NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217335784|ref|XP_047296310|]
View 

probable ATP-dependent RNA helicase DHX35 isoform X2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
54-644 5.88e-157

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: 472.64  E-value: 5.88e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  54 LPvfKYLAEAGWTAEGRVvGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVD 133
Cdd:COG1643    43 LP--LALLELGWGAGGRI-GMLEPRRLAARAAAERMAEELGEPVGETVGYRVRFEDKVSA-ATRIEVVTEGILLRELQRD 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 134 PLLTKYSVIMLDEAHERTLYTDIAIGLLKKIQKK-RGDLRLIVASATLDADKFRDFFNqnetsdPARdtcvILTVEGRTF 212
Cdd:COG1643   119 PELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLDAERFARLLG------DAP----VIESSGRTY 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 213 PVDIFYL--QSPVPDYIKSTVETVVKIHQtEGDGDVLAFLTGQEEvetvvsmlIEQARALARTGMKRHLRVLPMYAGLPS 290
Cdd:COG1643   189 PVEVRYRplPADERDLEDAVADAVREALA-EEPGDILVFLPGERE--------IRRTAEALRGRLPPDTEILPLYGRLSA 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 291 FEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGK 370
Cdd:COG1643   260 AEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGI 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 371 CYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKDCRLTePLGM 450
Cdd:COG1643   340 CYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARALLQELGALDADGRLT-PLGR 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 451 RIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFvvPPNQKS------HAHNKDSKWcQEHFLNYKGLVRAATV 524
Cdd:COG1643   419 ALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR--RGAAGSdllarlNLWRRLREQ-QREFLSYLRLREWRDL 495
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 525 REQLKKLLvkfQVPRKSSEGDPDLVLRCIVSGFFAN-AARFHSTGAYRTIRdDHELHIHPASVLYAEKpprWVIYNEVIQ 603
Cdd:COG1643   496 ARQLRRLL---GEGANEEPADYEAIGLLLALAYPDRiARRRGEGGRYLLAR-GRGAALFPGSPLAKKE---WLVAAELVG 568
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 2217335784 604 T---SKyyMRDVTAIESAWLLELAPHFYQQGTHLSLKAKRAKVQ 644
Cdd:COG1643   569 GaaeAR--IRLAAPIDPEWLEELAAHLIKRYSEPHWDKKRGRVV 610
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
54-644 5.88e-157

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 472.64  E-value: 5.88e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  54 LPvfKYLAEAGWTAEGRVvGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVD 133
Cdd:COG1643    43 LP--LALLELGWGAGGRI-GMLEPRRLAARAAAERMAEELGEPVGETVGYRVRFEDKVSA-ATRIEVVTEGILLRELQRD 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 134 PLLTKYSVIMLDEAHERTLYTDIAIGLLKKIQKK-RGDLRLIVASATLDADKFRDFFNqnetsdPARdtcvILTVEGRTF 212
Cdd:COG1643   119 PELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLDAERFARLLG------DAP----VIESSGRTY 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 213 PVDIFYL--QSPVPDYIKSTVETVVKIHQtEGDGDVLAFLTGQEEvetvvsmlIEQARALARTGMKRHLRVLPMYAGLPS 290
Cdd:COG1643   189 PVEVRYRplPADERDLEDAVADAVREALA-EEPGDILVFLPGERE--------IRRTAEALRGRLPPDTEILPLYGRLSA 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 291 FEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGK 370
Cdd:COG1643   260 AEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGI 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 371 CYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKDCRLTePLGM 450
Cdd:COG1643   340 CYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARALLQELGALDADGRLT-PLGR 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 451 RIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFvvPPNQKS------HAHNKDSKWcQEHFLNYKGLVRAATV 524
Cdd:COG1643   419 ALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR--RGAAGSdllarlNLWRRLREQ-QREFLSYLRLREWRDL 495
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 525 REQLKKLLvkfQVPRKSSEGDPDLVLRCIVSGFFAN-AARFHSTGAYRTIRdDHELHIHPASVLYAEKpprWVIYNEVIQ 603
Cdd:COG1643   496 ARQLRRLL---GEGANEEPADYEAIGLLLALAYPDRiARRRGEGGRYLLAR-GRGAALFPGSPLAKKE---WLVAAELVG 568
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 2217335784 604 T---SKyyMRDVTAIESAWLLELAPHFYQQGTHLSLKAKRAKVQ 644
Cdd:COG1643   569 GaaeAR--IRLAAPIDPEWLEELAAHLIKRYSEPHWDKKRGRVV 610
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
72-626 1.12e-129

