|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
7-789 |
0e+00 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 763.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 7 DLAEIGRGLPVAGHEDELREAIfgeGAPGAVVVQAPPGTGKTTFLPPLLANE---VSGKVICVAPRRVAVRAAAHRLHHL 83
Cdd:COG1643 2 SLITYPPDLPVSAVLPELLAAL---RAHQVVVLAAPPGAGKTTQLPLALLELgwgAGGRIGMLEPRRLAARAAAERMAEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 84 APTVPG--VGFTIRGEQ--TPSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRE-LRDDLR 158
Cdd:COG1643 79 LGEPVGetVGYRVRFEDkvSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPaLRPDLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 159 LVAMSATVESSRFAALIGG-DVVTITSPIYPLEVSYAPIAGRAecsRGFLSELARASREAAVASSDSVLVFVPGVREVRI 237
Cdd:COG1643 159 LLVMSATLDAERFARLLGDaPVIESSGRTYPVEVRYRPLPADE---RDLEDAVADAVREALAEEPGDILVFLPGEREIRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 238 VVEALEcdPRLPHGIEVYPLHGSLSSPEQDAALRADSQ---RIVVATSIAESSITVPGVRTVVDSGLSRVPKRDNLRGMT 314
Cdd:COG1643 236 TAEALR--GRLPPDTEILPLYGRLSAAEQDRAFAPAPHgrrRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 315 GLVTISTSQSSVEQRAGRAGREGPGTVVRCYSASDFQHFRAAISPEIASADLTQASLFVSAWG-GSFDSFPLLDAPPART 393
Cdd:COG1643 314 RLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGlGDPEDLPFLDPPPARA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 394 VEQAQATLEQLGAVDEHG-LTTIGKKLVALPTDPRLGRALLEAGSQ-----AAPVIASLGED--VRGDVDREL-PRLTAL 464
Cdd:COG1643 394 IADARALLQELGALDADGrLTPLGRALARLPLDPRLARMLLAAAELgclreAAILAALLSERdpRRGAAGSDLlARLNLW 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 465 ----------------PRVRREIARLKKLSTDRGKV------ATGTVVGLAFPSLIARNMGKD--YQLASGTR-VLAPD- 518
Cdd:COG1643 474 rrlreqqreflsylrlREWRDLARQLRRLLGEGANEepadyeAIGLLLALAYPDRIARRRGEGgrYLLARGRGaALFPGs 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 519 --FHAEWIAVADVSLGNIGTpRVRAAAVIDEEQALAILG----VKEEVKTSLVDGRVRGTLTKKAGAIVLSSIPCA-VGG 591
Cdd:COG1643 554 plAKKEWLVAAELVGGAAEA-RIRLAAPIDPEWLEELAAhlikRYSEPHWDKKRGRVVARERVRLGALVLVSRPLPgPDP 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 592 DVAKQALAKAISEEGLGLFVFSEKAQGLLDRLRLLHEAEGDPWPDVeSVDPLL-----WLGPELDALAQGKAASGIDMYP 666
Cdd:COG1643 633 EAAREALLRALRREGLDLLPWSKAARQLRARVEFLERKLGERWPDV-SDEALLatledWLAPYLTGVRSLKDLKRLDLLA 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 667 ALQRLLPWPEAARLGELTPERLEVPSGRSVAIDYSGERPVVRVKLQECFGLESSPVICG--KPVQFHLLSPAGRPLAVTD 744
Cdd:COG1643 712 ALRALLPWEQQQRLDELAPTHLTVPSGSRLPLDYSADGPPVAVRLQELFGLAETPGVADgrVPVPLHLLSPAGRPLQVTW 791
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 2223159747 745 DLASFWAGPYHGVRAEMRGRYPKHPWPEDPTTAVATAKTNRRLSK 789
Cdd:COG1643 792 DLPGFWRGSYAEVRKELRGRYPKHPWPDDPAAAAPTRRTKRRMPR 836
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
15-787 |
4.23e-173 |
|
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: 518.94 E-value: 4.23e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgEGAPgAVVVQAPPGTGKTTFLPPLL--ANEVSGKVICVAPRRVAVRAAAHRLHHLAPTVPG--V 90
Cdd:TIGR01970 1 LPIHAVLPALRDAL--AAHP-QVVLEAPPGAGKSTAVPLALldAPGIGGKIIMLEPRRLAARSAAQRLASQLGEAVGqtV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 91 GFTIRGEQ--TPSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRE-LRDDLRLVAMSATVE 167
Cdd:TIGR01970 78 GYRVRGENkvSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSsLREDLKILAMSATLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 168 SSRFAALIG-GDVVTITSPIYPLEVSYAPIAGRaecsRGFLSELARASREAAVASSDSVLVFVPGVREVRIVVEALEcdP 246
Cdd:TIGR01970 158 GERLSSLLPdAPVVESEGRSFPVEIRYLPLRGD----QRLEDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQLA--E 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 247 RLPHGIEVYPLHGSLSSPEQDAALRADSQ---RIVVATSIAESSITVPGVRTVVDSGLSRVPKRDNLRGMTGLVTISTSQ 323
Cdd:TIGR01970 232 RLDSDVLICPLYGELSLAAQDRAIKPDPQgrrKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 324 SSVEQRAGRAGREGPGTVVRCYSASDFQHFRAAISPEIASADLTQASLFVSAWGG-SFDSFPLLDAPPARTVEQAQATLE 402
Cdd:TIGR01970 312 ASATQRAGRAGRLEPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALELAQWGAkDPSDLRWLDAPPSVALAAARQLLQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 403 QLGAVD-EHGLTTIGKKLVALPTDPRLGRALLEAGSQ-----AAPVIASLGE--DVRG---DVDRELPRLTAL--PRVRR 469
Cdd:TIGR01970 392 RLGALDaQGRLTAHGKAMAALGCHPRLAAMLLSAHSTglaalACDLAALLEErgLPRQggaDLMNRLHRLQQGrqGRGQR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 470 EIARLKKLSTD--RGKV--------ATGTVVGLAFPSLIARNMGKD--YQLASGTRVLAPDFHA----EWIAVADVSLGN 533
Cdd:TIGR01970 472 AQQLAKKLRRRlrFSQAdsgaiashALGLLLALAFPDRIAKRRGQPgrYQLANGRGAVLSAEDAlarePWLVAADLGEGQ 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 534 IGT-PRVRAAAVIDE---EQALAILGVKEE-VKTSLVDGRVRGTLTKKAGAIVLSSIPCA-VGGDVAKQALAKAISEEGL 607
Cdd:TIGR01970 552 GKTaARILLAAPVDEallRQVLPDLVVQVDqVDWDETKGRLVAERQLRIGQLVLKSEPLAnPDPAQIAAALLNYVRQKGL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 608 GLFVFSEKAQGLLDRLRLLHEAEGD-PWPDVESVDPL----LWLGPELDALAQGKAASGIDMYPALQRLLPWPEAARLGE 682
Cdd:TIGR01970 632 SALNWTEELRQWRARVACARSWDPEaDWPDLSDEALLarleTWLEPYLAGVTSLSGLQELDLYDALKNLLPWELQQALDA 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 683 LTPERLEVPSGRSVAIDYS-GERPVVRVKLQECFGLESSPVICG--KPVQFHLLSPAGRPLAVTDDLASFWAGPYHGVRA 759
Cdd:TIGR01970 712 LLPTHWPVPTGNFIAIRYSlDGPPLLAVRLQELFGLAESPRVAQgrVPLTLELLSPAQRPLQVTRDLASFWAGAYREVKK 791
|
810 820
....*....|....*....|....*...
