGDILVFLTGQDEVEDVCEKLRELAgNLKNCDRLWVVP 333
Cdd:cd18791    1 FPVEVYYLEDilellgissekEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREEL-LSPDLGKLLVLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 334 CYGALPAREQMKAFDSTPHGTRKVVVATNIAEASITIPGICYVIDTGYVKLRAQHAANGVETLMRVTVSKASAEQRAGRA 413
Cdd:cd18791   80 LHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRA 159
                        170
                 ....*....|..
gi 351064569 414 GRIRPGKCYRLY 425
Cdd:cd18791  160 GRTRPGKCYRLY 171
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
72-242 4.56e-67

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: 218.89  E-value: 4.56e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  72 QQRIRLPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGRqIVITQPRRVAVVTLATRVAEEKDCIL 151
Cdd:cd17971    1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGK-IGCTQPRRVAAMSVAKRVAEEFGCCL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 152 GHDVGYTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSA 231
Cdd:cd17971   80 GQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSA 159
                        170
                 ....*....|.
gi 351064569 232 TLDAELFKDFF 242
Cdd:cd17971  160 TLDAVKFSQYF 170
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
77-243 3.43e-66

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: 216.21  E-value: 3.43e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGRQIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:cd17974    1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 157 YTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATLDAE 236
Cdd:cd17974   81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160

                 ....*..
gi 351064569 237 LFKDFFE 243
Cdd:cd17974  161 KFSAFFD 167
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
68-243 4.17e-66

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: 216.51  E-value: 4.17e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  68 LNIQQQRIRLPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWA-ADGRQIVITQPRRVAVVTLATRVAEE 146
Cdd:cd17973    4 FEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPhQPKKLVACTQPRRVAAMSVAQRVAEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 147 KDCILGHDVGYTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRI 226
Cdd:cd17973   84 MDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKL 163
                        170
                 ....*....|....*..
gi 351064569 227 IVSSATLDAELFKDFFE 243
Cdd:cd17973  164 IVMSATLDAGKFQKYFD 180
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
77-242 7.55e-64

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: 210.01  E-value: 7.55e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGrQIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:cd17983    1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYG-MIGCTQPRRVAAMSVAKRVSEEMGVELGEEVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 157 YTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATLDAE 236
Cdd:cd17983   80 YAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDAD 159

                 ....*.
gi 351064569 237 LFKDFF 242
Cdd:cd17983  160 KFADFF 165
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
77-238 1.78e-61

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: 204.51  E-value: 1.78e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGRQ----IVITQPRRVAVVTLATRVAEEKDcILG 152
Cdd:cd17982    1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESDnpgmIGITQPRRVAAVSMAKRVAEELN-VFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 153 HDVGYTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRND--------- 223
Cdd:cd17982   80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159
                        170
                 ....*....|....*.
gi 351064569 224 -LRIIVSSATLDAELF 238
Cdd:cd17982  160 pLKLVIMSATLRVEDF 175
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
77-242 6.99e-61

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: 202.39  E-value: 6.99e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGRqIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:cd17984    1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGM-IGVTQPRRVAAISVAQRVAEEMKCTLGSKVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 157 YTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRN-----DLRIIVSSA 231
Cdd:cd17984   80 YQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVVMSA 159
                        170
                 ....*....|.
gi 351064569 232 TLDAELFKDFF 242
Cdd:cd17984  160 TLELAKLSAFF 170
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
77-243 1.70e-52

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: 179.18  E-value: 1.70e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWaadgRQIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:cd17979    1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGF----RHIACTQPRRIACISLAKRVAFESLNQYGSKVA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 157 YTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATLDAE 236
Cdd:cd17979   77 YQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIE 156

                 ....*..
gi 351064569 237 LFKDFFE 243
Cdd:cd17979  157 LFSGYFE 163
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
77-260 5.12e-52

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: 178.03  E-value: 5.12e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGrQIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:cd17989    1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRG-LIGHTQPRRLAARSVAERIAEELKTELGGAVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 157 YTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATLDAE 236
Cdd:cd17989   80 YKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAE 159
                        170       180
                 ....*....|....*....|....
gi 351064569 237 LFKDFFemnetgnsdkDTAGIISV 260
Cdd:cd17989  160 RFSRHF----------NNAPIIEV 173
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
77-242 2.32e-47

