|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
51-724 |
3.33e-160 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 485.74 E-value: 3.33e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 51 PTFPIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKV 130
Cdd:COG1643 8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGETV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 131 GYQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLfQEKSpnRkEHLKVVVMS 210
Cdd:COG1643 88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDL-QPAL--R-PDLKLLVMS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 211 ATMELAKLSAFFGNCPIFDIPGRLYPVREKFCnligPRDRENTAYIQAIVKVTMDIhLNEMAGDILVFLTGQFEIEKSCE 290
Cdd:COG1643 164 ATLDAERFARLLGDAPVIESSGRTYPVEVRYR----PLPADERDLEDAVADAVREA-LAEEPGDILVFLPGEREIRRTAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 291 LLfqmaesvdydydvQDTTLDGLLILPCYGSMTTDQQRRIFLPPPPGIRKCVISTNISATSLTIDGIRYVVDGGFVKQLN 370
Cdd:COG1643 239 AL-------------RGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 371 HNPRLGLDILEVVPISKSEALQRSGRAGRTSSGKCFRIYSKDFWNQcMPDHVIPEIKRTSLTSVVLTLKCLAIHDVIRFP 450
Cdd:COG1643 306 YDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFAR-RPAFTDPEILRADLASLILELAAWGLGDPEDLP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 451 YLDPPNERLILEALKQLYQCDAIDRSGHVTRLGLSMVEFPLPPHLTCAVIKAASLDCEDLLLPIAAMLSVENVFIRPVDP 530
Cdd:COG1643 385 FLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 531 EYQkEAEQRHRELATKAGGFNDFATLAvifeqckssgapaswcqkhwiHWRclfsafRVEAQLRELIRKLKQQsdfpret 610
Cdd:COG1643 465 DLL-ARLNLWRRLREQQREFLSYLRLR---------------------EWR------DLARQLRRLLGEGANE------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 611 fEGPKHEVLRRCLCAGYFKNVA-RRSVGRTFCTMDGRGspVHIHPSSALHeqetKLEWIIFHEvLVTTKVYARI--VCPI 687
Cdd:COG1643 510 -EPADYEAIGLLLALAYPDRIArRRGEGGRYLLARGRG--AALFPGSPLA----KKEWLVAAE-LVGGAAEARIrlAAPI 581
|
650 660 670
....*....|....*....|....*....|....*....
gi 380816558 688 RYEWVRDLLPKL--HEFNAHdlSSVARREVRedARRRWT 724
Cdd:COG1643 582 DPEWLEELAAHLikRYSEPH--WDKKRGRVV--ARERVR 616
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
54-705 |
5.47e-127 |
|
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: 409.93 E-value: 5.47e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGYQ 133
Cdd:TIGR01967 67 PVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKVGYK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 134 VRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQekspnRKEHLKVVVMSATM 213
Cdd:TIGR01967 147 VRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLP-----RRPDLKIIITSATI 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 214 ELAKLSAFFGNCPIFDIPGRLYPVREKFCNLIGPRDRENTAYIQAIVKvTMDIHLNEMAGDILVFLTGQFEIEKSCELLf 293
Cdd:TIGR01967 222 DPERFSRHFNNAPIIEVSGRTYPVEVRYRPLVEEQEDDDLDQLEAILD-AVDELFAEGPGDILIFLPGEREIRDAAEIL- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 294 qmaesvdydydvQDTTLDGLLILPCYGSMTTDQQRRIFLPPPPgiRKCVISTNISATSLTIDGIRYVVDGGFVKQLNHNP 373
Cdd:TIGR01967 300 ------------RKRNLRHTEILPLYARLSNKEQQRVFQPHSG--RRIVLATNVAETSLTVPGIHYVIDTGTARISRYSY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 374 RLGLDILEVVPISKSEALQRSGRAGRTSSGKCFRIYSKDFWNQcMPDHVIPEIKRTSLTSVVLTLKCLAIHDVIRFPYLD 453
Cdd:TIGR01967 366 RTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNS-RPEFTDPEILRTNLASVILQMLALRLGDIAAFPFIE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 454 PPNERLILEALKQLYQCDAIDR---SGHVTRLGLSMVEFPLPPHLTCAVIKAASLDCEDLLLPIAAMLSVENVFIRPvdP 530
Cdd:TIGR01967 445 APDPRAIRDGFRLLEELGALDDdeaEPQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERP--M 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 531 EYQKEAEQRHRELATKAGGFNDFATLAVIFE---QCKSSGAPASWCQKHWIH------WRCLFSafrveaQLRELIRKLK 601
Cdd:TIGR01967 523 EKQQAADQAHARFKDPRSDFLSRVNLWRHIEeqrQALSANQFRNACRKQYLNylrvreWQDIYR------QLTQVVKELG 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 602 -QQSDFPREtfegpkHEVLRRCLCAGYFKNVARRSVGRTFctmDG-RGSPVHIHPSSALHEQETKleWIIFHEVLVTTKV 679
Cdd:TIGR01967 597 lKLNEEPAD------YDAIHKALLSGLLSQIGMKDEKHEY---DGaRGRKFHIFPGSPLFKKPPK--WVMAAELVETSKL 665
|
650 660
....*....|....*....|....*....
