|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
198-359 |
6.48e-85 |
|
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: 273.95 E-value: 6.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 198 NVVIISGGTGCGKTTQVPQFILDEAHENNKHVRVMVTQPRRIAAISIAERVARERGEPIGRTVGYQVRLDSRRSDDTVLT 277
Cdd:cd17917 2 QVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 278 YCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSATIegNMQLFSNYFENHSmdVI 357
Cdd:cd17917 82 FCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATL--DAEKFSSYFGGAP--VI 157
|
..
gi 17507503 358 RI 359
Cdd:cd17917 158 HI 159
|
|
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
630-988 |
7.97e-57 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 213.02 E-value: 7.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 630 LLDQVIQYLADSPvfGTILVFLPGYEDI---QQMLKAidcwknslKNMKNVIVLPLHSQMtSINHGD-IFKSVPKDTRKI 705
Cdd:COG1643 208 VADAVREALAEEP--GDILVFLPGEREIrrtAEALRG--------RLPPDTEILPLYGRL-SAAEQDrAFAPAPHGRRRI 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 706 ILATNIAEASITIEDVIFVVDTGKVKEKSFDHEAKLSTLTVKPIARSNADQRSGRAGRVANGYCIRLYTEQEYNSMPETQ 785
Cdd:COG1643 277 VLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 786 IAEMKRAAIYDVTLHAKLfapktLKISEFLSLA-PEPPEKESILQAITFLEQIGAFytpikiyDnsgneeglkndeeaen 864
Cdd:COG1643 357 DPEILRADLASLILELAA-----WGLGDPEDLPfLDPPPARAIADARALLQELGAL-------D---------------- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 865 senpEDPELTDLGRLMARLPLDPQLSRMLLFGLALKCLtpivNLVALLASrepyvlALSEdRDLqskmkfeMAQQDLSDH 944
Cdd:COG1643 409 ----ADGRLTPLGRALARLPLDPRLARMLLAAAELGCL----REAAILAA------LLSE-RDP-------RRGAAGSDL 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 17507503 945 LLYIRLCNEFCSKnnsqqnqfcRDHFLNFSTMRMVQGTRRQLLR 988
Cdd:COG1643 467 LARLNLWRRLREQ---------QREFLSYLRLREWRDLARQLRR 501
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
616-773 |
1.42e-54 |
|
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: 187.74 E-value: 1.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 616 LFYGSSSNNSVDYVLLDQVIQYLADSPVFGTILVFLPGYEDIQQMLKAIDCwKNSLKNMKNVIVLPLHSQMTSINHGDIF 695
Cdd:cd18791 15 LGISSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLRE-ELLSPDLGKLLVLPLHSSLPPEEQQRVF 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507503 696 KSVPKDTRKIILATNIAEASITIEDVIFVVDTGKVKEKSFDHEAKLSTLTVKPIARSNADQRSGRAGRVANGYCIRLY 773
Cdd:cd18791 94 EPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
|
|
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
180-372 |
9.51e-54 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 203.77 E-value: 9.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 180 SLPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNKhvRVMVTQPRRIAAISIAERVARERGEPIGRT 259
Cdd:COG1643 9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGG--RIGMLEPRRLAARAAAERMAEELGEPVGET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 260 VGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECL-KMRPDLKVILMSATI 338
Cdd:COG1643 87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSATL 166
|
170 180 190
....*....|....*....|....*....|....
gi 17507503 339 EGnmQLFSNYFENHSmdVIRIESRAFDVKVFYLD 372
Cdd:COG1643 167 DA--ERFARLLGDAP--VIESSGRTYPVEVRYRP 196
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
180-416 |
3.63e-40 |
|
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: 163.02 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 180 SLPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHenNKHVRVMVTQPRRIAAISIAERVARERGEPIGRT 259
Cdd:TIGR01967 65 NLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGR--GSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 260 VGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSATIE 339
Cdd:TIGR01967 143 VGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATID 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 340 gnMQLFSNYFENhsMDVIRIESRAFDVKVFY--LDQILAMTGYQPPESkAFFSTAEYEEEDWKDEIEAV--EREEKDKAK 415
Cdd:TIGR01967 223 --PERFSRHFNN--APIIEVSGRTYPVEVRYrpLVEEQEDDDLDQLEA-ILDAVDELFAEGPGDILIFLpgEREIRDAAE 297
|
.
