|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
136-763 |
0e+00 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 551.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 136 QLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEymrsLPGPKRG-VACTQPRRVAAMSVAQRVADEMDVMLG 214
Cdd:COG1643 9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGrIGMLEPRRLAARAAAERMAEELGEPVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 215 QEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVV-RQRSDLKVIVMSA 293
Cdd:COG1643 85 ETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 294 TLDAGKFQIYFDNCPLLTIPGRTHPVEIFYTP--EPERDYLEAAIRTVIQIHmcEEEEGDLLLFLTGQEEIDEACKRIKR 371
Cdd:COG1643 165 TLDAERFARLLGDAPVIESSGRTYPVEVRYRPlpADERDLEDAVADAVREAL--AEEPGDILVFLPGEREIRRTAEALRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 372 EVDDlgpevgDIKIIPLYSTLPPQQQQRIFEPPPPKkqngaiGRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRI 451
Cdd:COG1643 243 RLPP------DTEILPLYGRLSAAEQDRAFAPAPHG------RRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 452 RVESLLVTAISKASAQQRAGRAGRTRPGKCFRLYTEKAYKTeMQDNTYPEILRSNLGSVVLQLKKLGIDDLVHFDFMDPP 531
Cdd:COG1643 311 GVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFAR-RPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 532 APETLMRALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQcfVRPTEAkkaad 611
Cdd:COG1643 390 PARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERD--PRRGAA----- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 612 eakmrfahiDGDHLTLLNVYHAFKQNHEsvqwcydNFINYrslMSADNVRQQLSRIMDRFNLPRRSTDFTsrdyYINIRK 691
Cdd:COG1643 463 ---------GSDLLARLNLWRRLREQQR-------EFLSY---LRLREWRDLARQLRRLLGEGANEEPAD----YEAIGL 519
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1511959583 692 ALVTGYFMQVAHL-ERTGHYLTVKdNQVVQLHPSTVLdHKPEWVLYNEFVLTTKNY-IRTCTDIKPEWLVKIAP 763
Cdd:COG1643 520 LLALAYPDRIARRrGEGGRYLLAR-GRGAALFPGSPL-AKKEWLVAAELVGGAAEArIRLAAPIDPEWLEELAA 591
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
136-778 |
1.12e-159 |
|
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273900 [Multi-domain] Cd Length: 1283 Bit Score: 497.37 E-value: 1.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 136 QLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRslpGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQ 215
Cdd:TIGR01967 65 NLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGR---GSHGLIGHTQPRRLAARTVAQRIAEELGTPLGE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 216 EVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATL 295
Cdd:TIGR01967 142 KVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATI 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 296 DAGKFQIYFDNCPLLTIPGRTHPVEIFYTP------EPERDYLEAAIRTVIQihMCEEEEGDLLLFLTGQEEIDEACKRI 369
Cdd:TIGR01967 222 DPERFSRHFNNAPIIEVSGRTYPVEVRYRPlveeqeDDDLDQLEAILDAVDE--LFAEGPGDILIFLPGEREIRDAAEIL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 370 KREvddlgpEVGDIKIIPLYSTLPPQQQQRIFEPpppkkqngAIGRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNP 449
Cdd:TIGR01967 300 RKR------NLRHTEILPLYARLSNKEQQRVFQP--------HSGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 450 RIRVESLLVTAISKASAQQRAGRAGRTRPGKCFRLYTEKAYKTEmQDNTYPEILRSNLGSVVLQLKKLGIDDLVHFDFMD 529
Cdd:TIGR01967 366 RTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSR-PEFTDPEILRTNLASVILQMLALRLGDIAAFPFIE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 530 PPAPETLMRALELLNYLAALNDD---GDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQCFVRPTEA 606