gi 2223159747 760 EMRGRYPKHPWPEDPTTAVATAKTNRRL 787
Cdd:TIGR01970 792 EMKGRYPKHVWPDDPANAAPTKRTKPRG 819
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
15-785 |
6.95e-152 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 463.63 E-value: 6.95e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgEGAPgAVVVQAPPGTGKTTFLPP--LLANEVSGKVICVAPRRVAVRAAAHRLHHLAPTVPG--V 90
Cdd:PRK11664 4 LPVAAVLPELLTAL--KTAP-QVLLKAPTGAGKSTWLPLqlLQHGGINGKIIMLEPRRLAARNVAQRLAEQLGEKPGetV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 91 GFTIRGEQ--TPSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRE-LRDDLRLVAMSATVE 167
Cdd:PRK11664 81 GYRMRAESkvGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVQQgLRDDLKLLIMSATLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 168 SSRFAALIGgDVVTITSP--IYPLEVSYAPIAGraecSRGFLSELARASREAAVASSDSVLVFVPGVREVRIVVEALEcd 245
Cdd:PRK11664 161 NDRLQQLLP-DAPVIVSEgrSFPVERRYQPLPA----HQRFDEAVARATAELLRQESGSLLLFLPGVGEIQRVQEQLA-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 246 PRLPHGIEVYPLHGSLSSPEQDAALR---ADSQRIVVATSIAESSITVPGVRTVVDSGLSRVPKRDNLRGMTGLVTISTS 322
Cdd:PRK11664 234 SRVASDVLLCPLYGALSLAEQQKAILpapAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 323 QSSVEQRAGRAGREGPGTVVRCYSASDFQhfRAAIS--PEIASADLTQASLFVSAWGGSfDSFPL--LDAPPARTVEQAQ 398
Cdd:PRK11664 314 QASMTQRAGRAGRLEPGICLHLYSKEQAE--RAAAQsePEILHSDLSGLLLELLQWGCH-DPAQLswLDQPPAAALAAAK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 399 ATLEQLGAVDEHG-LTTIGKKLVALPTDPRLGRALLEAGSQ-------AAPVIASLGEDVRG---DVDRELPRLtaLPRV 467
Cdd:PRK11664 391 RLLQQLGALDGQGrLTARGRKMAALGNDPRLAAMLVAAKEDdeaalatAAKLAAILEEPPRSgssDLGVALSRK--QPHW 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 468 RREIARL-KKLSTDRGKV---ATGTVVGLAFPSLIARNMGKD--YQLASGTRVLAPDFHA----EWIAVADVSLGNIG-T 536
Cdd:PRK11664 469 QQRAQQLlKRLNVRGGEAdssLIAPLLALAFPDRIARRRGQDgrYQLANGMGAMLDADDAlsrhEWLIAPLLLQGSASpD 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 537 PRVRAAAVID----EEQALAILGVKEEVKTSLVDGRVRGTLTKKAGAIVLSSIPCAVGGD-VAKQALAKAISEEGLGLFV 611
Cdd:PRK11664 549 ARILLALPLDidelVQRCPQLVQQSDTVEWDEAKGTLRAWRRLQIGQLTVKVQPLAKPSEeELHQALLNWIRRKGLSVLN 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 612 FSEKAQGLLDRLRLLHE--AEGDpWPDVESVDPL----LWLGPELDALAQGKAASGIDMYPALQRLLPWPEAARLGELTP 685
Cdd:PRK11664 629 WTPEAEQLRLRLLCAAKwlPEYD-WPAVDDESLLasleTWLLPHMTGVRSLRGLKSLNIAQALRGLLDWPQRQRLDSELP 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 686 ERLEVPSGRSVAIDY-SGERPVVRVKLQECFGLESSPVICG--KPVQFHLLSPAGRPLAVTDDLASFWAGPYHGVRAEMR 762
Cdd:PRK11664 708 THYTVPTGSRIAIRYhEDNPPALAVRMQEMFGEAQSPTIAQgrVPLVLELLSPAQRPLQITRDLAAFWQGAYREVQKEMK 787
|
810 820
....*....|....*....|...
