|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
40-715 |
3.23e-173 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 516.94 E-value: 3.23e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 40 SLPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKmIGITQPRRIAAVTVAKRVAEECEVQLGQKV 119
Cdd:COG1643 9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGR-IGMLEPRRLAARAAAERMAEELGEPVGETV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 120 GYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKkiqrtrsqpvsektefgnva 199
Cdd:COG1643 88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLL-------------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 200 sQVQTTTRDangpqqngvlkgyqgrklsPLKLIIMSASLDARVFSEYFGGAKAVHVQGRQFPVDILYT--VHPESDYVDA 277
Cdd:COG1643 148 -DLQPALRP-------------------DLKLLVMSATLDAERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 278 TLVTIFQIHFEEkPGDILVFLTGQDEIESVERLVQERLQNIPEdkrkLLPLaiFSALPSEQQMKVFAPAPTGFRKVILAT 357
Cdd:COG1643 208 VADAVREALAEE-PGDILVFLPGEREIRRTAEALRGRLPPDTE----ILPL--YGRLSAAEQDRAFAPAPHGRRRIVLAT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 358 NIAETSITIPGIRYVIDPGFVKARSYDPSKGMESLDVVPASKAQTLQRSGRAGREGPGKSFRLYPEREFEKLEDSTKPEI 437
Cdd:COG1643 281 NIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 438 KRCNLSNIILQLKALGIDDIVGFDFIDKPSRGAIIKALAELHSLGALADDGKLeNPVGYQMSRLPLEPVYSKALILANQF 517
Cdd:COG1643 361 LRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARALLQELGALDADGRL-TPLGRALARLPLDPRLARMLLAAAEL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 518 NCLEEMLITVAVLSVEsifyDPRekREEARTsknhfasvegDHLTYLSVYRESDEFlekrkaagsgnnidkimkkwcKEN 597
Cdd:COG1643 440 GCLREAAILAALLSER----DPR--RGAAGS----------DLLARLNLWRRLREQ---------------------QRE 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 598 YVNSRSLKHARDIYRQIREHVeQIGFNVSSCGNDMLAfrRCLAASFFLKAAQRQLD-GTYRaLESGEVVHIHPTSVLFRa 676
Cdd:COG1643 483 FLSYLRLREWRDLARQLRRLL-GEGANEEPADYEAIG--LLLALAYPDRIARRRGEgGRYL-LARGRGAALFPGSPLAK- 557
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1032302368 677 KPECVIFnELMQTSkkyiKNLTI-----IDSLWLSELAPHHFQT 715
Cdd:COG1643 558 KEWLVAA-ELVGGA----AEARIrlaapIDPEWLEELAAHLIKR 596
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
40-711 |
9.90e-142 |
|
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: 447.29 E-value: 9.90e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 40 SLPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGkMIGITQPRRIAAVTVAKRVAEECEVQLGQKV 119
Cdd:TIGR01967 65 NLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHG-LIGHTQPRRLAARTVAQRIAEELGTPLGEKV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 120 GYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvsektefgnva 199
Cdd:TIGR01967 144 GYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPD------------ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 200 sqvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYFGGAKAVHVQGRQFPVDILY------TVHPESD 273
Cdd:TIGR01967 212 -----------------------------LKIIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYrplveeQEDDDLD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 274 YVDATLVTIFQIhFEEKPGDILVFLTGQDEI-ESVERLVQERLQNIpedkrKLLPLaiFSALPSEQQMKVFAPApTGfRK 352
Cdd:TIGR01967 263 QLEAILDAVDEL-FAEGPGDILIFLPGEREIrDAAEILRKRNLRHT-----EILPL--YARLSNKEQQRVFQPH-SG-RR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 353 VILATNIAETSITIPGIRYVIDPGFVKARSYDPSKGMESLDVVPASKAQTLQRSGRAGREGPGKSFRLYPEREFEKLEDS 432
Cdd:TIGR01967 333 IVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEF 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 433 TKPEIKRCNLSNIILQLKALGIDDIVGFDFIDKPSRGAIIKALAELHSLGALADDGKLEN--PVGYQMSRLPLEPVYSKA 510
Cdd:TIGR01967 413 TDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDEAEPQltPIGRQLAQLPVDPRLARM 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 511 LILANQFNCLEEMLITVAVLSVEsifyDPREKREE----ARTSKNHFASVEGDHLTYLSVYResdeFLEKRKAAGSGNNi 586
Cdd:TIGR01967 493 LLEAHRLGCLQEVLIIASALSIQ----DPRERPMEkqqaADQAHARFKDPRSDFLSRVNLWR----HIEEQRQALSANQ- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 587 dkiMKKWCKENYVNSRSLKHARDIYRQIREHVEQIGFNVSSCGNDMLAFRRCLAASFF----LKAAQRQLDGTyraleSG 662