Cdd:TIGR01967 445 APDPRAIRDGFRLLEELGALDDDeaePQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEK 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 607 KKAADEAKMRFAHIDGDHLTLLNVYHAFKQNHESV------QWCYDNFINYRSLMSADNVRQQLSRIMDRFNLPRRStdf 680
Cdd:TIGR01967 525 QQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALsanqfrNACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNE--- 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 681 TSRDYYInIRKALVTGYFMQVAHLERTGHYLTVKdNQVVQLHPSTVLDHK-PEWVLYNEFVLTTKNYIRTCTDIKPEWLV 759
Cdd:TIGR01967 602 EPADYDA-IHKALLSGLLSQIGMKDEKHEYDGAR-GRKFHIFPGSPLFKKpPKWVMAAELVETSKLYARLVAKIEPEWVE 679
|
650 660
....*....|....*....|
gi 1511959583 760 KIAPQYYDMSNF-PQCEAKR 778
Cdd:TIGR01967 680 PVAGHLIKKNYFePHWEKKR 699
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
136-762 |
6.09e-156 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 488.03 E-value: 6.09e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 136 QLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRslpGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQ 215
Cdd:PRK11131 72 NLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGR---GVKGLIGHTQPRRLAARTVANRIAEELETELGG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 216 EVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATL 295
Cdd:PRK11131 149 CVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 296 DAGKFQIYFDNCPLLTIPGRTHPVEIFYTP------EPERDYLEAAIRTVIQihMCEEEEGDLLLFLTGQEEI-DEACKR 368
Cdd:PRK11131 229 DPERFSRHFNNAPIIEVSGRTYPVEVRYRPiveeadDTERDQLQAIFDAVDE--LGREGPGDILIFMSGEREIrDTADAL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 369 IKREVDdlgpevgDIKIIPLYSTLPPQQQQRIFEPpppkkqngAIGRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYN 448
Cdd:PRK11131 307 NKLNLR-------HTEILPLYARLSNSEQNRVFQS--------HSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 449 PRIRVESLLVTAISKASAQQRAGRAGRTRPGKCFRLYTEKAY--KTEMQDntyPEILRSNLGSVVLQLKKLGIDDLVHFD 526
Cdd:PRK11131 372 YRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFlsRPEFTD---PEILRTNLASVILQMTALGLGDIAAFP 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 527 FMDPPAPETLMRALELLNYLAALNDDGD-----LTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQCFV 601
Cdd:PRK11131 449 FVEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRE 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 602 RPTEAKKAADEAKMRFAHIDGDHLTLLNVYHAFKQNHE---SVQW---CYDNFINYRSLMSADNVRQQLSRIMDRFNLPR 675
Cdd:PRK11131 529 RPMDKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKalsSNQFrrlCRTDYLNYLRVREWQDIYTQLRQVVKELGIPV 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 676 RSTDFTsrdyYINIRKALVTGYFMQVAHLERTGHYLTVKDNQVVQLHPSTVLDHK-PEWVLYNEFVLTTKNYIRTCTDIK 754
Cdd:PRK11131 609 NSEPAE----YREIHTALLTGLLSHIGMKDAEKQEYTGARNARFSIFPGSGLFKKpPKWVMVAELVETSRLWGRIAARIE 684
|
....*...
gi 1511959583 755 PEWLVKIA 762
Cdd:PRK11131 685 PEWIEPLA 692
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
125-312 |
1.58e-129 |
|
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: 383.69 E-value: 1.58e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 125 PRYYDILKKRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPgPKRGVACTQPRRVAAMSVAQR 204
Cdd:cd17973 1 QRYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQ-PKKLVACTQPRRVAAMSVAQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 205 VADEMDVMLGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRS 284
Cdd:cd17973 80 VAEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRP 159
|
170 180
....*....|....*....|....*...