gi 2223159747 763 GRYPKHPWPEDPTTAVATAKTNR 785
Cdd:PRK11664 788 GRYPKHVWPDDPANTAPTRRTKK 810
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
15-435 |
1.23e-66 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 241.12 E-value: 1.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgeGAPGAVVVQAPPGTGKTTFLPPL---LANEVSGKVICVAPRRVAVRAAAHRLHHLAPTVPG-- 89
Cdd:PRK11131 73 LPVSQKKQDILEAI---RDHQVVIVAGETGSGKTTQLPKIcleLGRGVKGLIGHTQPRRLAARTVANRIAEELETELGgc 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 90 VGFTIR-----GEQTpssRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAMSA 164
Cdd:PRK11131 150 VGYKVRfndqvSDNT---MVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 165 TVESSRFAA-LIGGDVVTITSPIYPLEVSYAPIAGRAECS-RGFLSELARASREAAVASSDSVLVFVPGVREVRIVVEAL 242
Cdd:PRK11131 227 TIDPERFSRhFNNAPIIEVSGRTYPVEVRYRPIVEEADDTeRDQLQAIFDAVDELGREGPGDILIFMSGEREIRDTADAL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 243 EcDPRLPHgIEVYPLHGSLSSPEQDAALRADS-QRIVVATSIAESSITVPGVRTVVDSGLSRVpKRDNLRGMTGLVTIS- 320
Cdd:PRK11131 307 N-KLNLRH-TEILPLYARLSNSEQNRVFQSHSgRRIVLATNVAETSLTVPGIKYVIDPGTARI-SRYSYRTKVQRLPIEp 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 321 TSQSSVEQRAGRAGREGPGTVVRCYSASDFQHFRAAISPEIASADLTQASLFVSAWG-GSFDSFPLLDAPPARTVEQAQA 399
Cdd:PRK11131 384 ISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGlGDIAAFPFVEAPDKRNIQDGVR 463
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2223159747 400 TLEQLGAVDEHG------LTTIGKKLVALPTDPRLGRALLEA 435
Cdd:PRK11131 464 LLEELGAITTDEqasaykLTPLGRQLAQLPVDPRLARMVLEA 505
|
|
| HrpB_C |
pfam08482 |
ATP-dependent helicase C-terminal; This domain is found near the C-terminus of bacterial ... |
656-773 |
1.61e-62 |
|
ATP-dependent helicase C-terminal; This domain is found near the C-terminus of bacterial ATP-dependent helicases such as HrpB.
Pssm-ID: 430021 [Multi-domain] Cd Length: 126 Bit Score: 205.36 E-value: 1.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 656 GKAASGIDMYPALQRLLPWPEAARLGELTPERLEVPSGRSVAIDYSGE--RPVVRVKLQECFGLESSPVICGK--PVQFH 731
Cdd:pfam08482 5 LADLKRLDLLAALRALLPWEQQQRLDRLAPEHLTVPSGSRIRIDYSAEggAPVLAVRLQELFGLAETPRIAGGrvPLTLH 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2223159747 732 LLSPAGRPLAVTDDLASFWAGPYHGVRAEMRGRYPKHPWPED 773
Cdd:pfam08482 85 LLSPAGRPVQVTRDLASFWAGSYAEVRKEMRGRYPKHPWPED 126
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
15-180 |
2.41e-57 |
|
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: 193.32 E-value: 2.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgeGAPGAVVVQAPPGTGKTTFLPPLLANEV---SGKVICVAPRRVAVRAAAHRLHHLAPTVPG-- 89
Cdd:cd17990 1 LPIAAVLPALRAAL---DAGGQVVLEAPPGAGKTTRVPLALLAELwiaGGKIIVLEPRRVAARAAARRLATLLGEAPGet 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 90 VGFTIRGEQ--TPSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRE-LRDDLRLVAMSATV 166
Cdd:cd17990 78 VGYRVRGESrvGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSATL 157
|
170
....*....|....
gi 2223159747 167 ESSRFAALIGGDVV 180
Cdd:cd17990 158 DGDGLAALLPEAPV 171
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
37-182 |
1.73e-42 |
|
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: 151.46 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 37 VVVQAPPGTGKTTFLPPLL-----ANEVSGKVICVAPRRVAVRAAAHRLHHLAPTVPG--VGFTIRGEQ--TPSSRVEFL 107
Cdd:cd17917 4 VVIVGETGSGKTTQVPQFLledglAKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGeeVGYQIRFESktSSKTRIKFC 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2223159747 108 TPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAMSATVESSRFAALIGG-DVVTI 182
Cdd:cd17917 84 TDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGaPVIHI 159
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
221-345 |
5.33e-42 |
|
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: 150.76 E-value: 5.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 221 SSDSVLVFVPGVREVRIVVEALECDPRLPHG--IEVYPLHGSLSSPEQDAALRADSQ---RIVVATSIAESSITVPGVRT 295
Cdd:cd18791 42 EPGDILVFLPGQEEIERLCELLREELLSPDLgkLLVLPLHSSLPPEEQQRVFEPPPPgvrKVVLATNIAETSITIPGVVY 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2223159747 296 VVDSGLSRVPKRDNLRGMTGLVTISTSQSSVEQRAGRAGREGPGTVVRCY 345
Cdd:cd18791 122 VIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
15-177 |
3.74e-28 |
|
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: 111.38 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgeGAPGAVVVQAPPGTGKTTFLPPLLANEVSGKVICVAPRRVAVRAAAHRLHH--LAPTVPGVGF 92
Cdd:cd17979 1 LPIAQYREKIIELL---KTHQVVIVAGDTGCGKSTQVPQYLLAAGFRHIACTQPRRIACISLAKRVAFesLNQYGSKVAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 93 TIRGE--QTPSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAMSATVESSR 170
Cdd:cd17979 78 QIRFErtRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIEL 157
|
....*..
gi 2223159747 171 FAALIGG 177
Cdd:cd17979 158 FSGYFEG 164
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
15-177 |
1.72e-27 |
|
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: 109.50 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgEGAPgAVVVQAPPGTGKTTFLPPLLANE--VSGK-----VICVAPRRVAVRAAAHRL-HHLAPT 86
Cdd:cd17976 1 LPVDSHKESILSAI--EQNP-VVVISGDTGCGKTTRIPQFILEDyvLRGRgarcnVVITQPRRISAVSVAQRVaHELGPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 87 V-PGVGFTIRGEQTPSSR---VEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAM 162
Cdd:cd17976 78 LrRNVGYQVRLESRPPPRggaLLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLM 157
|
170
....*....|....*
gi 2223159747 163 SATVESSRFAALIGG 177
Cdd:cd17976 158 SATGDNQRLSRYFGG 172
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
15-177 |
5.05e-27 |
|
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: 108.32 E-value: 5.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIFGEGApgaVVVQAPPGTGKTTFLPPLLANE---VSGKVICVAPRRVAVRAAAHRLHHLAPTVPG-- 89
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNV---VIVVGETGSGKTTQLTQYLHEDgytDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGee 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 90 VGFTIRGEQTPSSR--VEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAMSATVE 167
Cdd:cd17983 78 VGYAIRFEDCTSENtvIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMD 157
|
170
....*....|
gi 2223159747 168 SSRFAALIGG 177
Cdd:cd17983 158 ADKFADFFGN 167
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
15-173 |
1.30e-26 |
|
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: 107.20 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgeGAPGAVVVQAPPGTGKTTFLPPLLANE----VSGKVICVAPRRVAVRAAAHRLHHLAPTVPG- 89
Cdd:cd17974 1 LPVYPYRDDLLAAV---KEHQVLIIVGETGSGKTTQIPQYLHEAgytkGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 90 -VGFTIRGEQTPSSR--VEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAMSATV 166
Cdd:cd17974 78 eVGYSIRFEDCTSEKtvLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATM 157
|
....*..