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: 412.62  E-value: 1.12e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784   72 VGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYSVIMLDEAHERT 151
Cdd:TIGR01967  114 IGHTQPRRLAARTVAQRIAEELGTPLGEKVGYKVRFHDQVSS-NTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERS 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  152 LYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFNQNEtsdpardtcvILTVEGRTFPVDIFY-----LQSPVP-D 225
Cdd:TIGR01967  193 LNIDFLLGYLKQLLPRRPDLKIIITSATIDPERFSRHFNNAP----------IIEVSGRTYPVEVRYrplveEQEDDDlD 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  226 YIKSTVETVVKIHQtEGDGDVLAFLTGQEEVEtvvsmliEQARALARTGMkRHLRVLPMYAGLPSFEQMKVFErvSRSVR 305
Cdd:TIGR01967  263 QLEAILDAVDELFA-EGPGDILIFLPGEREIR-------DAAEILRKRNL-RHTEILPLYARLSNKEQQRVFQ--PHSGR 331
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  306 KVIVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQ 385
Cdd:TIGR01967  332 RIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPE 411
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  386 STVPEMQRSNLAPVILQLKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKD---CRLTePLGMRIAEFPLNPMFA 462
Cdd:TIGR01967  412 FTDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDeaePQLT-PIGRQLAQLPVDPRLA 490
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  463 KMLLESGNFGCSQEILSIAAMMQIQNIFVVPPNQK-----SHA--HNKDS-------------------------KWCQE 510
Cdd:TIGR01967  491 RMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQqaadqAHArfKDPRSdflsrvnlwrhieeqrqalsanqfrNACRK 570
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  511 HFLNYKGLVRAATVREQLKKLLVKFQVPRKSSEGDPDLVLRCIVSGFFANAARFHSTGAYRTIRdDHELHIHPASVLyAE 590
Cdd:TIGR01967  571 QYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKALLSGLLSQIGMKDEKHEYDGAR-GRKFHIFPGSPL-FK 648
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 2217335784  591 KPPRWVIYNEVIQTSKYYMRDVTAIESAWLLELAPH 626
Cdd:TIGR01967  649 KPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAGH 684
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
53-626 1.24e-121

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 391.35  E-value: 1.24e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784   53 KLPvfKYLAEAGWTAEGrVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFddcTDQLA--TRIKFLTDGMLVREM 130
Cdd:PRK11131   105 QLP--KICLELGRGVKG-LIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRF---NDQVSdnTMVKLMTDGILLAEI 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  131 MVDPLLTKYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFNQNEtsdpardtcvILTVEGR 210
Cdd:PRK11131   179 QQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAP----------IIEVSGR 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  211 TFPVDIFYlqSPV--------PDYIKSTVETVVKIhQTEGDGDVLAFLTGQEEVEtvvsmliEQARALARTGMkRHLRVL 282
Cdd:PRK11131   249 TYPVEVRY--RPIveeaddteRDQLQAIFDAVDEL-GREGPGDILIFMSGEREIR-------DTADALNKLNL-RHTEIL 317
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  283 PMYAGLPSFEQMKVFErvSRSVRKVIVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGR 362
Cdd:PRK11131   318 PLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGR 395
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  363 GGRSRSGKCYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKDC 442
Cdd:PRK11131   396 CGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDE 475
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  443 -----RLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQN---------------------------IF 490
Cdd:PRK11131   476 qasayKLT-PLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDprerpmdkqqasdekhrrfadkesdflAF 554
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  491 V-----VPPNQKSHAHNKDSKWCQEHFLNYkglVRaatVRE------QLKKLLVKFQVPRKSSEGDPDLVLRCIVSGFFA 559
Cdd:PRK11131   555 VnlwnyLQEQQKALSSNQFRRLCRTDYLNY---LR---VREwqdiytQLRQVVKELGIPVNSEPAEYREIHTALLTGLLS 628
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217335784  560 -----NAARFHSTGAyrtiRDDHeLHIHPASVLYaEKPPRWVIYNEVIQTSKYYMRDVTAIESAWLLELAPH 626
Cdd:PRK11131   629 higmkDAEKQEYTGA----RNAR-FSIFPGSGLF-KKPPKWVMVAELVETSRLWGRIAARIEPEWIEPLAQH 694
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
58-207 4.03e-103

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: 310.94  E-value: 4.03e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  58 KYLAEAGWTAEGRVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQLATRIKFLTDGMLVREMMVDPLLT 137
Cdd:cd17980    36 QYLAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVGYCIRFDDCTDPQATRIKFLTDGMLVREMMLDPLLT 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 138 KYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFNQNETSDPARDTCVILTV 207
Cdd:cd17980   116 KYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDAEKFRDFFNQNETNDPSKDTATILSV 185
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
428-512 1.13e-24

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: 98.85  E-value: 1.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 428 ALELLYALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFvVPPNQKSHAHNKDSKW 507
Cdd:pfam04408   1 ALELLYYLGALDEDGELT-PLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPF-VQPNFLDPRSAAKAAR 78