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: 165.86  E-value: 2.32e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLE----AGWAADGRQIVITQPRRVAVVTLATRVAEEKDCILG 152
Cdd:cd17975    1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEdlllNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 153 HD-----VGYTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRII 227
Cdd:cd17975   81 PGgknslCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
                        170
                 ....*....|....*
gi 351064569 228 VSSATLDAELFKDFF 242
Cdd:cd17975  161 LMSATVDCEKFSSYF 175
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
77-242 4.74e-45

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: 159.24  E-value: 4.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAgWAADGR----QIVITQPRRVAVVTLATRVAEEKDCILG 152
Cdd:cd17985    1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDN-SLQGPPlpvaNIICTQPRRISAISVAERVAQERAERVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 153 HDVGYTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSAT 232
Cdd:cd17985   80 QSVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSAT 159
                        170
                 ....*....|
gi 351064569 233 LDAELFKDFF 242
Cdd:cd17985  160 LNAELFSDYF 169
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
77-242 3.71e-44

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: 156.93  E-value: 3.71e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLL----EAGWAADGRqIVITQPRRVAVVTLATRVAEEK--DCI 150
Cdd:cd17981    1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILddaiERGKGSSCR-IVCTQPRRISAISVAERVAAERaeSCG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 151 LGHDVGYTVRFDD-VSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVS 229
Cdd:cd17981   80 LGNSTGYQIRLESrKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159
                        170
                 ....*....|...
gi 351064569 230 SATLDAELFKDFF 242
Cdd:cd17981  160 SATLNAEKFSDYF 172
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
77-238 1.12e-42

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: 152.49  E-value: 1.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGRqIVITQPRRVAVVTLATRVAEEKDCILGHDVG 156
Cdd:cd17990    1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGK-IIVLEPRRVAARAAARRLATLLGEAPGETVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 157 YTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQ-IRNDLRIIVSSATLDA 235
Cdd:cd17990   80 YRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSATLDG 159

                 ...
gi 351064569 236 ELF 238
Cdd:cd17990  160 DGL 162
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
70-242 4.70e-41

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: 149.98  E-value: 4.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  70 IQQQRIRLPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLE----AGWAADGrQIVITQPRRVAVVTLATRVAE 145
Cdd:cd17972   52 ILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDdfiqNDRAAEC-NIVVTQPRRISAVSVAERVAF 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 146 EKDCILGHDVGYTVRFDDVSDKD-TKVKFMTDGLLLREILADplLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDL 224
Cdd:cd17972  131 ERGEEVGKSCGYSVRFESVLPRPhASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDL 208
                        170
                 ....*....|....*...
gi 351064569 225 RIIVSSATLDAELFKDFF 242
Cdd:cd17972  209 RVILMSATIDTSMFCEYF 226
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
77-242 8.14e-39

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: 141.89  E-value: 8.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGwAADGR--QIVITQPRRVAVVTLATRVAEEKDCILGHD 154
Cdd:cd17987    1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDC-YANGIpcRIFCTQPRRLAAIAVAERVAAERGEKIGQT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 155 VGYTVRFDDVSDKDTKVKFMTDGLLLREILA-DPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSATL 233
Cdd:cd17987   80 VGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAAL 159

                 ....*....
gi 351064569 234 DAELFKDFF 242
Cdd:cd17987  160 DVNLFIRYF 168
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
77-244 1.23e-38

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: 141.49  E-value: 1.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGR-QIVITQPRRVAVVTLATRVAEEKDCILGHDV 155
Cdd:cd17988    1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYcNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 156 GYTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRND-LRIIVSSATLD 234
Cdd:cd17988   81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSATIS 160
                        170
                 ....*....|
gi 351064569 235 AELFKDFFEM 244
Cdd:cd17988  161 CKEFADYFTT 170
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
77-242 2.22e-38

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: 140.70  E-value: 2.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGwAADGR----QIVITQPRRVAVVTLATRVAEEKDCILG 152
Cdd:cd17976    1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDY-VLRGRgarcNVVITQPRRISAVSVAQRVAHELGPNLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 153 HDVGYTVRFDD-VSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSA 231
Cdd:cd17976   80 RNVGYQVRLESrPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSA 159
                        170
                 ....*....|.
gi 351064569 232 TLDAELFKDFF 242
Cdd:cd17976  160 TGDNQRLSRYF 170
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
77-237 1.77e-35