gi 17507503 416 Q 416
Cdd:TIGR01967 298 I 298
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
630-992 |
4.26e-39 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 159.46 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 630 LLDQVIQYLADSPvfGTILVFLPGYEDIQQMLKAIdcwknSLKNMKNVIVLPLHSQMTSINHGDIFKsvPKDTRKIILAT 709
Cdd:PRK11131 274 IFDAVDELGREGP--GDILIFMSGEREIRDTADAL-----NKLNLRHTEILPLYARLSNSEQNRVFQ--SHSGRRIVLAT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 710 NIAEASITIEDVIFVVDTGKVKEKSFDHEAKLSTLTVKPIARSNADQRSGRAGRVANGYCIRLYTEQEYNSMPETQIAEM 789
Cdd:PRK11131 345 NVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEI 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 790 KRAAIYDVTLhaKLFAPKTLKISEFlslaP--EPPEKESILQAITFLEQIGAFYTpikiydnsgneeglkndeeaenSEN 867
Cdd:PRK11131 425 LRTNLASVIL--QMTALGLGDIAAF----PfvEAPDKRNIQDGVRLLEELGAITT----------------------DEQ 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 868 PEDPELTDLGRLMARLPLDPQLSRMLLFGLALKCLTPIVNLVALLASREPYVLALseDRDLQSKMKFEMAQQDLSDHLLY 947
Cdd:PRK11131 477 ASAYKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPM--DKQQASDEKHRRFADKESDFLAF 554
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17507503 948 IRLCNEFcsknNSQQ-----NQF---CRDHFLNFSTMRMVQGTRRQlLRELVR 992
Cdd:PRK11131 555 VNLWNYL----QEQQkalssNQFrrlCRTDYLNYLRVREWQDIYTQ-LRQVVK 602
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
179-917 |
2.67e-38 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 155.47 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 179 NSLPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILdeaHENNKHVRVMVTQPRRIAAISIAERVARERGEPIGR 258
Cdd:PRK11664 2 SSLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLL---QHGGINGKIIMLEPRRLAARNVAQRLAEQLGEKPGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 259 TVGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDY---LLIALRECLkmRPDLKVILMS 335
Cdd:PRK11664 79 TVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLalaLLLDVQQGL--RDDLKLLIMS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 336 ATIegnmqlfsnyfENHSM-----DVIRIES--RAFDVKvfyldqilamTGYQPPESKAFFSTAeyeeedwkdeieaver 408
Cdd:PRK11664 157 ATL-----------DNDRLqqllpDAPVIVSegRSFPVE----------RRYQPLPAHQRFDEA---------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 409 eekdkakqraadsslstlskpvtkMAANTKRnspieerewtsgpcstpdgdiideramrqymniignpdirpvitvefrp 488
Cdd:PRK11664 200 ------------------------VARATAE------------------------------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 489 ttpnsvfindvkyttnpnqsaqaLLQQKrerclmprgpltftcenpasttksppsptptlgiSSGLAKFTPfgGFGEKQR 568
Cdd:PRK11664 207 -----------------------LLRQE----------------------------------SGSLLLFLP--GVGEIQR 227
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 569 ISTLLEkkfkeelktalpdrtvyyhpqmNDVVDKTDFSKLrfgekynlfYGSSSnnsvdyvlldqviqyLADspvfgtil 648
Cdd:PRK11664 228 VQEQLA----------------------SRVASDVLLCPL---------YGALS---------------LAE-------- 253
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 649 vflpgyediQQmlKAIdcwknslknmknvivLPlhsqmtsinhgdifksVPKDTRKIILATNIAEASITIEDVIFVVDTG 728
Cdd:PRK11664 254 ---------QQ--KAI---------------LP----------------APAGRRKVVLATNIAETSLTIEGIRLVVDSG 291
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 729 KVKEKSFDHEAKLSTLTVKPIARSNADQRSGRAGRVANGYCIRLYTEQEYNSMPETQIAEMkraaiydvtLHAKLFA--- 805
Cdd:PRK11664 292 LERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEI---------LHSDLSGlll 362
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 806 ---------PKTLKiseFLSLAPEPpekeSILQAITFLEQIGAFytpikiyDNSGneeglkndeeaensenpedpELTDL 876
Cdd:PRK11664 363 ellqwgchdPAQLS---WLDQPPAA----ALAAAKRLLQQLGAL-------DGQG--------------------RLTAR 408
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 17507503 877 GRLMARLPLDPQLSRMLLFG--LALKCLTPIVNLVALLasREP 917
Cdd:PRK11664 409 GRKMAALGNDPRLAAMLVAAkeDDEAALATAAKLAAIL--EEP 449
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
189-369 |
2.45e-28 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 113.74 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 189 QVLKSISSCN-VVIISGGTGCGKTTQVPQFILDEAHENnKHVRVMVTQPRRIAAISIAERVARERGEPIGRTVGYQVRLD 267
Cdd:smart00487 15 EAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 268 SR------RSDDTVLTYCTTGVLLRMLTSDPVA-SGITHIVMDEIHEReINTDYLLIALRECLKMRPDLKVILMSATIEG 340
Cdd:smart00487 94 KReqlrklESGKTDILVTTPGRLLDLLENDKLSlSNVDLVILDEAHRL-LDGGFGDQLEKLLKLLPKNVQLLLLSATPPE 172
|
170 180
....*....|....*....|....*....
