NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18396548|ref|NP_564296|]
View 

RNA helicase family protein [Arabidopsis thaliana]

Protein Classification

ATP-dependent RNA helicase( domain architecture ID 13388279)

DEAD/DEAH box containing ATP-dependent RNA helicase catalyzes the unwinding of RNA, similar to DEAH box protein 34 (DHX34) that is required for nonsense-mediated decay (NMD) degradation of mRNA transcripts containing premature stop codons

CATH:  3.40.50.300
EC:  3.6.4.13
Gene Ontology:  GO:0005524|GO:0003724|GO:0003676|GO:0016887|GO:0003723
PubMed:  34680866|19747077|22922795|20206133|21779027|20225155

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];
1-456 2.21e-171

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: 511.55  E-value: 2.21e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   1 MANLPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGED 80
Cdd:COG1643   7 PPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGET 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  81 VGYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASNFKVLITSATL 160
Cdd:COG1643  87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPALRPDLKLLVMSATL 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 161 DGEKVSEFFSGCPVLNVPGKLYPVEILY-SKERPVSYIESSLKVAIDIHVREPEGDILIFMTGQDDIEKLVSRLEEKVRS 239
Cdd:COG1643 167 DAERFARLLGDAPVIESSGRTYPVEVRYrPLPADERDLEDAVADAVREALAEEPGDILVFLPGEREIRRTAEALRGRLPP 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 240 laegscmDAIIYPLHGSLPPEMQVRVFSPPPPNCRRFIVSTNIAETSLTVDGVVYVIDSGYVKQRQYNPSSGMFSLDVIQ 319
Cdd:COG1643 247 -------DTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTER 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 320 ISKVQANQRAGRAGRTRPGKCYRLYPlavyRDDFL---DATIPEIQRTSLAGSVLYLKSLDLPDIDilKFDFLDAPSSES 396
Cdd:COG1643 320 ISQASANQRAGRAGRLAPGICYRLWS----EEDFArrpAFTDPEILRADLASLILELAAWGLGDPE--DLPFLDPPPARA 393

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 397 LEDALKQLYFIDAIDENGAITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLS 456
Cdd:COG1643 394 IADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLS 453
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 560-643 5.34e-24

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: 96.17  E-value: 5.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   560 LRKALCVGNANQIAERMLRHNGYRTLSfQSQLVQVHPSSVLsADNDGMMPNYVVYHELISTTRPFMRNVCAVDMAWVAPI 639
Cdd:pfam07717   1 LRAALAAGLYPNVARRDPKGKGYTTLS-DNQRVFIHPSSVL-FNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLF 78


                  ....
gi 18396548   640 KRKI 643
Cdd:pfam07717  79 APHI 82
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
1-456 2.21e-171

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 511.55  E-value: 2.21e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   1 MANLPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGED 80
Cdd:COG1643   7 PPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGET 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  81 VGYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASNFKVLITSATL 160
Cdd:COG1643  87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPALRPDLKLLVMSATL 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 161 DGEKVSEFFSGCPVLNVPGKLYPVEILY-SKERPVSYIESSLKVAIDIHVREPEGDILIFMTGQDDIEKLVSRLEEKVRS 239
Cdd:COG1643 167 DAERFARLLGDAPVIESSGRTYPVEVRYrPLPADERDLEDAVADAVREALAEEPGDILVFLPGEREIRRTAEALRGRLPP 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 240 laegscmDAIIYPLHGSLPPEMQVRVFSPPPPNCRRFIVSTNIAETSLTVDGVVYVIDSGYVKQRQYNPSSGMFSLDVIQ 319
Cdd:COG1643 247 -------DTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTER 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 320 ISKVQANQRAGRAGRTRPGKCYRLYPlavyRDDFL---DATIPEIQRTSLAGSVLYLKSLDLPDIDilKFDFLDAPSSES 396
Cdd:COG1643 320 ISQASANQRAGRAGRLAPGICYRLWS----EEDFArrpAFTDPEILRADLASLILELAAWGLGDPE--DLPFLDPPPARA 393

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 397 LEDALKQLYFIDAIDENGAITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLS 456
Cdd:COG1643 394 IADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLS 453
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
 3-639 5.47e-130

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: 415.32  E-value: 5.47e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548      3 NLPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVG 82
Cdd:TIGR01967   65 NLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKVG 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548     83 YAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRiRASNFKVLITSATLDG 162
Cdd:TIGR01967  145 YKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLP-RRPDLKIIITSATIDP 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    163 EKVSEFFSGCPVLNVPGKLYPVEILYskeRPVSYIE--------SSLKVAIDIHVREPEGDILIFMTGQDDIEKLVSRLE 234
Cdd:TIGR01967  224 ERFSRHFNNAPIIEVSGRTYPVEVRY---RPLVEEQedddldqlEAILDAVDELFAEGPGDILIFLPGEREIRDAAEILR 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    235 EkvRSLAegscmDAIIYPLHGSLPPEMQVRVFSPPppNCRRFIVSTNIAETSLTVDGVVYVIDSGYVKQRQYNPSSGMFS 314
Cdd:TIGR01967  301 K--RNLR-----HTEILPLYARLSNKEQQRVFQPH--SGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQR 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    315 LDVIQISKVQANQRAGRAGRTRPGKCYRLYPlavyRDDFLDA---TIPEIQRTSLAGSVLYLKSLDLPDIDilKFDFLDA 391
Cdd:TIGR01967  372 LPIEPISQASANQRKGRCGRVAPGICIRLYS----EEDFNSRpefTDPEILRTNLASVILQMLALRLGDIA--AFPFIEA 445

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    392 PSSESLEDALKQLYFIDAIDENGA---ITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLSAETtllpARSKP 468
Cdd:TIGR01967  446 PDPRAIRDGFRLLEELGALDDDEAepqLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQD----PRERP 521