Cdd:TIGR01967 564 ---FRNACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKALLSGLLsqigMKDEKHEYDGA-----RG 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1032302368 663 EVVHIHPTSVLFRAKPECVIFNELMQTSKKYIKNLTIIDSLWLSELAPH 711
Cdd:TIGR01967 636 RKFHIFPGSPLFKKPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAGH 684
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
40-711 |
3.24e-128 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 411.38 E-value: 3.24e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 40 SLPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGkMIGITQPRRIAAVTVAKRVAEECEVQLGQKV 119
Cdd:PRK11131 72 NLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKG-LIGHTQPRRLAARTVANRIAEELETELGGCV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 120 GYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvsektefgnva 199
Cdd:PRK11131 151 GYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPD------------ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 200 sqvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYFGGAKAVHVQGRQFPVDILY--TVHPESDYVDA 277
Cdd:PRK11131 219 -----------------------------LKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYrpIVEEADDTERD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 278 TLVTIFQIHFE---EKPGDILVFLTGQDEIesveRLVQERLQnipedKRKL-----LPLaiFSALPSEQQMKVFAPapTG 349
Cdd:PRK11131 270 QLQAIFDAVDElgrEGPGDILIFMSGEREI----RDTADALN-----KLNLrhteiLPL--YARLSNSEQNRVFQS--HS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 350 FRKVILATNIAETSITIPGIRYVIDPGFVKARSYDPSKGMESLDVVPASKAQTLQRSGRAGREGPGKSFRLYPEREFEKL 429
Cdd:PRK11131 337 GRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSR 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 430 EDSTKPEIKRCNLSNIILQLKALGIDDIVGFDFIDKPSRGAI---IKALAELHSLGALADDGKLE-NPVGYQMSRLPLEP 505
Cdd:PRK11131 417 PEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIqdgVRLLEELGAITTDEQASAYKlTPLGRQLAQLPVDP 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 506 VYSKALILANQFNCLEEMLITVAVLSVEsifyDPRE----KREEARTSKNHFASVEGDHLTYLSVYresdEFLEKRKAAG 581
Cdd:PRK11131 497 RLARMVLEAQKHGCVREVMIITSALSIQ----DPRErpmdKQQASDEKHRRFADKESDFLAFVNLW----NYLQEQQKAL 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 582 SGNNidkiMKKWCKENYVNSRSLKHARDIYRQIREHVEQIGFNVSSCGNDMLAFRRCLAASFFLKAAQRQLD-----GTY 656
Cdd:PRK11131 569 SSNQ----FRRLCRTDYLNYLRVREWQDIYTQLRQVVKELGIPVNSEPAEYREIHTALLTGLLSHIGMKDAEkqeytGAR 644
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1032302368 657 RALesgevVHIHPTSVLFRAKPECVIFNELMQTSKKYIKNLTIIDSLWLSELAPH 711
Cdd:PRK11131 645 NAR-----FSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARIEPEWIEPLAQH 694
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
41-255 |
3.98e-105 |
|
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: 318.14 E-value: 3.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCReGKMIGITQPRRIAAVTVAKRVAEECEVQLGQKVG 120
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFAR-GGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 121 YSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQPvsektefgnvas 200
Cdd:cd17978 80 YSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEQ------------ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032302368 201 qvqtttrdangpqqngvlkgyqgrKLSPLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17978 148 ------------------------KLSPLKVIIMSATLDADLFSEYFNGAPVLYI 178
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
41-505 |
4.64e-91 |
|
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: 302.07 E-value: 4.64e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFcrEGKMIGITQPRRIAAVTVAKRVAEECEVQLGQKVG 120
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPG--IGGKIIMLEPRRLAARSAAQRLASQLGEAVGQTVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 121 YSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALlkkiqrtrsqpvsektefgnvAS 200
Cdd:TIGR01970 79 YRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLAL---------------------AL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 201 QVQTTTRDangpqqngvlkgyqgrklsPLKLIIMSASLDARVFSEYFGGAKAVHVQGRQFPVDILY-TVHPESDYVDATL 279
