|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
135-750 |
0e+00 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 595.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEVGY 214
Cdd:COG1643 10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGETVGY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 215 SIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDV-AKVRPDLRLIISSATLEAK 293
Cdd:COG1643 90 RVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLqPALRPDLKLLVMSATLDAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 294 KFSEYFDSARIYLIPGRRYPVEKLFRKCPEP--DYLETVIRTVVQIHQTEAiGDILVFLTGQEEIETVETNLKRRMmdlg 371
Cdd:COG1643 170 RFARLLGDAPVIESSGRTYPVEVRYRPLPADerDLEDAVADAVREALAEEP-GDILVFLPGEREIRRTAEALRGRL---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 372 tkGSEIIICPIYSNLPTPLQAKVFEPAPKGTRKVVLATNIAETSLTIDGVKYVIDPGYCKINSYNPRTGMESLLVTPISK 451
Cdd:COG1643 245 --PPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 452 ASAAQRAGRSGRTGPGKCFRLYNIKD---LEPTTIPEIQRANLASVVLTLKSLGIQDVFNFDFMDPPPENALLKALELLY 528
Cdd:COG1643 323 ASANQRAGRAGRLAPGICYRLWSEEDfarRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARALLQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 529 ALGALDEIGEITKVGERMVEFPVDPMLSKMIVGSEKYKCSKEIITIAAMLSVgnsvfyrpknQQVFADKARMDFyedten 608
Cdd:COG1643 403 ELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSE----------RDPRRGAAGSDL------ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 609 vgdhIALLRVYNSWKEENystqwccEKFIQSKSMKRARDIRDQLLGLLnkiGVELTSNPNDLDAIKKAILAGFFPHSAKL 688
Cdd:COG1643 467 ----LARLNLWRRLREQQ-------REFLSYLRLREWRDLARQLRRLL---GEGANEEPADYEAIGLLLALAYPDRIARR 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063723004 689 QKN-GSY-----RRvkepqtVYVHPNSGLFGaspSKWLVYHELVLTTKEY-MRHTTEMKPEWLIEIAPH 750
Cdd:COG1643 533 RGEgGRYllargRG------AALFPGSPLAK---KEWLVAAELVGGAAEArIRLAAPIDPEWLEELAAH 592
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
135-753 |
1.27e-159 |
|
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: 497.37 E-value: 1.27e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEVGY 214
Cdd:TIGR01967 66 LPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKVGY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 215 SIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSATLEAKK 294
Cdd:TIGR01967 146 KVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPER 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 295 FSEYFDSARIYLIPGRRYPVEKLFRKCPEP------DYLETVIRTVVQIHQtEAIGDILVFLTGQEEI-ETVETNLKRRM 367
Cdd:TIGR01967 226 FSRHFNNAPIIEVSGRTYPVEVRYRPLVEEqedddlDQLEAILDAVDELFA-EGPGDILIFLPGEREIrDAAEILRKRNL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 368 mdlgtKGSEIIicPIYSNLPTPLQAKVFEPAPKgtRKVVLATNIAETSLTIDGVKYVIDPGYCKINSYNPRTGMESLLVT 447