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    469 SEKK--------RKHDEDSnlpngsgygDHIQLLQIF----ESWDRTNYDPV--WCKE---NGMQVRGMvfvKDVRRQLC 531
Cdd:TIGR01967  522 MEKQqaadqahaRFKDPRS---------DFLSRVNLWrhieEQRQALSANQFrnACRKqylNYLRVREW---QDIYRQLT 589

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    532 QIMQKISKDRLEVGAdgrksssrdDYRKLRKALCVGNANQIAERMLRHN--GYRTLSFqsqlvQVHPSSVLSadndGMMP 609
Cdd:TIGR01967  590 QVVKELGLKLNEEPA---------DYDAIHKALLSGLLSQIGMKDEKHEydGARGRKF-----HIFPGSPLF----KKPP 651

                          650       660       670
                   ....*....|....*....|....*....|
gi 18396548    610 NYVVYHELISTTRPFMRNVCAVDMAWVAPI 639
Cdd:TIGR01967  652 KWVMAAELVETSKLYARLVAKIEPEWVEPV 681
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 3-641 9.15e-118

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 382.49  E-value: 9.15e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548     3 NLPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVG 82
Cdd:PRK11131   72 NLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCVG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    83 YAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRaSNFKVLITSATLDG 162
Cdd:PRK11131  152 YKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRR-PDLKVIITSATIDP 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   163 EKVSEFFSGCPVLNVPGKLYPVEILYskeRPVSYIESSLKV--------AIDIHVREPEGDILIFMTGQDDIEKLVSRLE 234
Cdd:PRK11131  231 ERFSRHFNNAPIIEVSGRTYPVEVRY---RPIVEEADDTERdqlqaifdAVDELGREGPGDILIFMSGEREIRDTADALN 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   235 EkvRSLAegscmDAIIYPLHGSLPPEMQVRVFSppPPNCRRFIVSTNIAETSLTVDGVVYVIDSGYVKQRQYNPSSGMFS 314
Cdd:PRK11131  308 K--LNLR-----HTEILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQR 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   315 LDVIQISKVQANQRAGRAGRTRPGKCYRLYPlavyRDDFL---DATIPEIQRTSLAGSVLYLKSLDLPDIDilKFDFLDA 391
Cdd:PRK11131  379 LPIEPISQASANQRKGRCGRVSEGICIRLYS----EDDFLsrpEFTDPEILRTNLASVILQMTALGLGDIA--AFPFVEA 452

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   392 PSSESLEDALKQLYFIDAIDENGA-----ITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLSAETtllpARS 466
Cdd:PRK11131  453 PDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQD----PRE 528

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   467 KPSEKKR----KH----DEDSNLPNGSGYGDHIQLLQ------IFESWDRTNYdpvwckENGMQVRGMvfvKDVRRQLCQ 532
Cdd:PRK11131  529 RPMDKQQasdeKHrrfaDKESDFLAFVNLWNYLQEQQkalssnQFRRLCRTDY------LNYLRVREW---QDIYTQLRQ 599

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   533 IMQKISkdrLEVgadgrkSSSRDDYRKLRKALCVGNANQI----AERMlRHNGYRTLSFqsqlvQVHPSSVLSADNdgmm 608
Cdd:PRK11131  600 VVKELG---IPV------NSEPAEYREIHTALLTGLLSHIgmkdAEKQ-EYTGARNARF-----SIFPGSGLFKKP---- 660

                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 18396548   609 PNYVVYHELISTTRPFMRNVCAVDMAWVAP-----IKR 641
Cdd:PRK11131  661 PKWVMVAELVETSRLWGRIAARIEPEWIEPlaqhlIKR 698
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 4-177 1.36e-84

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: 264.22  E-value: 1.36e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVGY 83
Cdd:cd17978   1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  84 AIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRA----SNFKVLITSAT 159
Cdd:cd17978  81 SVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKeqklSPLKVIIMSAT 160

                       170
                ....*....|....*...
gi 18396548 160 LDGEKVSEFFSGCPVLNV 177
Cdd:cd17978 161 LDADLFSEYFNGAPVLYI 178
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 400-493 2.56e-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: 97.69  E-value: 2.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   400 ALKQLYFIDAIDENGAITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLSAETTLLP----------ARSKPS 469
Cdd:pfam04408   1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQpnfldprsaaKAARRR 80

                          90       100
                  ....*....|....*....|....
gi 18396548   470 EKKRKHDEDSNLPNGSGYGDHIQL 493
Cdd:pfam04408  81 RRAADEKARAKFARLDLEGDHLTL 104
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 560-643 5.34e-24

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: 96.17  E-value: 5.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   560 LRKALCVGNANQIAERMLRHNGYRTLSfQSQLVQVHPSSVLsADNDGMMPNYVVYHELISTTRPFMRNVCAVDMAWVAPI 639
Cdd:pfam07717   1 LRAALAAGLYPNVARRDPKGKGYTTLS-DNQRVFIHPSSVL-FNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLF 78


                  ....
gi 18396548   640 KRKI 643
Cdd:pfam07717  79 APHI 82
DEXDc smart00487
DEAD-like helicases superfamily;
17-186 1.37e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 93.33  E-value: 1.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548     17 VEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIA-ITQPRRVAAVSVARRVAQELDVPLGEDVGY------AIRFED 89
Cdd:smart00487  21 LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVlVLVPTRELAEQWAEELKKLGPSLGLKVVGLyggdskREQLRK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548     90 RTTSKTRIKYLTDGVLLRESLSNPM-LDDYSVIILDEAHERS--LNTDILLGLVKRLvrirASNFKVLITSATL--DGEK 164
Cdd:smart00487 101 LESGKTDILVTTPGRLLDLLENDKLsLSNVDLVILDEAHRLLdgGFGDQLEKLLKLL----PKNVQLLLLSATPpeEIEN 176