gi 380816558 680 YARIVCPIRYEWVRDLLPKL---HEFNAH 705
Cdd:TIGR01967 666 YARLVAKIEPEWVEPVAGHLikkNYFEPH 694
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
53-230 |
4.47e-121 |
|
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: 361.09 E-value: 4.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 53 FPIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGY 132
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGSKVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 133 QVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSPNRKEHLKVVVMSAT 212
Cdd:cd17984 81 QVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPNRKEHLKVVVMSAT 160
|
170
....*....|....*...
gi 380816558 213 MELAKLSAFFGNCPIFDI 230
Cdd:cd17984 161 LELAKLSAFFGNCPVFDI 178
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
51-699 |
7.14e-119 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 388.26 E-value: 7.14e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 51 PTFPIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKV 130
Cdd:PRK11131 71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 131 GYQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFqeksPNRKEhLKVVVMS 210
Cdd:PRK11131 151 GYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELL----PRRPD-LKVIITS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 211 ATMELAKLSAFFGNCPIFDIPGRLYPVREKFCNLIGPRDRENTAYIQAIVKvTMDIHLNEMAGDILVFLTGQFEIEKSCE 290
Cdd:PRK11131 226 ATIDPERFSRHFNNAPIIEVSGRTYPVEVRYRPIVEEADDTERDQLQAIFD-AVDELGREGPGDILIFMSGEREIRDTAD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 291 LLFQMaesvdydyDVQDTTldgllILPCYGSMTTDQQRRIFlpPPPGIRKCVISTNISATSLTIDGIRYVVDGGFVKQLN 370
Cdd:PRK11131 305 ALNKL--------NLRHTE-----ILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISR 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 371 HNPRLGLDILEVVPISKSEALQRSGRAGRTSSGKCFRIYSK-DFWNQcmPDHVIPEIKRTSLTSVVLTLKCLAIHDVIRF 449
Cdd:PRK11131 370 YSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEdDFLSR--PEFTDPEILRTNLASVILQMTALGLGDIAAF 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 450 PYLDPPNERLILEALKQLYQCDAI--DRSGHVTRL---GLSMVEFPLPPHLTCAVIKAASLDCEDLLLPIAAMLSVENVF 524
Cdd:PRK11131 448 PFVEAPDKRNIQDGVRLLEELGAIttDEQASAYKLtplGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPR 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 525 IRPVDPeyQKEAEQRHRELATKAGGFNDFATL-AVIFEQCK--SSGAPASWCQKHWIHWrclfsaFRVE------AQLRE 595
Cdd:PRK11131 528 ERPMDK--QQASDEKHRRFADKESDFLAFVNLwNYLQEQQKalSSNQFRRLCRTDYLNY------LRVRewqdiyTQLRQ 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 596 LIRKLkqqsDFPRETFEGPKHEVlRRCLCAGYFKNVARRSVGRTFCTmDGRGSPVHIHPSSALHEQETKleWIIFHEVLV 675
Cdd:PRK11131 600 VVKEL----GIPVNSEPAEYREI-HTALLTGLLSHIGMKDAEKQEYT-GARNARFSIFPGSGLFKKPPK--WVMVAELVE 671
|
650 660
....*....|....*....|....
gi 380816558 676 TTKVYARIVCPIRYEWVRDLLPKL 699
Cdd:PRK11131 672 TSRLWGRIAARIEPEWIEPLAQHL 695
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
69-230 |
1.66e-82 |
|
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: 259.70 E-value: 1.66e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 69 NSFLIVTGNTGSGKTTQLPKYLYEAGFS--QHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGYQVRFDDCSSKETAI 146
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAkgGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 147 KYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQekspnRKEHLKVVVMSATMELAKLSAFFGNCP 226
Cdd:cd17917 81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLR-----KRPDLKVILMSATLDAEKFSSYFGGAP 155
|
....
gi 380816558 227 IFDI 230
Cdd:cd17917 156 VIHI 159
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
54-230 |
2.53e-82 |
|
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: 259.98 E-value: 2.53e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGYQ 133
Cdd:cd17978 2 PIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVGYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 134 VRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSPNRKEHLKVVVMSATM 213
Cdd:cd17978 82 VRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEQKLSPLKVIIMSATL 161
|
170
....*....|....*..
gi 380816558 214 ELAKLSAFFGNCPIFDI 230
Cdd:cd17978 162 DADLFSEYFNGAPVLYI 178
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
52-231 |
4.45e-80 |
|
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: 254.33 E-value: 4.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 52 TFPIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVG 131
Cdd:cd17971 5 SLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLGQEVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 132 YQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQekspnRKEHLKVVVMSA 211
Cdd:cd17971 85 YTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQ-----KRPDLKLIVTSA 159
|
170 180
....*....|....*....|
gi 380816558 212 TMELAKLSAFFGNCPIFDIP 231
Cdd:cd17971 160 TLDAVKFSQYFYEAPIFTIP 179
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
54-230 |
1.33e-79 |
|
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: 252.77 E-value: 1.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGYQ 133
Cdd:cd17983 2 PIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 134 VRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQekspnRKEHLKVVVMSATM 213
Cdd:cd17983 82 IRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVA-----RRRDLKLIVTSATM 156
|
170
....*....|....*..
gi 380816558 214 ELAKLSAFFGNCPIFDI 230
Cdd:cd17983 157 DADKFADFFGNVPIFTI 173
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
62-548 |
2.63e-75 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 260.63 E-value: 2.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 62 IIQAVRDNSFLIVTGNTGSGKTTQLP-KYLYEAGFSqhGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGYQVRFDDCS 140
Cdd:PRK11664 13 LLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGIN--GKIIMLEPRRLAARNVAQRLAEQLGEKPGETVGYRMRAESKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 141 SKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLfQEkspNRKEHLKVVVMSATMELAKLSA 220
Cdd:PRK11664 91 GPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDV-QQ---GLRDDLKLLIMSATLDNDRLQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 221 FFGNCPIFDIPGRLYPVREKFCNLiGPRDRENTAYIQAIVKVtmdihLNEMAGDILVFLTGQFEIEKSCELLfqmAESVD 300
Cdd:PRK11664 167 LLPDAPVIVSEGRSFPVERRYQPL-PAHQRFDEAVARATAEL-----LRQESGSLLLFLPGVGEIQRVQEQL---ASRVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 301 YDYDvqdttldgllILPCYGSMTTDQQRRIFLPPPPGIRKCVISTNISATSLTIDGIRYVVDGGFVKQLNHNPRLGLDIL 380
Cdd:PRK11664 238 SDVL----------LCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 381 EVVPISKSEALQRSGRAGRTSSGKCFRIYSKDFWNQcMPDHVIPEIKRTSLTSVVLTLKCLAIHDVIRFPYLDPPNERLI 460
Cdd:PRK11664 308 VTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAER-AAAQSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAAL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 461 LEALKQLYQCDAIDRSGHVTRLGLSMVEFPLPPHLTCAVIKAASLDceDLLLPIAAML-------------SVENVFIRP 527
Cdd:PRK11664 387 AAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKEDD--EAALATAAKLaaileepprsgssDLGVALSRK 464
|
490 500
....*....|....*....|.
gi 380816558 528 vDPEYQKEAEQRHRELATKAG 548
Cdd:PRK11664 465 -QPHWQQRAQQLLKRLNVRGG 484
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
54-230 |
8.60e-71 |
|
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: 229.31 E-value: 8.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGM-IGVTQPRKVAAISVAQRVAEEMKCTLGSKVGY 132
Cdd:cd17974 2 PVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGkIGCTQPRRVAAMSVAARVAEEMGVKLGNEVGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 133 QVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLfqekSPNRKEhLKVVVMSAT 212
Cdd:cd17974 82 SIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDI----ARFRPD-LKLLISSAT 156
|
170
....*....|....*...
gi 380816558 213 MELAKLSAFFGNCPIFDI 230
Cdd:cd17974 157 MDAEKFSAFFDDAPIFRI 174
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
235-409 |
2.54e-70 |
|
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: 228.19 E-value: 2.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 235 YPVREKFCNLIGPR-----DRENTAYIQAIVKVTMDIHLNEMAGDILVFLTGQFEIEKSCELLFQMAESVDydydvqdtt 309
Cdd:cd18791 1 FPVEVYYLEDILELlgissEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPD--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 310 LDGLLILPCYGSMTTDQQRRIFLPPPPGIRKCVISTNISATSLTIDGIRYVVDGGFVKQLNHNPRLGLDILEVVPISKSE 389
Cdd:cd18791 72 LGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKAS 151
|
170 180
....*....|....*....|
gi 380816558 390 ALQRSGRAGRTSSGKCFRIY 409
Cdd:cd18791 152 AEQRAGRAGRTRPGKCYRLY 171
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
54-230 |
3.13e-67 |
|
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: 220.36 E-value: 3.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHG--MIGVTQPRKVAAISVAQRVAEEMKCTLGSKVG 131
Cdd:cd17973 14 PVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPkkLVACTQPRRVAAMSVAQRVAEEMDVKLGEEVG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 132 YQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQekspnRKEHLKVVVMSA 211
Cdd:cd17973 94 YSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVR-----RRPDLKLIVMSA 168
|
170
....*....|....*....
gi 380816558 212 TMELAKLSAFFGNCPIFDI 230
Cdd:cd17973 169 TLDAGKFQKYFDNAPLLKV 187
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
54-231 |
1.21e-65 |
|
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350740 [Multi-domain] Cd Length: 191 Bit Score: 216.45 E-value: 1.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQH-----GMIGVTQPRKVAAISVAQRVAEEMKcTLGS 128
Cdd:cd17982 2 PILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPesdnpGMIGITQPRRVAAVSMAKRVAEELN-VFGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 129 KVGYQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLL-------KKLFqeKSPNRK 201
Cdd:cd17982 81 EVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLsrivplrAKLY--LQDQTV 158
|
170 180 190
....*....|....*....|....*....|
gi 380816558 202 EHLKVVVMSATMelaKLSAFFGNCPIFDIP 231
Cdd:cd17982 159 KPLKLVIMSATL---RVEDFTENKLLFPRP 185
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
54-222 |
7.45e-63 |
|
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: 208.48 E-value: 7.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHG-MIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGY 132
Cdd:cd17980 2 PVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGrVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 133 QVRFDDCSSK-ETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQekspnRKEHLKVVVMSA 211
Cdd:cd17980 82 CIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQK-----KRGDLRLIVASA 156
|
170
....*....|.
gi 380816558 212 TMELAKLSAFF 222
Cdd:cd17980 157 TLDAEKFRDFF 167
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
54-230 |
3.12e-58 |
|
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: 195.75 E-value: 3.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGYQ 133
Cdd:cd17989 2 PVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAVGYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 134 VRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFqeksPNRKEhLKVVVMSATM 213
Cdd:cd17989 82 VRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLL----PRRPD-LKVIITSATI 156
|
170
....*....|....*..
gi 380816558 214 ELAKLSAFFGNCPIFDI 230
Cdd:cd17989 157 DAERFSRHFNNAPIIEV 173
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
54-230 |
1.48e-49 |
|
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: 171.86 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQhgmIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGYQ 133
Cdd:cd17979 2 PIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH---IACTQPRRIACISLAKRVAFESLNQYGSKVAYQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 134 VRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQekspnRKEHLKVVVMSATM 213
Cdd:cd17979 79 IRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLR-----LRPDLKLILMSATI 153
|
170
....*....|....*..
gi 380816558 214 ELAKLSAFFGNCPIFDI 230
Cdd:cd17979 154 NIELFSGYFEGAPVVQV 170
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
54-223 |
1.28e-43 |
|
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: 155.74 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGF--SQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVG 131
Cdd:cd17988 2 PIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYkrGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 132 YQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSpnrkEHLKVVVMSA 211
Cdd:cd17988 82 YQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNS----RHVKIILMSA 157
|
170
....*....|..
gi 380816558 212 TMELAKLSAFFG 223
Cdd:cd17988 158 TISCKEFADYFT 169
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
54-230 |
3.37e-42 |
|
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: 151.53 E-value: 3.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLY----EAGFSQHGMIGVTQPRKVAAISVAQRVAEEM--KCTLG 127
Cdd:cd17981 2 PSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILddaiERGKGSSCRIVCTQPRRISAISVAERVAAERaeSCGLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 128 SKVGYQVRFDDCSSKETA-IKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFqekspNRKEHLKV 206
Cdd:cd17981 82 NSTGYQIRLESRKPRKQGsILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLL-----PFRSDLKV 156
|
170 180
....*....|....*....|....
gi 380816558 207 VVMSATMELAKLSAFFGNCPIFDI 230
Cdd:cd17981 157 ILMSATLNAEKFSDYFNNCPMIHI 180
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
54-228 |
2.11e-40 |
|
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: 146.32 E-value: 2.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGYQ 133
Cdd:cd17990 2 PIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVGYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 134 VRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEkspnRKEHLKVVVMSATM 213
Cdd:cd17990 82 VRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQL----LRDDLRLLAMSATL 157
|
170
....*....|....*
gi 380816558 214 ELAKLSAFFGNCPIF 228
Cdd:cd17990 158 DGDGLAALLPEAPVV 172
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
54-227 |
7.59e-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: 144.94 E-value: 7.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYE----AGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSK 129
Cdd:cd17976 2 PVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEdyvlRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRRN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 130 VGYQVRFDD-CSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSpnrkeHLKVVV 208
Cdd:cd17976 82 VGYQVRLESrPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNP-----ELRVVL 156
|
170
....*....|....*....
gi 380816558 209 MSATMELAKLSAFFGNCPI 227
Cdd:cd17976 157 MSATGDNQRLSRYFGGCPV 175
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
54-230 |
9.73e-39 |
|
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: 141.90 E-value: 9.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGF----SQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSK 129
Cdd:cd17985 2 PAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLqgppLPVANIICTQPRRISAISVAERVAQERAERVGQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 130 VGYQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSpnrkeHLKVVVM 209
Cdd:cd17985 82 VGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRP-----DLKVILM 156
|
170 180
....*....|....*....|.
gi 380816558 210 SATMELAKLSAFFGNCPIFDI 230
Cdd:cd17985 157 SATLNAELFSDYFNSCPVIHI 177
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
54-230 |
1.91e-38 |
|
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: 140.73 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYE---AGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKV 130
Cdd:cd17977 2 PVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEyclSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIGHEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 131 GYQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEkspnRKEhLKVVVMS 210
Cdd:cd17977 82 GYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLS----RPE-LKLVIIT 156
|
170 180
....*....|....*....|
gi 380816558 211 ATMELAKLSAFFGNCPIFDI 230
Cdd:cd17977 157 CPHLSSKLLSYYGNVPLIEV 176
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
53-230 |
7.57e-38 |
|
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: 139.28 E-value: 7.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 53 FPIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYE-----AGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLG 127
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEdlllnGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 128 -----SKVGYQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSpnrke 202
Cdd:cd17975 81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRS----- 155
|
170 180
....*....|....*....|....*...
gi 380816558 203 HLKVVVMSATMELAKLSAFFGNCPIFDI 230
Cdd:cd17975 156 DLHLILMSATVDCEKFSSYFTHCPILRI 183
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
54-230 |
2.13e-37 |
|
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350745 [Multi-domain] Cd Length: 176 Bit Score: 138.04 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHG--MIGVTQPRKVAAISVAQRVAEEMKCTLGSKVG 131
Cdd:cd17987 2 PVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIpcRIFCTQPRRLAAIAVAERVAAERGEKIGQTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 132 YQVRFDDCSSKETAIKYMTDGCLLKHIL-GDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSpnrkeHLKVVVMS 210
Cdd:cd17987 82 YQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHP-----NLKLILSS 156
|
170 180
....*....|....*....|
gi 380816558 211 ATMELAKLSAFFGNCPIFDI 230
Cdd:cd17987 157 AALDVNLFIRYFGSCPVIYI 176
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
53-230 |
9.24e-36 |
|
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: 133.48 E-value: 9.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 53 FPIQKQRKKIIQAVRDNS-FLIVTGNTGSGKTTQLPKYLYEAGFS---QHGMIGVTQPRKVAAISVAQRVAEEMKCTLGS 128
Cdd:cd17986 1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFALSrgfQKGQVTVTQPHPLAARSLALRVADEMDLNLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 129 KVGYQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEkspnRKEHLKVVV 208
Cdd:cd17986 81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQ----RPELRVVVV 156
|
170 180
....*....|....*....|..
gi 380816558 209 MSATMElAKLSAFFGNCPIFDI 230
Cdd:cd17986 157 TSPALE-PKLRAFWGNPPVVHV 177
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
54-230 |
4.44e-35 |
|
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: 133.42 E-value: 4.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAgFSQHGM-----IGVTQPRKVAAISVAQRVAEEMKCTLGS 128
Cdd:cd17972 60 PVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDD-FIQNDRaaecnIVVTQPRRISAVSVAERVAFERGEEVGK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 129 KVGYQVRFDDCSSK-ETAIKYMTDGCLLKHIlgDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSpnrkeHLKVV 207
Cdd:cd17972 139 SCGYSVRFESVLPRpHASILFCTVGVLLRKL--EAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYP-----DLRVI 211
|
170 180
....*....|....*....|...
gi 380816558 208 VMSATMELAKLSAFFGNCPIFDI 230
Cdd:cd17972 212 LMSATIDTSMFCEYFFNCPVIEV 234
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
48-236 |
7.57e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 105.65 E-value: 7.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 48 GTTPTFPIQKQ-RKKIIQAVRDnsfLIVTGNTGSGKTTQLPKYLYEAGFSQ-HGMIGVTQPRKVAAISVAQRVAEEMKCT 125
Cdd:smart00487 5 GFEPLRPYQKEaIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 126 LGSKVGY------QVRFDDCSSKETAIKYMTDGCLLKHILGDP-NLTKFSVIILDEAHERT--LTTDILFGLLKKLfqek 196
Cdd:smart00487 82 GLKVVGLyggdskREQLRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLLdgGFGDQLEKLLKLL---- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 380816558 197 spnrKEHLKVVVMSATM--ELAKLSAFFGNCPIFDIPGRLYP 236
Cdd:smart00487 158 ----PKNVQLLLLSATPpeEIENLLELFLNDPVFIDVGFTPL 195
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
463-547 |
7.93e-19 |
|
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: 82.29 E-value: 7.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 463 ALKQLYQCDAIDRSGHVTRLGLSMVEFPLPPHLTCAVIKAASLDCEDLLLPIAAMLSVENVFIRPVDPEYQKEAEQRHRE 542
Cdd:pfam04408 1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAARRR 80
|
....*
gi 380816558 543 LATKA 547
Cdd:pfam04408 81 RRAAD 85
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
619-699 |
7.99e-19 |
|
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: 81.53 E-value: 7.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 619 LRRCLCAGYFKNVARR-SVGRTFCTMDGrGSPVHIHPSSAL-HEQETKLEWIIFHEVLVTTKVYARIVCPIRYEWVRDLL 696
Cdd:pfam07717 1 LRAALAAGLYPNVARRdPKGKGYTTLSD-NQRVFIHPSSVLfNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFA 79
|
...
gi 380816558 697 PKL 699
Cdd:pfam07717 80 PHI 82
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
469-557 |
3.89e-17 |
|
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: 76.54 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 469 QCDAIDRSGHVTRLGLSMVEFPLPPHLTCAVIKAASLDCEDLLLPIAAMLSVENVFIRpvdpEYQKEAEQRHRELATKAG 548
Cdd:smart00847 1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPK----EKREDADAARRRFADPES 76
|
....*....
gi 380816558 549 gfnDFATLA 557
Cdd:smart00847 77 ---DHLTLL 82
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
61-412 |
2.54e-14 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 76.94 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 61 KIIQAVRDNSFLIVTGNTGSGKTTQLPK------YLYeAGFSQHGMIGVT-QPRKVAaISVAqRVA--EEMKCTLGSKVG 131
Cdd:PHA02653 171 KIFEAWISRKPVVLTGGTGVGKTSQVPKlllwfnYLF-GGFDNLDKIDPNfIERPIV-LSLP-RVAlvRLHSITLLKSLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 132 yqvrFDDCSSKETAIKY--MTD----------GCLLK-HILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLfqeksP 198
Cdd:PHA02653 248 ----FDEIDGSPISLKYgsIPDelintnpkpyGLVFStHKLTLNKLFDYGTVIIDEVHEHDQIGDIIIAVARKH-----I 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 199 NRKEHLkvVVMSATME--LAKLSAFFGNcPIF-DIPG-RLYPVREKFC-NLIGPRDR------ENTAYIQAIVKVTMDih 267
Cdd:PHA02653 319 DKIRSL--FLMTATLEddRDRIKEFFPN-PAFvHIPGgTLFPISEVYVkNKYNPKNKrayieeEKKNIVTALKKYTPP-- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 268 lNEMAGDILVFLTGQfeieksCELLFQMAESVDYDYDV-----QDTTLDGLLilpcygsmttdqqRRIFLPPPPGIrkcV 342
Cdd:PHA02653 394 -KGSSGIVFVASVSQ------CEEYKKYLEKRLPIYDFyiihgKVPNIDEIL-------------EKVYSSKNPSI---I 450
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380816558 343 ISTNISATSLTIDGIRYVVDGG--FVKQlnhnPRLGLDILevvpISKSEALQRSGRAGRTSSGKCFRIYSKD 412
Cdd:PHA02653 451 ISTPYLESSVTIRNATHVYDTGrvYVPE----PFGGKEMF----ISKSMRTQRKGRVGRVSPGTYVYFYDLD 514
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
312-399 |
3.39e-11 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 59.92 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 312 GLLILPCYGSMTTDQQRRIFLPPPPGIRKCVISTNISATSLTIDGIRYVVDGGFvkqlnhnprlgldilevvPISKSEAL 391
Cdd:smart00490 11 GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL------------------PWSPASYI 72
|
....*...