gi 17507503 341 NMQLFSNYFENHSMDVIRIESRAFDVKVF 369
Cdd:smart00487 173 EIENLLELFLNDPVFIDVGFTPLEPIEQF 201
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
869-947 |
1.49e-18 |
|
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: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 869 EDPELTDLGRLMARLPLDPQLSRMLLFGLALKCLTPIVNLVALLASREPYVLALSEDRDLQSKMKFEMA----------- 937
Cdd:pfam04408 13 EDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAARRRRraadekarakf 92
|
90
....*....|..
gi 17507503 938 --QQDLSDHLLY 947
Cdd:pfam04408 93 arLDLEGDHLTL 104
|
|
| R3H |
smart00393 |
Putative single-stranded nucleic acids-binding domain; |
21-100 |
2.76e-17 |
|
Putative single-stranded nucleic acids-binding domain;
Pssm-ID: 214647 Cd Length: 79 Bit Score: 77.73 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 21 NGFDASRVLPRGTDNDTRKEYRRVANEIIRsFLKSGQKNTTLEPMGRDQRKVMHEVALLNEMTTKSHGREPDRYMILSKR 100
Cdd:smart00393 1 ADFLPVTLDALSYRPRRREELIELELEIAR-FVKSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKRRVVISKK 79
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
869-948 |
7.14e-16 |
|
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: 73.84 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 869 EDPELTDLGRLMARLPLDPQLSRMLLFGLALKCLTPIVNLVALLASREPYVLALSEDRDlQSKMKFemaQQDLSDHLLYI 948
Cdd:smart00847 7 DDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKREDAD-AARRRF---ADPESDHLTLL 82
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
189-345 |
3.91e-14 |
|
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: 71.50 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 189 QVLKSISSCNVVIISGGTGCGKTT--QVPqfILDEAHENNKHVRVMVTQPRRIAAISIAERvARERGEPIGRTVGYQVRL 266
Cdd:pfam00270 6 EAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTRELAEQIYEE-LKKLGKGLGLKVASLLGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 267 DSRRSDDTVL-----TYCTTGVLLRMLTSDPVASGITHIVMDEIHerEINTDYLLIALRECLK-MRPDLKVILMSATIEG 340
Cdd:pfam00270 83 DSRKEQLEKLkgpdiLVGTPGRLLDLLQERKLLKNLKLLVLDEAH--RLLDMGFGPDLEEILRrLPKKRQILLLSATLPR 160
|
....*
gi 17507503 341 NMQLF 345
Cdd:pfam00270 161 NLEDL 165
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
1023-1116 |
1.96e-11 |
|
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: 61.11 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 1023 IQAVIAAGCYPFIGVSASESNLKKvQTFNDKPAFLHPSSMVkkqivkmgKSEKSPRVEYVAFQEMcqMPSDRsLSMKTVT 1102
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGKGYT-TLSDNQRVFIHPSSVL--------FNEKTFPPEWVVYQEL--VETTK-VYIRTVT 68
|
90
....*....|....
gi 17507503 1103 VIPSMTALLFTGPI 1116
Cdd:pfam07717 69 AISPEWLLLFAPHI 82
|
|
| R3H |
pfam01424 |
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ... |
42-99 |
1.60e-10 |
|
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.