                          170       180
                   ....*....|....*....|..
gi 18396548    165 VSEFFSGCPVLNVPGKLYPVEI 186
Cdd:smart00487 177 LLELFLNDPVFIDVGFTPLEPI 198
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
1-456 2.21e-171

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 511.55  E-value: 2.21e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   1 MANLPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGED 80
Cdd:COG1643   7 PPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGET 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  81 VGYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASNFKVLITSATL 160
Cdd:COG1643  87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPALRPDLKLLVMSATL 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 161 DGEKVSEFFSGCPVLNVPGKLYPVEILY-SKERPVSYIESSLKVAIDIHVREPEGDILIFMTGQDDIEKLVSRLEEKVRS 239
Cdd:COG1643 167 DAERFARLLGDAPVIESSGRTYPVEVRYrPLPADERDLEDAVADAVREALAEEPGDILVFLPGEREIRRTAEALRGRLPP 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 240 laegscmDAIIYPLHGSLPPEMQVRVFSPPPPNCRRFIVSTNIAETSLTVDGVVYVIDSGYVKQRQYNPSSGMFSLDVIQ 319
Cdd:COG1643 247 -------DTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTER 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 320 ISKVQANQRAGRAGRTRPGKCYRLYPlavyRDDFL---DATIPEIQRTSLAGSVLYLKSLDLPDIDilKFDFLDAPSSES 396
Cdd:COG1643 320 ISQASANQRAGRAGRLAPGICYRLWS----EEDFArrpAFTDPEILRADLASLILELAAWGLGDPE--DLPFLDPPPARA 393

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 397 LEDALKQLYFIDAIDENGAITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLS 456
Cdd:COG1643 394 IADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLS 453
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
 3-639 5.47e-130

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: 415.32  E-value: 5.47e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548      3 NLPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVG 82
Cdd:TIGR01967   65 NLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKVG 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548     83 YAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRiRASNFKVLITSATLDG 162
Cdd:TIGR01967  145 YKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLP-RRPDLKIIITSATIDP 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    163 EKVSEFFSGCPVLNVPGKLYPVEILYskeRPVSYIE--------SSLKVAIDIHVREPEGDILIFMTGQDDIEKLVSRLE 234
Cdd:TIGR01967  224 ERFSRHFNNAPIIEVSGRTYPVEVRY---RPLVEEQedddldqlEAILDAVDELFAEGPGDILIFLPGEREIRDAAEILR 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    235 EkvRSLAegscmDAIIYPLHGSLPPEMQVRVFSPPppNCRRFIVSTNIAETSLTVDGVVYVIDSGYVKQRQYNPSSGMFS 314
Cdd:TIGR01967  301 K--RNLR-----HTEILPLYARLSNKEQQRVFQPH--SGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQR 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    315 LDVIQISKVQANQRAGRAGRTRPGKCYRLYPlavyRDDFLDA---TIPEIQRTSLAGSVLYLKSLDLPDIDilKFDFLDA 391
Cdd:TIGR01967  372 LPIEPISQASANQRKGRCGRVAPGICIRLYS----EEDFNSRpefTDPEILRTNLASVILQMLALRLGDIA--AFPFIEA 445

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    392 PSSESLEDALKQLYFIDAIDENGA---ITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLSAETtllpARSKP 468
Cdd:TIGR01967  446 PDPRAIRDGFRLLEELGALDDDEAepqLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQD----PRERP 521

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    469 SEKK--------RKHDEDSnlpngsgygDHIQLLQIF----ESWDRTNYDPV--WCKE---NGMQVRGMvfvKDVRRQLC 531
Cdd:TIGR01967  522 MEKQqaadqahaRFKDPRS---------DFLSRVNLWrhieEQRQALSANQFrnACRKqylNYLRVREW---QDIYRQLT 589

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    532 QIMQKISKDRLEVGAdgrksssrdDYRKLRKALCVGNANQIAERMLRHN--GYRTLSFqsqlvQVHPSSVLSadndGMMP 609
Cdd:TIGR01967  590 QVVKELGLKLNEEPA---------DYDAIHKALLSGLLSQIGMKDEKHEydGARGRKF-----HIFPGSPLF----KKPP 651

                          650       660       670
                   ....*....|....*....|....*....|
gi 18396548    610 NYVVYHELISTTRPFMRNVCAVDMAWVAPI 639
Cdd:TIGR01967  652 KWVMAAELVETSKLYARLVAKIEPEWVEPV 681
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 3-641 9.15e-118

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 382.49  E-value: 9.15e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548     3 NLPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVG 82
Cdd:PRK11131   72 NLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCVG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    83 YAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRaSNFKVLITSATLDG 162
Cdd:PRK11131  152 YKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRR-PDLKVIITSATIDP 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   163 EKVSEFFSGCPVLNVPGKLYPVEILYskeRPVSYIESSLKV--------AIDIHVREPEGDILIFMTGQDDIEKLVSRLE 234
Cdd:PRK11131  231 ERFSRHFNNAPIIEVSGRTYPVEVRY---RPIVEEADDTERdqlqaifdAVDELGREGPGDILIFMSGEREIRDTADALN 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   235 EkvRSLAegscmDAIIYPLHGSLPPEMQVRVFSppPPNCRRFIVSTNIAETSLTVDGVVYVIDSGYVKQRQYNPSSGMFS 314
Cdd:PRK11131  308 K--LNLR-----HTEILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQR 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   315 LDVIQISKVQANQRAGRAGRTRPGKCYRLYPlavyRDDFL---DATIPEIQRTSLAGSVLYLKSLDLPDIDilKFDFLDA 391
Cdd:PRK11131  379 LPIEPISQASANQRKGRCGRVSEGICIRLYS----EDDFLsrpEFTDPEILRTNLASVILQMTALGLGDIA--AFPFVEA 452