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: 132.33  E-value: 1.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIV-GETGCGKSTQVPQ----FLLEAGWAADgrQIVITQPRRVAVVTLATRVAEEKDCIL 151
Cdd:cd17986    1 LPIWAAKFTFLEQLESPSGIVLVsGEPGSGKSTQVPQwcaeFALSRGFQKG--QVTVTQPHPLAARSLALRVADEMDLNL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 152 GHDVGYTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLR-IIVSS 230
Cdd:cd17986   79 GHEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRvVVVTS 158

                 ....*..
gi 351064569 231 ATLDAEL 237
Cdd:cd17986  159 PALEPKL 165
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
77-231 8.21e-35

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: 130.33  E-value: 8.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  77 LPIFKNRGHILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGRQ--IVITQPRRVAVVTLATRVAEEKDCILGHD 154
Cdd:cd17977    1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAHYQHgvVVCTQVHKQTAVWLALRVADEMDVNIGHE 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351064569 155 VGYTVRFDDVSDKDTKVKFMTDGLLLREILADPLLSKYSIIMIDEAHERSCNTDILLGLLRKIIQIRNDLRIIVSSA 231
Cdd:cd17977   81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITC 157
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
484-568 1.23e-27

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: 106.58  E-value: 1.23e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   484 ALGAIDETSQLTsPLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQDVFitPYRQRHQADVIRKKFAVEEGD 563
Cdd:smart00847   1 ELGALDDDGRLT-PLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESD 77

                   ....*
gi 351064569   564 HMTML 568
Cdd:smart00847  78 HLTLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
479-567 1.68e-27

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: 106.94  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  479 LELLYALGAIDETSQLTsPLGLQMAEFPLPPMHSKCLLKSAEFGCSTEMVTIVAMMQIQDVFITPY-------------R 545
Cdd:pfam04408   2 LELLYYLGALDEDGELT-PLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNfldprsaakaarrR 80
                          90       100
                  ....*....|....*....|....
gi 351064569  546 QRHQADVIRKKFAVE--EGDHMTM 567
Cdd:pfam04408  81 RRAADEKARAKFARLdlEGDHLTL 104
DEXDc smart00487
DEAD-like helicases superfamily;
86-243 1.08e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 99.49  E-value: 1.08e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569    86 ILYMCERYRTIIIVGETGCGKSTQVPQFLLEAGWAADGRQIVITQPRRVAVVTLATRVAEEKDCILGHDVGYTV------ 159
Cdd:smart00487  17 IEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGgdskre 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   160 RFDDVSDKDTKVKFMTDGLLLREILADPL-LSKYSIIMIDEAHERS--CNTDILLGLLRKiiqIRNDLRIIVSSATLDAE 236
Cdd:smart00487  97 QLRKLESGKTDILVTTPGRLLDLLENDKLsLSNVDLVILDEAHRLLdgGFGDQLEKLLKL---LPKNVQLLLLSATPPEE 173

                   ....*..
gi 351064569   237 LFKDFFE 243
Cdd:smart00487 174 IENLLEL 180
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
64-425 8.05e-18

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 87.73  E-value: 8.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  64 PYASLNIQQQRIRLPIFKNRghilymceryRTIIIVGETGCGKSTQVPQFLLEAGWAADG-------------RQIVITQ 130
Cdd:PHA02653 160 PLASLQPDVQLKIFEAWISR----------KPVVLTGGTGVGKTSQVPKLLLWFNYLFGGfdnldkidpnfieRPIVLSL 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 131 PRrVAVVTLATRVAEEK---DCILGHDVgyTVRFDDVSDKDTKVKFMTDGLLL---REILADplLSKYSIIMIDEAHERS 204
Cdd:PHA02653 230 PR-VALVRLHSITLLKSlgfDEIDGSPI--SLKYGSIPDELINTNPKPYGLVFsthKLTLNK--LFDYGTVIIDEVHEHD 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 205 CNTDILLGLLRK-IIQIRNdlrIIVSSATL--DAELFKDFFemnetgnsdkDTAGIISVEGRT-HPV--AVHHTKTSVPD 278
Cdd:PHA02653 305 QIGDIIIAVARKhIDKIRS---LFLMTATLedDRDRIKEFF----------PNPAFVHIPGGTlFPIseVYVKNKYNPKN 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 279 YCQSA------VDTVINIHKHENPGDILVFLTGQDEVEDVCEKLRELAGNLKncdrLWVVpcYGALP-AREQMKAFDSTP 351
Cdd:PHA02653 372 KRAYIeeekknIVTALKKYTPPKGSSGIVFVASVSQCEEYKKYLEKRLPIYD----FYII--HGKVPnIDEILEKVYSSK 445
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351064569 352 HGTrkVVVATNIAEASITIPGICYVIDTGYVKLRAQHAanGVETLmrvtVSKASAEQRAGRAGRIRPGKCYRLY 425
Cdd:PHA02653 446 NPS--IIISTPYLESSVTIRNATHVYDTGRVYVPEPFG--GKEMF----ISKSMRTQRKGRVGRVSPGTYVYFY 511
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
284-416 4.59e-15