gi 1511959583 285 DLKVIVMSATLDAGKFQIYFDNCPLLTI 312
Cdd:cd17973 160 DLKLIVMSATLDAGKFQKYFDNAPLLKV 187
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
137-597 |
6.23e-110 |
|
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: 354.46 E-value: 6.23e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQwcveYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQE 216
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPL----ALLDAPGIGGKIIMLEPRRLAARSAAQRLASQLGEAVGQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 217 VGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQ-RSDLKVIVMSATL 295
Cdd:TIGR01970 77 VGYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSATL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 296 DAGKFQIYFDNCPLLTIPGRTHPVEIFYTPEPERDYLEAAIRTVIQiHMCEEEEGDLLLFLTGQEEIDEACKRIKrevDD 375
Cdd:TIGR01970 157 DGERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVE-HALASETGSILVFLPGQAEIRRVQEQLA---ER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 376 LGPEVgdiKIIPLYSTLPPQQQQRIFEPPPPKKqngaigRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRIRVES 455
Cdd:TIGR01970 233 LDSDV---LICPLYGELSLAAQDRAIKPDPQGR------RKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 456 LLVTAISKASAQQRAGRAGRTRPGKCFRLYTE-KAYKTEMQDNtyPEILRSNLGSVVLQLKKLGIDDLVHFDFMDPPAPE 534
Cdd:TIGR01970 304 LETVRISQASATQRAGRAGRLEPGVCYRLWSEeQHQRLPAQDE--PEILQADLSGLALELAQWGAKDPSDLRWLDAPPSV 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1511959583 535 TLMRALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVP 597
Cdd:TIGR01970 382 ALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALLEER 444
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
136-594 |
5.86e-92 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 306.08 E-value: 5.86e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 136 QLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPqwcVEYMRSLPGPKRgVACTQPRRVAAMSVAQRVADEMDVMLGQ 215
Cdd:PRK11664 3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLP---LQLLQHGGINGK-IIMLEPRRLAARNVAQRLAEQLGEKPGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 216 EVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVvrQ---RSDLKVIVMS 292
Cdd:PRK11664 79 TVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDV--QqglRDDLKLLIMS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 293 ATLDAGKFQIYFDNCPLLTIPGRTHPVEIFYTPEPERDYLEAAIRTVIQiHMCEEEEGDLLLFLTGQEEIdeacKRIKRE 372
Cdd:PRK11664 157 ATLDNDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRFDEAVARATA-ELLRQESGSLLLFLPGVGEI----QRVQEQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 373 VDDLGPEvgDIKIIPLYSTLPPQQQQRIFEPPPPKKqngaigRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRIR 452
Cdd:PRK11664 232 LASRVAS--DVLLCPLYGALSLAEQQKAILPAPAGR------RKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 453 VESLLVTAISKASAQQRAGRAGRTRPGKCFRLYTEKAYKTEMQDNTyPEILRSNLGSVVLQLKKLGIDDLVHFDFMDPPA 532
Cdd:PRK11664 304 LTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSE-PEILHSDLSGLLLELLQWGCHDPAQLSWLDQPP 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511959583 533 PETLMRALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYncSNEVLSITAML 594
Cdd:PRK11664 383 AAALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKED--DEAALATAAKL 442
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
153-312 |
1.85e-89 |
|
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438707 [Multi-domain] Cd Length: 159 Bit Score: 278.57 E-value: 1.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 153 HQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRgVACTQPRRVAAMSVAQRVADEMDVMLGQEVGYSIRFEDCSSAKTI 232
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGR-IVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 233 LKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLDAGKFQIYFDNCPLLTI 312
Cdd:cd17917 80 IKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
317-485 |
3.12e-83 |
|
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: 262.47 E-value: 3.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 317 HPVEIFYTPEP-----------ERDYLEAAIRTVIQIHmCEEEEGDLLLFLTGQEEIDEACKRIKREVddLGPEVGDIKI 385
Cdd:cd18791 1 FPVEVYYLEDIlellgissekeDPDYVDAAVRLILQIH-RTEEPGDILVFLPGQEEIERLCELLREEL--LSPDLGKLLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 386 IPLYSTLPPQQQQRIFEPPPPKKqngaigRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRIRVESLLVTAISKAS 465
Cdd:cd18791 78 LPLHSSLPPEEQQRVFEPPPPGV------RKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKAS 151
|
170 180
....*....|....*....|
gi 1511959583 466 AQQRAGRAGRTRPGKCFRLY 485
Cdd:cd18791 152 AEQRAGRAGRTRPGKCYRLY 171
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
137-312 |
2.02e-80 |
|
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: 255.51 E-value: 2.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKrgVACTQPRRVAAMSVAQRVADEMDVMLGQE 216
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGK--IGCTQPRRVAAMSVAARVAEEMGVKLGNE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 217 VGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLD 296
Cdd:cd17974 79 VGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMD 158
|
170
....*....|....*.