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   392 PSSESLEDALKQLYFIDAIDENGA-----ITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLSAETtllpARS 466
Cdd:PRK11131  453 PDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQD----PRE 528

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   467 KPSEKKR----KH----DEDSNLPNGSGYGDHIQLLQ------IFESWDRTNYdpvwckENGMQVRGMvfvKDVRRQLCQ 532
Cdd:PRK11131  529 RPMDKQQasdeKHrrfaDKESDFLAFVNLWNYLQEQQkalssnQFRRLCRTDY------LNYLRVREW---QDIYTQLRQ 599

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   533 IMQKISkdrLEVgadgrkSSSRDDYRKLRKALCVGNANQI----AERMlRHNGYRTLSFqsqlvQVHPSSVLSADNdgmm 608
Cdd:PRK11131  600 VVKELG---IPV------NSEPAEYREIHTALLTGLLSHIgmkdAEKQ-EYTGARNARF-----SIFPGSGLFKKP---- 660

                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 18396548   609 PNYVVYHELISTTRPFMRNVCAVDMAWVAP-----IKR 641
Cdd:PRK11131  661 PKWVMVAELVETSRLWGRIAARIEPEWIEPlaqhlIKR 698
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 4-457 1.94e-101

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: 329.03  E-value: 1.94e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548     4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLS-QILHRHGYtkSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVG 82
Cdd:TIGR01970   1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPlALLDAPGI--GGKIIMLEPRRLAARSAAQRLASQLGEAVGQTVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    83 YAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGL---VKRLVRiraSNFKVLITSAT 159
Cdd:TIGR01970  79 YRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALaldVQSSLR---EDLKILAMSAT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   160 LDGEKVSEFFSGCPVLNVPGKLYPVEILYSKERPVSYIESSLKVAIDIHVREPEGDILIFMTGQDDIEKLVSRLEEKVRS 239
Cdd:TIGR01970 156 LDGERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQLAERLDS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   240 laegscmDAIIYPLHGSLPPEMQVRVFSPPPPNCRRFIVSTNIAETSLTVDGVVYVIDSGYVKQRQYNPSSGMFSLDVIQ 319
Cdd:TIGR01970 236 -------DVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVR 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   320 ISKVQANQRAGRAGRTRPGKCYRLYPLAVYRdDFLDATIPEIQRTSLAGSVLYLKSLDLPDIDILKfdFLDAPSSESLED 399
Cdd:TIGR01970 309 ISQASATQRAGRAGRLEPGVCYRLWSEEQHQ-RLPAQDEPEILQADLSGLALELAQWGAKDPSDLR--WLDAPPSVALAA 385

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18396548   400 ALKQLYFIDAIDENGAITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLSA 457
Cdd:TIGR01970 386 ARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALLEE 443
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 4-177 1.36e-84

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: 264.22  E-value: 1.36e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVGY 83
Cdd:cd17978   1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  84 AIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRA----SNFKVLITSAT 159
Cdd:cd17978  81 SVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKeqklSPLKVIIMSAT 160

                       170
                ....*....|....*...
gi 18396548 160 LDGEKVSEFFSGCPVLNV 177
Cdd:cd17978 161 LDADLFSEYFNGAPVLYI 178
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 20-177 9.34e-84

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: 261.24  E-value: 9.34e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  20 NSVVVIIGETGSGKSTQLSQILHRHGYTK--SGVIAITQPRRVAAVSVARRVAQELDVPLGEDVGYAIRFEDRTTSKTRI 97
Cdd:cd17917   1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKggKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  98 KYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRaSNFKVLITSATLDGEKVSEFFSGCPVLNV 177
Cdd:cd17917  81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKR-PDLKVILMSATLDAEKFSSYFGGAPVIHI 159
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 1-466 3.18e-81

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 274.88  E-value: 3.18e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    1 MANLPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLS-QILHRHGYTksGVIAITQPRRVAAVSVARRVAQELDVPLGE 79
Cdd:PRK11664   1 MSSLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGIN--GKIIMLEPRRLAARNVAQRLAEQLGEKPGE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   80 DVGYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGL---VKRLVRiraSNFKVLIT 156
Cdd:PRK11664  79 TVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALlldVQQGLR---DDLKLLIM 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  157 SATLDGEKVSEFFSGCPVLNVPGKLYPVEILYSKERPVSYIESSLKVAIDIHVREPEGDILIFMTGQDDIEKLVSRLEEK 236
Cdd:PRK11664 156 SATLDNDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRFDEAVARATAELLRQESGSLLLFLPGVGEIQRVQEQLASR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  237 VRSlaegscmDAIIYPLHGSLPPEMQVRVFSPPPPNCRRFIVSTNIAETSLTVDGVVYVIDSGYVKQRQYNPSSGMFSLD 316
Cdd:PRK11664 236 VAS-------DVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLV 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  317 VIQISKVQANQRAGRAGRTRPGKCYRLYP------LAVYRDdfldatiPEIQRTSLAGSVLYLKSLDLPDIDILKfdFLD 390
Cdd:PRK11664 309 TQRISQASMTQRAGRAGRLEPGICLHLYSkeqaerAAAQSE-------PEILHSDLSGLLLELLQWGCHDPAQLS--WLD 379

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18396548  391 APSSESLEDALKQLYFIDAIDENGAITRIGRTMSDLPLEPSLSRTLIEANETGclSQALTVVAMLSAettLL--PARS 466
Cdd:PRK11664 380 QPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKEDD--EAALATAAKLAA---ILeePPRS 452
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
 4-177 1.10e-78