Cdd:TIGR01970 138 DVQSSLRE-------------------DLKILAMSATLDGERLSSLLPDAPVVESEGRSFPVEIRYlPLRGDQRLEDAVS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 280 VTIFQIhFEEKPGDILVFLTGQDEIESVERLVQERLQNipedKRKLLPLaiFSALPSEQQMKVFAPAPTGFRKVILATNI 359
Cdd:TIGR01970 199 RAVEHA-LASETGSILVFLPGQAEIRRVQEQLAERLDS----DVLICPL--YGELSLAAQDRAIKPDPQGRRKVVLATNI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 360 AETSITIPGIRYVIDPGFVKARSYDPSKGMESLDVVPASKAQTLQRSGRAGREGPGKSFRLYPEREFEKLEDSTKPEIKR 439
Cdd:TIGR01970 272 AETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQRLPAQDEPEILQ 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032302368 440 CNLSNIILQLKALGIDDIVGFDFIDKPSRGAIIKALAELHSLGALADDGKLeNPVGYQMSRLPLEP 505
Cdd:TIGR01970 352 ADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGRL-TAHGKAMAALGCHP 416
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
40-530 |
2.43e-84 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 283.74 E-value: 2.43e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 40 SLPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLP-QFLYNAGFcrEGKMIgITQPRRIAAVTVAKRVAEECEVQLGQK 118
Cdd:PRK11664 3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGI--NGKII-MLEPRRLAARNVAQRLAEQLGEKPGET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 119 VGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLkkiqrtrsqpvsektefgnv 198
Cdd:PRK11664 80 VGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALL-------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 199 aSQVQTTTRDangpqqngvlkgyqgrklsPLKLIIMSASLDARVFSEYFGGAKAVHVQGRQFPVDILYTVHPESDY-VDA 277
Cdd:PRK11664 140 -LDVQQGLRD-------------------DLKLLIMSATLDNDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRfDEA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 278 TLVTIFQIhFEEKPGDILVFLTGQDEIesveRLVQERLQNIPEDKRKLLPLaiFSALPSEQQMKVFAPAPTGFRKVILAT 357
Cdd:PRK11664 200 VARATAEL-LRQESGSLLLFLPGVGEI----QRVQEQLASRVASDVLLCPL--YGALSLAEQQKAILPAPAGRRKVVLAT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 358 NIAETSITIPGIRYVIDPGFVKARSYDPSKGMESLDVVPASKAQTLQRSGRAGREGPGKSFRLYPEREFEKLEDSTKPEI 437
Cdd:PRK11664 273 NIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEI 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 438 KRCNLSNIILQLKALGIDDIVGFDFIDKPSRGAIIKALAELHSLGALADDGKLeNPVGYQMSRLPLEPVYSKALILANQF 517
Cdd:PRK11664 353 LHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQGRL-TARGRKMAALGNDPRLAAMLVAAKED 431
|
490
....*....|...
gi 1032302368 518 NclEEMLITVAVL 530
Cdd:PRK11664 432 D--EAALATAAKL 442
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
57-255 |
1.66e-76 |
|
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: 242.75 E-value: 1.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 57 NDILIIVGETGSGKTTQLPQFLYNAGFCREGK-MIGITQPRRIAAVTVAKRVAEECEVQLGQKVGYSIRFDDTTSGSTRL 135
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGKgRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 136 KYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRsqpvsektefgnvasqvqtttrdangpqqn 215
Cdd:cd17917 81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKR------------------------------ 130
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1032302368 216 gvlkgyqgrklSPLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17917 131 -----------PDLKVILMSATLDAEKFSSYFGGAPVIHI 159
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
260-421 |
2.98e-76 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350178 [Multi-domain] Cd Length: 171 Bit Score: 242.44 E-value: 2.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 260 FPVDILYT-----------VHPESDYVDATLVTIFQIHFEEKPGDILVFLTGQDEIESVERLVQERLQNipEDKRKLLPL 328
Cdd:cd18791 1 FPVEVYYLedilellgissEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLS--PDLGKLLVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 329 AIFSALPSEQQMKVFAPAPTGFRKVILATNIAETSITIPGIRYVIDPGFVKARSYDPSKGMESLDVVPASKAQTLQRSGR 408
Cdd:cd18791 79 PLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGR 158
|
170
....*....|...