                  ....*
gi 2217335784 508 CQEHF 512
Cdd:pfam04408  79 RRRRA 83
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
434-510 8.42e-18

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: 78.46  E-value: 8.42e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217335784  434 ALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFvvPPNQKSHAHNKDSKWCQE 510
Cdd:smart00847   1 ELGALDDDGRLT-PLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADP 74
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
54-644 5.88e-157

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 472.64  E-value: 5.88e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  54 LPvfKYLAEAGWTAEGRVvGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVD 133
Cdd:COG1643    43 LP--LALLELGWGAGGRI-GMLEPRRLAARAAAERMAEELGEPVGETVGYRVRFEDKVSA-ATRIEVVTEGILLRELQRD 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 134 PLLTKYSVIMLDEAHERTLYTDIAIGLLKKIQKK-RGDLRLIVASATLDADKFRDFFNqnetsdPARdtcvILTVEGRTF 212
Cdd:COG1643   119 PELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLDAERFARLLG------DAP----VIESSGRTY 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 213 PVDIFYL--QSPVPDYIKSTVETVVKIHQtEGDGDVLAFLTGQEEvetvvsmlIEQARALARTGMKRHLRVLPMYAGLPS 290
Cdd:COG1643   189 PVEVRYRplPADERDLEDAVADAVREALA-EEPGDILVFLPGERE--------IRRTAEALRGRLPPDTEILPLYGRLSA 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 291 FEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGK 370
Cdd:COG1643   260 AEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGI 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 371 CYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKDCRLTePLGM 450
Cdd:COG1643   340 CYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARALLQELGALDADGRLT-PLGR 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 451 RIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFvvPPNQKS------HAHNKDSKWcQEHFLNYKGLVRAATV 524
Cdd:COG1643   419 ALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR--RGAAGSdllarlNLWRRLREQ-QREFLSYLRLREWRDL 495
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 525 REQLKKLLvkfQVPRKSSEGDPDLVLRCIVSGFFAN-AARFHSTGAYRTIRdDHELHIHPASVLYAEKpprWVIYNEVIQ 603
Cdd:COG1643   496 ARQLRRLL---GEGANEEPADYEAIGLLLALAYPDRiARRRGEGGRYLLAR-GRGAALFPGSPLAKKE---WLVAAELVG 568
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 2217335784 604 T---SKyyMRDVTAIESAWLLELAPHFYQQGTHLSLKAKRAKVQ 644
Cdd:COG1643   569 GaaeAR--IRLAAPIDPEWLEELAAHLIKRYSEPHWDKKRGRVV 610
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
72-626 1.12e-129

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: 412.62  E-value: 1.12e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784   72 VGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYSVIMLDEAHERT 151
Cdd:TIGR01967  114 IGHTQPRRLAARTVAQRIAEELGTPLGEKVGYKVRFHDQVSS-NTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERS 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  152 LYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFNQNEtsdpardtcvILTVEGRTFPVDIFY-----LQSPVP-D 225
Cdd:TIGR01967  193 LNIDFLLGYLKQLLPRRPDLKIIITSATIDPERFSRHFNNAP----------IIEVSGRTYPVEVRYrplveEQEDDDlD 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  226 YIKSTVETVVKIHQtEGDGDVLAFLTGQEEVEtvvsmliEQARALARTGMkRHLRVLPMYAGLPSFEQMKVFErvSRSVR 305
Cdd:TIGR01967  263 QLEAILDAVDELFA-EGPGDILIFLPGEREIR-------DAAEILRKRNL-RHTEILPLYARLSNKEQQRVFQ--PHSGR 331
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  306 KVIVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQ 385
Cdd:TIGR01967  332 RIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPE 411
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  386 STVPEMQRSNLAPVILQLKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKD---CRLTePLGMRIAEFPLNPMFA 462
Cdd:TIGR01967  412 FTDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDeaePQLT-PIGRQLAQLPVDPRLA 490
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  463 KMLLESGNFGCSQEILSIAAMMQIQNIFVVPPNQK-----SHA--HNKDS-------------------------KWCQE 510
Cdd:TIGR01967  491 RMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQqaadqAHArfKDPRSdflsrvnlwrhieeqrqalsanqfrNACRK 570
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  511 HFLNYKGLVRAATVREQLKKLLVKFQVPRKSSEGDPDLVLRCIVSGFFANAARFHSTGAYRTIRdDHELHIHPASVLyAE 590
Cdd:TIGR01967  571 QYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKALLSGLLSQIGMKDEKHEYDGAR-GRKFHIFPGSPL-FK 648
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 2217335784  591 KPPRWVIYNEVIQTSKYYMRDVTAIESAWLLELAPH 626
Cdd:TIGR01967  649 KPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAGH 684
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
53-626 1.24e-121