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: 248.53  E-value: 1.10e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVGY 83
Cdd:cd17983   1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  84 AIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRiRASNFKVLITSATLDGE 163
Cdd:cd17983  81 AIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVA-RRRDLKLIVTSATMDAD 159

                       170
                ....*....|....
gi 18396548 164 KVSEFFSGCPVLNV 177
Cdd:cd17983 160 KFADFFGNVPIFTI 173
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 182-344 2.79e-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: 242.05  E-value: 2.79e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 182 YPVEILYSKE-----------RPVSYIESSLKVAIDIHVREPEGDILIFMTGQDDIEKLVSRLEEKVRSlaeGSCMDAII 250
Cdd:cd18791   1 FPVEVYYLEDilellgissekEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLS---PDLGKLLV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 251 YPLHGSLPPEMQVRVFSPPPPNCRRFIVSTNIAETSLTVDGVVYVIDSGYVKQRQYNPSSGMFSLDVIQISKVQANQRAG 330
Cdd:cd18791  78 LPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAG 157

                       170
                ....*....|....
gi 18396548 331 RAGRTRPGKCYRLY 344
Cdd:cd18791 158 RAGRTRPGKCYRLY 171
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
 4-178 5.60e-73

DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350729 [Multi-domain]  Cd Length: 179  Bit Score: 233.91  E-value: 5.60e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVGY 83
Cdd:cd17971   6 LPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLGQEVGY 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  84 AIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRaSNFKVLITSATLDGE 163
Cdd:cd17971  86 TIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKR-PDLKLIVTSATLDAV 164

                       170
                ....*....|....*
gi 18396548 164 KVSEFFSGCPVLNVP 178
Cdd:cd17971 165 KFSQYFYEAPIFTIP 179
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 4-177 1.52e-72

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: 232.78  E-value: 1.52e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGV-IAITQPRRVAAVSVARRVAQELDVPLGEDVG 82
Cdd:cd17974   1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGkIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  83 YAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRaSNFKVLITSATLDG 162
Cdd:cd17974  81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFR-PDLKLLISSATMDA 159

                       170
                ....*....|....*
gi 18396548 163 EKVSEFFSGCPVLNV 177
Cdd:cd17974 160 EKFSAFFDDAPIFRI 174
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
 4-177 3.27e-72

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: 232.31  E-value: 3.27e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSG--VIAITQPRRVAAVSVARRVAQELDVPLGEDV 81
Cdd:cd17973  13 LPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPkkLVACTQPRRVAAMSVAQRVAEEMDVKLGEEV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  82 GYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRaSNFKVLITSATLD 161
Cdd:cd17973  93 GYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRR-PDLKLIVMSATLD 171

                       170
                ....*....|....*.
gi 18396548 162 GEKVSEFFSGCPVLNV 177
Cdd:cd17973 172 AGKFQKYFDNAPLLKV 187
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 4-169 3.45e-66

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: 216.18  E-value: 3.45e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSG-VIAITQPRRVAAVSVARRVAQELDVPLGEDVG 82
Cdd:cd17980   1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGrVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  83 YAIRFEDRTTS-KTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASnFKVLITSATLD 161
Cdd:cd17980  81 YCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGD-LRLIVASATLD 159


                ....*...
gi 18396548 162 GEKVSEFF 169
Cdd:cd17980 160 AEKFRDFF 167
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
 4-177 4.11e-66

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: 215.87  E-value: 4.11e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVGY 83
Cdd:cd17984   1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGSKVGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  84 AIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASN----FKVLITSAT 159
Cdd:cd17984  81 QVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPNrkehLKVVVMSAT 160

                       170
                ....*....|....*...
gi 18396548 160 LDGEKVSEFFSGCPVLNV 177
Cdd:cd17984 161 LELAKLSAFFGNCPVFDI 178
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
 4-168 7.76e-65

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: 212.98  E-value: 7.76e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTK-----SGVIAITQPRRVAAVSVARRVAQELDVPlG 78
Cdd:cd17982   1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSpesdnPGMIGITQPRRVAAVSMAKRVAEELNVF-G 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  79 EDVGYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASNF------- 151
Cdd:cd17982  80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKLYlqdqtvk 159

                       170
                ....*....|....*....
gi 18396548 152 --KVLITSATLdgeKVSEF 168
Cdd:cd17982 160 plKLVIMSATL---RVEDF 175
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
 4-177 8.23e-59

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: 196.14  E-value: 8.23e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVGY 83
Cdd:cd17989   1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAVGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  84 AIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRiRASNFKVLITSATLDGE 163
Cdd:cd17989  81 KVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLP-RRPDLKVIITSATIDAE 159

                       170
                ....*....|....
gi 18396548 164 KVSEFFSGCPVLNV 177
Cdd:cd17989 160 RFSRHFNNAPIIEV 173
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 4-177 1.54e-51

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: 176.48  E-value: 1.54e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKsgvIAITQPRRVAAVSVARRVAQELDVPLGEDVGY 83
Cdd:cd17979   1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH---IACTQPRRIACISLAKRVAFESLNQYGSKVAY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  84 AIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRAsNFKVLITSATLDGE 163
Cdd:cd17979  78 QIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRP-DLKLILMSATINIE 156

                       170
                ....*....|....
gi 18396548 164 KVSEFFSGCPVLNV 177
Cdd:cd17979 157 LFSGYFEGAPVVQV 170
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
 4-177 2.29e-44

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: 157.38  E-value: 2.29e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQ-----ILHRHGYTKSGVIAITQPRRVAAVSVARRVAQEL---DV 75
Cdd:cd17975   1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQflledLLLNGGTAQKCNIVCTQPRRISAMSLATRVCEELgceSG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  76 PLGED--VGYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRaSNFKV 153
Cdd:cd17975  81 PGGKNslCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKR-SDLHL 159