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: 71.47  E-value: 4.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  284 VDTVINIHKHENPGDILVFLTGQDEVEdvCEKLRELAGnlKNCDRLwvvpcYGALPAREQMKAFDSTPHGTRKVVVATNI 363
Cdd:pfam00271   3 LEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKEG--IKVARL-----HGDLSQEEREEILEDFRKGKIDVLVATDV 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 351064569  364 AEASITIPGICYVIDTGYVKlraqhaangvetlmrvtvSKASAEQRAGRAGRI 416
Cdd:pfam00271  74 AERGLDLPDVDLVINYDLPW------------------NPASYIQRIGRAGRA 108
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
628-704 3.28e-14

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: 68.43  E-value: 3.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  628 IRQCLVTGFFSQAAQYHYTGK-YMTVKESFPFNMYKgSSIMFKKD--YPKWVIFTEVMQDS---IRDVTVIEPEWLYELA 701
Cdd:pfam07717   1 LRAALAAGLYPNVARRDPKGKgYTTLSDNQRVFIHP-SSVLFNEKtfPPEWVVYQELVETTkvyIRTVTAISPEWLLLFA 79

                  ...
gi 351064569  702 PHY 704
Cdd:pfam07717  80 PHI 82
HELICc smart00490
helicase superfamily c-terminal domain;
317-416 2.30e-12

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 63.00  E-value: 2.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   317 RELAGNLKNCDrLWVVPCYGALPAREQMKAFDSTPHGTRKVVVATNIAEASITIPGICYVIDtgyvklraqhaangvetl 396
Cdd:smart00490   1 EELAELLKELG-IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVII------------------ 61
                           90       100
                   ....*....|....*....|
gi 351064569   397 MRVTVSKASAEQRAGRAGRI 416
Cdd:smart00490  62 YDLPWSPASYIQRIGRAGRA 81
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
97-232 2.29e-10

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: 59.34  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569  97 IIVGETGCGKSTQVPQFLLEAGwAADGRQIVITQPRRvavvTLATRVAEEKDCILGHD--VGYTVRFDDVSDK------D 168
Cdd:cd00046    5 LITAPTGSGKTLAALLAALLLL-LKKGKKVLVLVPTK----ALALQTAERLRELFGPGirVAVLVGGSSAEEReknklgD 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351064569 169 TKVKFMTDGLLLREILADPLL--SKYSIIMIDEAHERSCNTD-ILLGLLRKIIQIRNDLRIIVSSAT 232
Cdd:cd00046   80 ADIIIATPDMLLNLLLREDRLflKDLKLIIVDEAHALLIDSRgALILDLAVRKAGLKNAQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
96-237 1.17e-05

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: 46.08  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   96 IIIVGETGCGKST--QVPqfLLEAGWAAD-GRQIVITQPRRVavvtLATRVAEE-KDCILGHDVGYTVRFDDVSDKD--- 168
Cdd:pfam00270  17 VLVQAPTGSGKTLafLLP--ALEALDKLDnGPQALVLAPTRE----LAEQIYEElKKLGKGLGLKVASLLGGDSRKEqle 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351064569  169 ----TKVKFMTDGLLLREILADPLLSKYSIIMIDEAHErscntdiLLGL-----LRKII-QIRNDLRIIVSSATLDAEL 237
Cdd:pfam00270  91 klkgPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAHR-------LLDMgfgpdLEEILrRLPKKRQILLLSATLPRNL 162
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
102-251 5.61e-05