gi 1032302368 409 AGREGPGKSFRLY 421
Cdd:cd18791 159 AGRTRPGKCYRLY 171
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
36-247 |
1.08e-69 |
|
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: 225.44 E-value: 1.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 36 EHRRSLPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKmIGITQPRRIAAVTVAKRVAEECEVQL 115
Cdd:cd17971 1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGK-IGCTQPRRVAAMSVAKRVAEEFGCCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 116 GQKVGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvsektef 195
Cdd:cd17971 80 GQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPD-------- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032302368 196 gnvasqvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYF 247
Cdd:cd17971 152 ---------------------------------LKLIVTSATLDAVKFSQYF 170
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
32-255 |
2.97e-68 |
|
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: 221.91 E-value: 2.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 32 QKIAEHRRSLPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCR-EGKMIGITQPRRIAAVTVAKRVAEE 110
Cdd:cd17973 4 FEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHqPKKLVACTQPRRVAAMSVAQRVAEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 111 CEVQLGQKVGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvs 190
Cdd:cd17973 84 MDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPD--- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032302368 191 ektefgnvasqvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17973 161 --------------------------------------LKLIVMSATLDAGKFQKYFDNAPLLKV 187
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
41-250 |
6.15e-67 |
|
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: 218.14 E-value: 6.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKMIGITQPRRIAAVTVAKRVAEECEVQLGQKVG 120
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 121 YSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvsektefgnvas 200
Cdd:cd17974 81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPD------------- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1032302368 201 qvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYFGGA 250
Cdd:cd17974 148 ----------------------------LKLLISSATMDAEKFSAFFDDA 169
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
41-255 |
1.77e-66 |
|
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: 216.94 E-value: 1.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGkMIGITQPRRIAAVTVAKRVAEECEVQLGQKVG 120
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYG-MIGCTQPRRVAAMSVAKRVSEEMGVELGEEVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 121 YSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvsektefgnvas 200
Cdd:cd17983 80 YAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRD------------- 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032302368 201 qvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17983 147 ----------------------------LKLIVTSATMDADKFADFFGNVPIFTI 173
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
41-245 |
1.48e-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: 214.91 E-value: 1.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGF----CREGKMIGITQPRRIAAVTVAKRVAEECEVqLG 116
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFgspeSDNPGMIGITQPRRVAAVSMAKRVAEELNV-FG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 117 QKVGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQPVSEKTefg 196
Cdd:cd17982 80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKLYLQDQ--- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1032302368 197 nvasqvqtttrdangpqqngvlkgyqgrKLSPLKLIIMSASLDARVFSE 245
Cdd:cd17982 157 ----------------------------TVKPLKLVIMSATLRVEDFTE 177
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
41-255 |
3.09e-63 |
|
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: 208.56 E-value: 3.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGkMIGITQPRRIAAVTVAKRVAEECEVQLGQKVG 120
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHG-MIGVTQPRRVAAISVAQRVAEEMKCTLGSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 121 YSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIqrtrsqpvsektefgnvas 200
Cdd:cd17984 80 YQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKL------------------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032302368 201 qvqtttrdangpqqngVLKGYQGRKlSPLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17984 141 ----------------FQEKSPNRK-EHLKVVVMSATLELAKLSAFFGNCPVFDI 178
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
41-247 |
5.30e-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: 208.09 E-value: 5.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKMIGITQPRRIAAVTVAKRVAEECEVQLGQKVG 120
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 121 YSIRFDD-TTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvsektefgnva 199
Cdd:cd17980 81 YCIRFDDcTDPQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGD------------ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1032302368 200 sqvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYF 247
Cdd:cd17980 149 -----------------------------LRLIVASATLDAEKFRDFF 167
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
41-255 |
1.64e-49 |
|
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: 171.10 E-value: 1.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGkMIGITQPRRIAAVTVAKRVAEECEVQLGQKVG 120