                       170       180
                ....*....|....*....|....
gi 18396548 154 LITSATLDGEKVSEFFSGCPVLNV 177
Cdd:cd17975 160 ILMSATVDCEKFSSYFTHCPILRI 183
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 4-184 5.45e-44

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: 156.12  E-value: 5.45e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHgYTKSGV---IAITQPRRVAAVSVARRVAQELDVPLGED 80
Cdd:cd17988   1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDH-YYKRGKycnIVVTQPRRIAAISIARRVSQEREWTLGSL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  81 VGYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASNFKVLITSATL 160
Cdd:cd17988  80 VGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRHVKIILMSATI 159

                       170       180
                ....*....|....*....|....
gi 18396548 161 DGEKVSEFFSgcpVLNVPGKLYPV 184
Cdd:cd17988 160 SCKEFADYFT---TPNNPAYVFEV 180
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 4-177 1.34e-43

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: 154.95  E-value: 1.34e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKS-GV---IAITQPRRVAAVSVARRVAQELDVPLGE 79
Cdd:cd17976   1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGrGArcnVVITQPRRISAVSVAQRVAHELGPNLRR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  80 DVGYAIRFEDRTTSK-TRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASnFKVLITSA 158
Cdd:cd17976  81 NVGYQVRLESRPPPRgGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPE-LRVVLMSA 159

                       170
                ....*....|....*....
gi 18396548 159 TLDGEKVSEFFSGCPVLNV 177
Cdd:cd17976 160 TGDNQRLSRYFGGCPVVRV 178
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 4-177 1.90e-43

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: 154.62  E-value: 1.90e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQ-ILHRH---GYTKSGVIAITQPRRVAAVSVARRVAQEL--DVPL 77
Cdd:cd17981   1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQfILDDAierGKGSSCRIVCTQPRRISAISVAERVAAERaeSCGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  78 GEDVGYAIRFEDRTTSK-TRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRaSNFKVLIT 156
Cdd:cd17981  81 GNSTGYQIRLESRKPRKqGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFR-SDLKVILM 159

                       170       180
                ....*....|....*....|.
gi 18396548 157 SATLDGEKVSEFFSGCPVLNV 177
Cdd:cd17981 160 SATLNAEKFSDYFNNCPMIHI 180
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 4-175 9.81e-43

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: 9.81e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVGY 83
Cdd:cd17990   1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  84 AIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASNFKVLITSATLDGE 163
Cdd:cd17990  81 RVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQLLRDDLRLLAMSATLDGD 160

                       170
                ....*....|..
gi 18396548 164 KVSEFFSGCPVL 175
Cdd:cd17990 161 GLAALLPEAPVV 172
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 4-177 1.01e-40

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: 146.91  E-value: 1.01e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQIL----HRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGE 79
Cdd:cd17985   1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFIldnsLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  80 DVGYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRaSNFKVLITSAT 159
Cdd:cd17985  81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQR-PDLKVILMSAT 159

                       170
                ....*....|....*...
gi 18396548 160 LDGEKVSEFFSGCPVLNV 177
Cdd:cd17985 160 LNAELFSDYFNSCPVIHI 177
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 4-177 7.97e-38

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: 140.74  E-value: 7.97e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQ-ILH---RHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGE 79
Cdd:cd17972  59 LPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQyILDdfiQNDRAAECNIVVTQPRRISAVSVAERVAFERGEEVGK 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  80 DVGYAIRFEDRTTSK-TRIKYLTDGVLLRESLSNpmLDDYSVIILDEAHERSLNTDILLGLVKRLVRIrASNFKVLITSA 158
Cdd:cd17972 139 SCGYSVRFESVLPRPhASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLLVVLRDVVQA-YPDLRVILMSA 215

                       170
                ....*....|....*....
gi 18396548 159 TLDGEKVSEFFSGCPVLNV 177
Cdd:cd17972 216 TIDTSMFCEYFFNCPVIEV 234
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 4-177 1.41e-37

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: 138.04  E-value: 1.41e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYtKSGV---IAITQPRRVAAVSVARRVAQELDVPLGED 80
Cdd:cd17987   1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCY-ANGIpcrIFCTQPRRLAAIAVAERVAAERGEKIGQT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  81 VGYAIRFEDRTTSKTRIKYLTDGVLLRESLS-NPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRiRASNFKVLITSAT 159
Cdd:cd17987  80 VGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQ-KHPNLKLILSSAA 158

                       170
                ....*....|....*...
gi 18396548 160 LDGEKVSEFFSGCPVLNV 177
Cdd:cd17987 159 LDVNLFIRYFGSCPVIYI 176
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
 4-177 5.73e-36

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: 133.41  E-value: 5.73e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRH---GYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGED 80
Cdd:cd17977   1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYclsAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIGHE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  81 VGYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASnFKVLITSATL 160
Cdd:cd17977  81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPE-LKLVIITCPH 159

                       170
                ....*....|....*..
gi 18396548 161 DGEKVSEFFSGCPVLNV 177
Cdd:cd17977 160 LSSKLLSYYGNVPLIEV 176
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
 4-177 8.34e-34

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: 127.32  E-value: 8.34e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   4 LPILQFEEKIVETVEKNS-VVVIIGETGSGKSTQLSQILHRHGYTKS---GVIAITQPRRVAAVSVARRVAQELDVPLGE 79
Cdd:cd17986   1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFALSRGfqkGQVTVTQPHPLAARSLALRVADEMDLNLGH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  80 DVGYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRlVRIRASNFK-VLITSA 158
Cdd:cd17986  81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKD-VRLQRPELRvVVVTSP 159