gi 2223159747 167 ESSRFAA 173
Cdd:cd17974 158 DAEKFSA 164
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
6-171 |
3.82e-26 |
|
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: 105.96 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 6 FDLAEIGRGLPVAGHEDELREAIFGEGApgaVVVQAPPGTGKTTFLPPL-----LANEVSGKVICVAPRRVAVRAAAHRL 80
Cdd:cd17973 4 FEILEKRRELPVWEQKEDFLKLLKNNQI---LVLVGETGSGKTTQIPQFvlddeLPHQPKKLVACTQPRRVAAMSVAQRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 81 HHLAPTVPG--VGFTIRGEQTPSSR--VEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDD 156
Cdd:cd17973 81 AEEMDVKLGeeVGYSIRFEDCSSAKtiLKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPD 160
|
170
....*....|....*
gi 2223159747 157 LRLVAMSATVESSRF 171
Cdd:cd17973 161 LKLIVMSATLDAGKF 175
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
15-171 |
4.69e-26 |
|
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: 105.90 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIFGEGApgaVVVQAPPGTGKTTFLPPLL-----ANEVSGKVICVA---PRRVAVRAAAHRLHHlAPT 86
Cdd:cd17982 1 LPILAEEQEIMEAINENPV---VIICGETGSGKTTQVPQFLyeagfGSPESDNPGMIGitqPRRVAAVSMAKRVAE-ELN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 87 VPG--VGFTIRGEQT--PSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDD------ 156
Cdd:cd17982 77 VFGkeVSYQIRYDSTvsENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdq 156
|
170
....*....|....*....
gi 2223159747 157 ----LRLVAMSATVESSRF 171
Cdd:cd17982 157 tvkpLKLVIMSATLRVEDF 175
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
15-172 |
1.55e-25 |
|
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: 104.07 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgeGAPGAVVVQAPPGTGKTTFLPPL---LANEVSGKVICVAPRRVAVRAAAHRLHHLAPTVPG-- 89
Cdd:cd17989 1 LPVSQKRDEIAKAI---AENQVVIIAGETGSGKTTQLPKIcleLGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGga 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 90 VGFTIR-GEQT-PSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAMSATVE 167
Cdd:cd17989 78 VGYKVRfTDQTsDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATID 157
|
....*
gi 2223159747 168 SSRFA 172
Cdd:cd17989 158 AERFS 162
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
15-177 |
4.66e-25 |
|
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: 102.82 E-value: 4.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgeGAPGAVVVQAPPGTGKTTFLPPLLANEVSGKVICVA---PRRVAVRAAAHRLHHLAPTVPG-- 89
Cdd:cd17978 1 LPIYSARKRLLEEL---RKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGMIGitqPRRVAAVSVAKRVAEEMGVELGql 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 90 VGFTIRGEQ--TPSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDD-----LRLVAM 162
Cdd:cd17978 78 VGYSVRFDDvtSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEqklspLKVIIM 157
|
170
....*....|....*
gi 2223159747 163 SATVESSRFAALIGG 177
Cdd:cd17978 158 SATLDADLFSEYFNG 172
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
14-172 |
4.78e-25 |
|
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: 102.56 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 14 GLPVAGHEDELREAIFGEGApgaVVVQAPPGTGKTTFLPPLLANE---VSGKVICVAPRRVAVRAAAHRLHHLAPTVPG- 89
Cdd:cd17971 5 SLPIYKLKEQLIQAVHDNQI---LVVIGETGSGKTTQITQYLAEAgytSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLGq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 90 -VGFTIRGEQ--TPSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAMSATV 166
Cdd:cd17971 82 eVGYTIRFEDctSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSATL 161
|
....*.
gi 2223159747 167 ESSRFA 172
Cdd:cd17971 162 DAVKFS 167
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
36-171 |
6.86e-25 |
|
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: 102.55 E-value: 6.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 36 AVVVQAPPGTGKTTFLPPLLANE---VSGKVI-CVAPRRVAVRAAAHRLHHLAPTVPG--VGFTIRGEQTPSS---RVEF 106
Cdd:cd17980 19 TIVIVGETGCGKSTQIPQYLAEAgwtAGGRVVgCTQPRRVAAVTVAGRVAEEMGAVLGheVGYCIRFDDCTDPqatRIKF 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2223159747 107 LTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAMSATVESSRF 171
Cdd:cd17980 99 LTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDAEKF 163
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
15-172 |
8.62e-24 |
|
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: 99.22 E-value: 8.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIFGEGApgaVVVQAPPGTGKTTFLP-----PLLANEVSGK---VICVAPRRVAVRAAAHRLHHL--A 84
Cdd:cd17975 1 LPVFKHRESILETLKRHRV---VVVAGETGSGKSTQVPqflleDLLLNGGTAQkcnIVCTQPRRISAMSLATRVCEElgC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 85 PTVPG-----VGFTIRGEQ--TPSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDL 157
Cdd:cd17975 78 ESGPGgknslCGYQIRMESrtGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDL 157
|
170
....*....|....*
gi 2223159747 158 RLVAMSATVESSRFA 172
Cdd:cd17975 158 HLILMSATVDCEKFS 172
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
37-177 |
1.49e-23 |
|
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: 98.37 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 37 VVVQAPPGTGKTTFLPP-LLANEVSG------KVICVAPRR-----VAVRAAAHRLHHLAPTVpgvGFTIRGEQTPSS-- 102
Cdd:cd17985 20 LVISGMTGCGKTTQIPQfILDNSLQGpplpvaNIICTQPRRisaisVAERVAQERAERVGQSV---GYQIRLESVKSSat 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2223159747 103 RVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAMSATVESSRFAALIGG 177
Cdd:cd17985 97 RLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATLNAELFSDYFNS 171
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
15-172 |
1.71e-20 |
|
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: 89.52 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgeGAPGAVVVQAPPGTGKTTFLPPLLANEV-------SGKVICVAPRR-----VAVRAAAHRLHH 82
Cdd:cd17981 1 LPSYGMKQEIINMI---DNNQVTVISGETGCGKTTQVTQFILDDAiergkgsSCRIVCTQPRRisaisVAERVAAERAES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 83 LApTVPGVGFTIRGE-QTPSSR--VEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRL 159
Cdd:cd17981 78 CG-LGNSTGYQIRLEsRKPRKQgsILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKV 156
|
170
....*....|...