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 391.35  E-value: 1.24e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784   53 KLPvfKYLAEAGWTAEGrVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFddcTDQLA--TRIKFLTDGMLVREM 130
Cdd:PRK11131   105 QLP--KICLELGRGVKG-LIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRF---NDQVSdnTMVKLMTDGILLAEI 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  131 MVDPLLTKYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFNQNEtsdpardtcvILTVEGR 210
Cdd:PRK11131   179 QQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAP----------IIEVSGR 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  211 TFPVDIFYlqSPV--------PDYIKSTVETVVKIhQTEGDGDVLAFLTGQEEVEtvvsmliEQARALARTGMkRHLRVL 282
Cdd:PRK11131   249 TYPVEVRY--RPIveeaddteRDQLQAIFDAVDEL-GREGPGDILIFMSGEREIR-------DTADALNKLNL-RHTEIL 317
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  283 PMYAGLPSFEQMKVFErvSRSVRKVIVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGR 362
Cdd:PRK11131   318 PLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGR 395
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  363 GGRSRSGKCYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKDC 442
Cdd:PRK11131   396 CGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDE 475
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  443 -----RLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQN---------------------------IF 490
Cdd:PRK11131   476 qasayKLT-PLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDprerpmdkqqasdekhrrfadkesdflAF 554
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  491 V-----VPPNQKSHAHNKDSKWCQEHFLNYkglVRaatVRE------QLKKLLVKFQVPRKSSEGDPDLVLRCIVSGFFA 559
Cdd:PRK11131   555 VnlwnyLQEQQKALSSNQFRRLCRTDYLNY---LR---VREwqdiytQLRQVVKELGIPVNSEPAEYREIHTALLTGLLS 628
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217335784  560 -----NAARFHSTGAyrtiRDDHeLHIHPASVLYaEKPPRWVIYNEVIQTSKYYMRDVTAIESAWLLELAPH 626
Cdd:PRK11131   629 higmkDAEKQEYTGA----RNAR-FSIFPGSGLF-KKPPKWVMVAELVETSRLWGRIAARIEPEWIEPLAQH 694
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
58-207 4.03e-103

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: 310.94  E-value: 4.03e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  58 KYLAEAGWTAEGRVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQLATRIKFLTDGMLVREMMVDPLLT 137
Cdd:cd17980    36 QYLAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVGYCIRFDDCTDPQATRIKFLTDGMLVREMMLDPLLT 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 138 KYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFNQNETSDPARDTCVILTV 207
Cdd:cd17980   116 KYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDAEKFRDFFNQNETNDPSKDTATILSV 185
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
60-489 5.63e-88

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: 291.67  E-value: 5.63e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  60 LAEAGWTAEGRVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKY 139
Cdd:TIGR01970  36 LALLDAPGIGGKIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYRVRGENKVSR-RTRLEVVTEGILTRMIQDDPELDGV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 140 SVIMLDEAHERTLYTDIAIGLLKKIQKK-RGDLRLIVASATLDADKFRDFFNQnetsdpardtCVILTVEGRTFPVDIFY 218
Cdd:TIGR01970 115 GALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSATLDGERLSSLLPD----------APVVESEGRSFPVEIRY 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 219 LQSPVPDYIKSTVETVVKIHQTEGDGDVLAFLTGQEEVETVVSMLIEQARAlartgmkrHLRVLPMYAGLPSFEQMKVFE 298
Cdd:TIGR01970 185 LPLRGDQRLEDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQLAERLDS--------DVLICPLYGELSLAAQDRAIK 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 299 RVSRSVRKVIVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEE 378
Cdd:TIGR01970 257 PDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEE 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 379 AFDKLPQSTVPEMQRSNLAPVILQLKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKDCRLTEpLGMRIAEFPLN 458
Cdd:TIGR01970 337 QHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGRLTA-HGKAMAALGCH 415
                         410       420       430
                  ....*....|....*....|....*....|.
gi 2217335784 459 PMFAKMLLESGNFGCSQEILSIAAMMQIQNI 489
Cdd:TIGR01970 416 PRLAAMLLSAHSTGLAALACDLAALLEERGL 446
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
212-375 4.47e-76

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: 4.47e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 212 FPVDIFYLQSPV-----------PDYIKSTVETVVKIHQTEGDGDVLAFLTGQEEVETVVSMLieqaRALARTGMKRHLR 280
Cdd:cd18791     1 FPVEVYYLEDILellgissekedPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELL----REELLSPDLGKLL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 281 VLPMYAGLPSFEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRA 360
Cdd:cd18791    77 VLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRA 156
                         170
                  ....*....|....*
gi 2217335784 361 GRGGRSRSGKCYRLY 375
Cdd:cd18791   157 GRAGRTRPGKCYRLY 171
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
69-483 3.73e-73