gi 1511959583 297 AGKFQIYFDNCPLLTI 312
Cdd:cd17974 159 AEKFSAFFDDAPIFRI 174
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
137-312 |
1.20e-79 |
|
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: 253.43 E-value: 1.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEymrslPGPKRG--VACTQPRRVAAMSVAQRVADEMDVMLG 214
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYE-----AGFARGgmIGITQPRRVAAVSVAKRVAEEMGVELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 215 QEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQR-----SDLKVI 289
Cdd:cd17978 76 QLVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVI 155
|
170 180
....*....|....*....|...
gi 1511959583 290 VMSATLDAGKFQIYFDNCPLLTI 312
Cdd:cd17978 156 IMSATLDADLFSEYFNGAPVLYI 178
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
133-313 |
8.17e-77 |
|
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: 245.86 E-value: 8.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 133 KRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPkrgVACTQPRRVAAMSVAQRVADEMDVM 212
Cdd:cd17971 2 QRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGK---IGCTQPRRVAAMSVAKRVAEEFGCC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 213 LGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMS 292
Cdd:cd17971 79 LGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTS 158
|
170 180
....*....|....*....|.
gi 1511959583 293 ATLDAGKFQIYFDNCPLLTIP 313
Cdd:cd17971 159 ATLDAVKFSQYFYEAPIFTIP 179
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
137-312 |
7.51e-75 |
|
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: 240.44 E-value: 7.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPkrgVACTQPRRVAAMSVAQRVADEMDVMLGQE 216
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGM---IGCTQPRRVAAMSVAKRVSEEMGVELGEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 217 VGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLD 296
Cdd:cd17983 78 VGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMD 157
|
170
....*....|....*.
gi 1511959583 297 AGKFQIYFDNCPLLTI 312
Cdd:cd17983 158 ADKFADFFGNVPIFTI 173
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
137-312 |
1.80e-69 |
|
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: 226.58 E-value: 1.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGpkRGVACTQPRRVAAMSVAQRVADEMDVMLGQE 216
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGG--RVVGCTQPRRVAAVTVAGRVAEEMGAVLGHE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 217 VGYSIRFEDCSS-AKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATL 295
Cdd:cd17980 79 VGYCIRFDDCTDpQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATL 158
|
170 180
....*....|....*....|....*..
gi 1511959583 296 DAGKFQIYF----------DNCPLLTI 312
Cdd:cd17980 159 DAEKFRDFFnqnetndpskDTATILSV 185
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
137-310 |
3.62e-62 |
|
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: 206.60 E-value: 3.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQE 216
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIGHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 217 VGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLD 296
Cdd:cd17977 81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPHL 160
|
170
....*....|....
gi 1511959583 297 AGKFQIYFDNCPLL 310
Cdd:cd17977 161 SSKLLSYYGNVPLI 174
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
137-312 |
9.73e-62 |
|
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: 205.47 E-value: 9.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDIlVRHQSFVLV-GETGSGKTTQIPQWCVEYMRSLPGpkrGVACTQPRRVAAMSVAQRVADEMDVMLGQ 215
Cdd:cd17984 1 LPIQKQRKKLVQA-VRDNSFLIVtGNTGSGKTTQLPKYLYEAGFSQHG---MIGVTQPRRVAAISVAQRVAEEMKCTLGS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 216 EVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRS-----DLKVIV 290
Cdd:cd17984 77 KVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVV 156
|
170 180
....*....|....*....|..
gi 1511959583 291 MSATLDAGKFQIYFDNCPLLTI 312
Cdd:cd17984 157 MSATLELAKLSAFFGNCPVFDI 178
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
137-312 |
1.12e-56 |
|
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: 191.51 E-value: 1.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRslpGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQE 216
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGR---GIRGLIGHTQPRRLAARSVAERIAEELKTELGGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 217 VGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLD 296
Cdd:cd17989 78 VGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATID 157
|
170
....*....|....*.
gi 1511959583 297 AGKFQIYFDNCPLLTI 312
Cdd:cd17989 158 AERFSRHFNNAPIIEV 173
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
137-295 |
2.11e-54 |
|
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: 186.02 E-value: 2.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRG--VACTQPRRVAAMSVAQRVADEMDVMlG 214
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESDNPgmIGITQPRRVAAVSMAKRVAEELNVF-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 215 QEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSD--------- 285
Cdd:cd17982 80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159
|
170
....*....|.
gi 1511959583 286 -LKVIVMSATL 295
Cdd:cd17982 160 pLKLVIMSATL 170
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
137-312 |
2.66e-54 |
|
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: 185.10 E-value: 2.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLV-GETGSGKTTQIPQWCVEYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQ 215
Cdd:cd17986 1 LPIWAAKFTFLEQLESPSGIVLVsGEPGSGKSTQVPQWCAEFALSRGFQKGQVTVTQPHPLAARSLALRVADEMDLNLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 216 EVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATL 295
Cdd:cd17986 81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPA 160
|
170
....*....|....*..
gi 1511959583 296 DAGKFQIYFDNCPLLTI 312
Cdd:cd17986 161 LEPKLRAFWGNPPVVHV 177
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
137-312 |
1.77e-53 |
|
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: 183.12 E-value: 1.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEymRSLPGPKRGVA---CTQPRRVAAMSVAQRVADEMDVML 213
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILD--NSLQGPPLPVAniiCTQPRRISAISVAERVAQERAERV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 214 GQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSA 293
Cdd:cd17985 79 GQSVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSA 158
|
170
....*....|....*....
gi 1511959583 294 TLDAGKFQIYFDNCPLLTI 312
Cdd:cd17985 159 TLNAELFSDYFNSCPVIHI 177
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
137-312 |
6.31e-52 |
|
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: 178.41 E-value: 6.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCveymrsLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQE 216
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYL------LAAGFRHIACTQPRRIACISLAKRVAFESLNQYGSK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 217 VGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLD 296
Cdd:cd17979 75 VAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATIN 154
|
170
....*....|....*.
gi 1511959583 297 AGKFQIYFDNCPLLTI 312
Cdd:cd17979 155 IELFSGYFEGAPVVQV 170
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
137-312 |
2.13e-49 |
|
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: 171.95 E-value: 2.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVE-YMRSLPGPKRGVACTQPRRVAAMSVAQRVADEM--DVML 213
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDdAIERGKGSSCRIVCTQPRRISAISVAERVAAERaeSCGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 214 GQEVGYSIRFEDCSSAK--TILkYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVM 291
Cdd:cd17981 81 GNSTGYQIRLESRKPRKqgSIL-YCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159
|
170 180
....*....|....*....|.
gi 1511959583 292 SATLDAGKFQIYFDNCPLLTI 312
Cdd:cd17981 160 SATLNAEKFSDYFNNCPMIHI 180
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
137-312 |
2.02e-48 |
|
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: 169.33 E-value: 2.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKR--GVACTQPRRVAAMSVAQRVADEmdvmLG 214
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLLNGGTAQkcNIVCTQPRRISAMSLATRVCEE----LG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 215 QE---------VGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSD 285
Cdd:cd17975 77 CEsgpggknslCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSD 156
|
170 180
....*....|....*....|....*..
gi 1511959583 286 LKVIVMSATLDAGKFQIYFDNCPLLTI 312
Cdd:cd17975 157 LHLILMSATVDCEKFSSYFTHCPILRI 183
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
137-312 |
3.88e-46 |
|
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: 162.69 E-value: 3.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRgVACTQPRRVAAMSVAQRVADEMDVMLGQE 216
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCR-IFCTQPRRLAAIAVAERVAAERGEKIGQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 217 VGYSIRFEDCSSAKTILKYMTDGMLLREAMN-DPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATL 295
Cdd:cd17987 80 VGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAAL 159
|
170
....*....|....*..
gi 1511959583 296 DAGKFQIYFDNCPLLTI 312
Cdd:cd17987 160 DVNLFIRYFGSCPVIYI 176
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
137-310 |
1.29e-41 |
|
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: 149.79 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIP----QWCVEYMRSlpgpkrgVACTQPRRVAAMSVAQRVADEMDVM 212
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPlallAELWIAGGK-------IIVLEPRRVAARAAARRLATLLGEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 213 LGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEvVRQ--RSDLKVIV 290
Cdd:cd17990 74 PGETVGYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLE-VQQllRDDLRLLA 152
|
170 180
....*....|....*....|
gi 1511959583 291 MSATLDAGKFQIYFDNCPLL 310
Cdd:cd17990 153 MSATLDGDGLAALLPEAPVV 172
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
137-312 |
5.26e-40 |
|
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: 145.32 E-value: 5.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVE-YMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQ 215
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEdYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 216 EVGYSIRFEDCSSAKT-ILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSAT 294
Cdd:cd17976 81 NVGYQVRLESRPPPRGgALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
|
170
....*....|....*...