gi 2223159747 160 VAMSATVESSRFA 172
Cdd:cd17981 157 ILMSATLNAEKFS 169
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
15-182 |
9.95e-20 |
|
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: 87.22 E-value: 9.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgEGAPgAVVVQAPPGTGKTTFLPPLLAN---EVSGKVICVAPRRVAVRAAAHRLHHLAPTVPG-- 89
Cdd:cd17984 1 LPIQKQRKKLVQAV--RDNS-FLIVTGNTGSGKTTQLPKYLYEagfSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 90 VGFTIRGEQTPSSR--VEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRD-----DLRLVAM 162
Cdd:cd17984 78 VGYQVRFDDCSSKEtaIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVVM 157
|
170 180
....*....|....*....|.
gi 2223159747 163 SATVESSRFAALIGG-DVVTI 182
Cdd:cd17984 158 SATLELAKLSAFFGNcPVFDI 178
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
37-190 |
2.47e-19 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 86.78 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 37 VVVQAPPGTGKTTFLP-PLLA---NEVSGKVICVAPRRVAVRAAAHRLHHLAPTVPGVGFTIRGEQTPSSRVEFL----- 107
Cdd:smart00487 27 VILAAPTGSGKTLAALlPALEalkRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLesgkt 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 108 -----TPGVLLRRMLHDP-ELSGVDAVIVDEVHER--QLDTDIVLGMlveLRELRDDLRLVAMSATVESS--RFAALIGG 177
Cdd:smart00487 107 dilvtTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKL---LKLLPKNVQLLLLSATPPEEieNLLELFLN 183
|
170
....*....|...
gi 2223159747 178 DVVTITSPIYPLE 190
Cdd:smart00487 184 DPVFIDVGFTPLE 196
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
15-171 |
3.30e-19 |
|
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: 87.58 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIFGEGApgaVVVQAPPGTGKTTFLPPLLANE-------VSGKVICVAPRR-----VAVRAAAHRLHH 82
Cdd:cd17972 59 LPVKKFREEILEAISNNPV---VIIRGATGCGKTTQVPQYILDDfiqndraAECNIVVTQPRRisavsVAERVAFERGEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 83 LAPTVpgvGFTIRGEQT---PSSRVEFLTPGVLLRRMlhDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRL 159
Cdd:cd17972 136 VGKSC---GYSVRFESVlprPHASILFCTVGVLLRKL--EAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRV 210
|
170
....*....|..
gi 2223159747 160 VAMSATVESSRF 171
Cdd:cd17972 211 ILMSATIDTSMF 222
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
15-177 |
1.66e-18 |
|
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: 83.73 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgEGAPgAVVVQAPPGTGKTTFLPPLL-----ANEVSGKVICVAPRRVAV-----RAAAHRLHHLA 84
Cdd:cd17987 1 LPVFEKQEQIVRII--KENK-VVLIVGETGSGKTTQIPQFLlddcyANGIPCRIFCTQPRRLAAiavaeRVAAERGEKIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 85 PTVpgvGFTIRGEQ--TPSSRVEFLTPGVLLRR-MLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVA 161
Cdd:cd17987 78 QTV---GYQIRLESrvSPKTLLTFCTNGVLLRTlMAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLIL 154
|
170
....*....|....*.
gi 2223159747 162 MSATVESSRFAALIGG 177
Cdd:cd17987 155 SSAALDVNLFIRYFGS 170
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
2-339 |
1.66e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 80.45 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 2 TRELFDLAEIGRGLPVAGHEDELR----EAI-----FGEGAPGAVVVQAPPGTGKT-TFLppLLANEV--SGKVICVAPR 69
Cdd:COG1061 59 ERELAEAEALEAGDEASGTSFELRpyqqEALeallaALERGGGRGLVVAPTGTGKTvLAL--ALAAELlrGKRVLVLVPR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 70 RVAVRAAAHRLHHLAPTVPGVGftirGEQTPSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHErqldtdIVLGMLVE 149
Cdd:COG1061 137 RELLEQWAEELRRFLGDPLAGG----GKKDSDAPITVATYQSLARRAHLDELGDRFGLVIIDEAHH------AGAPSYRR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 150 LRELRDDLRLVAMSATVESS----RFAALIGGDVVTITSP------------IYPLEVSYAPIAGRAECSRGFLSELARA 213
Cdd:COG1061 207 ILEAFPAAYRLGLTATPFRSdgreILLFLFDGIVYEYSLKeaiedgylappeYYGIRVDLTDERAEYDALSERLREALAA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 214 SREAAV----------ASSDSVLVFVPGVREVRIVVEALEcdprlPHGIEVYPLHGSLSSPEQD---AALRADSQRIVVA 280
Cdd:COG1061 287 DAERKDkilrellrehPDDRKTLVFCSSVDHAEALAELLN-----EAGIRAAVVTGDTPKKEREeilEAFRDGELRILVT 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2223159747 281 TSIAESSITVPGVRTVVdsglsrvpkrdnlrgmtgLVTISTSQSSVEQRAGRAGREGPG 339
Cdd:COG1061 362 VDVLNEGVDVPRLDVAI------------------LLRPTGSPREFIQRLGRGLRPAPG 402
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
220-337 |
2.34e-14 |
|
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: 69.55 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 220 ASSDSVLVFVPGVREVRIvvEALecdpRLPHGIEVYPLHGSLSSPEQDAAL---RADSQRIVVATSIAESSITVPGVRTV 296
Cdd:pfam00271 13 ERGGKVLIFSQTKKTLEA--ELL----LEKEGIKVARLHGDLSQEEREEILedfRKGKIDVLVATDVAERGLDLPDVDLV 86
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2223159747 297 VDSGLSRVPkrdnlrgmtglvtistsqSSVEQRAGRAGREG 337
Cdd:pfam00271 87 INYDLPWNP------------------ASYIQRIGRAGRAG 109
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