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 251.38  E-value: 3.73e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  69 GRVVgVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYSVIMLDEAH 148
Cdd:PRK11664   49 GKII-MLEPRRLAARNVAQRLAEQLGEKPGETVGYRMRAESKVGP-NTRLEVVTEGILTRMIQRDPELSGVGLVILDEFH 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 149 ERTLYTDIAIGLLKKIQKK-RGDLRLIVASATLDADKFRDFFnqnetsdParDTCVILTvEGRTFPVDIFYLQSPVPDYI 227
Cdd:PRK11664  127 ERSLQADLALALLLDVQQGlRDDLKLLIMSATLDNDRLQQLL-------P--DAPVIVS-EGRSFPVERRYQPLPAHQRF 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 228 KSTVETVVKIHQTEGDGDVLAFLTGQEEVETVVSMLIEQaralartgMKRHLRVLPMYAGLPSFEQMKVFERVSRSVRKV 307
Cdd:PRK11664  197 DEAVARATAELLRQESGSLLLFLPGVGEIQRVQEQLASR--------VASDVLLCPLYGALSLAEQQKAILPAPAGRRKV 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 308 IVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQST 387
Cdd:PRK11664  269 VLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQS 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 388 VPEMQRSNLAPVILQLKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLE 467
Cdd:PRK11664  349 EPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQGRLT-ARGRKMAALGNDPRLAAMLVA 427
                         410
                  ....*....|....*.
gi 2217335784 468 SGNFgcSQEILSIAAM 483
Cdd:PRK11664  428 AKED--DEAALATAAK 441
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
58-191 9.13e-66

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: 213.09  E-value: 9.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  58 KYLAEAGWTAEGRV-VGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLL 136
Cdd:cd17917    20 QFLLEDGLAKGGKGrIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSS-KTRIKFCTDGILLRELLSDPLL 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217335784 137 TKYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFNQ 191
Cdd:cd17917    99 SGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGG 153
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
58-190 4.74e-64

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: 209.13  E-value: 4.74e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  58 KYLAEAGwTAEGRVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLT 137
Cdd:cd17978    36 QYLYEAG-FARGGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVGYSVRFDDVTSE-ETRIKYMTDGMLLREAIGDPLLS 113
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217335784 138 KYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGD-----LRLIVASATLDADKFRDFFN 190
Cdd:cd17978   114 KYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEqklspLKVIIMSATLDADLFSEYFN 171
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
49-189 6.26e-60

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: 198.48  E-value: 6.26e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  49 QQRQKLPVFK-------------------------------YLAEAGWTAEGRVvGVTQPRRVAAVTVAGRVAEERGAVL 97
Cdd:cd17971     1 EQRESLPIYKlkeqliqavhdnqilvvigetgsgkttqitqYLAEAGYTSRGKI-GCTQPRRVAAMSVAKRVAEEFGCCL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  98 GHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVAS 177
Cdd:cd17971    80 GQEVGYTIRFEDCTSP-ETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTS 158
                         170
                  ....*....|..
gi 2217335784 178 ATLDADKFRDFF 189
Cdd:cd17971   159 ATLDAVKFSQYF 170
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
58-191 2.80e-56

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: 188.48  E-value: 2.80e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  58 KYLAEAGWTAEGRVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLT 137
Cdd:cd17974    36 QYLHEAGYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGNEVGYSIRFEDCTSE-KTVLKYMTDGMLLREFLTEPDLA 114
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217335784 138 KYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFNQ 191
Cdd:cd17974   115 SYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAEKFSAFFDD 168
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
68-190 1.74e-55

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: 186.85  E-value: 1.74e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  68 EGRVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYSVIMLDEA 147
Cdd:cd17973    59 PKKLVACTQPRRVAAMSVAQRVAEEMDVKLGEEVGYSIRFEDCSSA-KTILKYMTDGMLLREAMSDPLLSRYSVIILDEA 137
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217335784 148 HERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFN 190
Cdd:cd17973   138 HERTLATDILMGLLKEVVRRRPDLKLIVMSATLDAGKFQKYFD 180
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
58-189 2.00e-52

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: 178.04  E-value: 2.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  58 KYLAEAGWTAEGrVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLT 137
Cdd:cd17983    36 QYLHEDGYTDYG-MIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGYAIRFEDCTSE-NTVIKYMTDGILLRESLRDPDLD 113
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217335784 138 KYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFF 189
Cdd:cd17983   114 KYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDADKFADFF 165
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
53-189 9.99e-47