Pssm-ID: 460206 Cd Length: 60 Bit Score: 57.89 E-value: 1.60e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 17507503 42 RRVANEIIRsFLKSGQKNTTLEPMGRDQRKVMHEVALLNEMTTKSHGREPDRYMILSK 99
Cdd:pfam01424 4 EQLAEKLAE-FVKDTGKSLELPPMSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
|
|
| R3H |
cd02325 |
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ... |
42-99 |
6.75e-08 |
|
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100064 Cd Length: 59 Bit Score: 50.31 E-value: 6.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 17507503 42 RRVANEIIRSFLKSGQKNT-TLEPMGRDQRKVMHEVALLNEMTTKSHGREPDRYMILSK 99
Cdd:cd02325 1 REEREEELEAFAKDAAGKSlELPPMNSYERKLIHDLAEYYGLKSESEGEGPNRRVVITK 59
|
|
| Jag |
COG1847 |
Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General ... |
38-100 |
4.27e-04 |
|
Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General function prediction only];
Pssm-ID: 441452 [Multi-domain] Cd Length: 143 Bit Score: 42.02 E-value: 4.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17507503 38 RKEYRRVANEIIRSFLKSGqKNTTLEPMGRDQRKVMHEvALLNEM--TTKSHGREPDRYMILSKR 100
Cdd:COG1847 80 EEELEELARRAAEKVKRTG-KPVELEPMSPYERRIIHD-ALADDPgvETESEGEEPYRRVVISPK 142
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
198-359 |
6.48e-85 |
|
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: 273.95 E-value: 6.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 198 NVVIISGGTGCGKTTQVPQFILDEAHENNKHVRVMVTQPRRIAAISIAERVARERGEPIGRTVGYQVRLDSRRSDDTVLT 277
Cdd:cd17917 2 QVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 278 YCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSATIegNMQLFSNYFENHSmdVI 357
Cdd:cd17917 82 FCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATL--DAEKFSSYFGGAP--VI 157
|
..
gi 17507503 358 RI 359
Cdd:cd17917 158 HI 159
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
181-359 |
5.88e-65 |
|
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: 217.79 E-value: 5.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHEN--NKHVRVMVTQPRRIAAISIAERVARERGEPIGR 258
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGppLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 259 TVGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSATI 338
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
|
170 180
....*....|....*....|.
gi 17507503 339 egNMQLFSNYFenHSMDVIRI 359
Cdd:cd17985 161 --NAELFSDYF--NSCPVIHI 177
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
173-351 |
9.77e-62 |
|
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: 210.85 E-value: 9.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 173 ELQKV---RNSLPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNK--HVRVMVTQPRRIAAISIAER 247
Cdd:cd17972 48 NLQQIlqeRELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRaaECNIVVTQPRRISAVSVAER 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 248 VARERGEPIGRTVGYQVRLDS--RRSDDTVLtYCTTGVLLRMLTSDpvASGITHIVMDEIHEREINTDYLLIALRECLKM 325
Cdd:cd17972 128 VAFERGEEVGKSCGYSVRFESvlPRPHASIL-FCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLLVVLRDVVQA 204
|
170 180
....*....|....*....|....*.
gi 17507503 326 RPDLKVILMSATIEGNMqlFSNYFEN 351
Cdd:cd17972 205 YPDLRVILMSATIDTSM--FCEYFFN 228
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
181-351 |
1.14e-60 |
|
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: 205.45 E-value: 1.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNKHVRVMVTQPRRIAAISIAERVARERGEPIGRTV 260
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 261 GYQVRLDSRRSDDTVLTYCTTGVLLRMLTS-DPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSATIE 339
Cdd:cd17987 81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160
|
170
....*....|..
gi 17507503 340 GNmqLFSNYFEN 351
Cdd:cd17987 161 VN--LFIRYFGS 170
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
181-354 |
2.04e-60 |
|
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: 205.08 E-value: 2.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNK--HVRVMVTQPRRIAAISIAERVARERGE--PI 256
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKgsSCRIVCTQPRRISAISVAERVAAERAEscGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 257 GRTVGYQVRLDSRRS-DDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMS 335
Cdd:cd17981 81 GNSTGYQIRLESRKPrKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
|
170
....*....|....*....