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRG-LIGHTQPRRLAARSVAERIAEELKTELGGAVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 121 YSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvsektefgnvas 200
Cdd:cd17989 80 YKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPD------------- 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032302368 201 qvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17989 147 ----------------------------LKVIITSATIDAERFSRHFNNAPIIEV 173
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
41-255 |
7.93e-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: 169.16 E-value: 7.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCRegkmIGITQPRRIAAVTVAKRVAEECEVQLGQKVG 120
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH----IACTQPRRIACISLAKRVAFESLNQYGSKVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 121 YSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvsektefgnvas 200
Cdd:cd17979 77 YQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPD------------- 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1032302368 201 qvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17979 144 ----------------------------LKLILMSATINIELFSGYFEGAPVVQV 170
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
41-255 |
1.06e-37 |
|
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: 138.43 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKM---IGITQPRRIAAVTVAKRVAEECEVQLGQ 117
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPvanIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 118 KVGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvsektefgn 197
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPD---------- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032302368 198 vasqvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17985 151 -------------------------------LKVILMSATLNAELFSDYFNSCPVIHI 177
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
41-247 |
1.36e-37 |
|
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: 138.51 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKM----IGITQPRRIAAVTVAKRVAEE--CEVQ 114
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLLNGGTAqkcnIVCTQPRRISAMSLATRVCEElgCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 115 LGQK---VGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvse 191
Cdd:cd17975 81 PGGKnslCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSD---- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1032302368 192 ktefgnvasqvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYF 247
Cdd:cd17975 157 -------------------------------------LHLILMSATVDCEKFSSYF 175
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
41-255 |
6.27e-37 |
|
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: 136.51 E-value: 6.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYN-------AGFCRegkmIGITQPRRIAAVTVAKRVA-EECE 112
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDdaiergkGSSCR----IVCTQPRRISAISVAERVAaERAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 113 -VQLGQKVGYSIRFDDT---TSGStrLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQp 188
Cdd:cd17981 77 sCGLGNSTGYQIRLESRkprKQGS--ILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSD- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032302368 189 vsektefgnvasqvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17981 154 ----------------------------------------LKVILMSATLNAEKFSDYFNNCPMIHI 180
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
41-253 |
2.72e-36 |
|
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: 134.38 E-value: 2.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKMIgITQPRRIAAVTVAKRVAEECEVQLGQKVG 120
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKII-VLEPRRVAARAAARRLATLLGEAPGETVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 121 YSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRsqpvsektefgnvas 200
Cdd:cd17990 80 YRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQLL--------------- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1032302368 201 qvqtttRDangpqqngvlkgyqgrklsPLKLIIMSASLDARVFSEYFGGAKAV 253
Cdd:cd17990 145 ------RD-------------------DLRLLAMSATLDGDGLAALLPEAPVV 172
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
41-255 |
4.51e-36 |
|
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: 133.80 E-value: 4.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLY-----NAGFCRegkmIGITQPRRIAAVTVAKRVAEECEVQL 115
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLddcyaNGIPCR----IFCTQPRRLAAIAVAERVAAERGEKI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 116 GQKVGYSIRFDDTTSGSTRLKYMTDGLLLReALLDPH--LSRYSVIIVDEAHDRSVHTDVLLALLKKIQrtrsqpvsekt 193
Cdd:cd17987 77 GQTVGYQIRLESRVSPKTLLTFCTNGVLLR-TLMAGDsaLSTVTHVIVDEVHERDRFSDFLLTKLRDIL----------- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032302368 194 efgnvasqvqtttrdangpqqngvlkgyqgRKLSPLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17987 145 ------------------------------QKHPNLKLILSSAALDVNLFIRYFGSCPVIYI 176
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
41-248 |
6.77e-36 |
|
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: 133.40 E-value: 6.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKM-IGITQPRRIAAVTVAKRVAEECEVQLGQKV 119
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCnIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 120 GYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQPVsektefgnva 199