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: 162.72  E-value: 9.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  53 KLPvfKYLAEAGWTAEGRVvGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMV 132
Cdd:cd17984    33 QLP--KYLYEAGFSQHGMI-GVTQPRRVAAISVAQRVAEEMKCTLGSKVGYQVRFDDCSSK-ETAIKYMTDGCLLRHILA 108
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217335784 133 DPLLTKYSVIMLDEAHERTLYTDIAIGLLKKI--QKKRG---DLRLIVASATLDADKFRDFF 189
Cdd:cd17984   109 DPNLTKYSVIILDEAHERSLTTDILFGLLKKLfqEKSPNrkeHLKVVVMSATLELAKLSAFF 170
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
53-187 1.30e-45

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: 160.21  E-value: 1.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  53 KLPVFKYlaEAGWTAE----GRVVGVTQPRRVAAVTVAGRVAEERGaVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVR 128
Cdd:cd17982    33 QVPQFLY--EAGFGSPesdnPGMIGITQPRRVAAVSMAKRVAEELN-VFGKEVSYQIRYDSTVSE-NTKIKFMTDGVLLK 108
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335784 129 EMMVDPLLTKYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGD----------LRLIVASATLDADKFRD 187
Cdd:cd17982   109 EIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvkpLKLVIMSATLRVEDFTE 177
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
53-190 4.37e-36

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: 133.35  E-value: 4.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  53 KLPvfKYLAEAGWTAEGrVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMV 132
Cdd:cd17989    33 QLP--KICLELGRGIRG-LIGHTQPRRLAARSVAERIAEELKTELGGAVGYKVRFTDQTSD-ETCVKLMTDGILLAETQT 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217335784 133 DPLLTKYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFN 190
Cdd:cd17989   109 DRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAERFSRHFN 166
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
56-191 4.04e-33

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: 124.86  E-value: 4.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  56 VFKYLAEAGWTAegrvVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDcTDQLATRIKFLTDGMLVREMMVDPL 135
Cdd:cd17979    34 VPQYLLAAGFRH----IACTQPRRIACISLAKRVAFESLNQYGSKVAYQIRFER-TRTLATKLLFLTEGLLLRQIQRDAS 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217335784 136 LTKYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFNQ 191
Cdd:cd17979   109 LPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIELFSGYFEG 164
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
60-185 5.61e-32

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: 122.06  E-value: 5.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  60 LAEAGWTAEGRVVgVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKY 139
Cdd:cd17990    38 LLAELWIAGGKII-VLEPRRVAARAAARRLATLLGEAPGETVGYRVRGESRVGR-RTRVEVVTEGVLLRRLQRDPELSGV 115
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2217335784 140 SVIMLDEAHERTLYTDIAIGLLKKIQK-KRGDLRLIVASATLDADKF 185
Cdd:cd17990   116 GAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSATLDGDGL 162
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
62-190 7.14e-30

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: 116.10  E-value: 7.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  62 EAGWTAEGRVVgVTQPRRVAAVTVAGRVAEERG--AVLGHEVGYCIRFDDCTDQLATRIKFLTDGMLVREMMVDPLLTKY 139
Cdd:cd17981    44 ERGKGSSCRIV-CTQPRRISAISVAERVAAERAesCGLGNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNV 122
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217335784 140 SVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFN 190
Cdd:cd17981   123 SHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMSATLNAEKFSDYFN 173
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
71-178 3.73e-28

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: 111.07  E-value: 3.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  71 VVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYSVIMLDEAHER 150
Cdd:cd17977    51 VVVCTQVHKQTAVWLALRVADEMDVNIGHEVGYVIPFENCCTN-ETILRYCTDDMLLREMMSDPLLESYGVIILDDAHER 129
                          90       100
                  ....*....|....*....|....*...
gi 2217335784 151 TLYTDIAIGLLKKIQKKRGDLRLIVASA 178
Cdd:cd17977   130 TVSTDVLLGLLKDVLLSRPELKLVIITC 157
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
75-190 2.21e-27

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: 109.16  E-value: 2.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  75 TQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYSVIMLDEAHERTLYT 154
Cdd:cd17985    56 TQPRRISAISVAERVAQERAERVGQSVGYQIRLESVKSS-ATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEES 134
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217335784 155 DIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFN 190
Cdd:cd17985   135 DFLLLVLKDLMVQRPDLKVILMSATLNAELFSDYFN 170
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
60-191 2.30e-27

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: 109.23  E-value: 2.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  60 LAEAGWTAEGRVVGVTQPRRVAAVTVAGRVAEERGAVLG-----HEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDP 134
Cdd:cd17975    42 LLLNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESGpggknSLCGYQIRMESRTGE-ATRLLYCTTGVLLRKLQEDG 120
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217335784 135 LLTKYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFNQ 191
Cdd:cd17975   121 LLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLILMSATVDCEKFSSYFTH 177
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
72-188 7.28e-27