gi 17507503 336 ATIegNMQLFSNYFENHSM 354
Cdd:cd17981 161 ATL--NAEKFSDYFNNCPM 177
|
|
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
630-988 |
7.97e-57 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 213.02 E-value: 7.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 630 LLDQVIQYLADSPvfGTILVFLPGYEDI---QQMLKAidcwknslKNMKNVIVLPLHSQMtSINHGD-IFKSVPKDTRKI 705
Cdd:COG1643 208 VADAVREALAEEP--GDILVFLPGEREIrrtAEALRG--------RLPPDTEILPLYGRL-SAAEQDrAFAPAPHGRRRI 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 706 ILATNIAEASITIEDVIFVVDTGKVKEKSFDHEAKLSTLTVKPIARSNADQRSGRAGRVANGYCIRLYTEQEYNSMPETQ 785
Cdd:COG1643 277 VLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 786 IAEMKRAAIYDVTLHAKLfapktLKISEFLSLA-PEPPEKESILQAITFLEQIGAFytpikiyDnsgneeglkndeeaen 864
Cdd:COG1643 357 DPEILRADLASLILELAA-----WGLGDPEDLPfLDPPPARAIADARALLQELGAL-------D---------------- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 865 senpEDPELTDLGRLMARLPLDPQLSRMLLFGLALKCLtpivNLVALLASrepyvlALSEdRDLqskmkfeMAQQDLSDH 944
Cdd:COG1643 409 ----ADGRLTPLGRALARLPLDPRLARMLLAAAELGCL----REAAILAA------LLSE-RDP-------RRGAAGSDL 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 17507503 945 LLYIRLCNEFCSKnnsqqnqfcRDHFLNFSTMRMVQGTRRQLLR 988
Cdd:COG1643 467 LARLNLWRRLREQ---------QREFLSYLRLREWRDLARQLRR 501
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
181-349 |
4.56e-56 |
|
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: 192.31 E-value: 4.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNK--HVRVMVTQPRRIAAISIAERVARERGEPIGR 258
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRgaRCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 259 TVGYQVRLDSRR-SDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSAT 337
Cdd:cd17976 81 NVGYQVRLESRPpPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
|
170
....*....|..
gi 17507503 338 ieGNMQLFSNYF 349
Cdd:cd17976 161 --GDNQRLSRYF 170
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
616-773 |
1.42e-54 |
|
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: 187.74 E-value: 1.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 616 LFYGSSSNNSVDYVLLDQVIQYLADSPVFGTILVFLPGYEDIQQMLKAIDCwKNSLKNMKNVIVLPLHSQMTSINHGDIF 695
Cdd:cd18791 15 LGISSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLRE-ELLSPDLGKLLVLPLHSSLPPEEQQRVF 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507503 696 KSVPKDTRKIILATNIAEASITIEDVIFVVDTGKVKEKSFDHEAKLSTLTVKPIARSNADQRSGRAGRVANGYCIRLY 773
Cdd:cd18791 94 EPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
|
|
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
180-372 |
9.51e-54 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 203.77 E-value: 9.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 180 SLPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNKhvRVMVTQPRRIAAISIAERVARERGEPIGRT 259
Cdd:COG1643 9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGG--RIGMLEPRRLAARAAAERMAEELGEPVGET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 260 VGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECL-KMRPDLKVILMSATI 338
Cdd:COG1643 87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSATL 166
|
170 180 190
....*....|....*....|....*....|....
gi 17507503 339 EGnmQLFSNYFENHSmdVIRIESRAFDVKVFYLD 372
Cdd:COG1643 167 DA--ERFARLLGDAP--VIESSGRTYPVEVRYRP 196
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
181-349 |
1.52e-53 |
|
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: 185.40 E-value: 1.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNKHVRVMVTQPRRIAAISIAERVARERGEPIGRTV 260
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 261 GYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPD-LKVILMSATIe 339
Cdd:cd17988 81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSATI- 159
|
170
....*....|
gi 17507503 340 gNMQLFSNYF 349
Cdd:cd17988 160 -SCKEFADYF 168
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
181-359 |
1.63e-50 |
|
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: 176.64 E-value: 1.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNKHVR---VMVTQPRRIAAISIAERVARERGE--- 254
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLLNGGTAQkcnIVCTQPRRISAMSLATRVCEELGCesg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 255 PIGRT--VGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVI 332
Cdd:cd17975 81 PGGKNslCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
|
170 180
....*....|....*....|....*..