Cdd:cd17988 81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRHV---------- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1032302368 200 sqvqtttrdangpqqngvlkgyqgrklsplKLIIMSASLDARVFSEYFG 248
Cdd:cd17988 151 ------------------------------KIILMSATISCKEFADYFT 169
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
41-255 |
1.19e-33 |
|
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: 127.22 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCR-EGKM--IGITQPRRIAAVTVAKRVAEECEVQLGQ 117
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRgRGARcnVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 118 KVGYSIRFDDT--TSGSTRLkYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQpvsektef 195
Cdd:cd17976 81 NVGYQVRLESRppPRGGALL-FCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPE-------- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 196 gnvasqvqtttrdangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17976 152 ---------------------------------LRVVLMSATGDNQRLSRYFGGCPVVRV 178
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
32-255 |
1.53e-33 |
|
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: 128.80 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 32 QKIAEHRRSLPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLY-------NAGFCRegkmIGITQPRRIAAVTVA 104
Cdd:cd17972 50 QQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILddfiqndRAAECN----IVVTQPRRISAVSVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 105 KRVAEECEVQLGQKVGYSIRFDDTTS---GStrLKYMTDGLLLREalLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKki 181
Cdd:cd17972 126 ERVAFERGEEVGKSCGYSVRFESVLPrphAS--ILFCTVGVLLRK--LEAGIRGISHVIVDEIHERDINTDFLLVVLR-- 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032302368 182 qrtrsqpvsektefgnvasQVQTTTRDangpqqngvlkgyqgrklspLKLIIMSASLDARVFSEYFGGAKAVHV 255
Cdd:cd17972 200 -------------------DVVQAYPD--------------------LRVILMSATIDTSMFCEYFFNCPVIEV 234
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
41-187 |
2.65e-32 |
|
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: 123.40 E-value: 2.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLynAGFCREGK----MIGITQPRRIAAVTVAKRVAEECEVQLG 116
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWC--AEYCLSAHyqhgVVVCTQVHKQTAVWLALRVADEMDVNIG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032302368 117 QKVGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQ 187
Cdd:cd17977 79 HEVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPE 149
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
41-185 |
9.45e-29 |
|
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: 113.07 E-value: 9.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 41 LPIASVEKRLVEEVQ-KNDILIIVGETGSGKTTQLPQ----FLYNAGFCRegKMIGITQPRRIAAVTVAKRVAEECEVQL 115
Cdd:cd17986 1 LPIWAAKFTFLEQLEsPSGIVLVSGEPGSGKSTQVPQwcaeFALSRGFQK--GQVTVTQPHPLAARSLALRVADEMDLNL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 116 GQKVGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTR 185
Cdd:cd17986 79 GHEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQR 148
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
480-564 |
1.95e-24 |
|
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: 97.34 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 480 SLGALADDGKLeNPVGYQMSRLPLEPVYSKALILANQFNCLEEMLITVAVLSVESIFydPREKREEARTSKNHFASVEGD 559
Cdd:smart00847 1 ELGALDDDGRL-TPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESD 77
|
....*
gi 1032302368 560 HLTYL 564
Cdd:smart00847 78 HLTLL 82
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
474-563 |
3.59e-23 |
|
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: 94.61 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 474 ALAELHSLGALADDGKLeNPVGYQMSRLPLEPVYSKALILANQFNCLEEMLITVAVLSVESIFYDP-------------- 539
Cdd:pfam04408 1 ALELLYYLGALDEDGEL-TPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprsaakaarr 79
|
90 100
....*....|....*....|....*
gi 1032302368 540 -REKREEARTSKNHFASVEGDHLTY 563
Cdd:pfam04408 80 rRRAADEKARAKFARLDLEGDHLTL 104
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
60-185 |
2.08e-20 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 89.86 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 60 LIIVGETGSGKTTQLPQFLYNAGFCREGKMIGITQPRRIAAVTVAKRVAEECEVQLGQKVGY------SIRFDDTTSGST 133
Cdd:smart00487 27 VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLyggdskREQLRKLESGKT 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1032302368 134 RLKYMTDGLLLREALLDP-HLSRYSVIIVDEAHDRS--VHTDVLLALLKKIQRTR 185
Cdd:smart00487 107 DILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLLdgGFGDQLEKLLKLLPKNV 161
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
636-711 |
4.99e-20 |
|
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: 84.61 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 636 RRCLAASFFLKAAQRQLDG-TYRALESGEVVHIHPTSVLFRA---KPECVIFNELMQTSKKYIKNLTIIDSLWLSELAPH 711
Cdd:pfam07717 2 RAALAAGLYPNVARRDPKGkGYTTLSDNQRVFIHPSSVLFNEktfPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAPH 81
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
322-413 |
1.23e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 63.77 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 322 KRKLLPLAIFSALPSEQQMKVFAPAPTGFRKVILATNIAETSITIPGIRYVIDpgfvkarsYDPskgmesldvvPASKAQ 401
Cdd:smart00490 9 ELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVII--------YDL----------PWSPAS 70
|
90
....*....|..