                       170
                ....*....|....*....
gi 18396548 159 TLDgEKVSEFFSGCPVLNV 177
Cdd:cd17986 160 ALE-PKLRAFWGNPPVVHV 177
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 400-493 2.56e-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: 97.69  E-value: 2.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   400 ALKQLYFIDAIDENGAITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLSAETTLLP----------ARSKPS 469
Cdd:pfam04408   1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQpnfldprsaaKAARRR 80

                          90       100
                  ....*....|....*....|....
gi 18396548   470 EKKRKHDEDSNLPNGSGYGDHIQL 493
Cdd:pfam04408  81 RRAADEKARAKFARLDLEGDHLTL 104
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 560-643 5.34e-24

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: 96.17  E-value: 5.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   560 LRKALCVGNANQIAERMLRHNGYRTLSfQSQLVQVHPSSVLsADNDGMMPNYVVYHELISTTRPFMRNVCAVDMAWVAPI 639
Cdd:pfam07717   1 LRAALAAGLYPNVARRDPKGKGYTTLS-DNQRVFIHPSSVL-FNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLF 78


                  ....
gi 18396548   640 KRKI 643
Cdd:pfam07717  79 APHI 82
DEXDc smart00487
DEAD-like helicases superfamily;
17-186 1.37e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 93.33  E-value: 1.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548     17 VEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIA-ITQPRRVAAVSVARRVAQELDVPLGEDVGY------AIRFED 89
Cdd:smart00487  21 LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVlVLVPTRELAEQWAEELKKLGPSLGLKVVGLyggdskREQLRK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548     90 RTTSKTRIKYLTDGVLLRESLSNPM-LDDYSVIILDEAHERS--LNTDILLGLVKRLvrirASNFKVLITSATL--DGEK 164
Cdd:smart00487 101 LESGKTDILVTTPGRLLDLLENDKLsLSNVDLVILDEAHRLLdgGFGDQLEKLLKLL----PKNVQLLLLSATPpeEIEN 176

                          170       180
                   ....*....|....*....|..
gi 18396548    165 VSEFFSGCPVLNVPGKLYPVEI 186
Cdd:smart00487 177 LLELFLNDPVFIDVGFTPLEPI 198
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 407-494 3.29e-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: 79.62  E-value: 3.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    407 IDAIDENGAITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLSaettllpARSKPSEKKRKHDEDSNLPNGSG 486
Cdd:smart00847   2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLS-------VGDPRPKEKREDADAARRRFADP 74


                   ....*...
gi 18396548    487 YGDHIQLL 494
Cdd:smart00847  75 ESDHLTLL 82
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 12-380 6.18e-17

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 85.03  E-value: 6.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   12 KIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGV--------------IAITQPRrvaaVSVARRVAQELDVPL 77
Cdd:PHA02653 171 KIFEAWISRKPVVLTGGTGVGKTSQVPKLLLWFNYLFGGFdnldkidpnfierpIVLSLPR----VALVRLHSITLLKSL 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   78 GedvgyairFEDRTTSKTRIKY--LTD----------GVLL---RESLSNpmLDDYSVIILDEAHERSLNTDILLGLVKR 142
Cdd:PHA02653 247 G--------FDEIDGSPISLKYgsIPDelintnpkpyGLVFsthKLTLNK--LFDYGTVIIDEVHEHDQIGDIIIAVARK 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  143 LV-RIRASnfkVLITsATL--DGEKVSEFFSGCPVLNVPG-KLYPVEILYSKER-----PVSYIESSLK---VAIDIHVR 210
Cdd:PHA02653 317 HIdKIRSL---FLMT-ATLedDRDRIKEFFPNPAFVHIPGgTLFPISEVYVKNKynpknKRAYIEEEKKnivTALKKYTP 392

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  211 EPEGDILIFMTGQDDIEKLVSRLEEKVRSLAegscmdaiIYPLHGSLP--PEMQVRVFSPPPPNcrrFIVSTNIAETSLT 288
Cdd:PHA02653 393 PKGSSGIVFVASVSQCEEYKKYLEKRLPIYD--------FYIIHGKVPniDEILEKVYSSKNPS---IIISTPYLESSVT 461

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  289 VDGVVYVIDSGyvkqRQYNPSSgmFSLDVIQISKVQANQRAGRAGRTRPGKCYRLYPLAvyrddfLDATIPEIQRTSLAG 368
Cdd:PHA02653 462 IRNATHVYDTG----RVYVPEP--FGGKEMFISKSMRTQRKGRVGRVSPGTYVYFYDLD------LLKPIKRIDSEFLHN 529

                        410
                 ....*....|....
gi 18396548  369 SVLYLK--SLDLPD 380
Cdd:PHA02653 530 YILYAKyfNLTLPE 543
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 201-334 1.80e-12

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 64.15  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548   201 LKVAIDIHVREPEGDILIFMTGQDDIEKLVSRLEEKVRslaegscmdaiIYPLHGSLPPEMQVRVFSPPPPNCRRFIVST 280
Cdd:pfam00271   3 LEALLELLKKERGGKVLIFSQTKKTLEAELLLEKEGIK-----------VARLHGDLSQEEREEILEDFRKGKIDVLVAT 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18396548   281 NIAETSLTVDGVVYVIDSGYVkqrqYNPSsgmfsldviqiskvQANQRAGRAGR 334
Cdd:pfam00271  72 DVAERGLDLPDVDLVINYDLP----WNPA--------------SYIQRIGRAGR 107
HELICc smart00490
helicase superfamily c-terminal domain;
250-334 1.27e-11

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 60.69  E-value: 1.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    250 IYPLHGSLPPEMQVRVFSPPPPNCRRFIVSTNIAETSLTVDGVVYVIDSGYVkqrqynpssgmfsldviqISKVQANQRA 329
Cdd:smart00490  14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP------------------WSPASYIQRI 75