126-348 |
4.87e-14 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 75.78 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 126 DAVIVDEVHERQLDTDIVLGMLvelRELRDDLR-LVAMSATVESSRFAAL----------IGGDVVTITSPIYpLEVSYA 194
Cdd:PHA02653 293 GTVIIDEVHEHDQIGDIIIAVA---RKHIDKIRsLFLMTATLEDDRDRIKeffpnpafvhIPGGTLFPISEVY-VKNKYN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 195 PIAGRA--ECSRGFLSELARASREAAvasSDSVLVFVPGVREVRIVVEALEcdPRLPhGIEVYPLHGSLssPEQDAALRA 272
Cdd:PHA02653 369 PKNKRAyiEEEKKNIVTALKKYTPPK---GSSGIVFVASVSQCEEYKKYLE--KRLP-IYDFYIIHGKV--PNIDEILEK 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 273 --DSQR--IVVATSIAESSITVPGVRTVVDSGLSRVPKrdnlrgMTGLVTISTSQSSVEQRAGRAGREGPGTVVRCYSAS 348
Cdd:PHA02653 441 vySSKNpsIIISTPYLESSVTIRNATHVYDTGRVYVPE------PFGGKEMFISKSMRTQRKGRVGRVSPGTYVYFYDLD 514
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
15-172 |
7.71e-13 |
|
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: 67.53 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 15 LPVAGHEDELREAIfgeGAPGAVVVQAPPGTGKTTFLPPLLANEVSGK-----VICVAPRRVAVRAAAHRLHHLAPTVPG 89
Cdd:cd17988 1 LPIYAKREEILSLI---EANSVVIIKGATGCGKTTQLPQFILDHYYKRgkycnIVVTQPRRIAAISIARRVSQEREWTLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 90 --VGFTI--RGEQTPSSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLgmLVELRELRDDLRLVA---M 162
Cdd:cd17988 78 slVGYQVglERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLL--LVVRRLLRTNSRHVKiilM 155
|
170
....*....|
gi 2223159747 163 SATVESSRFA 172
Cdd:cd17988 156 SATISCKEFA 165
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
250-337 |
8.77e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.16 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 250 HGIEVYPLHGSLSSPEQDAAL---RADSQRIVVATSIAESSITVPGVRTVVDSGLSRvpkrdnlrgmtglvtistSQSSV 326
Cdd:smart00490 10 LGIKVARLHGGLSQEEREEILdkfNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPW------------------SPASY 71
|
90
....*....|.
gi 2223159747 327 EQRAGRAGREG 337
Cdd:smart00490 72 IQRIGRAGRAG 82
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
31-176 |
4.36e-12 |
|
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: 65.30 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 31 EGAPGAVVVQAPPGTGKTTFLPPLLANEV------SGKVICVAPRRVAVRAAAHRLHHLAPTVPG--VGFTIRGEQ--TP 100
Cdd:cd17986 15 ESPSGIVLVSGEPGSGKSTQVPQWCAEFAlsrgfqKGQVTVTQPHPLAARSLALRVADEMDLNLGheVGYSIPQEDctGP 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2223159747 101 SSRVEFLTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAMSATVESSRFAALIG 176
Cdd:cd17986 95 NTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPALEPKLRAFWG 170
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
37-166 |
2.30e-10 |
|
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: 59.95 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 37 VVVQAPPGTGKTT-FLPPLLA----NEVSGKVICVAPRRVAVRAAAHRLHHLA-PTVPGVGFTIRGEQTPS-----SRVE 105
Cdd:pfam00270 17 VLVQAPTGSGKTLaFLLPALEaldkLDNGPQALVLAPTRELAEQIYEELKKLGkGLGLKVASLLGGDSRKEqleklKGPD 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2223159747 106 FL--TPGVLLRRMLHDPELSGVDAVIVDEVHeRQLDTDIVLGMLVELRELRDDLRLVAMSATV 166
Cdd:pfam00270 97 ILvgTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
37-176 |
4.80e-10 |
|
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: 59.45 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 37 VVVQAPPGTGKTTFLPP------LLANEVSGKVICVAPRRVAVRAAAHRLHHLAPTVPG--VGFTIRGEQ--TPSSRVEF 106
Cdd:cd17977 20 VIVSGDAKTGKSSQIPQwcaeycLSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIGheVGYVIPFENccTNETILRY 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 107 LTPGVLLRRMLHDPELSGVDAVIVDEVHERQLDTDIVLGMLVELRELRDDLRLVAMSATVESSRFAALIG 176
Cdd:cd17977 100 CTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPHLSSKLLSYYG 169
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
37-173 |
7.06e-08 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 52.59 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 37 VVVQAPPGTGKT--TFLPPLLA----NEVSGKVICVAPRRVAVRAAAHRLHHLAP-TVPGVGFTIR-GEQTPSSRVEFL- 107
Cdd:cd17922 4 VLIAAPTGSGKTeaAFLPALSSladePEKGVQVLYISPLKALINDQERRLEEPLDeIDLEIPVAVRhGDTSQSEKAKQLk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 108 -TPGVL------LRRML----HDPELSGVDAVIVDEVHErQLDTD---IVLGMLVELRELRD-DLRLVAMSATVESSRFA 172
Cdd:cd17922 84 nPPGILittpesLELLLvnkkLRELFAGLRYVVVDEIHA-LLGSKrgvQLELLLERLRKLTGrPLRRIGLSATLGNLEEA 162
|
.
gi 2223159747 173 A 173
Cdd:cd17922 163 A 163
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
400-478 |
8.06e-08 |
|
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: 51.08 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 400 TLEQLGAVDEHG-LTTIGKKLVALPTDPRLGRALLEAGSQ--AAPVIA--------------SLGEDVRGDVDRELPRLT 462
Cdd:pfam04408 4 LLYYLGALDEDGeLTPLGRKMAELPLDPRLAKMLLAAAELgcLDEVLTivaalsvrdpfvqpNFLDPRSAAKAARRRRRA 83
|
90
....*....|....*.