Cdd:TIGR01967 305 -----RHTEIL--PLYARLSNKEQQRVFQPHSG--RRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 448 PISKASAAQRAGRSGRTGPGKCFRLYNIKDLEPT---TIPEIQRANLASVVLTLKSLGIQDVFNFDFMDPPPENALLKAL 524
Cdd:TIGR01967 376 PISQASANQRKGRCGRVAPGICIRLYSEEDFNSRpefTDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGF 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 525 ELLYALGALDE---IGEITKVGERMVEFPVDPMLSKMIVGSEKYKCSKEIITIAAMLSVgNSVFYRPKNQQVFADKARMD 601
Cdd:TIGR01967 456 RLLEELGALDDdeaEPQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSI-QDPRERPMEKQQAADQAHAR 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 602 FYEDTEnvgDHIALLRVYNSWKEENYST------QWCCEKFIQSKSMKRARDIRDQLLGLLNKIGVELTSNPNDLDAIKK 675
Cdd:TIGR01967 535 FKDPRS---DFLSRVNLWRHIEEQRQALsanqfrNACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHK 611
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063723004 676 AILAGFFPHSAKLQKNGSYRRVKEpQTVYVHPNSGLFGASPsKWLVYHELVLTTKEYMRHTTEMKPEWLIEIAPHYYK 753
Cdd:TIGR01967 612 ALLSGLLSQIGMKDEKHEYDGARG-RKFHIFPGSPLFKKPP-KWVMAAELVETSKLYARLVAKIEPEWVEPVAGHLIK 687
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
133-753 |
2.75e-147 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 464.92 E-value: 2.75e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 133 EFLPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEV 212
Cdd:PRK11131 71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 213 GYSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSATLEA 292
Cdd:PRK11131 151 GYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 293 KKFSEYFDSARIYLIPGRRYPVEKLFRKCPEP------DYLETVIRTVVQIhQTEAIGDILVFLTGQEEIETVETNLKRR 366
Cdd:PRK11131 231 ERFSRHFNNAPIIEVSGRTYPVEVRYRPIVEEaddterDQLQAIFDAVDEL-GREGPGDILIFMSGEREIRDTADALNKL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 367 mmDLgtKGSEIIicPIYSNLPTPLQAKVFEpaPKGTRKVVLATNIAETSLTIDGVKYVIDPGYCKINSYNPRTGMESLLV 446
Cdd:PRK11131 310 --NL--RHTEIL--PLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 447 TPISKASAAQRAGRSGRTGPGKCFRLYNIKDLE--PT-TIPEIQRANLASVVLTLKSLGIQDVFNFDFMDPPPENALLKA 523
Cdd:PRK11131 382 EPISQASANQRKGRCGRVSEGICIRLYSEDDFLsrPEfTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDG 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 524 LELLYALGAL-----DEIGEITKVGERMVEFPVDPMLSKMIVGSEKYKCSKEIITIAAMLSVGNSVfYRPKNQQVFADKA 598
Cdd:PRK11131 462 VRLLEELGAIttdeqASAYKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPR-ERPMDKQQASDEK 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 599 RMDFyEDTENvgDHIALLRVYNSWKEEN---YSTQW---CCEKFIQSKSMKRARDIRDQLLGLLNKIGVELTSNPNDLDA 672
Cdd:PRK11131 541 HRRF-ADKES--DFLAFVNLWNYLQEQQkalSSNQFrrlCRTDYLNYLRVREWQDIYTQLRQVVKELGIPVNSEPAEYRE 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 673 IKKAILAGFFPH-----SAKLQKNGSyRRVKepqtVYVHPNSGLFGASPsKWLVYHELVLTTKEYMRHTTEMKPEWLIEI 747
Cdd:PRK11131 618 IHTALLTGLLSHigmkdAEKQEYTGA-RNAR----FSIFPGSGLFKKPP-KWVMVAELVETSRLWGRIAARIEPEWIEPL 691
|
....*.