                   ....*
gi 18396548    330 GRAGR 334
Cdd:smart00490  76 GRAGR 80
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 20-159 3.74e-11

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: 61.65  E-value: 3.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  20 NSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDvpLGEDVGYAIRFED------RTTS 93
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLRELFG--PGIRVAVLVGGSSaeerekNKLG 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18396548  94 KTRIKYLTDGVLLRESLSN--PMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASNFKVLITSAT 159
Cdd:cd00046  79 DADIIIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
AAA_22 pfam13401
AAA domain;
21-155 6.69e-09

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 54.66  E-value: 6.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    21 SVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLgedvgyairfEDRTTSKTRIKYL 100
Cdd:pfam13401   6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALGLPL----------SGRLSKEELLAAL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18396548   101 TDGVLlreslsnpMLDDYSVIILDEAHERSLNtdiLLGLVKRLVRIRASNFKVLI 155
Cdd:pfam13401  76 QQLLL--------ALAVAVVLIIDEAQHLSLE---ALEELRDLLNLSSKLLQLIL 119
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 11-161 4.49e-06

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: 47.24  E-value: 4.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548    11 EKIVETVEKNSVVVIIGETGSGKST--QLSqILHRHGYTKSGVIA-ITQPRRVAA---VSVARRVAQELDVPLGEDV-GY 83
Cdd:pfam00270   5 AEAIPAILEGRDVLVQAPTGSGKTLafLLP-ALEALDKLDNGPQAlVLAPTRELAeqiYEELKKLGKGLGLKVASLLgGD 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18396548    84 AIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHErsLNTDILLGLVKRLVRIRASNFKVLITSATLD 161
Cdd:pfam00270  84 SRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAHR--LLDMGFGPDLEEILRRLPKKRQILLLSATLP 159
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
 29-127 1.08e-05

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 46.00  E-value: 1.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  29 TGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAqeldvplGEDVGYAIRFEDRTTS-KTRIKYLTDGVLLR 107
Cdd:cd17931  10 PGAGKTTRVLPQIIREAIKKRLRTLVLAPTRVVAAEMYEALR-------GLPIRYRTGAVKEEHGgNEIVDYMCHGTFTC 82

                        90       100
                ....*....|....*....|
gi 18396548 108 ESLSNPMLDDYSVIILDEAH 127
Cdd:cd17931  83 RLLSPKRVPNYNLIIMDEAH 102
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 19-160 1.12e-04

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: 43.13  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548     19 KNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVGYAIRfedrtTSKTRIK 98
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLR-----LALALAR 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18396548     99 YLtdgvllreslsnpmldDYSVIILDEAHerSLNTDILLGLVKRLVRIRASNFKVLITSATL 160
Cdd:smart00382  76 KL----------------KPDVLILDEIT--SLLDAEQEALLLLLEELRLLLLLKSEKNLTV 119
FlhF cd17873
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ...
 22-213 2.47e-03

signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).


Pssm-ID: 349782 [Multi-domain]  Cd Length: 189  Bit Score: 39.45  E-value: 2.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548  22 VVVIIGETGSGKSTQLSQILHRHGYTKSGVIAI--TQPRRVAAVSVARRVAQELDVPLgedvgyairfedrttsktriKY 99
Cdd:cd17873   2 VIALVGPTGVGKTTTLAKLAARYVLKKGKKVALitTDTYRIGAVEQLKTYAEIMGIPV--------------------EV 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396548 100 LTDGVLLRESLSNpmLDDYSVIILDEAHeRSLNTDILLglvKRLVRIRASNFKV---LITSATLDGE---KVSEFFSGCP 173
Cdd:cd17873  62 AEDPEDLADALER--LSDRDLILIDTAG-RSPRDKEQL---EELKELLGAGEDIevhLVLSATTKAKdlkEIIERFSPLG 135

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18396548 174 VLNV----------PGKLYpvEILYSKERPVSYIESSLKVAIDIHVREPE 213
Cdd:cd17873 136 YRGLiltkldettsLGSVL--SVLAESQLPVSYVTTGQRVPEDIEVASPL 183
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 16-64 2.52e-03

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 39.76  E-value: 2.52e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 18396548  16 TVEKNSVVVIIGETGSGKSTQLSQIL---HRHgytkSGVIAItqPRRVAAVS 64
Cdd:cd03250  27 EVPKGELVAIVGPVGSGKSSLLSALLgelEKL----SGSVSV--PGSIAYVS 72
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 16-54 5.19e-03

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 38.52  E-value: 5.19e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18396548  16 TVEKNSVVVIIGETGSGKSTqLSQILHRHGYTKSGVIAI 54
Cdd:cd03228  24 TIKPGEKVAIVGPSGSGKST-LLKLLLRLYDPTSGEILI 61
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
 118-160 6.71e-03

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 38.43  E-value: 6.71e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 18396548 118 YSVIILDEAHerSLNTDILLGLVKRLVRIRAS-NFKVLITSATL 160
Cdd:cd17930 131 NSVVVLDEVQ--AYDPEYMALLLKALLELLGElGGPVVLMTATL 172
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 16-52 7.46e-03

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 38.64  E-value: 7.46e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 18396548  16 TVEKNSVVVIIGETGSGKSTqLSQILHRHGYTKSGVI 52
Cdd:cd03257  27 SIKKGETLGLVGESGSGKST-LARAILGLLKPTSGSI 62
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 16-37 8.94e-03

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 38.28  E-value: 8.94e-03
                        10        20
                ....*....|....*....|..
gi 18396548  16 TVEKNSVVVIIGETGSGKSTQL 37
Cdd:cd03262  22 TVKKGEVVVIIGPSGSGKSTLL 43
 
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