gi 380816558 392 QRSGRAGR 399
Cdd:smart00490 73 QRIGRAGR 80
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
69-212 |
7.72e-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: 55.10 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 69 NSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKctLGSKVGYQVRFDDCSSKETAIK- 147
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLRELFG--PGIRVAVLVGGSSAEEREKNKLg 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380816558 148 -----YMTDGCLLKHILGD--PNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSPNrkehLKVVVMSAT 212
Cdd:cd00046 79 dadiiIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKN----AQVILLSAT 146
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
260-399 |
5.80e-08 |
|
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: 51.44 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 260 VKVTMDIHLNEMAGDILVFLTGQFEIEksCELLFQmaesvdydydvqdttLDGLLILPCYGSMTTDQQRRIFLPPPPGIR 339
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLE--AELLLE---------------KEGIKVARLHGDLSQEEREEILEDFRKGKI 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 340 KCVISTNISATSLTIDGIRYVVDGGFvkqlnhnprlgldilevvPISKSEALQRSGRAGR 399
Cdd:pfam00271 66 DVLVATDVAERGLDLPDVDLVINYDL------------------PWNPASYIQRIGRAGR 107
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
54-213 |
2.49e-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: 51.09 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 54 PIQKQrkkIIQAVRDNSFLIVTGNTGSGKTT--QLPkYLYEAGFSQHGMIG-VTQPRKVAAI---SVAQRVAEEMKCTLG 127
Cdd:pfam00270 2 PIQAE---AIPAILEGRDVLVQAPTGSGKTLafLLP-ALEALDKLDNGPQAlVLAPTRELAEqiyEELKKLGKGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 128 SKVGYQVRFDDCSS-KETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHErtlTTDILFG-LLKKLFQEKSPNRkehlK 205
Cdd:pfam00270 78 SLLGGDSRKEQLEKlKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAHR---LLDMGFGpDLEEILRRLPKKR----Q 150
|
....*...
gi 380816558 206 VVVMSATM 213
Cdd:pfam00270 151 ILLLSATL 158
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
71-176 |
1.14e-04 |
|
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350689 [Multi-domain] Cd Length: 151 Bit Score: 42.92 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 71 FLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAeemkctlGSKVGYQ---VRFDDcsSKETAIK 147
Cdd:cd17931 3 LTVLDLHPGAGKTTRVLPQIIREAIKKRLRTLVLAPTRVVAAEMYEALR-------GLPIRYRtgaVKEEH--GGNEIVD 73
|
90 100
....*....|....*....|....*....
gi 380816558 148 YMTDGCLLKHILGDPNLTKFSVIILDEAH 176
Cdd:cd17931 74 YMCHGTFTCRLLSPKRVPNYNLIIMDEAH 102
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
70-218 |
2.57e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.56 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 70 SFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEmkctlgskvgYQVRFDDCSSKETAIKYM 149
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRA----------LGLPLSGRLSKEELLAAL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380816558 150 TDGCLLKHILGdpnltkfsVIILDEAHErtLTTDILFgLLKKLFqekspNRKEHLKVVVMSATMELAKL 218
Cdd:pfam13401 76 QQLLLALAVAV--------VLIIDEAQH--LSLEALE-ELRDLL-----NLSSKLLQLILVGTPELREL 128
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
166-291 |
3.65e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 40.59 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 166 KFSVIILDEAH----ERTLTTDILFGLlkklfqeKSPNRkehlkvVVMSAT-MELaKLSAFFGncpIFDI--PGRLYPV- 237
Cdd:COG0553 358 DWDLVILDEAQhiknPATKRAKAVRAL-------KARHR------LALTGTpVEN-RLEELWS---LLDFlnPGLLGSLk 420
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 380816558 238 --REKFCNLIGPRDRENTAYIQAIVKVTMdihLNEMAGDILVFLTGQFEIEKSCEL 291
Cdd:COG0553 421 afRERFARPIEKGDEEALERLRRLLRPFL---LRRTKEDVLKDLPEKTEETLYVEL 473
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
67-214 |
7.67e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 38.38 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 67 RDNSFLIVTGNTGSGKTTqlpkYLYEAGFSQH-GMIGVTQPrkvaaisvaqrvAEEMKCTLGSKVGYQVRFDDCSSKETA 145
Cdd:cd03243 27 GSGRLLLITGPNMGGKST----YLRSIGLAVLlAQIGCFVP------------AESASIPLVDRIFTRIGAEDSISDGRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380816558 146 iKYMTDGCLLKHILGdpNLTKFSVIILDEAHERTLTTD---ILFGLLKKLFQEKS----------PNRKEHLKVVVMSAT 212
Cdd:cd03243 91 -TFMAELLELKEILS--LATPRSLVLIDELGRGTSTAEglaIAYAVLEHLLEKGCrtlfathfheLADLPEQVPGVKNLH 167
|
..
gi 380816558 213 ME 214
Cdd:cd03243 168 ME 169
|
|
| |