gi 1063723004 748 APHYYK 753
Cdd:PRK11131 692 AQHLIK 697
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
135-578 |
1.02e-116 |
|
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: 372.56 E-value: 1.02e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIP-QYLQEAGYTkrGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEVG 213
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPlALLDAPGIG--GKIIMLEPRRLAARSAAQRLASQLGEAVGQTVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 214 YSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDV-AKVRPDLRLIISSATLEA 292
Cdd:TIGR01970 79 YRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVqSSLREDLKILAMSATLDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 293 KKFSEYFDSARIYLIPGRRYPVEKLFRKCPEPDYLET-VIRTVVQIHQTEAiGDILVFLTGQEEIETVETNLKRRMmdlg 371
Cdd:TIGR01970 159 ERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDaVSRAVEHALASET-GSILVFLPGQAEIRRVQEQLAERL---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 372 tkGSEIIICPIYSNLPTPLQAKVFEPAPKGTRKVVLATNIAETSLTIDGVKYVIDPGYCKINSYNPRTGMESLLVTPISK 451
Cdd:TIGR01970 234 --DSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 452 ASAAQRAGRSGRTGPGKCFRLYN---IKDLEPTTIPEIQRANLASVVLTLKSLGIQDVFNFDFMDPPPENALLKALELLY 528
Cdd:TIGR01970 312 ASATQRAGRAGRLEPGVCYRLWSeeqHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQ 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1063723004 529 ALGALDEIGEITKVGERMVEFPVDPMLSKMIVGSEKYKCSKEIITIAAML 578
Cdd:TIGR01970 392 RLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALL 441
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
135-307 |
4.63e-104 |
|
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: 317.14 E-value: 4.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRG-KIGCTQPRRVAAMSVASRVAQEVGVKLGHEVG 213
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGgKIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 214 YSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSATLEAK 293
Cdd:cd17974 81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160
|
170
....*....|....
gi 1063723004 294 KFSEYFDSARIYLI 307
Cdd:cd17974 161 KFSAFFDDAPIFRI 174
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
135-578 |
2.79e-102 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 333.81 E-value: 2.79e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELL-KLIEENQVLvIVGETGSGKTTQIP-QYLQEAGYTkrGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEV 212
Cdd:PRK11664 4 LPVAAVLPELLtALKTAPQVL-LKAPTGAGKSTWLPlQLLQHGGIN--GKIIMLEPRRLAARNVAQRLAEQLGEKPGETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 213 GYSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDV-AKVRPDLRLIISSATLE 291
Cdd:PRK11664 81 GYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVqQGLRDDLKLLIMSATLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 292 AKKFSEYFDSARIYLIPGRRYPVEKLFRKCPEPDYLET-VIRTVVQIHQTEAiGDILVFLTGQEEIETVETNLKRRMmdl 370
Cdd:PRK11664 161 NDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRFDEaVARATAELLRQES-GSLLLFLPGVGEIQRVQEQLASRV--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 371 gtkGSEIIICPIYSNLPTPLQAKVFEPAPKGTRKVVLATNIAETSLTIDGVKYVIDPGYCKINSYNPRTGMESLLVTPIS 450
Cdd:PRK11664 237 ---ASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 451 KASAAQRAGRSGRTGPGKCFRLYNIKDLE-----PTtiPEIQRANLASVVLTLKSLGIQDVFNFDFMDPPPENALLKALE 525
Cdd:PRK11664 314 QASMTQRAGRAGRLEPGICLHLYSKEQAEraaaqSE--PEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1063723004 526 LLYALGALDEIGEITKVGERMVEFPVDPMLSKMIVGSEKYkcSKEIITIAAML 578
Cdd:PRK11664 392 LLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKED--DEAALATAAKL 442
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
130-308 |
6.93e-97 |
|
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: 298.63 E-value: 6.93e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 130 EGREFLPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLG 209
Cdd:cd17971 1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 210 HEVGYSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSAT 289
Cdd:cd17971 81 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSAT 160
|
170
....*....|....*....
gi 1063723004 290 LEAKKFSEYFDSARIYLIP 308
Cdd:cd17971 161 LDAVKFSQYFYEAPIFTIP 179
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
135-307 |
5.07e-90 |
|
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: 280.50 E-value: 5.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEVGY 214
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 215 SIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSATLEAKK 294
Cdd:cd17983 81 AIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDADK 160
|
170
....*....|...