gi 1511959583 295 LDAGKFQIYFDNCPLLTI 312
Cdd:cd17976 161 GDNQRLSRYFGGCPVVRV 178
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
125-312 |
6.35e-38 |
|
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350730 [Multi-domain] Cd Length: 234 Bit Score: 141.51 E-value: 6.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 125 PRYYDILKKRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCV-EYMRSLPGPKRGVACTQPRRVAAMSVAQ 203
Cdd:cd17972 47 HNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILdDFIQNDRAAECNIVVTQPRRISAVSVAE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 204 RVADEMDVMLGQEVGYSIRFEDCSSAK--TILkYMTDGMLLREAMNDplLERYGVIILDEAHERTLATDILMGVLKEVVR 281
Cdd:cd17972 127 RVAFERGEEVGKSCGYSVRFESVLPRPhaSIL-FCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLLVVLRDVVQ 203
|
170 180 190
....*....|....*....|....*....|.
gi 1511959583 282 QRSDLKVIVMSATLDAGKFQIYFDNCPLLTI 312
Cdd:cd17972 204 AYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
137-304 |
6.18e-34 |
|
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: 128.39 E-value: 6.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 137 LPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRslpgpKRGVAC----TQPRRVAAMSVAQRVADEMDVM 212
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYY-----KRGKYCnivvTQPRRIAAISIARRVSQEREWT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 213 LGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSD-LKVIVM 291
Cdd:cd17988 76 LGSLVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILM 155
|
170
....*....|...
gi 1511959583 292 SATLDAGKFQIYF 304
Cdd:cd17988 156 SATISCKEFADYF 168
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
539-627 |
2.03e-30 |
|
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: 115.41 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 539 ALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQCFVRPTE------------- 605
Cdd:pfam04408 1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80
|
90 100
....*....|....*....|....
gi 1511959583 606 AKKAADEAKMRFAHID--GDHLTL 627
Cdd:pfam04408 81 RRAADEKARAKFARLDleGDHLTL 104
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
689-765 |
3.86e-29 |
|
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.
Pssm-ID: 400182 [Multi-domain] Cd Length: 82 Bit Score: 110.81 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 689 IRKALVTGYFMQVAHLERTGH-YLTVKDNQVVQLHPSTVL----DHKPEWVLYNEFVLTTKNYIRTCTDIKPEWLVKIAP 763
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGKgYTTLSDNQRVFIHPSSVLfnekTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80
|
..
gi 1511959583 764 QY 765
Cdd:pfam07717 81 HI 82
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
545-628 |
2.38e-28 |
|
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: 108.51 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 545 YLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQcfVRPTEAKKAADEAKMRFAHIDGDH 624
Cdd:smart00847 1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD--PRPKEKREDADAARRRFADPESDH 78
|
....
gi 1511959583 625 LTLL 628
Cdd:smart00847 79 LTLL 82
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
149-322 |
6.05e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 108.73 E-value: 6.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 149 ILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKrgVACTQPRRVAAMSVAQRVADEMDVMLGQEVGY------SIR 222
Cdd:smart00487 20 LLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGR--VLVLVPTRELAEQWAEELKKLGPSLGLKVVGLyggdskREQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 223 FEDCSSAKTILKYMTDGMLLREAMNDPL-LERYGVIILDEAHERT--LATDILMGVLKEVvrqRSDLKVIVMSATL--DA 297
Cdd:smart00487 98 LRKLESGKTDILVTTPGRLLDLLENDKLsLSNVDLVILDEAHRLLdgGFGDQLEKLLKLL---PKNVQLLLLSATPpeEI 174
|
170 180
....*....|....*....|....*..
gi 1511959583 298 GKFQIYFDNCPLLTIPGRT--HPVEIF 322
Cdd:smart00487 175 ENLLELFLNDPVFIDVGFTplEPIEQF 201
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
148-486 |
9.24e-15 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 78.10 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 148 DILVRHQSFVLVGETGSGKTTQIPQ--WCVEYM---------RSLPGPKRGVACTQPRR--VAAMSVAQRvademdvmlg 214
Cdd:PHA02653 174 EAWISRKPVVLTGGTGVGKTSQVPKllLWFNYLfggfdnldkIDPNFIERPIVLSLPRValVRLHSITLL---------- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 215 qevgYSIRFEDCSSAKTILKY--MTDGMLLREAMNDPL-----------LERYGVIILDEAHERTLATDILMGVL-KEVV 280
Cdd:PHA02653 244 ----KSLGFDEIDGSPISLKYgsIPDELINTNPKPYGLvfsthkltlnkLFDYGTVIIDEVHEHDQIGDIIIAVArKHID 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 281 RQRSdlkVIVMSATL--DAGKFQIYFDNCPLLTIPGRT-HPV-EIF----YTPEPERDYLEAAIRTVIQ-IHMCEEEEG- 350
Cdd:PHA02653 320 KIRS---LFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPIsEVYvknkYNPKNKRAYIEEEKKNIVTaLKKYTPPKGs 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 351 DLLLFLTGQEEIDEACKRIKREVDDLG--------PEVGDIkIIPLYSTLPPQqqqrifeppppkkqngaigrkVVVSTN 422
Cdd:PHA02653 397 SGIVFVASVSQCEEYKKYLEKRLPIYDfyiihgkvPNIDEI-LEKVYSSKNPS---------------------IIISTP 454
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1511959583 423 IAETSLTIDGVVFVIDPGfakqKVYNP-----RIRVesllvtaISKASAQQRAGRAGRTRPGKCFRLYT 486
Cdd:PHA02653 455 YLESSVTIRNATHVYDTG----RVYVPepfggKEMF-------ISKSMRTQRKGRVGRVSPGTYVYFYD 512
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
382-475 |
2.79e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 63.00 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 382 DIKIIPLYSTLPPQQQQRIFEPPPPKKqngaigRKVVVSTNIAETSLTIDGVVFVIDPGFakqkvynprirvesllvtAI 461
Cdd:smart00490 11 GIKVARLHGGLSQEEREEILDKFNNGK------IKVLVATDVAERGLDLPGVDLVIIYDL------------------PW 66
|
90
....*....|....
gi 1511959583 462 SKASAQQRAGRAGR 475
Cdd:smart00490 67 SPASYIQRIGRAGR 80
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
156-294 |
1.45e-09 |
|
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: 57.03 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 156 FVLVGETGSGKTTQIPQWCVEYMRSlPGPKRGVACtqPRRVAAMSVAQRVADEMDvmLGQEVGYSIRFEDcSSAKTILK- 234
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLK-KGKKVLVLV--PTKALALQTAERLRELFG--PGIRVAVLVGGSS-AEEREKNKl 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1511959583 235 ------YMTDGMLLR--EAMNDPLLERYGVIILDEAHERTLATD-ILMGVLKEVVRQRSDLKVIVMSAT 294
Cdd:cd00046 78 gdadiiIATPDMLLNllLREDRLFLKDLKLIIVDEAHALLIDSRgALILDLAVRKAGLKNAQVILLSAT 146
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
336-475 |
8.16e-09 |
|
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: 53.75 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 336 IRTVIQIhMCEEEEGDLLLFLTGQEEIDeaCKRIKREvddlgpevGDIKIIPLYSTLPPQQQQRIFEPPPPKKqngaigR 415
Cdd:pfam00271 3 LEALLEL-LKKERGGKVLIFSQTKKTLE--AELLLEK--------EGIKVARLHGDLSQEEREEILEDFRKGK------I 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 416 KVVVSTNIAETSLTIDGVVFVIDPGFakqkVYNPrirvesllvtaiskASAQQRAGRAGR 475
Cdd:pfam00271 66 DVLVATDVAERGLDLPDVDLVINYDL----PWNP--------------ASYIQRIGRAGR 107
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
157-294 |
5.62e-08 |
|
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: 52.55 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 157 VLVGETGSGKTTQIPQwcvEYMRSLPGPKRGVACTQPRRVAAMSVAQrvademdVMLGQEVGY---SIRFEDcsSAKTIL 233
Cdd:cd17931 5 VLDLHPGAGKTTRVLP---QIIREAIKKRLRTLVLAPTRVVAAEMYE-------ALRGLPIRYrtgAVKEEH--GGNEIV 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511959583 234 KYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVrQRSDLKVIVMSAT 294
Cdd:cd17931 73 DYMCHGTFTCRLLSPKRVPNYNLIIMDEAHFTDPASIAARGYIHTRV-EMGEAAVIFMTAT 132
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
154-296 |
1.09e-07 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 52.24 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 154 QSFVLVGETGSGKTT--QIPqwCVEYMRSLPGPKRGVaCTQPRRVAA---MSVAQRVADEMDVMLGQEVGYSIRFEDCSS 228
Cdd:pfam00270 15 RDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQAL-VLAPTRELAeqiYEELKKLGKGLGLKVASLLGGDSRKEQLEK 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 229 AKTI-LKYMTDGMLLREAMNDPLLERYGVIILDEAHErtLATDILMGVLKEVVRQ-RSDLKVIVMSATLD 296
Cdd:pfam00270 92 LKGPdILVGTPGRLLDLLQERKLLKNLKLLVLDEAHR--LLDMGFGPDLEEILRRlPKKRQILLLSATLP 159
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
416-485 |
8.88e-05 |
|
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: 41.54 E-value: 8.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511959583 416 KVVVSTNIAETSLTIDGVVFVIDPGFAkqkvynprirvesllvtaISKASAQQRAGRAGR--TRPGKCFRLY 485
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDPP------------------SSAASYIQRVGRAGRggKDEGEVILFV 77
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
153-263 |
5.36e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 40.79 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 153 HQSF-VLVGETGSGKTTQipqwCVEYMRSLPGPKRGVACTQPRrvAAMSVAqrvadEMDVMLGQEVGYSIRFEDCSSAkt 231
Cdd:pfam13401 4 GAGIlVLTGESGTGKTTL----LRRLLEQLPEVRDSVVFVDLP--SGTSPK-----DLLRALLRALGLPLSGRLSKEE-- 70
|
90 100 110
....*....|....*....|....*....|....
gi 1511959583 232 ilkymtdgmlLREAMNDPLLERY--GVIILDEAH 263
Cdd:pfam13401 71 ----------LLAALQQLLLALAvaVVLIIDEAQ 94
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
254-472 |
3.99e-03 |
|
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: 40.45 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 254 YGVIILDEAH---ERTLAtdILMGVLKEVVRQRSdlKVIVMSATLdagkfqiyfdncPLLTIPGRTHPVE-IFYTPEPER 329
Cdd:COG1203 269 NSVIILDEVQaypPYMLA--LLLRLLEWLKNLGG--SVILMTATL------------PPLLREELLEAYElIPDEPEELP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 330 DYLEAAIRTVIQIHMCEEEEGDLLlfltgqEEIDEACKRIK------------REV-DDLGPEVGDIKIIpLYST-LPPQ 395
Cdd:COG1203 333 EYFRAFVRKRVELKEGPLSDEELA------ELILEALHKGKsvlvivntvkdaQELyEALKEKLPDEEVY-LLHSrFCPA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 396 QQQRI-------FEPPppkkqngaiGRKVVVSTNIAETSLTID-GVVFvIDPGfakqkvynPrirVESLLvtaiskasaq 467
Cdd:COG1203 406 DRSEIekeikerLERG---------KPCILVSTQVVEAGVDIDfDVVI-RDLA--------P---LDSLI---------- 454
|
....*
gi 1511959583 468 QRAGR 472
Cdd:COG1203 455 QRAGR 459
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
152-301 |
7.65e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.74 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511959583 152 RHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRgVACTQPRRVAAMSVAQRVADEMDVMLGQevgysirfedcssakt 231
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-IDGEDILEEVLDQLLLIIVGGKKASGSG---------------- 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1511959583 232 ilkymtdGMLLREAMNDPLLERYGVIILDEAH----ERTLATDILMGVLKEVVRQRSDLKVIVMSATLDAGKFQ 301
Cdd:smart00382 64 -------ELRLRLALALARKLKPDVLILDEITslldAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| |