gi 2223159747 463 ALPRVRREIARLKKLS 478
Cdd:pfam04408 84 ADEKARAKFARLDLEG 99
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
37-342 |
1.15e-07 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 55.61 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 37 VVVQAPPGTGKT-TFLPPLL---ANEVSGKVICVAPRRvavrAAAH----RLHHLA-PTVPGVG-FTIRGEqTP------ 100
Cdd:COG1205 74 VVIATPTASGKSlAYLLPVLealLEDPGATALYLYPTK----ALARdqlrRLRELAeALGLGVRvATYDGD-TPpeerrw 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 101 ---SSRVEFLTPGVLLRRMLHDPE-----LSGVDAVIVDEVHE-RQldtdiVLGM---LVeLRELR-------DDLRLVA 161
Cdd:COG1205 149 ireHPDIVLTNPDMLHYGLLPHHTrwarfFRNLRYVVIDEAHTyRG-----VFGShvaNV-LRRLRricrhygSDPQFIL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 162 MSATVESSR--FAALIGGDVVTIT---SPIYPLE-VSYAPIAGRAECSRGFLSELARASREAAVASSdSVLVFVPGVREV 235
Cdd:COG1205 223 ASATIGNPAehAERLTGRPVTVVDedgSPRGERTfVLWNPPLVDDGIRRSALAEAARLLADLVREGL-RTLVFTRSRRGA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 236 ----RIVVEALEcDPRLPHGIEVYplHGSLSsPEQ----DAALRADSQRIVVATSIAESSITVPGVRTVVDSGlsrVPKr 307
Cdd:COG1205 302 ellaRYARRALR-EPDLADRVAAY--RAGYL-PEErreiERGLRSGELLGVVSTNALELGIDIGGLDAVVLAG---YPG- 373
|
330 340 350
....*....|....*....|....*....|....*.
gi 2223159747 308 dnlrgmtglvtistSQSSVEQRAGRAGREG-PGTVV 342
Cdd:COG1205 374 --------------TRASFWQQAGRAGRRGqDSLVV 395
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
37-165 |
1.90e-07 |
|
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: 50.86 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 37 VVVQAPPGTGKTTFLPP---LLANEVSGKVICVAPRR-VAVRAAAH---RLHHLAPTVPGVGFTIRGEQT----PSSRVE 105
Cdd:cd00046 4 VLITAPTGSGKTLAALLaalLLLLKKGKKVLVLVPTKaLALQTAERlreLFGPGIRVAVLVGGSSAEEREknklGDADII 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2223159747 106 FLTPGVLLRRMLHD--PELSGVDAVIVDEVHERQLDTD-IVLGMLVELRELRDDLRLVAMSAT 165
Cdd:cd00046 84 IATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRgALILDLAVRKAGLKNAQVILLSAT 146
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
403-473 |
2.42e-07 |
|
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: 48.80 E-value: 2.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2223159747 403 QLGAVDEHG-LTTIGKKLVALPTDPRLGRALLEAGSQ--AAPVIASLGEDVRGDVdRELPRLTALPRVRREIAR 473
Cdd:smart00847 1 ELGALDDDGrLTPLGRKMAELPLDPRLAKMLLAAAEFgcLDEILTIVAMLSVGDP-RPKEKREDADAARRRFAD 73
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
37-339 |
1.44e-06 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 51.82 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 37 VVVQAPPGTGKTtflppLLA-----NEV--SGKVICVAPrrvaVRAAAH--------RLHHLAPTVpGV---GFTIRGEQ 98
Cdd:COG1204 41 LVVSAPTASGKT-----LIAelailKALlnGGKALYIVP----LRALASekyrefkrDFEELGIKV-GVstgDYDSDDEW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 99 TPSSRVEFLTP---GVLLRrmlHDPE-LSGVDAVIVDEVHerQLDTD---IVLGMLVE-LRELRDDLRLVAMSATVESSR 170
Cdd:COG1204 111 LGRYDILVATPeklDSLLR---NGPSwLRDVDLVVVDEAH--LIDDEsrgPTLEVLLArLRRLNPEAQIVALSATIGNAE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 171 -FAALIGGDVVTIT-SP-------IYPLEVSYAPIAgraecSRGFLSELARASReaAVASSDSVLVFVPGVREVRIVVEA 241
Cdd:COG1204 186 eIAEWLDAELVKSDwRPvplnegvLYDGVLRFDDGS-----RRSKDPTLALALD--LLEEGGQVLVFVSSRRDAESLAKK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 242 L--ECDPRLPHG------------IEV-------YPL-----------HGSLSSPEQDA---ALRADSQRIVVATS-IAE 285
Cdd:COG1204 259 LadELKRRLTPEereeleelaeelLEVseethtnEKLadclekgvafhHAGLPSELRRLvedAFREGLIKVLVATPtLAA 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2223159747 286 ssitvpGV----RTVVdsglsrVpkRDNLRGmtGLVTISTSQssVEQRAGRAGRegPG 339
Cdd:COG1204 339 ------GVnlpaRRVI------I--RDTKRG--GMVPIPVLE--FKQMAGRAGR--PG 376
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
23-185 |
8.75e-06 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 46.87 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 23 ELREAIFGEGApgAVVVQAPPGTGKTTFLppLLA-----NEVSGKVICVAPRRVAVRAAAHRLHH-LAPTVPGVG----- 91
Cdd:cd17921 8 EALRALYLSGD--SVLVSAPTSSGKTLIA--ELAilralATSGGKAVYIAPTRALVNQKEADLRErFGPLGKNVGlltgd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 92 FTIRGEQTPSSRVEFLTP---GVLLRRmLHDPELSGVDAVIVDEVH-----ERqldtdivlGMLVE-----LRELRDDLR 158
Cdd:cd17921 84 PSVNKLLLAEADILVATPeklDLLLRN-GGERLIQDVRLVVVDEAHligdgER--------GVVLElllsrLLRINKNAR 154
|
170 180
....*....|....*....|....*...