gi 1032302368 402 TLQRSGRAGREG 413
Cdd:smart00490 71 YIQRIGRAGRAG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
281-413 |
2.18e-12 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 63.77 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 281 TIFQIHFEEKPGDILVFLtgqdeiESVERLVQERLQNipedKRKLLPLAIFSALPSEQQMKVFAPAPTGFRKVILATNIA 360
Cdd:pfam00271 5 ALLELLKKERGGKVLIFS------QTKKTLEAELLLE----KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVA 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1032302368 361 ETSITIPGIRYVIDpgfvkarsYDPSKGMESLdvvpaskaqtLQRSGRAGREG 413
Cdd:pfam00271 75 ERGLDLPDVDLVIN--------YDLPWNPASY----------IQRIGRAGRAG 109
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
19-455 |
3.31e-08 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 56.91 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 19 NPKSPTVSPFsmrqkiaehrRSLPIaSVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFL--YN---AGFCREGKMIGIT 93
Cdd:PHA02653 152 NPEPFSKIPL----------ASLQP-DVQLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLlwFNylfGGFDNLDKIDPNF 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 94 QPRRIaaVTVAKRVAEeceVQLGQKVgY--SIRFDDTTSGSTRLKY--MTD----------GLLLR-EALLDPHLSRYSV 158
Cdd:PHA02653 221 IERPI--VLSLPRVAL---VRLHSIT-LlkSLGFDEIDGSPISLKYgsIPDelintnpkpyGLVFStHKLTLNKLFDYGT 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 159 IIVDEAHDRSVHTDVLLALL-KKIQRTRSqpvsektefgnvasqvqtttrdangpqqngvlkgyqgrklsplkLIIMSAS 237
Cdd:PHA02653 295 VIIDEVHEHDQIGDIIIAVArKHIDKIRS--------------------------------------------LFLMTAT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 238 L--DARVFSEYFGGAKAVHVQGRQ-FPVDILYtVHPESD------YVDATLVTIFQIHFEEKPGD---ILVFLTGQDEIE 305
Cdd:PHA02653 331 LedDRDRIKEFFPNPAFVHIPGGTlFPISEVY-VKNKYNpknkraYIEEEKKNIVTALKKYTPPKgssGIVFVASVSQCE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 306 SVERLVQERLQNipedkrkLLPLAIFSALPSEQQM--KVFA-PAPTgfrkVILATNIAETSITIPGIRYVIDPG--FVKA 380
Cdd:PHA02653 410 EYKKYLEKRLPI-------YDFYIIHGKVPNIDEIleKVYSsKNPS----IIISTPYLESSVTIRNATHVYDTGrvYVPE 478
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032302368 381 rsydPSKGMESLdvvpASKAQTLQRSGRAGREGPGKSFRLYPEREFekledstKPeIKRCN---LSNIILQLKALGID 455
Cdd:PHA02653 479 ----PFGGKEMF----ISKSMRTQRKGRVGRVSPGTYVYFYDLDLL-------KP-IKRIDsefLHNYILYAKYFNLT 540
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
60-183 |
1.09e-07 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 51.64 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 60 LIIVGETGSGKTTQLPQFLYNAGFCREGKMIgITQPRRIAAVTVAKRVAEEceVQLGQKVGYSIRFDD------TTSGST 133
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGKKVL-VLVPTKALALQTAERLREL--FGPGIRVAVLVGGSSaeerekNKLGDA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1032302368 134 RLKYMTDGLLLR--EALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQR 183
Cdd:cd00046 81 DIIIATPDMLLNllLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRK 132
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
60-165 |
5.13e-05 |
|
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: 44.16 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 60 LIIVGETGSGKTT--QLPqFLYNAGFCREGKMIGITQPRRIAA---VTVAKRVAEECEVQLGQKV-GYSIRFDDTTSGST 133
Cdd:pfam00270 17 VLVQAPTGSGKTLafLLP-ALEALDKLDNGPQALVLAPTRELAeqiYEELKKLGKGLGLKVASLLgGDSRKEQLEKLKGP 95
|
90 100 110
....*....|....*....|....*....|..