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: 107.68  E-value: 7.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  72 VGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMVDPLLTKYSVIMLDEAHERT 151
Cdd:cd17986    53 VTVTQPHPLAARSLALRVADEMDLNLGHEVGYSIPQEDCTGP-NTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERS 131
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2217335784 152 LYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDF 188
Cdd:cd17986   132 VASDSLLGLLKDVRLQRPELRVVVVTSPALEPKLRAF 168
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
428-512 1.13e-24

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: 98.85  E-value: 1.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 428 ALELLYALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFvVPPNQKSHAHNKDSKW 507
Cdd:pfam04408   1 ALELLYYLGALDEDGELT-PLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPF-VQPNFLDPRSAAKAAR 78

                  ....*
gi 2217335784 508 CQEHF 512
Cdd:pfam04408  79 RRRRA 83
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
72-189 4.52e-23

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: 96.79  E-value: 4.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  72 VGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQLATRIKFLTDGMLVREMMVDPLLTKYSVIMLDEAHERT 151
Cdd:cd17976    53 VVITQPRRISAVSVAQRVAHELGPNLRRNVGYQVRLESRPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERD 132
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2217335784 152 LYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFF 189
Cdd:cd17976   133 VNTDFLLILLKGVLQLNPELRVVLMSATGDNQRLSRYF 170
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
75-190 7.32e-23

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: 96.05  E-value: 7.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  75 TQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQlATRIKFLTDGMLVREMMV-DPLLTKYSVIMLDEAHERTLY 153
Cdd:cd17987    54 TQPRRLAAIAVAERVAAERGEKIGQTVGYQIRLESRVSP-KTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRF 132
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2217335784 154 TDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFN 190
Cdd:cd17987   133 SDFLLTKLRDILQKHPNLKLILSSAALDVNLFIRYFG 169
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
7-189 8.03e-23

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: 97.60  E-value: 8.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784   7 PVKFWRPGT-----EGPGVSISEERQSLA-ENSGTTVVYNPYAALSIEQQRQKLPVFKYLAEAGWT-AEGRVV------- 72
Cdd:cd17972     6 PQSNWNPWTssnidEGPLAFATPEQISMDlKNELMYQREQDHNLQQILQERELLPVKKFREEILEAiSNNPVViirgatg 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  73 --------------------------GVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQLATRIKFLTDGML 126
Cdd:cd17972    86 cgkttqvpqyilddfiqndraaecniVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRPHASILFCTVGVL 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217335784 127 VREMmvDPLLTKYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFF 189
Cdd:cd17972   166 LRKL--EAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYF 226
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
549-626 1.33e-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: 89.23  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 549 VLRCIVSGFFANAARF-HSTGAYRTIRDDHELHIHPASVLY--AEKPPRWVIYNEVIQTSKYYMRDVTAIESAWLLELAP 625
Cdd:pfam07717   1 LRAALAAGLYPNVARRdPKGKGYTTLSDNQRVFIHPSSVLFneKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80

                  .
gi 2217335784 626 H 626
Cdd:pfam07717  81 H 81
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
74-189 4.74e-18

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: 82.16  E-value: 4.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  74 VTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDcTDQLATRIKFLTDGMLVREMMVDPLLTKYSVIMLDEAHERTLY 153
Cdd:cd17988    53 VTQPRRIAAISIARRVSQEREWTLGSLVGYQVGLER-PASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQE 131
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2217335784 154 TDIAIGLLKK-IQKKRGDLRLIVASATLDADKFRDFF 189
Cdd:cd17988   132 LDFLLLVVRRlLRTNSRHVKIILMSATISCKEFADYF 168
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
434-510 8.42e-18

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: 78.46  E-value: 8.42e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217335784  434 ALGGLDKDCRLTePLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFvvPPNQKSHAHNKDSKWCQE 510
Cdd:smart00847   1 ELGALDDDGRLT-PLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADP 74
HELICc smart00490
helicase superfamily c-terminal domain;
270-365 4.82e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 67.62  E-value: 4.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784  270 LARTGMKRHLRVLPMYAGLPSFEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDCGFvklraynprtaieclvvv 349
Cdd:smart00490   3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL------------------ 64
                           90
                   ....*....|....*.
gi 2217335784  350 PVSQASANQRAGRGGR 365
Cdd:smart00490  65 PWSPASYIQRIGRAGR 80
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
231-365 8.18e-13