gi 1063723004 295 FSEYFDSARIYLI 307
Cdd:cd17983 161 FADFFGNVPIFTI 173
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
151-304 |
8.62e-89 |
|
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: 276.65 E-value: 8.62e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 151 NQVLVIVGETGSGKTTQIPQYLQEAGYTK--RGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEVGYSIRFEDCTSEKTVI 228
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKggKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723004 229 KYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSATLEAKKFSEYFDSARI 304
Cdd:cd17917 81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPV 156
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
130-304 |
1.32e-88 |
|
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: 277.37 E-value: 1.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 130 EGREFLPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGK--IGCTQPRRVAAMSVASRVAQEVGVK 207
Cdd:cd17973 8 EKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKklVACTQPRRVAAMSVAQRVAEEMDVK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 208 LGHEVGYSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISS 287
Cdd:cd17973 88 LGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIVMS 167
|
170
....*....|....*..
gi 1063723004 288 ATLEAKKFSEYFDSARI 304
Cdd:cd17973 168 ATLDAGKFQKYFDNAPL 184
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
135-304 |
7.27e-85 |
|
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: 267.30 E-value: 7.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEVGY 214
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 215 SIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVR-----PDLRLIISSAT 289
Cdd:cd17978 81 SVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVIIMSAT 160
|
170
....*....|....*
gi 1063723004 290 LEAKKFSEYFDSARI 304
Cdd:cd17978 161 LDADLFSEYFNGAPV 175
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
135-301 |
4.65e-79 |
|
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: 252.00 E-value: 4.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGK-IGCTQPRRVAAMSVASRVAQEVGVKLGHEVG 213
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRvVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 214 YSIRFEDCTSE-KTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSATLEA 292
Cdd:cd17980 81 YCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160
|
....*....
gi 1063723004 293 KKFSEYFDS 301
Cdd:cd17980 161 EKFRDFFNQ 169
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
312-473 |
6.96e-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: 243.21 E-value: 6.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 312 YPVEKLFRK-----------CPEPDYLETVIRTVVQIHQTEAIGDILVFLTGQEEIETVETNLkrRMMDLGTKGSEIIIC 380
Cdd:cd18791 1 FPVEVYYLEdilellgisseKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELL--REELLSPDLGKLLVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 381 PIYSNLPTPLQAKVFEPAPKGTRKVVLATNIAETSLTIDGVKYVIDPGYCKINSYNPRTGMESLLVTPISKASAAQRAGR 460
Cdd:cd18791 79 PLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGR 158
|
170
....*....|...
gi 1063723004 461 SGRTGPGKCFRLY 473
Cdd:cd18791 159 AGRTRPGKCYRLY 171
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
135-307 |
2.57e-68 |
|
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: 223.19 E-value: 2.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEVGY 214
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGSKVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 215 SIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRP-----DLRLIISSAT 289
Cdd:cd17984 81 QVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVVMSAT 160
|
170
....*....|....*...
gi 1063723004 290 LEAKKFSEYFDSARIYLI 307
Cdd:cd17984 161 LELAKLSAFFGNCPVFDI 178
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
135-304 |
5.73e-65 |
|
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: 214.24 E-value: 5.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEVGY 214
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 215 SIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSATLEAKK 294
Cdd:cd17989 81 KVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAER 160
|
170
....*....|
gi 1063723004 295 FSEYFDSARI 304
Cdd:cd17989 161 FSRHFNNAPI 170
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
135-297 |
1.21e-59 |
|
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: 200.27 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKR-----GKIGCTQPRRVAAMSVASRVAQEVGVkLG 209
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPesdnpGMIGITQPRRVAAVSMAKRVAEELNV-FG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 210 HEVGYSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPD--------- 280
Cdd:cd17982 80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159
|
170
....*....|....*...
gi 1063723004 281 -LRLIISSATLEAKKFSE 297
Cdd:cd17982 160 pLKLVIMSATLRVEDFTE 177
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
135-304 |
1.12e-56 |
|
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: 191.50 E-value: 1.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKrgkIGCTQPRRVAAMSVASRVAQEVGVKLGHEVGY 214
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH---IACTQPRRIACISLAKRVAFESLNQYGSKVAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 215 SIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSATLEAKK 294
Cdd:cd17979 78 QIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIEL 157
|
170
....*....|
gi 1063723004 295 FSEYFDSARI 304
Cdd:cd17979 158 FSGYFEGAPV 167
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
135-301 |
6.34e-54 |
|
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: 184.28 E-value: 6.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEaGYTKRGK-----IGCTQPRRVAAMSVASRVAQEVG--VK 207
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILD-DAIERGKgsscrIVCTQPRRISAISVAERVAAERAesCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 208 LGHEVGYSIRFED-CTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIIS 286
Cdd:cd17981 80 LGNSTGYQIRLESrKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159
|
170
....*....|....*
gi 1063723004 287 SATLEAKKFSEYFDS 301
Cdd:cd17981 160 SATLNAEKFSDYFNN 174
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
135-307 |
2.41e-49 |
|
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: 171.56 E-value: 2.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEA----GYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGH 210
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNslqgPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 211 EVGYSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSATL 290
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
|
170
....*....|....*..
gi 1063723004 291 EAKKFSEYFDSARIYLI 307
Cdd:cd17985 161 NAELFSDYFNSCPVIHI 177
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
135-302 |
2.90e-47 |
|
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: 165.77 E-value: 2.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQE---AGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGHE 211
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEyclSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIGHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 212 VGYSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSATLE 291
Cdd:cd17977 81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPHL 160
|
170
....*....|.
gi 1063723004 292 AKKFSEYFDSA 302
Cdd:cd17977 161 SSKLLSYYGNV 171
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
135-301 |
3.86e-47 |
|
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: 165.39 E-value: 3.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRG--KIGCTQPRRVAAMSVASRVAQEVGVKLGHEV 212
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIpcRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 213 GYSIRFEDCTSEKTVIKYMTDGMLLRELLI-EPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSATLE 291
Cdd:cd17987 81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160
|
170
....*....|
gi 1063723004 292 AKKFSEYFDS 301
Cdd:cd17987 161 VNLFIRYFGS 170
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
135-302 |
1.45e-46 |
|
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: 163.66 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEVGY 214
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 215 SIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKV-RPDLRLIISSATLEAK 293
Cdd:cd17990 81 RVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQLlRDDLRLLAMSATLDGD 160
|
....*....
gi 1063723004 294 KFSEYFDSA 302
Cdd:cd17990 161 GLAALLPEA 169
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
135-307 |
1.73e-46 |
|
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: 163.93 E-value: 1.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQE-----AGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLG 209
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEdlllnGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 210 -----HEVGYSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLI 284
Cdd:cd17975 81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
|
170 180
....*....|....*....|...
gi 1063723004 285 ISSATLEAKKFSEYFDSARIYLI 307
Cdd:cd17975 161 LMSATVDCEKFSSYFTHCPILRI 183
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
135-299 |
2.39e-46 |
|
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: 163.42 E-value: 2.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGC----TQPRRVAAMSVASRVAQEVGVKLGH 210
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCnvviTQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 211 EVGYSIRFEDCTSEKT-VIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISSAT 289
Cdd:cd17976 81 NVGYQVRLESRPPPRGgALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
|
170
....*....|
gi 1063723004 290 LEAKKFSEYF 299
Cdd:cd17976 161 GDNQRLSRYF 170
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
132-299 |
9.33e-44 |
|
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: 158.07 E-value: 9.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 132 REFLPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAgYTKRGK-----IGCTQPRRVAAMSVASRVAQEVGV 206
Cdd:cd17972 56 RELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDD-FIQNDRaaecnIVVTQPRRISAVSVAERVAFERGE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 207 KLGHEVGYSIRFEDCTSEK-TVIKYMTDGMLLRELliEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLII 285
Cdd:cd17972 135 EVGKSCGYSVRFESVLPRPhASILFCTVGVLLRKL--EAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVIL 212
|
170
....*....|....
gi 1063723004 286 SSATLEAKKFSEYF 299
Cdd:cd17972 213 MSATIDTSMFCEYF 226
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
135-293 |
7.68e-42 |
|
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: 150.43 E-value: 7.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIV-GETGSGKTTQIPQYLQEAGYTKR---GKIGCTQPRRVAAMSVASRVAQEVGVKLGH 210
Cdd:cd17986 1 LPIWAAKFTFLEQLESPSGIVLVsGEPGSGKSTQVPQWCAEFALSRGfqkGQVTVTQPHPLAARSLALRVADEMDLNLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 211 EVGYSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRL-IISSAT 289
Cdd:cd17986 81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVvVVTSPA 160
|
....
gi 1063723004 290 LEAK 293
Cdd:cd17986 161 LEPK 164
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
135-301 |
1.26e-40 |
|
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: 147.26 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 135 LPIHGYREELLKLIEENQVLVIVGETGSGKTTQIPQYLQEAgYTKRGK---IGCTQPRRVAAMSVASRVAQEVGVKLGHE 211
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDH-YYKRGKycnIVVTQPRRIAAISIARRVSQEREWTLGSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 212 VGYSIRFEDCTSEKTVIKYMTDGMLLRELLIEPKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPD-LRLIISSATL 290
Cdd:cd17988 80 VGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSATI 159
|
170
....*....|.
gi 1063723004 291 EAKKFSEYFDS 301
Cdd:cd17988 160 SCKEFADYFTT 170
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
523-615 |
1.55e-29 |
|
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: 112.72 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 523 ALELLYALGALDEIGEITKVGERMVEFPVDPMLSKMIVGSEKYKCSKEIITIAAMLSVGNsVFYRP----KNQQVFADKA 598
Cdd:pfam04408 1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRD-PFVQPnfldPRSAAKAARR 79
|
90 100
....*....|....*....|....*
gi 1063723004 599 RMDFYED--------TENVGDHIAL 615
Cdd:pfam04408 80 RRRAADEkarakfarLDLEGDHLTL 104
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
130-313 |
9.19e-28 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 111.43 E-value: 9.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 130 EGREFLPIHGYREELLKLIEEN-QVLVIVGETGSGKTTQIPQYLQEAGY-TKRGKIGCTQPRRVAAMSVASRVAQEVGVK 207
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKrGKGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 208 LGHEVGY------SIRFEDCTSEKTVIKYMTDGMLLRELLIEP-KLDSYSVIIIDEAHERTLS--TDILFALVKdvaKVR 278
Cdd:smart00487 82 GLKVVGLyggdskREQLRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLLDGgfGDQLEKLLK---LLP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063723004 279 PDLRLIISSATL--EAKKFSEYFDSARIYLIPGRRYP 313
Cdd:smart00487 159 KNVQLLLLSATPpeEIENLLELFLNDPVFIDVGFTPL 195
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
529-616 |
5.47e-25 |
|
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.
Pssm-ID: 214852 [Multi-domain] Cd Length: 82 Bit Score: 98.88 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 529 ALGALDEIGEITKVGERMVEFPVDPMLSKMIVGSEKYKCSKEIITIAAMLSVGNsvfYRPKNQQVFADKARMDFYEDTen 608
Cdd:smart00847 1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD---PRPKEKREDADAARRRFADPE-- 75
|
....*...
gi 1063723004 609 vGDHIALL 616
Cdd:smart00847 76 -SDHLTLL 82
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
673-751 |
2.70e-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: 96.94 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 673 IKKAILAGFFPHSAKL-QKNGSYRRVKEPQTVYVHPNSGLF--GASPSKWLVYHELVLTTKEYMRHTTEMKPEWLIEIAP 749
Cdd:pfam07717 1 LRAALAAGLYPNVARRdPKGKGYTTLSDNQRVFIHPSSVLFneKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80
|
..
gi 1063723004 750 HY 751
Cdd:pfam07717 81 HI 82
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
151-480 |
4.53e-14 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 76.17 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 151 NQVLVIVGETGSGKTTQIPQ------YLQeAGYTKRGKIGCTQPRRVAAMSVAsRVAQevgVKLgHEVGY--SIRFEDCT 222
Cdd:PHA02653 179 RKPVVLTGGTGVGKTSQVPKlllwfnYLF-GGFDNLDKIDPNFIERPIVLSLP-RVAL---VRL-HSITLlkSLGFDEID 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 223 SEKTVIKY--MTD----------GMLL--RELLIEpKLDSYSVIIIDEAHERTLSTDILFALV-KDVAKVRpdlRLIISS 287
Cdd:PHA02653 253 GSPISLKYgsIPDelintnpkpyGLVFstHKLTLN-KLFDYGTVIIDEVHEHDQIGDIIIAVArKHIDKIR---SLFLMT 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 288 ATLEAKK--FSEYFDSARIYLIPG-RRYPVEKLFRKCPE--PD---YLETVIRTVVQIHQT---EAIGDILVFLTGQEEI 356
Cdd:PHA02653 329 ATLEDDRdrIKEFFPNPAFVHIPGgTLFPISEVYVKNKYnpKNkraYIEEEKKNIVTALKKytpPKGSSGIVFVASVSQC 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 357 ETVETNLKRRMMDLG-------TKGSEIIICPIYSNLptplqakvfEPApkgtrkVVLATNIAETSLTIDGVKYVIDPGY 429
Cdd:PHA02653 409 EEYKKYLEKRLPIYDfyiihgkVPNIDEILEKVYSSK---------NPS------IIISTPYLESSVTIRNATHVYDTGR 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1063723004 430 CKINSynPRTGMESLlvtpISKASAAQRAGRSGRTGPGKCFRLYNIKDLEP 480
Cdd:PHA02653 474 VYVPE--PFGGKEMF----ISKSMRTQRKGRVGRVSPGTYVYFYDLDLLKP 518
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
376-465 |
4.22e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 65.31 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 376 EIIICPIYSNLPTPLQAKVFEPAPKGTRKVVLATNIAETSLTIDGVKYVIDPGYckinsynprtgmesllvtPISKASAA 455
Cdd:smart00490 11 GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL------------------PWSPASYI 72
|
90
....*....|
gi 1063723004 456 QRAGRSGRTG 465
Cdd:smart00490 73 QRIGRAGRAG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
331-465 |
1.25e-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: 64.92 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 331 IRTVVQIHQTEAIGDILVFLTGQEEIEtvETNLKRRmmdlgtkgSEIIICPIYSNLPTPLQAKVFEPAPKGTRKVVLATN 410
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLE--AELLLEK--------EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATD 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063723004 411 IAETSLTIDGVKYVIDpgyckinsYNPRTGMESLLvtpiskasaaQRAGRSGRTG 465
Cdd:pfam00271 73 VAERGLDLPDVDLVIN--------YDLPWNPASYI----------QRIGRAGRAG 109
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
154-289 |
2.24e-08 |
|
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: 53.56 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 154 LVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVK-----LGHEVGYSIRFEDCTSEKTVI 228
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLRELFGPGirvavLVGGSSAEEREKNKLGDADII 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063723004 229 kYMTDGMLLRELLIE--PKLDSYSVIIIDEAHERTLSTD-ILFALVKDVAKVRPDLRLIISSAT 289
Cdd:cd00046 84 -IATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRgALILDLAVRKAGLKNAQVILLSAT 146
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
145-290 |
9.21e-08 |
|
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: 52.24 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 145 LKLIEENQVLVIVGETGSGKTT--QIPqYLQEAGYTKRGKIG-CTQPRRVAA---MSVASRVAQEVGVKLGHEVGYSIRF 218
Cdd:pfam00270 8 IPAILEGRDVLVQAPTGSGKTLafLLP-ALEALDKLDNGPQAlVLAPTRELAeqiYEELKKLGKGLGLKVASLLGGDSRK 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063723004 219 EDCTSEKTV-IKYMTDGMLLRELLIEPKLDSYSVIIIDEAHeRTLSTDILFALVKDVAKVRPDLRLIISSATL 290
Cdd:pfam00270 87 EQLEKLKGPdILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
152-258 |
1.26e-07 |
|
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: 51.78 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 152 QVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQE-VGVKLGhevgySIRFEDctSEKTVIKY 230
Cdd:cd17931 2 QLTVLDLHPGAGKTTRVLPQIIREAIKKRLRTLVLAPTRVVAAEMYEALRGLpIRYRTG-----AVKEEH--GGNEIVDY 74
|
90 100
....*....|....*....|....*...
gi 1063723004 231 MTDGMLLRELLIEPKLDSYSVIIIDEAH 258
Cdd:cd17931 75 MCHGTFTCRLLSPKRVPNYNLIIMDEAH 102
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
152-271 |
1.91e-07 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 50.42 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 152 QVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEvgysirfedcTSEKTVIKYM 231
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALGLPLSGR----------LSKEELLAAL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1063723004 232 TDgmLLRELLIEPkldsysVIIIDEAHErtLSTDILFALV 271
Cdd:pfam13401 76 QQ--LLLALAVAV------VLIIDEAQH--LSLEALEELR 105
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
404-473 |
6.70e-04 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 38.84 E-value: 6.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063723004 404 KVVLATNIAETSLTIDGVKYVIDPGYckinsynprtgmesllvtPISKASAAQRAGRSGRTG--PGKCFRLY 473
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDP------------------PSSAASYIQRVGRAGRGGkdEGEVILFV 77
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
141-298 |
8.03e-04 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 42.50 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 141 REELLKLI----------EENQVLVIVGETGSGKTT---QIPQYLQEAGYtKRGKIgCTQPRRVAAMSVASRVAQEVGVK 207
Cdd:PRK00771 75 YEELVKLLgeeteplvlpLKPQTIMLVGLQGSGKTTtaaKLARYFKKKGL-KVGLV-AADTYRPAAYDQLKQLAEKIGVP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 208 LGHEVGysirfedctsEKTVIKYMTDGMllrelliePKLDSYSVIIIDEAHERTLSTDILFALVKDVAKVRPDLRLIISS 287
Cdd:PRK00771 153 FYGDPD----------NKDAVEIAKEGL--------EKFKKADVIIVDTAGRHALEEDLIEEMKEIKEAVKPDEVLLVID 214
|
170
....*....|....*..
gi 1063723004 288 ATL------EAKKFSEY 298
Cdd:PRK00771 215 ATIgqqaknQAKAFHEA 231
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
153-297 |
2.08e-03 |
|
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) 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 cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349769 [Multi-domain] Cd Length: 193 Bit Score: 40.05 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 153 VLVIVGETGSGKTTQIPQ---YLQEAGytKRGKIGCTQPRRVAAMSVASRVAQEVGVKLghevgysirFEDCTSEKTVIk 229
Cdd:cd03115 2 VILLVGLQGSGKTTTLAKlarYYQEKG--KKVLLIAADTFRAAAVEQLKTLAEKLGVPV---------FESYTGTDPAS- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063723004 230 ymtdgmLLRELLIEPKLDSYSVIIIDEAHeRTLSTDILFALVKDVAKV-RPDLRLIISSATL------EAKKFSE 297
Cdd:cd03115 70 ------IAQEAVEKAKLEGYDVLLVDTAG-RLQKDEPLMEELKKVKEVeSPDEVLLVLDATTgqealsQAKAFNE 137
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
151-287 |
3.17e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.89 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723004 151 NQVLVIVGETGSGKTTQIPQYLQEAGYTKRGKIGCTQPRRVAAMSVASRVAQEVGVKLGHEVGYSIRfedctsektviky 230
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLR------------- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063723004 231 mtdgmLLRELLIEPKLDsysVIIIDEAH------ERTLSTDILFALVKDVAKVRPDLRLIISS 287
Cdd:smart00382 69 -----LALALARKLKPD---VLILDEITslldaeQEALLLLLEELRLLLLLKSEKNLTVILTT 123
|
|
| |