gi 2223159747 159 LVAMSATVESSR-FAALIgGDVVTITSP 185
Cdd:cd17921 155 FVGLSATLPNAEdLAEWL-GVEDLIRFD 181
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
38-165 |
7.10e-04 |
|
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350689 [Multi-domain] Cd Length: 151 Bit Score: 41.00 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 38 VVQAPPGTGKTTFLPPLLANEV---SGKVICVAPRRVAVRAAAHRLHHLAPTVPGVGFTIrgEQTPSSRVEFLTPGVLLR 114
Cdd:cd17931 5 VLDLHPGAGKTTRVLPQIIREAikkRLRTLVLAPTRVVAAEMYEALRGLPIRYRTGAVKE--EHGGNEIVDYMCHGTFTC 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2223159747 115 RMLHDPELSGVDAVIVDEVHerQLDTDIVLGM-LVELRELRDDLRLVAMSAT 165
Cdd:cd17931 83 RLLSPKRVPNYNLIIMDEAH--FTDPASIAARgYIHTRVEMGEAAVIFMTAT 132
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
195-347 |
1.46e-03 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 39.94 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 195 PIAGRAECSRGFLSELARASREAAVASSDSVLVFVPGVREVRIVVEAL-ECDPRLPHGIEVYPLHGSLSSPEQD---AAL 270
Cdd:cd18796 11 PVAPEIFPWAGESGADAYAEVIFLLERHKSTLVFTNTRSQAERLAQRLrELCPDRVPPDFIALHHGSLSRELREeveAAL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2223159747 271 RADSQRIVVATSIAESSITVPGVRTVVDSGlsrVPKrdnlrgmtglvtistSQSSVEQRAGRAGREGPGTVVRCYSA 347
Cdd:cd18796 91 KRGDLKVVVATSSLELGIDIGDVDLVIQIG---SPK---------------SVARLLQRLGRSGHRPGAASKGRLVP 149
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
277-338 |
2.07e-03 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 37.68 E-value: 2.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2223159747 277 IVVATSIAESSITVPGVRTVVdsglsrvpkrdnlrgmtgLVTISTSQSSVEQRAGRAGREGP 338
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVI------------------FFDPPSSAASYIQRVGRAGRGGK 68
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
39-122 |
2.69e-03 |
|
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain] Cd Length: 234 Bit Score: 40.31 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 39 VQAPPGTGKTT---FLPPLLANEVSGKVICVAPRRVAVRAAAHRLHHLAPTVPGVGFTIRgEQTPSSrVEFLTPGVLLRR 115
Cdd:cd18039 21 IQGPPGTGKTVtsaTIVYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLCAKSR-EAVESP-VSFLALHNQVRN 98
|
....*..
gi 2223159747 116 MLHDPEL 122
Cdd:cd18039 99 LDSAEKL 105
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
25-161 |
4.16e-03 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 38.35 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 25 REAIFGEGAPGAVVVQAPPGTGKTTFLPPLLA-----NEVSGKVICVAPRRVAVRAAAHRLHHLAPTVPG-VGFTIRGeq 98
Cdd:pfam13245 2 REAVRTALPSKVVLLTGGPGTGKTTTIRHIVAllvalGGVSFPILLAAPTGRAAKRLSERTGLPASTIHRlLGFDDLE-- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2223159747 99 tpssrvefltPGVLLRRMLHDPElsgVDAVIVDEVHerqlDTDIVLgMLVELRELRDDLRLVA 161
Cdd:pfam13245 80 ----------AGGFLRDEEEPLD---GDLLIVDEFS----MVDLPL-AYRLLKALPDGAQLLL 124
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
122-282 |
4.35e-03 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 40.47 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 122 LSGVDAVIVDEVHErqldtdiVLG---------MLVELRELR-DDLRLVAMSATVES-SRFAALIGG-----DVVTITSP 185
Cdd:COG1201 159 LRGVRTVIVDEIHA-------LAGskrgvhlalSLERLRALApRPLQRIGLSATVGPlEEVARFLVGyedprPVTIVDAG 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 186 ---------IYPLEVSYAPIAGRAECSRGFLSELArasreAAVASSDSVLVFVPGVREVRIVVEAL-ECDPRLPHGIEVY 255
Cdd:COG1201 232 agkkpdlevLVPVEDLIERFPWAGHLWPHLYPRVL-----DLIEAHRTTLVFTNTRSQAERLFQRLnELNPEDALPIAAH 306
|
170 180 190
....*....|....*....|....*....|.
gi 2223159747 256 plHGSLsSPEQ----DAALRADSQRIVVATS 282
Cdd:COG1201 307 --HGSL-SREQrlevEEALKAGELRAVVATS 334
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
37-183 |
7.70e-03 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 38.58 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 37 VVVQAPPGTGKT-TFLPPLLAN-----EVSGK---VICVAPRR--------VAVRAAAHRLHHLAPTVPGVGFTiRGEQT 99
Cdd:cd00268 30 VIGQAQTGSGKTlAFLLPILEKllpepKKKGRgpqALVLAPTRelamqiaeVARKLGKGTGLKVAAIYGGAPIK-KQIEA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2223159747 100 PSSRVEFL--TPGVLL----RRMLHdpeLSGVDAVIVDEV-------HERQLDtDIvlgmlveLRELRDDLRLVAMSATV 166
Cdd:cd00268 109 LKKGPDIVvgTPGRLLdlieRGKLD---LSNVKYLVLDEAdrmldmgFEEDVE-KI-------LSALPKDRQTLLFSATL 177
|
170
....*....|....*....
gi 2223159747 167 ESS--RFAALIGGDVVTIT 183
Cdd:cd00268 178 PEEvkELAKKFLKNPVRIE 196
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
25-73 |
8.55e-03 |
|
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain] Cd Length: 191 Bit Score: 38.36 E-value: 8.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2223159747 25 REAI-FGEGAPGAVVVQAPPGTGKTTFLPPLLANEV--SGKVICVAPRRVAV 73
Cdd:cd18044 7 KEAVkFALSQKDVALIHGPPGTGKTTTVVEIILQAVkrGEKVLACAPSNIAV 58
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
37-73 |
9.84e-03 |
|
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong 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: 438708 [Multi-domain] Cd Length: 121 Bit Score: 36.83 E-value: 9.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2223159747 37 VVVQAPPGTGKTTFLPPLLANEVSG----KVICVAPRRVAV 73
Cdd:cd17934 2 SLIQGPPGTGKTTTIAAIVLQLLKGlrgkRVLVTAQSNVAV 42
|
|
| |