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: 64.92  E-value: 8.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 231 VETVVKIHQTEGDGDVLAFLTGQEEVETvvSMLIEqaralartgmKRHLRVLPMYAGLPSFEQMKVFERVSRSVRKVIVA 310
Cdd:pfam00271   3 LEALLELLKKERGGKVLIFSQTKKTLEA--ELLLE----------KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVA 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217335784 311 TNVAETSITISGIVYVIDCGFVklraYNPRTAIeclvvvpvsqasanQRAGRGGR 365
Cdd:pfam00271  71 TDVAERGLDLPDVDLVINYDLP----WNPASYI--------------QRIGRAGR 107
DEXDc smart00487
DEAD-like helicases superfamily;
59-193 6.19e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 56.35  E-value: 6.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784   59 YLAEAGWTAEGRVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYcIRFDDCTDQLA------TRIKFLTDGMLVREMMV 132
Cdd:smart00487  44 PALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGL-YGGDSKREQLRklesgkTDILVTTPGRLLDLLEN 122
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217335784  133 DPL-LTKYSVIMLDEAHERT--LYTDIAIGLLKKIQKKRgdlRLIVASATL--DADKFRDFFNQNE 193
Cdd:smart00487 123 DKLsLSNVDLVILDEAHRLLdgGFGDQLEKLLKLLPKNV---QLLLLSATPpeEIENLLELFLNDP 185
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
136-376 1.65e-08

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 57.68  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 136 LTKYSVIMLDEAHERTLYTDIAIGLLKkiqKKRGDLR-LIVASATL--DADKFRDFFNqnetsDPArdtcvILTVEGRT- 211
Cdd:PHA02653  289 LFDYGTVIIDEVHEHDQIGDIIIAVAR---KHIDKIRsLFLMTATLedDRDRIKEFFP-----NPA-----FVHIPGGTl 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 212 FPVDIFYL---QSPvPDYIKSTVETVVKIHQTEGDGDVLAFLTGQEEVETvVSMLIEQARALArtgmKRH--LRVLPMYA 286
Cdd:PHA02653  356 FPISEVYVknkYNP-KNKRAYIEEEKKNIVTALKKYTPPKGSSGIVFVAS-VSQCEEYKKYLE----KRLpiYDFYIIHG 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 287 GLPSFEQM--KVF--ERVSrsvrkVIVATNVAETSITISGIVYVIDCGfvklRAYNPRtaieclvvvP-------VSQAS 355
Cdd:PHA02653  430 KVPNIDEIleKVYssKNPS-----IIISTPYLESSVTIRNATHVYDTG----RVYVPE---------PfggkemfISKSM 491
                         250       260
                  ....*....|....*....|.
gi 2217335784 356 ANQRAGRGGRSRSGKCYRLYT 376
Cdd:PHA02653  492 RTQRKGRVGRVSPGTYVYFYD 512
PRK13766 PRK13766
Hef nuclease; Provisional
230-380 2.28e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 44.48  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 230 TVETVVKIHQTEGDGDVLAFLTGQEEVETVVSMLIE----------QARALARTGMKRHlrvlpmyaglpsfEQMKVFER 299
Cdd:PRK13766  352 LREIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKegikavrfvgQASKDGDKGMSQK-------------EQIEILDK 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 300 VSRSVRKVIVATNVAETSITISGIVYVIdcgFvklraYNPrtaieclvvVPvSQASANQRAGRGGRSRSGKCYRLYTE-- 377
Cdd:PRK13766  419 FRAGEFNVLVSTSVAEEGLDIPSVDLVI---F-----YEP---------VP-SEIRSIQRKGRTGRQEEGRVVVLIAKgt 480

                  ....*
gi 2217335784 378 --EAF 380
Cdd:PRK13766  481 rdEAY 485
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
298-375 7.68e-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: 38.45  E-value: 7.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 298 ERVSRSVrKVIVATNVAETSITISGIVYVIDCGFVKlraynprtaieclvvvpvSQASANQRAGRGGR--SRSGKCYRLY 375
Cdd:cd18785    17 EEIASSL-EILVATNVLGEGIDVPSLDTVIFFDPPS------------------SAASYIQRVGRAGRggKDEGEVILFV 77
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
221-374 8.44e-03

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 37.34  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 221 SPVPDYIKSTVETVVKIHQTEGDGDVLAFLTGQEEVETVVSML------------IEQARALARTGMKRHlrvlpmyagl 288
Cdd:cd18801     8 HPKLEKLEEIVKEHFKKKQEGSDTRVIIFSEFRDSAEEIVNFLskirpgiratrfIGQASGKSSKGMSQK---------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335784 289 psfEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIdCgfvklraYNPrtaieclVVVPVSQAsanQRAGRGGRSRS 368
Cdd:cd18801    78 ---EQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLII-C-------YDA-------SPSPIRMI---QRMGRTGRKRQ 136

                  ....*.
gi 2217335784 369 GKCYRL 374
Cdd:cd18801   137 GRVVVL 142
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH