|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
4-779 |
0e+00 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 755.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 4 NLSVIGAGLPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPI---AHNVTGGKVIVVAPRRVAVRAAAHHL-EQLDr 79
Cdd:COG1643 2 SLITYPPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLAlleLGWGAGGRIGMLEPRRLAARAAAERMaEELG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 80 nscdQPSTHRVGYTIRGER--SRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRE-LRDD 156
Cdd:COG1643 81 ----EPVGETVGYRVRFEDkvSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPaLRPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 157 LTVIAMSATVDAPRFAELLspeHPAPIVETHAEIHPLELHYQPAAERialSRSYMDHVCTVTQRAVAHSTDSALVFLPTI 236
Cdd:COG1643 157 LKLLVMSATLDAERFARLL---GDAPVIESSGRTYPVEVRYRPLPAD---ERDLEDAVADAVREALAEEPGDILVFLPGE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 237 AAVTTVVSALEQR--TSVPVYPLHGQLTSSEQDAALR---AGRQRIVVATSIAESSLTVPGVRIVVDAGLSRVPKRDRAR 311
Cdd:COG1643 231 REIRRTAEALRGRlpPDTEILPLYGRLSAAEQDRAFApapHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 312 DLTGLVTTSTSQAQADQRAGRAGREGPGTVYRLYSAAEFQHFPDHVTPEIRSADLTQAALCLTAWGCTDPAQFPLLSTPP 391
Cdd:COG1643 311 GVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 392 KQSWEQAVDTLRDIGALNAAGQITELGRTLATLPTDPRLGASLL-----HCGGGAAPTIAALSLD------ARGDIP--- 457
Cdd:COG1643 391 ARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLaaaelGCLREAAILAALLSERdprrgaAGSDLLarl 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 458 RAIAAMSHQQ----------RFTREVARLAGFV-------PDSECTPGEAIARAWPKNVARRDGDS--YLMAGGSRAELG 518
Cdd:COG1643 471 NLWRRLREQQreflsylrlrEWRDLARQLRRLLgeganeePADYEAIGLLLALAYPDRIARRRGEGgrYLLARGRGAALF 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 519 -VSSLSGHEWLAVAQASLTHRGSVIRSAAPISEAAAVDIIG--VAERTEATL--VDGSLRGTRIRHAGAITLSTTNV-KV 592
Cdd:COG1643 551 pGSPLAKKEWLVAAELVGGAAEARIRLAAPIDPEWLEELAAhlIKRYSEPHWdkKRGRVVARERVRLGALVLVSRPLpGP 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 593 EGELAEQALAEGIRTHGLELFTFSDKATELRDRLRHLHEYYGEPWPDVDaaDPTL------WLGPEIAALVAGTPAARID 666
Cdd:COG1643 631 DPEAAREALLRALRREGLDLLPWSKAARQLRARVEFLERKLGERWPDVS--DEALlatledWLAPYLTGVRSLKDLKRLD 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 667 LYPALQRLLPWPEATRLDELAPAVLELPNGRRARISYAGDRPVLSTKLQDCFGLLESPIVC-GR-PLQFHLLSPAGRPLA 744
Cdd:COG1643 709 LLAALRALLPWEQQQRLDELAPTHLTVPSGSRLPLDYSADGPPVAVRLQELFGLAETPGVAdGRvPVPLHLLSPAGRPLQ 788
|
810 820 830
....*....|....*....|....*....|....*
gi 753871158 745 VTDTLDSFWAGPYQQVRSDMRGRYPKHPWPEDPLT 779
Cdd:COG1643 789 VTWDLPGFWRGSYAEVRKELRGRYPKHPWPDDPAA 823
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
12-779 |
8.60e-177 |
|
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: 528.18 E-value: 8.60e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVP--PIAHNVTGGKVIVVAPRRVAVRAAAHHLEQLdrnsCDQPSTHR 89
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPlaLLDAPGIGGKIIMLEPRRLAARSAAQRLASQ----LGEAVGQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 90 VGYTIRGER--SRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRE-LRDDLTVIAMSATV 166
Cdd:TIGR01970 77 VGYRVRGENkvSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSsLREDLKILAMSATL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 167 DAPRFAELLsPEhpAPIVETHAEIHPLELHYQPAAERIALsrsyMDHVCTVTQRAVAHSTDSALVFLPTIAAVTTVVSAL 246
Cdd:TIGR01970 157 DGERLSSLL-PD--APVVESEGRSFPVEIRYLPLRGDQRL----EDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 247 EQR--TSVPVYPLHGQLTSSEQDAALR---AGRQRIVVATSIAESSLTVPGVRIVVDAGLSRVPKRDRARDLTGLVTTST 321
Cdd:TIGR01970 230 AERldSDVLICPLYGELSLAAQDRAIKpdpQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 322 SQAQADQRAGRAGREGPGTVYRLYSAAEFQHFPDHVTPEIRSADLTQAALCLTAWGCTDPAQFPLLSTPPKQSWEQAVDT 401
Cdd:TIGR01970 310 SQASATQRAGRAGRLEPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 402 LRDIGALNAAGQITELGRTLATLPTDPRLGASLLHCGGGA----APTIAALsLDARG-------DIPRAIAAMS------ 464
Cdd:TIGR01970 390 LQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGlaalACDLAAL-LEERGlprqggaDLMNRLHRLQqgrqgr 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 465 --HQQRFTREVARLAGF-VPDSECTPGEAI----ARAWPKNVARRDGDS--YLMAGGSRAELGV-SSLSGHEWLAVA--Q 532
Cdd:TIGR01970 469 gqRAQQLAKKLRRRLRFsQADSGAIASHALglllALAFPDRIAKRRGQPgrYQLANGRGAVLSAeDALAREPWLVAAdlG 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 533 ASLTHRGSVIRSAAPISEAAAV----DIIGVAERTEATLVDGSLRGTRIRHAGAITLSTTNV-KVEGELAEQALAEGIRT 607
Cdd:TIGR01970 549 EGQGKTAARILLAAPVDEALLRqvlpDLVVQVDQVDWDETKGRLVAERQLRIGQLVLKSEPLaNPDPAQIAAALLNYVRQ 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 608 HGLELFTFSDKATELRDRLRHLHEYYGE-PWPDVD----AADPTLWLGPEIAALVAGTPAARIDLYPALQRLLPWPEATR 682
Cdd:TIGR01970 629 KGLSALNWTEELRQWRARVACARSWDPEaDWPDLSdealLARLETWLEPYLAGVTSLSGLQELDLYDALKNLLPWELQQA 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 683 LDELAPAVLELPNGRRARISYAGD-RPVLSTKLQDCFGLLESPIVCG--RPLQFHLLSPAGRPLAVTDTLDSFWAGPYQQ 759
Cdd:TIGR01970 709 LDALLPTHWPVPTGNFIAIRYSLDgPPLLAVRLQELFGLAESPRVAQgrVPLTLELLSPAQRPLQVTRDLASFWAGAYRE 788
|
810 820
....*....|....*....|
gi 753871158 760 VRSDMRGRYPKHPWPEDPLT 779
Cdd:TIGR01970 789 VKKEMKGRYPKHVWPDDPAN 808
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
12-777 |
5.12e-159 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 482.12 E-value: 5.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPP--IAHNVTGGKVIVVAPRRVAVRAAAHHL-EQLDrnscdQPSTH 88
Cdd:PRK11664 4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLqlLQHGGINGKIIMLEPRRLAARNVAQRLaEQLG-----EKPGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 89 RVGYTIRGER--SRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRE-LRDDLTVIAMSAT 165
Cdd:PRK11664 79 TVGYRMRAESkvGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVQQgLRDDLKLLIMSAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 166 VDAPRFAELLsPEhpAPIVETHAEIHPLELHYQP--AAERIAlsrsymDHVCTVTQRAVAHSTDSALVFLPTIAAVTTVV 243
Cdd:PRK11664 159 LDNDRLQQLL-PD--APVIVSEGRSFPVERRYQPlpAHQRFD------EAVARATAELLRQESGSLLLFLPGVGEIQRVQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 244 SALEQRTS--VPVYPLHGQLTSSEQDAALR---AGRQRIVVATSIAESSLTVPGVRIVVDAGLSRVPKRDRARDLTGLVT 318
Cdd:PRK11664 230 EQLASRVAsdVLLCPLYGALSLAEQQKAILpapAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 319 TSTSQAQADQRAGRAGREGPGTVYRLYSAAEFQHFPDHVTPEIRSADLTQAALCLTAWGCTDPAQFPLLSTPPKQSWEQA 398
Cdd:PRK11664 310 QRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 399 VDTLRDIGALNAAGQITELGRTLATLPTDPRLgASLLHCGGG---AAPTIAALSLDARGDIPRAIAA-MSH--------- 465
Cdd:PRK11664 390 KRLLQQLGALDGQGRLTARGRKMAALGNDPRL-AAMLVAAKEddeAALATAAKLAAILEEPPRSGSSdLGValsrkqphw 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 466 QQRFTREVARL--AGFVPDSECTPgEAIARAWPKNVARRDGDS--YLMAGGSRAELGV-SSLSGHEWLAVAQASLTHRGs 540
Cdd:PRK11664 469 QQRAQQLLKRLnvRGGEADSSLIA-PLLALAFPDRIARRRGQDgrYQLANGMGAMLDAdDALSRHEWLIAPLLLQGSAS- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 541 virSAAPISEAAAVDIIGVAER-----TEATLVD-----GSLRGTRIRHAGAITLSTTNV-KVEGELAEQALAEGIRTHG 609
Cdd:PRK11664 547 ---PDARILLALPLDIDELVQRcpqlvQQSDTVEwdeakGTLRAWRRLQIGQLTVKVQPLaKPSEEELHQALLNWIRRKG 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 610 LELFTFSDKATELRDRLRHLHEYYGE-PWPDVDaaDPTL------WLGPEIAALVAGTPAARIDLYPALQRLLPWPEATR 682
Cdd:PRK11664 624 LSVLNWTPEAEQLRLRLLCAAKWLPEyDWPAVD--DESLlasletWLLPHMTGVRSLRGLKSLNIAQALRGLLDWPQRQR 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 683 LDELAPAVLELPNGRRARISYAGDR-PVLSTKLQDCFGLLESPIVC-GR-PLQFHLLSPAGRPLAVTDTLDSFWAGPYQQ 759
Cdd:PRK11664 702 LDSELPTHYTVPTGSRIAIRYHEDNpPALAVRMQEMFGEAQSPTIAqGRvPLVLELLSPAQRPLQITRDLAAFWQGAYRE 781
|
810
....*....|....*...
gi 753871158 760 VRSDMRGRYPKHPWPEDP 777
Cdd:PRK11664 782 VQKEMKGRYPKHVWPDDP 799
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
12-480 |
1.35e-65 |
|
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: 237.74 E-value: 1.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHNV---TGGKVIVVAPRRVAVRAAAHHL-EQLDrnscdQPST 87
Cdd:TIGR01967 66 LPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELgrgSHGLIGHTQPRRLAARTVAQRIaEELG-----TPLG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 88 HRVGYTIRGERSRGD--LVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAMSAT 165
Cdd:TIGR01967 141 EKVGYKVRFHDQVSSntLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSAT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 166 VDAPRFAELLSPehpAPIVETHAEIHPLELHYQPAAERI-ALSRSYMDHVCTVTQRAVAHSTDSALVFLPTIAAVTTVVS 244
Cdd:TIGR01967 221 IDPERFSRHFNN---APIIEVSGRTYPVEVRYRPLVEEQeDDDLDQLEAILDAVDELFAEGPGDILIFLPGEREIRDAAE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 245 ALEQRT--SVPVYPLHGQLTSSEQDAALRAG-RQRIVVATSIAESSLTVPGVRIVVDAGLSRVPKRDRARDLTGLVTTST 321
Cdd:TIGR01967 298 ILRKRNlrHTEILPLYARLSNKEQQRVFQPHsGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPI 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 322 SQAQADQRAGRAGREGPGTVYRLYSAAEFQHFPDHVTPEIRSADLTQAALCLTAWGCTDPAQFPLLSTPPKQSWEQAVDT 401
Cdd:TIGR01967 378 SQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 402 LRDIGALN---AAGQITELGRTLATLPTDPRLG-----ASLLHCGGGAAPTIAALSLDARGDIP--RAIAAMSHQQRFTR 471
Cdd:TIGR01967 458 LEELGALDddeAEPQLTPIGRQLAQLPVDPRLArmlleAHRLGCLQEVLIIASALSIQDPRERPmeKQQAADQAHARFKD 537
|
....*....
gi 753871158 472 EVARLAGFV 480
Cdd:TIGR01967 538 PRSDFLSRV 546
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
12-435 |
5.45e-59 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 218.01 E-value: 5.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHNVTGGKVIVVA---PRRVAVRAAAHHL-EQLDrnsCDQPST 87
Cdd:PRK11131 73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGhtqPRRLAARTVANRIaEELE---TELGGC 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 88 hrVGYTIRGERSRGD--LVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAMSAT 165
Cdd:PRK11131 150 --VGYKVRFNDQVSDntMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSAT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 166 VDAPRFAELLspeHPAPIVETHAEIHPLELHYQPAAERIALS-RSYMDHVCTVTQRAVAHSTDSALVFLPTIAAVTTVVS 244
Cdd:PRK11131 228 IDPERFSRHF---NNAPIIEVSGRTYPVEVRYRPIVEEADDTeRDQLQAIFDAVDELGREGPGDILIFMSGEREIRDTAD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 245 ALEQRT--SVPVYPLHGQLTSSEQDAALR--AGRqRIVVATSIAESSLTVPGVRIVVDAGLSRVPKRDRARDLTGLVTTS 320
Cdd:PRK11131 305 ALNKLNlrHTEILPLYARLSNSEQNRVFQshSGR-RIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEP 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 321 TSQAQADQRAGRAGREGPGTVYRLYSAAEFQHFPDHVTPEIRSADLTQAALCLTAWGCTDPAQFPLLSTPPKQSWEQAVD 400
Cdd:PRK11131 384 ISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVR 463
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 753871158 401 TLRDIGALNAAG-----QITELGRTLATLPTDPRLGASLL 435
Cdd:PRK11131 464 LLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVL 503
|
|
| HrpB_C |
pfam08482 |
ATP-dependent helicase C-terminal; This domain is found near the C-terminus of bacterial ... |
663-776 |
1.01e-58 |
|
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: 194.96 E-value: 1.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 663 ARIDLYPALQRLLPWPEATRLDELAPAVLELPNGRRARISYAGD--RPVLSTKLQDCFGLLESPIVCG--RPLQFHLLSP 738
Cdd:pfam08482 9 KRLDLLAALRALLPWEQQQRLDRLAPEHLTVPSGSRIRIDYSAEggAPVLAVRLQELFGLAETPRIAGgrVPLTLHLLSP 88
|
90 100 110
....*....|....*....|....*....|....*...
gi 753871158 739 AGRPLAVTDTLDSFWAGPYQQVRSDMRGRYPKHPWPED 776
Cdd:pfam08482 89 AGRPVQVTRDLASFWAGSYAEVRKEMRGRYPKHPWPED 126
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
12-186 |
3.00e-52 |
|
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: 179.45 E-value: 3.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHN---VTGGKVIVVAPRRVAVRAAAHHLEQLDRNSCDQpsth 88
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAelwIAGGKIIVLEPRRVAARAAARRLATLLGEAPGE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 89 RVGYTIRGERSRGDL--VEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRE-LRDDLTVIAMSAT 165
Cdd:cd17990 77 TVGYRVRGESRVGRRtrVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSAT 156
|
170 180
....*....|....*....|.
gi 753871158 166 VDAPRFAELLSpehPAPIVET 186
Cdd:cd17990 157 LDGDGLAALLP---EAPVVES 174
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
191-345 |
9.87e-44 |
|
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: 155.38 E-value: 9.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 191 HPLELHYQPAAERIALSRSYM------DHVCTVTQRAVAHSTD-SALVFLPTIAAVTTVVSALEQRTSVP------VYPL 257
Cdd:cd18791 1 FPVEVYYLEDILELLGISSEKedpdyvDAAVRLILQIHRTEEPgDILVFLPGQEEIERLCELLREELLSPdlgkllVLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 258 HGQLTSSEQDAALR---AGRQRIVVATSIAESSLTVPGVRIVVDAGLSRVPKRDRARDLTGLVTTSTSQAQADQRAGRAG 334
Cdd:cd18791 81 HSSLPPEEQQRVFEpppPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAG 160
|
170
....*....|.
gi 753871158 335 REGPGTVYRLY 345
Cdd:cd18791 161 RTRPGKCYRLY 171
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
28-173 |
2.00e-40 |
|
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: 145.68 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 28 HRMAVVQAPPGTGKTTLVPPI-----AHNVTGGKVIVVAPRRVAVRAAAHHLeqldRNSCDQPSTHRVGYTIRGERSRGD 102
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFlledgLAKGGKGRIVCTQPRRIAAISVAERV----AEERGEKLGEEVGYQIRFESKTSS 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 753871158 103 --LVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAMSATVDAPRFAE 173
Cdd:cd17917 77 ktRIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSS 149
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
12-173 |
1.48e-28 |
|
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: 112.58 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPP--IAHNVTGGK-----VIVVAPRRVAVRAAAHHL-EQLDRNScd 83
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQfiLEDYVLRGRgarcnVVITQPRRISAVSVAQRVaHELGPNL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 84 qpsTHRVGYTIRGER---SRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVI 160
Cdd:cd17976 79 ---RRNVGYQVRLESrppPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVV 155
|
170
....*....|...
gi 753871158 161 AMSATVDAPRFAE 173
Cdd:cd17976 156 LMSATGDNQRLSR 168
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
12-183 |
4.07e-27 |
|
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: 108.36 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHNV----TGGKVIVVAPRRVAVRAAAHHLEQldrnSCDQPST 87
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAgytkGGGKIGCTQPRRVAAMSVAARVAE----EMGVKLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 88 HRVGYTIRGE--RSRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAMSAT 165
Cdd:cd17974 77 NEVGYSIRFEdcTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSAT 156
|
170
....*....|....*...
gi 753871158 166 VDAPRFAELLSpehPAPI 183
Cdd:cd17974 157 MDAEKFSAFFD---DAPI 171
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
12-185 |
2.47e-26 |
|
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: 105.99 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHNVTGGKVIVVAPRRVAVRAAAHHL--EQLDRNSCdqpsthR 89
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRHIACTQPRRIACISLAKRVafESLNQYGS------K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 90 VGYTIRGERSRGDLVE--FVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAMSATVD 167
Cdd:cd17979 75 VAYQIRFERTRTLATKllFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATIN 154
|
170
....*....|....*...
gi 753871158 168 APRFAELLSpehPAPIVE 185
Cdd:cd17979 155 IELFSGYFE---GAPVVQ 169
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
12-173 |
3.90e-26 |
|
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: 105.90 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHN--VTGGKVI-VVAPRRVAVRAAAHHLEQldrnSCDQPSTH 88
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEagFARGGMIgITQPRRVAAVSVAKRVAE----EMGVELGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 89 RVGYTIRGE--RSRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDD-----LTVIA 161
Cdd:cd17978 77 LVGYSVRFDdvTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEqklspLKVII 156
|
170
....*....|..
gi 753871158 162 MSATVDAPRFAE 173
Cdd:cd17978 157 MSATLDADLFSE 168
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
12-172 |
6.07e-25 |
|
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: 102.69 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPP------IAHNVTGGK--VIVVAPRRV-AVRAAAHHLEQLDRNSC 82
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQflledlLLNGGTAQKcnIVCTQPRRIsAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 83 DQPSTHRVGYTIRGERSRGDLVE--FVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVI 160
Cdd:cd17975 81 PGGKNSLCGYQIRMESRTGEATRllYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
|
170
....*....|..
gi 753871158 161 AMSATVDAPRFA 172
Cdd:cd17975 161 LMSATVDCEKFS 172
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
12-184 |
2.60e-24 |
|
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: 100.69 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPP-IAHNVTGG------KVIVVAPRR-----VAVRAAAHHLEQLDr 79
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQfILDNSLQGpplpvaNIICTQPRRisaisVAERVAQERAERVG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 80 nscdqpstHRVGYTIRGE--RSRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDL 157
Cdd:cd17985 80 --------QSVGYQIRLEsvKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDL 151
|
170 180
....*....|....*....|....*..
gi 753871158 158 TVIAMSATVDAPRFAELLspeHPAPIV 184
Cdd:cd17985 152 KVILMSATLNAELFSDYF---NSCPVI 175
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
12-171 |
2.64e-24 |
|
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: 100.62 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHN---VTGGKVIVVA-PRRVAVRAAAHHL-EQLDRNScdqps 86
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEagwTAGGRVVGCTqPRRVAAVTVAGRVaEEMGAVL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 87 THRVGYTIRGERSRGDL---VEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAMS 163
Cdd:cd17980 76 GHEVGYCIRFDDCTDPQatrIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVAS 155
|
....*...
gi 753871158 164 ATVDAPRF 171
Cdd:cd17980 156 ATLDAEKF 163
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
12-171 |
3.24e-24 |
|
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: 100.57 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPP------IAHNvTGGKVIVVAPRRVAVRAAAHHL-EQLDRNSCDQ 84
Cdd:cd17973 13 LPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQfvlddeLPHQ-PKKLVACTQPRRVAAMSVAQRVaEEMDVKLGEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 85 psthrVGYTIRGE--RSRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAM 162
Cdd:cd17973 92 -----VGYSIRFEdcSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIVM 166
|
....*....
gi 753871158 163 SATVDAPRF 171
Cdd:cd17973 167 SATLDAGKF 175
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
12-173 |
8.52e-24 |
|
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: 99.15 E-value: 8.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHN--VTGGK-----VIVVAPRR-----VAVRAAAHHLEQLDR 79
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDdaIERGKgsscrIVCTQPRRisaisVAERVAAERAESCGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 80 -NScdqpsthrVGYTIRGE----RSRGDLVeFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELR 154
Cdd:cd17981 81 gNS--------TGYQIRLEsrkpRKQGSIL-YCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFR 151
|
170
....*....|....*....
gi 753871158 155 DDLTVIAMSATVDAPRFAE 173
Cdd:cd17981 152 SDLKVILMSATLNAEKFSD 170
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
12-185 |
9.90e-24 |
|
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: 98.68 E-value: 9.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHNVTGGKVIVVA---PRRVAVRAAAHHL-EQLDrnscdQPST 87
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGLIGhtqPRRLAARSVAERIaEELK-----TELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 88 HRVGYTIR--GERSRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAMSAT 165
Cdd:cd17989 76 GAVGYKVRftDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSAT 155
|
170 180
....*....|....*....|
gi 753871158 166 VDAPRFAELLSpehPAPIVE 185
Cdd:cd17989 156 IDAERFSRHFN---NAPIIE 172
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
12-172 |
1.85e-23 |
|
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: 97.92 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHN---VTGGKVIVVAPRRVAVRAAAHHL-EQLDRNSCDQpst 87
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEdgyTDYGMIGCTQPRRVAAMSVAKRVsEEMGVELGEE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 88 hrVGYTIRGE--RSRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAMSAT 165
Cdd:cd17983 78 --VGYAIRFEdcTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSAT 155
|
....*..
gi 753871158 166 VDAPRFA 172
Cdd:cd17983 156 MDADKFA 162
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
11-173 |
5.70e-22 |
|
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: 93.70 E-value: 5.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 11 GLPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHNV---TGGKVIVVAPRRVAVRAAAHHLEQldRNSCDQpsT 87
Cdd:cd17971 5 SLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAgytSRGKIGCTQPRRVAAMSVAKRVAE--EFGCCL--G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 88 HRVGYTIRGE--RSRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAMSAT 165
Cdd:cd17971 81 QEVGYTIRFEdcTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSAT 160
|
....*...
gi 753871158 166 VDAPRFAE 173
Cdd:cd17971 161 LDAVKFSQ 168
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
12-185 |
5.53e-21 |
|
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: 92.59 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVP-----PIAHNVTGGK--VIVVAPRRVAVRAAAhhlEQLDRNSCDQ 84
Cdd:cd17972 59 LPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPqyildDFIQNDRAAEcnIVVTQPRRISAVSVA---ERVAFERGEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 85 PStHRVGYTIRGE----RSRGDLVeFVTPGVLLRRLISNpeLDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVI 160
Cdd:cd17972 136 VG-KSCGYSVRFEsvlpRPHASIL-FCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVI 211
|
170 180
....*....|....*....|....*
gi 753871158 161 AMSATVDAPRFAELLSpehPAPIVE 185
Cdd:cd17972 212 LMSATIDTSMFCEYFF---NCPVIE 233
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
24-194 |
7.85e-19 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 85.62 E-value: 7.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 24 ALRIHRMAVVQAPPGTGKTTLVP-PIA---HNVTGGKVIVVAPRRVAVRAAAHHLEQLDRNSCDQPSTHRVGYTIRG--- 96
Cdd:smart00487 20 LLSGLRDVILAAPTGSGKTLAALlPALealKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREqlr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 97 --ERSRGDLVeFVTPGVLLRRLISNP-ELDGVSAVVVDEVHER--QLDTDLVLGMlveLRELRDDLTVIAMSATvdAPRF 171
Cdd:smart00487 100 klESGKTDIL-VTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKL---LKLLPKNVQLLLLSAT--PPEE 173
|
170 180
....*....|....*....|...
gi 753871158 172 AELLSPEHPAPIVETHAEIHPLE 194
Cdd:smart00487 174 IENLLELFLNDPVFIDVGFTPLE 196
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
12-185 |
9.95e-19 |
|
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: 84.71 E-value: 9.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPI--------AHNVTGGKVIVVAPRRVAVRAAAHHLeqldRNSCD 83
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFlyeagfgsPESDNPGMIGITQPRRVAAVSMAKRV----AEELN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 84 QPStHRVGYTIRGERSRGDL--VEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDD----- 156
Cdd:cd17982 77 VFG-KEVSYQIRYDSTVSENtkIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqd 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 753871158 157 -----LTVIAMSATVDAPRFAE--LLSPEHPaPIVE 185
Cdd:cd17982 156 qtvkpLKLVIMSATLRVEDFTEnkLLFPRPP-PVIK 190
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
12-186 |
5.61e-18 |
|
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350746 [Multi-domain] Cd Length: 180 Bit Score: 82.55 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPP--IAHNVTGGK---VIVVAPRRVAVRAAAHHLEQldRNSCDQPS 86
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQfiLDHYYKRGKycnIVVTQPRRIAAISIARRVSQ--EREWTLGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 87 ThrVGYTIRGER--SRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLgmLVELRELRDD---LTVIA 161
Cdd:cd17988 79 L--VGYQVGLERpaSEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLL--LVVRRLLRTNsrhVKIIL 154
|
170 180
....*....|....*....|....*.
gi 753871158 162 MSATVDAPRFAELLS-PEHPAPIVET 186
Cdd:cd17988 155 MSATISCKEFADYFTtPNNPAYVFEV 180
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
12-173 |
2.32e-17 |
|
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: 80.67 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPIAHNV---TGGKVIVVAPRRVAVRAAAHHLEQldRNSCDQPSTh 88
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAgfsQHGMIGVTQPRRVAAISVAQRVAE--EMKCTLGSK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 89 rVGYTIRGE--RSRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRD-----DLTVIA 161
Cdd:cd17984 78 -VGYQVRFDdcSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVV 156
|
170
....*....|..
gi 753871158 162 MSATVDAPRFAE 173
Cdd:cd17984 157 MSATLELAKLSA 168
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
12-171 |
5.22e-16 |
|
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: 76.41 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPPI-----AHNVTGGKVIVVAPRRVAVRAAAHHLEQLDRNSCDQPs 86
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFllddcYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 87 thrVGYTIRGER--SRGDLVEFVTPGVLLRRLISNPE-LDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAMS 163
Cdd:cd17987 80 ---VGYQIRLESrvSPKTLLTFCTNGVLLRTLMAGDSaLSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSS 156
|
....*...
gi 753871158 164 ATVDAPRF 171
Cdd:cd17987 157 AALDVNLF 164
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
224-337 |
6.79e-15 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 71.09 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 224 HSTDSALVFLPTIAAVTTvvSALEQRTSVPVYPLHGQLTSSEQDAAL---RAGRQRIVVATSIAESSLTVPGVRIVVDAG 300
Cdd:pfam00271 13 ERGGKVLIFSQTKKTLEA--ELLLEKEGIKVARLHGDLSQEEREEILedfRKGKIDVLVATDVAERGLDLPDVDLVINYD 90
|
90 100 110
....*....|....*....|....*....|....*..
gi 753871158 301 LSRVPkrdrardltglvttstsqAQADQRAGRAGREG 337
Cdd:pfam00271 91 LPWNP------------------ASYIQRIGRAGRAG 109
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
28-339 |
1.03e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 74.68 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 28 HRMAVVQAPPGTGKTTL---VppIAHNVTGGKVIVVAPRRVAVRAAAHHLEQLDRNScdqpsthrvgYTIRGERSRGDLV 104
Cdd:COG1061 100 GGRGLVVAPTGTGKTVLalaL--AAELLRGKRVLVLVPRRELLEQWAEELRRFLGDP----------LAGGGKKDSDAPI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 105 EFVTPGVLLRRLISNPELDGVSAVVVDEVHErqldtdLVLGMLVELRELRDDLTVIAMSAT--------VDAPRF----- 171
Cdd:COG1061 168 TVATYQSLARRAHLDELGDRFGLVIIDEAHH------AGAPSYRRILEAFPAAYRLGLTATpfrsdgreILLFLFdgivy 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 172 ----AELLSPEHPAPI------VETHAEIHPLELHYQPAAERIALSRSYMDHVCTVTQRAVAhSTDSALVFLPTIAAVTT 241
Cdd:COG1061 242 eyslKEAIEDGYLAPPeyygirVDLTDERAEYDALSERLREALAADAERKDKILRELLREHP-DDRKTLVFCSSVDHAEA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 242 VVSALEQRtSVPVYPLHGQLTSSEQD---AALRAGRQRIVVATSIAESSLTVPGVRIVVdaglsrvpkrdrardltgLVT 318
Cdd:COG1061 321 LAELLNEA-GIRAAVVTGDTPKKEREeilEAFRDGELRILVTVDVLNEGVDVPRLDVAI------------------LLR 381
|
330 340
....*....|....*....|.
gi 753871158 319 TSTSQAQADQRAGRAGREGPG 339
Cdd:COG1061 382 PTGSPREFIQRLGRGLRPAPG 402
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
12-164 |
3.47e-13 |
|
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: 68.31 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAVVQAPPGTGKTTLVPP-------IAHNVTGGKVIVVAPRRVAVRAAAHHLEQLDRNScdq 84
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeyclSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 85 psTHRVGYTIRGER--SRGDLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIAM 162
Cdd:cd17977 78 --GHEVGYVIPFENccTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVII 155
|
..
gi 753871158 163 SA 164
Cdd:cd17977 156 TC 157
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
22-175 |
2.25e-12 |
|
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: 65.73 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 22 IDALRIHRMAVVQAPPGTGKTT--LVPPIAH---NVTGGKVIVVAPRRVAVRAAAHHLEQLDRNSCDQPSTHRVGYTIRG 96
Cdd:pfam00270 8 IPAILEGRDVLVQAPTGSGKTLafLLPALEAldkLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGDSRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 97 ERSR---GDLVeFVTPGVLLRRLISNPELDGVSAVVVDEVHeRQLDTDLVLGMLVELRELRDDLTVIAMSATvdAPRFAE 173
Cdd:pfam00270 88 QLEKlkgPDIL-VGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKKRQILLLSAT--LPRNLE 163
|
..
gi 753871158 174 LL 175
Cdd:pfam00270 164 DL 165
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
252-337 |
7.20e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 61.84 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 252 VPVYPLHGQLTSSEQDAAL---RAGRQRIVVATSIAESSLTVPGVRIVVDAGLSRvpkrdrardltglvttstSQAQADQ 328
Cdd:smart00490 12 IKVARLHGGLSQEEREEILdkfNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPW------------------SPASYIQ 73
|
....*....
gi 753871158 329 RAGRAGREG 337
Cdd:smart00490 74 RIGRAGRAG 82
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
12-185 |
3.27e-11 |
|
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: 62.61 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 12 LPVAQSTTTLIDALRIHRMAV-VQAPPGTGKTTLVP------PIAHNVTGGKVIVVAPRRVAVRAAAHHL-EQLDRNScd 83
Cdd:cd17986 1 LPIWAAKFTFLEQLESPSGIVlVSGEPGSGKSTQVPqwcaefALSRGFQKGQVTVTQPHPLAARSLALRVaDEMDLNL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 84 qpsTHRVGYTIRGERSRG--DLVEFVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELRDDLTVIA 161
Cdd:cd17986 79 ---GHEVGYSIPQEDCTGpnTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVV 155
|
170 180
....*....|....*....|....
gi 753871158 162 MSATVDAPRfaeLLSPEHPAPIVE 185
Cdd:cd17986 156 VTSPALEPK---LRAFWGNPPVVH 176
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
32-165 |
1.57e-10 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 59.72 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 32 VVQAPPGTGKTTLVPPIAHNV---TGGKVIVVAPRR-VAVRAAAHHLEQLDRNSCDQPSTHRVGYTIRGERSRGDL-VEF 106
Cdd:cd00046 5 LITAPTGSGKTLAALLAALLLllkKGKKVLVLVPTKaLALQTAERLRELFGPGIRVAVLVGGSSAEEREKNKLGDAdIII 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 753871158 107 VTPGVLLRRLISN--PELDGVSAVVVDEVHERQLDTD-LVLGMLVELRELRDDLTVIAMSAT 165
Cdd:cd00046 85 ATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRgALILDLAVRKAGLKNAQVILLSAT 146
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
398-449 |
1.15e-09 |
|
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: 56.09 E-value: 1.15e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 753871158 398 AVDTLRDIGALNAAGQITELGRTLATLPTDPRLG-----ASLLHCGGGAAPTIAALS 449
Cdd:pfam04408 1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAkmllaAAELGCLDEVLTIVAALS 57
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
405-472 |
3.20e-08 |
|
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: 51.50 E-value: 3.20e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 753871158 405 IGALNAAGQITELGRTLATLPTDPRLGASLLHCG--GGAAPTIAALSLDARGDIP---RAIAAMSHQQRFTRE 472
Cdd:smart00847 2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAefGCLDEILTIVAMLSVGDPRpkeKREDADAARRRFADP 74
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
126-353 |
2.76e-07 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 54.21 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 126 SAVVVDEVHERQLDTDLVLGMLvelRELRDDLT-VIAMSATV--DAPRFAELLspehPAPIVethaeIH-------PLEL 195
Cdd:PHA02653 293 GTVIIDEVHEHDQIGDIIIAVA---RKHIDKIRsLFLMTATLedDRDRIKEFF----PNPAF-----VHipggtlfPISE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 196 HYQPAAERIALSRSYM----DHVCTVTQRAVAHSTDSALVFLPTIAAVTTVVSALEQR-TSVPVYPLHGQLTSSeqDAAL 270
Cdd:PHA02653 361 VYVKNKYNPKNKRAYIeeekKNIVTALKKYTPPKGSSGIVFVASVSQCEEYKKYLEKRlPIYDFYIIHGKVPNI--DEIL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 271 R----AGRQRIVVATSIAESSLTVPGVRIVVDAGLSRVPKrdrarDLTGlVTTSTSQAQADQRAGRAGREGPGTVYRLYS 346
Cdd:PHA02653 439 EkvysSKNPSIIISTPYLESSVTIRNATHVYDTGRVYVPE-----PFGG-KEMFISKSMRTQRKGRVGRVSPGTYVYFYD 512
|
....*..
gi 753871158 347 AAEFQHF 353
Cdd:PHA02653 513 LDLLKPI 519
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
29-186 |
2.59e-06 |
|
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: 47.93 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 29 RMAVVQAPPGTGKTTLVPP--IAHNV-TGGKVIVVAPRRVAVRAAAHHLEQLDRNscdqpstHRVGyTIRGERSRGDLVE 105
Cdd:cd17931 2 QLTVLDLHPGAGKTTRVLPqiIREAIkKRLRTLVLAPTRVVAAEMYEALRGLPIR-------YRTG-AVKEEHGGNEIVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 106 FVTPGVLLRRLISNPELDGVSAVVVDEVHERQLDTDLVLGMLVELRELrDDLTVIAMSAT----VDAPrfaellsPEHPA 181
Cdd:cd17931 74 YMCHGTFTCRLLSPKRVPNYNLIIMDEAHFTDPASIAARGYIHTRVEM-GEAAVIFMTATppgtVTPF-------PQSNH 145
|
....*
gi 753871158 182 PIVET 186
Cdd:cd17931 146 PIEDF 150
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
32-339 |
8.02e-06 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 49.12 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 32 VVQAPPGTGKTTLVP-PIAHNV-TGGKVIVVAPrrvaVRAAAH--------HLEQLDrnscdqpstHRVG-----YTIRG 96
Cdd:COG1204 42 VVSAPTASGKTLIAElAILKALlNGGKALYIVP----LRALASekyrefkrDFEELG---------IKVGvstgdYDSDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 97 ERSRGDLVEFVTP---GVLLRRliSNPELDGVSAVVVDEVHerQLDTD---LVLGMLVE-LRELRDDLTVIAMSATVDAP 169
Cdd:COG1204 109 EWLGRYDILVATPeklDSLLRN--GPSWLRDVDLVVVDEAH--LIDDEsrgPTLEVLLArLRRLNPEAQIVALSATIGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 170 R-FAELLspehPAPIVEThaEIHPLEL----HYQPAAERIALSRSYMDHVCTVTQRAVAHSTdSALVFLPT--------- 235
Cdd:COG1204 185 EeIAEWL----DAELVKS--DWRPVPLnegvLYDGVLRFDDGSRRSKDPTLALALDLLEEGG-QVLVFVSSrrdaeslak 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 236 -IAAVTTVVSALEQRTSV---------------PVYPL-----------HGQLTSSEQDA---ALRAGRQRIVVATS-IA 284
Cdd:COG1204 258 kLADELKRRLTPEEREELeelaeellevseethTNEKLadclekgvafhHAGLPSELRRLvedAFREGLIKVLVATPtLA 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 753871158 285 EssltvpGV-----RIVVdaglsRVPKRDRARDLTGLvttstsqaqaD--QRAGRAGRegPG 339
Cdd:COG1204 338 A------GVnlparRVII-----RDTKRGGMVPIPVL----------EfkQMAGRAGR--PG 376
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
248-767 |
8.27e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 49.49 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 248 QRTSVPVYP-----LHGQLTSSEQDAALRAGRQRIVVATSIAESSLTVPGVRIVVDAGLSRVPKRDRARDLTGLVTTSTS 322
Cdd:COG3321 859 RRVPLPTYPfqredAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAA 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 323 QAQADQRAGRAGREGPGTVYRLYSAAEFQHFPDHVTPEIRSADLTQAALCLTAWGCTDPAQFPLLSTPPKQSWEQAVDTL 402
Cdd:COG3321 939 AAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAA 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 403 RDIGALNAAGQITELGRTLATLPTDPRLGASLLHCGGGAAPTIAALSLDARGDIPRAIAAMsHQQRFTREVARLAGFVPD 482
Cdd:COG3321 1019 AALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELAL-AAAALALAAALAAAALAL 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 483 SECTPGEAIARAWPKNVARRDGDSYLMAGGSRAELGVSSLSGHEWLAVAQASLTHRGSVIRSAAPISEAAAVDIIGVAER 562
Cdd:COG3321 1098 ALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 563 TEATLVDGSLRGTRIRHAGAITLSTTNVKVEGELAEQALAEGIRTHGLELFTFSDKATELRDRLRHLHEYYGEPWPDVDA 642
Cdd:COG3321 1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 643 ADPTLWLGPEIAALVAGTPAARIDLYPALQRLLPWPEATRLDELAPAVLELPNGRRARISYAGDRPVLSTKLQDCFGLLE 722
Cdd:COG3321 1258 ALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAV 1337
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 753871158 723 SPIVCGRPLQFHLLSPAGRPLAVTDTLDSFWAGPYQQVRSDMRGR 767
Cdd:COG3321 1338 AAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALA 1382
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
126-342 |
1.17e-05 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 48.54 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 126 SAVVVDEVHErqLDTDLvLGMLVE-LRELRD-DLTVIAMSATVdaPRFAELLSPEHPAPIVETHAEIHplELHYQPAAER 203
Cdd:COG1203 270 SVIILDEVQA--YPPYM-LALLLRlLEWLKNlGGSVILMTATL--PPLLREELLEAYELIPDEPEELP--EYFRAFVRKR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 204 IALSRSYMDHVcTVTQRAV--AHSTDSALVFLPTIAAVTTVVSALEQR-TSVPVYPLHGQLTS---SEQ----DAALRAG 273
Cdd:COG1203 343 VELKEGPLSDE-ELAELILeaLHKGKSVLVIVNTVKDAQELYEALKEKlPDEEVYLLHSRFCPadrSEIekeiKERLERG 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 753871158 274 RQRIVVATSIAESSLTvpgvrivVDAglsrvpkrDRA-RDLTGLvttstsqaqaD---QRAGRAGREG----PGTVY 342
Cdd:COG1203 422 KPCILVSTQVVEAGVD-------IDF--------DVViRDLAPL----------DsliQRAGRCNRHGrkeeEGNVY 473
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
32-355 |
1.57e-05 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 48.22 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 32 VVQAPPGTGKT---TLvpPIAHNVTGGK-----VIVVAPRR-----VA--VRAAAHHL-----------------EQLDR 79
Cdd:COG0513 43 LGQAQTGTGKTaafLL--PLLQRLDPSRprapqALILAPTRelalqVAeeLRKLAKYLglrvatvyggvsigrqiRALKR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 80 NscdqpsthrvgytirgersrgdlVEFV--TPGVLL----RRLISnpeLDGVSAVVVDEVhERQLDtdlvLGMLVELREL 153
Cdd:COG0513 121 G-----------------------VDIVvaTPGRLLdlieRGALD---LSGVETLVLDEA-DRMLD----MGFIEDIERI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 154 RDDL-----TVIaMSATVDAprfaellspehpapivethaEIHPLELHYQPAAERIALSRSYMDHVcTVTQRAV------ 222
Cdd:COG0513 170 LKLLpkerqTLL-FSATMPP--------------------EIRKLAKRYLKNPVRIEVAPENATAE-TIEQRYYlvdkrd 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 223 ----------AHSTDSALVFLPTIAAVTTVVSALEQRtSVPVYPLHGQLTSSEQDAAL---RAGRQRIVVATSIAESSLT 289
Cdd:COG0513 228 klellrrllrDEDPERAIVFCNTKRGADRLAEKLQKR-GISAAALHGDLSQGQRERALdafRNGKIRVLVATDVAARGID 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 290 VPGVRIVVDAGLSRVPK----RdrardlTGlvttstsqaqadqRAGRAGREgpGTVYRLYSAAEFQHFPD 355
Cdd:COG0513 307 IDDVSHVINYDLPEDPEdyvhR------IG-------------RTGRAGAE--GTAISLVTPDERRLLRA 355
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
22-337 |
2.61e-05 |
|
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: 47.91 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 22 IDALRIHRMAVVQAPPGTGKT---TLvpPIAHNVT---GGKVIVVAPRRvavrAAAH----HLEQLDRNSCDQPSTHRV- 90
Cdd:COG1205 65 IEAARAGKNVVIATPTASGKSlayLL--PVLEALLedpGATALYLYPTK----ALARdqlrRLRELAEALGLGVRVATYd 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 91 GYTIRGER----SRGDLVeFVTP-----GVLL-----RRLISNPELdgvsaVVVDEVHE-RQldtdlVLGM---LVeLRE 152
Cdd:COG1205 139 GDTPPEERrwirEHPDIV-LTNPdmlhyGLLPhhtrwARFFRNLRY-----VVIDEAHTyRG-----VFGShvaNV-LRR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 153 LR-------DDLTVIAMSATVDAPR-FAELLSPEHPAPIVETHAEIHPLE-LHYQPAAERIALSRSYMDHVCTVTQRAVA 223
Cdd:COG1205 207 LRricrhygSDPQFILASATIGNPAeHAERLTGRPVTVVDEDGSPRGERTfVLWNPPLVDDGIRRSALAEAARLLADLVR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 224 HSTdSALVFLPTIAAVTTVVSALEQRTSVPVYPL-----HGQLTSSEQ---DAALRAGRQRIVVATSIAESSLTVPGVRI 295
Cdd:COG1205 287 EGL-RTLVFTRSRRGAELLARYARRALREPDLADrvaayRAGYLPEERreiERGLRSGELLGVVSTNALELGIDIGGLDA 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 753871158 296 VVDAGlsrVPKrdrardltglvttstSQAQADQRAGRAGREG 337
Cdd:COG1205 366 VVLAG---YPG---------------TRASFWQQAGRAGRRG 389
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
31-171 |
1.51e-04 |
|
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: 42.96 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 31 AVVQAPPGTGKT--TLVPPI----AHNVTGGKVIVVAPRRVAVRAAAHHLEQ-LDRNSCDQPSTHRVGYTIRGERSRgDL 103
Cdd:cd17922 4 VLIAAPTGSGKTeaAFLPALsslaDEPEKGVQVLYISPLKALINDQERRLEEpLDEIDLEIPVAVRHGDTSQSEKAK-QL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 104 VEfvTPGVL------LRRLISNPELD----GVSAVVVDEVHErQLDTD---LVLGMLVELRELRD-DLTVIAMSATV--- 166
Cdd:cd17922 83 KN--PPGILittpesLELLLVNKKLRelfaGLRYVVVDEIHA-LLGSKrgvQLELLLERLRKLTGrPLRRIGLSATLgnl 159
|
....*.
gi 753871158 167 -DAPRF 171
Cdd:cd17922 160 eEAAAF 165
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
28-67 |
3.05e-04 |
|
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: 43.00 E-value: 3.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 753871158 28 HRMAVVQAPPGTGKTTLVPPIAHNV---TGGKVIVVAPRRVAV 67
Cdd:cd18039 16 RPLSLIQGPPGTGKTVTSATIVYHLvkqGNGPVLVCAPSNVAV 58
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
31-179 |
7.84e-04 |
|
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: 41.09 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 31 AVVQAPPGTGKTTLVP-PIAHNVT--GGKVIVVAPrrvaVRAAAHHLEQlDRNSCDQPSTHRVGYTIRGERSRGDLVE-- 105
Cdd:cd17921 20 VLVSAPTSSGKTLIAElAILRALAtsGGKAVYIAP----TRALVNQKEA-DLRERFGPLGKNVGLLTGDPSVNKLLLAea 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 106 ---FVTP---GVLLRRLiSNPELDGVSAVVVDEVH-----ERqldtdlvlGMLVE-----LRELRDDLTVIAMSATVDAP 169
Cdd:cd17921 95 dilVATPeklDLLLRNG-GERLIQDVRLVVVDEAHligdgER--------GVVLElllsrLLRINKNARFVGLSATLPNA 165
|
170
....*....|.
gi 753871158 170 R-FAELLSPEH 179
Cdd:cd17921 166 EdLAEWLGVED 176
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
229-364 |
7.97e-04 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 42.55 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753871158 229 ALVFLPTIAAVTTVVSALEQRTSVP----VYplhgqltSSEQD-----AALRAGRQRIVVATSIAESSLTVPGVR-IVVD 298
Cdd:COG4098 322 LLIFVPTIELLEQLVALLQKLFPEEriagVH-------AEDPErkekvQAFRDGEIPILVTTTILERGVTFPNVDvAVLG 394
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 753871158 299 AGlsrvpkrDRARDLTGLVttstsqaqadQRAGRAGR--EGP-GTVYrlysaaeFQHfpDHVTPEIRSA 364
Cdd:COG4098 395 AD-------HPVFTEAALV----------QIAGRVGRsaDYPtGEVI-------FFH--HGKTRAMKRA 437
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
22-68 |
9.87e-04 |
|
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members 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: 350801 [Multi-domain] Cd Length: 127 Bit Score: 39.87 E-value: 9.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 753871158 22 IDALRIHRMAVVQAPPGTGKT-TLVPPIAHNV-TGGKVIVVAPRRVAVR 68
Cdd:cd18043 8 IISARNGKNVVIQGPPGTGKSqTIANIIANALaRGKRVLFVSEKKAALD 56
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
23-61 |
1.14e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 42.22 E-value: 1.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 753871158 23 DALRIHRMAVVQAPPGTGKT--TLVPPIAHNVTGGKVIVVA 61
Cdd:COG1199 28 RALAEGRHLLIEAGTGTGKTlaYLVPALLAARETGKKVVIS 68
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
277-345 |
1.27e-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: 38.07 E-value: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 753871158 277 IVVATSIAESSLTVPGVRIVVDAGLSRvpkrdrardltglvttstSQAQADQRAGRAGREG--PGTVYRLY 345
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPS------------------SAASYIQRVGRAGRGGkdEGEVILFV 77
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
24-67 |
1.46e-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: 40.67 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 753871158 24 ALRIHRMAVVQAPPGTGKT-TLVPPIAHNVT-GGKVIVVAPRRVAV 67
Cdd:cd18044 13 ALSQKDVALIHGPPGTGKTtTVVEIILQAVKrGEKVLACAPSNIAV 58
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| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
257-302 |
2.78e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 39.25 E-value: 2.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 753871158 257 LHGQLTSSEQDAALRAGRQR---IVVATSIAESSLTVPG--VRIVVDA---GLS 302
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGevdILVSTTVIEVGVDVPNatVMVIEDAerfGLS 120
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| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
31-67 |
5.41e-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: 37.60 E-value: 5.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 753871158 31 AVVQAPPGTGKTTLVPPIAHN----VTGGKVIVVAPRRVAV 67
Cdd:cd17934 2 SLIQGPPGTGKTTTIAAIVLQllkgLRGKRVLVTAQSNVAV 42
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| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
24-67 |
9.83e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 38.48 E-value: 9.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 753871158 24 ALRIHRMAVVQAPPGTGKTTLVPPIAH---------NVTGGKVIVVAPRRVAV 67
Cdd:pfam13086 9 ALSSSHFTLIQGPPGTGKTTTIVELIRqllsypatsAAAGPRILVCAPSNAAV 61
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