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: 44.56  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 102 TGCGKSTqVPQFLLEAGWAADGRQIVITQPRRvAVVtlATRVAEEKDC--ILGHDVG-----YTVRFDDVSDKD----TK 170
Cdd:cd17921   26 TSSGKTL-IAELAILRALATSGGKAVYIAPTR-ALV--NQKEADLRERfgPLGKNVGlltgdPSVNKLLLAEADilvaTP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 171 VKFmtDGLLLReiLADPLLSKYSIIMIDEAH-----ERScntDILLGLLRKIIQIRNDLRIIVSSATLD-AELFKDFFEM 244
Cdd:cd17921  102 EKL--DLLLRN--GGERLIQDVRLVVVDEAHligdgERG---VVLELLLSRLLRINKNARFVGLSATLPnAEDLAEWLGV 174

                 ....*..
gi 351064569 245 NETGNSD 251
Cdd:cd17921  175 EDLIRFD 181
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
253-419 1.11e-04

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 43.02  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 253 DTAGIISVEGRTHPVAVHHTKTsvpdycqsAVDTVI-NIHKHENpgdILVFLTGQDEVEDVCEKLRELAGNLKNCDRlwv 331
Cdd:cd18796    5 DIKVILPVAPEIFPWAGESGAD--------AYAEVIfLLERHKS---TLVFTNTRSQAERLAQRLRELCPDRVPPDF--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 332 VPCYGALPAREQ-------MKAfdstphGTRKVVVATNIAEASItipgicyviDTGYVKLRAQHAAngvetlmrvTVSKA 404
Cdd:cd18796   71 IALHHGSLSRELreeveaaLKR------GDLKVVVATSSLELGI---------DIGDVDLVIQIGS---------PKSVA 126
                        170
                 ....*....|....*
gi 351064569 405 SAEQRAGRAGRiRPG 419
Cdd:cd18796  127 RLLQRLGRSGH-RPG 140
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
290-420 1.88e-04

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 42.24  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569 290 IHKHENPGDILVFLTGQDEVEDVCEKLRELAgnlkncdrlwvvpCYGALPAREQMKAFDSTPHGTRKVVVATNIAEASIT 369
Cdd:cd18789   43 LKRHEQGDKIIVFTDNVEALYRYAKRLLKPF-------------ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGID 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 351064569 370 IPgicyvidtgyvklraqhAANgveTLMRVTVSKASAEQRAGRAGRI-RPGK 420
Cdd:cd18789  110 LP-----------------EAN---VAIQISGHGGSRRQEAQRLGRIlRPKK 141
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
356-425 3.76e-04

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: 39.61  E-value: 3.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351064569 356 KVVVATNIAEASITIPGICYVIDTGYVKlraqhaangvetlmrvtvSKASAEQRAGRAGRI--RPGKCYRLY 425
Cdd:cd18785   24 EILVATNVLGEGIDVPSLDTVIFFDPPS------------------SAASYIQRVGRAGRGgkDEGEVILFV 77
AAA_22 pfam13401
AAA domain;
96-229 1.42e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569   96 IIIVGETGCGKSTQVpQFLLEAGWAADGRQIVITQPRRVAVVTLATRVAEEkdciLGHDVGYTVRFDDvsdkdtkvkfmt 175
Cdd:pfam13401   8 LVLTGESGTGKTTLL-RRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRA----LGLPLSGRLSKEE------------ 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 351064569  176 dgllLREILADPLLSKYS--IIMIDEAHerscntDILLGLLRKIIQIRNDLRIIVS 229
Cdd:pfam13401  71 ----LLAALQQLLLALAVavVLIIDEAQ------HLSLEALEELRDLLNLSSKLLQ 116
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
92-230 4.39e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.51  E-value: 4.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351064569    92 RYRTIIIVGETGCGKSTqvpqFLLEAGWAADGRQivitqpRRVAVVTLATRVAEEKDCILGHDVGYTVRFDDVsdkdtkv 171
Cdd:smart00382   1 PGEVILIVGPPGSGKTT----LARALARELGPPG------GGVIYIDGEDILEEVLDQLLLIIVGGKKASGSG------- 63
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351064569   172 kfmtdGLLLREILADPLLSKYSIIMIDEAH------ERSCNTDILLGLLRKIIQIRNDLRIIVSS 230
Cdd:smart00382  64 -----ELRLRLALALARKLKPDVLILDEITslldaeQEALLLLLEELRLLLLLKSEKNLTVILTT 123
 
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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