gi 17507503 333 LMSATIEGnmQLFSNYFeNHSmDVIRI 359
Cdd:cd17975 161 LMSATVDC--EKFSSYF-THC-PILRI 183
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
181-351 |
1.87e-48 |
|
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: 170.32 E-value: 1.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENnkhvrVMVTQPRRIAAISIAERVARERGEPIGRTV 260
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH-----IACTQPRRIACISLAKRVAFESLNQYGSKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 261 GYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSATIeg 340
Cdd:cd17979 76 AYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATI-- 153
|
170
....*....|.
gi 17507503 341 NMQLFSNYFEN 351
Cdd:cd17979 154 NIELFSGYFEG 164
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
173-351 |
3.08e-47 |
|
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: 167.59 E-value: 3.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 173 ELQKVRNSLPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNKHVRVMVTQPRRIAAISIAERVARER 252
Cdd:cd17973 5 EILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKLVACTQPRRVAAMSVAQRVAEEM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 253 GEPIGRTVGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVI 332
Cdd:cd17973 85 DVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLI 164
|
170
....*....|....*....
gi 17507503 333 LMSATIEGnmQLFSNYFEN 351
Cdd:cd17973 165 VMSATLDA--GKFQKYFDN 181
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
181-351 |
9.64e-46 |
|
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: 162.91 E-value: 9.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNKhvRVMVTQPRRIAAISIAERVARERGEPIGRTV 260
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGG--MIGITQPRRVAAVSVAKRVAEEMGVELGQLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 261 GYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMR-----PDLKVILMS 335
Cdd:cd17978 79 GYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVIIMS 158
|
170
....*....|....*.
gi 17507503 336 ATIEgnMQLFSNYFEN 351
Cdd:cd17978 159 ATLD--ADLFSEYFNG 172
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
181-340 |
1.21e-45 |
|
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: 162.50 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNKhvRVMVTQPRRIAAISIAERVARERGEPIGRTV 260
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG--KIIVLEPRRVAARAAARRLATLLGEAPGETV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 261 GYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLK-MRPDLKVILMSATIE 339
Cdd:cd17990 79 GYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSATLD 158
|
.
gi 17507503 340 G 340
Cdd:cd17990 159 G 159
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
181-350 |
4.60e-45 |
|
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: 161.10 E-value: 4.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFiLDEAHENNKHVRVMVTQPRRIAAISIAERVARERGEPIGRTV 260
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQY-LAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 261 GYQVRLDSRRSDD-TVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSATIE 339
Cdd:cd17980 80 GYCIRFDDCTDPQaTRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLD 159
|
170
....*....|.
gi 17507503 340 GNmqLFSNYFE 350
Cdd:cd17980 160 AE--KFRDFFN 168
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
181-351 |
1.10e-42 |
|
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: 153.77 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILdeahENNKHVRVMV--TQPRRIAAISIAERVARERGEPIGR 258
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICL----ELGRGIRGLIghTQPRRLAARSVAERIAEELKTELGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 259 TVGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSATI 338
Cdd:cd17989 77 AVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATI 156
|
170
....*....|...
gi 17507503 339 EgnMQLFSNYFEN 351
Cdd:cd17989 157 D--AERFSRHFNN 167
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
181-351 |
1.16e-42 |
|
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: 153.81 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFiLDEAHENNKHVRVMVTQPRRIAAISIAERVARERGEPIGRTV 260
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQY-LHEAGYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGNEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 261 GYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSATIeg 340
Cdd:cd17974 80 GYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATM-- 157
|
170
....*....|.
gi 17507503 341 NMQLFSNYFEN 351
Cdd:cd17974 158 DAEKFSAFFDD 168
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
178-351 |
6.34e-41 |
|
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: 149.17 E-value: 6.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 178 RNSLPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNKhvRVMVTQPRRIAAISIAERVARERGEPIG 257
Cdd:cd17971 3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRG--KIGCTQPRRVAAMSVAKRVAEEFGCCLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 258 RTVGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSAT 337
Cdd:cd17971 81 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSAT 160
|
170
....*....|....
gi 17507503 338 IEGnmQLFSNYFEN 351
Cdd:cd17971 161 LDA--VKFSQYFYE 172
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
181-351 |
2.03e-40 |
|
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: 147.22 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFIldeaHENNKHVRVMV--TQPRRIAAISIAERVARERGEPIGR 258
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYL----HEDGYTDYGMIgcTQPRRVAAMSVAKRVSEEMGVELGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 259 TVGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSATI 338
Cdd:cd17983 77 EVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATM 156
|
170
....*....|...