gi 1032302368 134 RLKYMTDGLLLREALLDPHLSRYSVIIVDEAH 165
Cdd:pfam00270 96 DILVGTPGRLLDLLQERKLLKNLKLLVLDEAH 127
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
352-421 |
1.42e-04 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 40.77 E-value: 1.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032302368 352 KVILATNIAETSITIPGIRYVIDPGFVKarsydpskgmesldvvpaSKAQTLQRSGRAGREG--PGKSFRLY 421
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDPPS------------------SAASYIQRVGRAGRGGkdEGEVILFV 77
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|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
66-165 |
1.22e-03 |
|
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: 39.84 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 66 TGSGKTTQ-LPQFLYNAGfcREGKMIGITQPRRIAAVTVAkrvaeecEVQLGQKVGYSI-RFDDTTSGSTRLKYMTDGLL 143
Cdd:cd17931 10 PGAGKTTRvLPQIIREAI--KKRLRTLVLAPTRVVAAEMY-------EALRGLPIRYRTgAVKEEHGGNEIVDYMCHGTF 80
|
90 100
....*....|....*....|...
gi 1032302368 144 LrEALLDPHL-SRYSVIIVDEAH 165
Cdd:cd17931 81 T-CRLLSPKRvPNYNLIIMDEAH 102
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
267-420 |
1.73e-03 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain] Cd Length: 143 Bit Score: 39.26 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 267 TVHPESDYVDATLVTIFQIHFEEKPGDILVFLTGQDeieSVERLVQERLQNIPEDKRKllplaIF---------SALPSE 337
Cdd:cd18801 6 KIHPKLEKLEEIVKEHFKKKQEGSDTRVIIFSEFRD---SAEEIVNFLSKIRPGIRAT-----RFigqasgkssKGMSQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 338 QQMKVFAPAPTGFRKVILATNIAETSITIPGIRYVIdpgfvkarSYDPSKgmesldvvpaSKAQTLQRSGRAGREGPGKS 417
Cdd:cd18801 78 EQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLII--------CYDASP----------SPIRMIQRMGRTGRKRQGRV 139
|
...
gi 1032302368 418 FRL 420
Cdd:cd18801 140 VVL 142
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
59-190 |
3.63e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 59 ILIIVGETGSGKTTQLPQFLYNAGFCREGKmIGITQPRRIAAVTVAKRVAEEcevqlgqkvgysirFDDTTSGSTRLKYM 138
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQLPEVRDSV-VFVDLPSGTSPKDLLRALLRA--------------LGLPLSGRLSKEEL 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1032302368 139 TDglLLREALLdpHLSRYSVIIVDEAHDRSvhtDVLLALLKKIQRTRSQPVS 190
Cdd:pfam13401 72 LA--ALQQLLL--ALAVAVVLIIDEAQHLS---LEALEELRDLLNLSSKLLQ 116
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
265-413 |
8.08e-03 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain] Cd Length: 131 Bit Score: 37.10 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032302368 265 LYTVHPESDYVDATLVTIFQIHFEEKpgdILVFLtgqDEIESVERLVQE-RLQNIPedkrkllPLAIFSALPSEQQMKVF 343
Cdd:cd18787 4 LYVVVEEEEKKLLLLLLLLEKLKPGK---AIIFV---NTKKRVDRLAELlEELGIK-------VAALHGDLSQEERERAL 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032302368 344 ApaptGFR----KVILATNIAETSITIPGIRYVIdpgfvkarSYDPskgmesldvvPASKAQTLQRSGR---AGREG 413
Cdd:cd18787 71 K----KFRsgkvRVLVATDVAARGLDIPGVDHVI--------NYDL----------PRDAEDYVHRIGRtgrAGRKG 125
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