gi 17507503 339 egNMQLFSNYFEN 351
Cdd:cd17983 157 --DADKFADFFGN 167
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
189-347 |
2.15e-40 |
|
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: 147.89 E-value: 2.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 189 QVLKSISSCNVVIISGGTGCGKTTQVPQFiLDEA----HENNKHVRVMVTQPRRIAAISIAERVARERGEPiGRTVGYQV 264
Cdd:cd17982 9 EIMEAINENPVVIICGETGSGKTTQVPQF-LYEAgfgsPESDNPGMIGITQPRRVAAVSMAKRVAEELNVF-GKEVSYQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 265 RLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPD----------LKVILM 334
Cdd:cd17982 87 RYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvkpLKLVIM 166
|
170
....*....|....*...
gi 17507503 335 SATIE-----GNMQLFSN 347
Cdd:cd17982 167 SATLRvedftENKLLFPR 184
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
180-416 |
3.63e-40 |
|
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: 163.02 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 180 SLPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHenNKHVRVMVTQPRRIAAISIAERVARERGEPIGRT 259
Cdd:TIGR01967 65 NLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGR--GSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 260 VGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSATIE 339
Cdd:TIGR01967 143 VGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATID 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 340 gnMQLFSNYFENhsMDVIRIESRAFDVKVFY--LDQILAMTGYQPPESkAFFSTAEYEEEDWKDEIEAV--EREEKDKAK 415
Cdd:TIGR01967 223 --PERFSRHFNN--APIIEVSGRTYPVEVRYrpLVEEQEDDDLDQLEA-ILDAVDELFAEGPGDILIFLpgEREIRDAAE 297
|
.
gi 17507503 416 Q 416
Cdd:TIGR01967 298 I 298
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
630-992 |
4.26e-39 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 159.46 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 630 LLDQVIQYLADSPvfGTILVFLPGYEDIQQMLKAIdcwknSLKNMKNVIVLPLHSQMTSINHGDIFKsvPKDTRKIILAT 709
Cdd:PRK11131 274 IFDAVDELGREGP--GDILIFMSGEREIRDTADAL-----NKLNLRHTEILPLYARLSNSEQNRVFQ--SHSGRRIVLAT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 710 NIAEASITIEDVIFVVDTGKVKEKSFDHEAKLSTLTVKPIARSNADQRSGRAGRVANGYCIRLYTEQEYNSMPETQIAEM 789
Cdd:PRK11131 345 NVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEI 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 790 KRAAIYDVTLhaKLFAPKTLKISEFlslaP--EPPEKESILQAITFLEQIGAFYTpikiydnsgneeglkndeeaenSEN 867
Cdd:PRK11131 425 LRTNLASVIL--QMTALGLGDIAAF----PfvEAPDKRNIQDGVRLLEELGAITT----------------------DEQ 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 868 PEDPELTDLGRLMARLPLDPQLSRMLLFGLALKCLTPIVNLVALLASREPYVLALseDRDLQSKMKFEMAQQDLSDHLLY 947
Cdd:PRK11131 477 ASAYKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPM--DKQQASDEKHRRFADKESDFLAF 554
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17507503 948 IRLCNEFcsknNSQQ-----NQF---CRDHFLNFSTMRMVQGTRRQlLRELVR 992
Cdd:PRK11131 555 VNLWNYL----QEQQkalssNQFrrlCRTDYLNYLRVREWQDIYTQ-LRQVVK 602
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
181-351 |
1.13e-38 |
|
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: 142.69 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHenNKHVRVMVTQPRRIAAISIAERVARERGEPIGRTV 260
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGF--SQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 261 GYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRP-----DLKVILMS 335
Cdd:cd17984 79 GYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVVMS 158
|
170
....*....|....*.
gi 17507503 336 ATIEgnMQLFSNYFEN 351
Cdd:cd17984 159 ATLE--LAKLSAFFGN 172
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
179-917 |
2.67e-38 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 155.47 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 179 NSLPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILdeaHENNKHVRVMVTQPRRIAAISIAERVARERGEPIGR 258
Cdd:PRK11664 2 SSLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLL---QHGGINGKIIMLEPRRLAARNVAQRLAEQLGEKPGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 259 TVGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDY---LLIALRECLkmRPDLKVILMS 335
Cdd:PRK11664 79 TVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLalaLLLDVQQGL--RDDLKLLIMS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 336 ATIegnmqlfsnyfENHSM-----DVIRIES--RAFDVKvfyldqilamTGYQPPESKAFFSTAeyeeedwkdeieaver 408
Cdd:PRK11664 157 ATL-----------DNDRLqqllpDAPVIVSegRSFPVE----------RRYQPLPAHQRFDEA---------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 409 eekdkakqraadsslstlskpvtkMAANTKRnspieerewtsgpcstpdgdiideramrqymniignpdirpvitvefrp 488
Cdd:PRK11664 200 ------------------------VARATAE------------------------------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 489 ttpnsvfindvkyttnpnqsaqaLLQQKrerclmprgpltftcenpasttksppsptptlgiSSGLAKFTPfgGFGEKQR 568
Cdd:PRK11664 207 -----------------------LLRQE----------------------------------SGSLLLFLP--GVGEIQR 227
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 569 ISTLLEkkfkeelktalpdrtvyyhpqmNDVVDKTDFSKLrfgekynlfYGSSSnnsvdyvlldqviqyLADspvfgtil 648
Cdd:PRK11664 228 VQEQLA----------------------SRVASDVLLCPL---------YGALS---------------LAE-------- 253
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 649 vflpgyediQQmlKAIdcwknslknmknvivLPlhsqmtsinhgdifksVPKDTRKIILATNIAEASITIEDVIFVVDTG 728
Cdd:PRK11664 254 ---------QQ--KAI---------------LP----------------APAGRRKVVLATNIAETSLTIEGIRLVVDSG 291
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 729 KVKEKSFDHEAKLSTLTVKPIARSNADQRSGRAGRVANGYCIRLYTEQEYNSMPETQIAEMkraaiydvtLHAKLFA--- 805
Cdd:PRK11664 292 LERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEI---------LHSDLSGlll 362
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 806 ---------PKTLKiseFLSLAPEPpekeSILQAITFLEQIGAFytpikiyDNSGneeglkndeeaensenpedpELTDL 876
Cdd:PRK11664 363 ellqwgchdPAQLS---WLDQPPAA----ALAAAKRLLQQLGAL-------DGQG--------------------RLTAR 408
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 17507503 877 GRLMARLPLDPQLSRMLLFG--LALKCLTPIVNLVALLasREP 917
Cdd:PRK11664 409 GRKMAALGNDPRLAAMLVAAkeDDEAALATAAKLAAIL--EEP 449
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
180-370 |
6.09e-38 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 155.60 E-value: 6.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 180 SLPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILdeahENNKHVRVMV--TQPRRIAAISIAERVARERGEPIG 257
Cdd:PRK11131 72 NLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICL----ELGRGVKGLIghTQPRRLAARTVANRIAEELETELG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 258 RTVGYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSAT 337
Cdd:PRK11131 148 GCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSAT 227
|
170 180 190
....*....|....*....|....*....|...
gi 17507503 338 IEgnMQLFSNYFENhsMDVIRIESRAFDVKVFY 370
Cdd:PRK11131 228 ID--PERFSRHFNN--APIIEVSGRTYPVEVRY 256
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
181-371 |
1.11e-35 |
|
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: 147.22 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 181 LPASKYCDQVLKSISSCNVVIISGGTGCGKTTQVPQFILDEAHENNKhvrVMVTQPRRIAAISIAERVARERGEPIGRTV 260
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGGK---IIMLEPRRLAARSAAQRLASQLGEAVGQTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 261 GYQVRLDSRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDY-LLIALRECLKMRPDLKVILMSATIE 339
Cdd:TIGR01970 78 GYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLgLALALDVQSSLREDLKILAMSATLD 157
|
170 180 190
....*....|....*....|....*....|..
gi 17507503 340 GnmQLFSNYFENHSmdVIRIESRAFDVKVFYL 371
Cdd:TIGR01970 158 G--ERLSSLLPDAP--VVESEGRSFPVEIRYL 185
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
189-369 |
2.45e-28 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 113.74 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 189 QVLKSISSCN-VVIISGGTGCGKTTQVPQFILDEAHENnKHVRVMVTQPRRIAAISIAERVARERGEPIGRTVGYQVRLD 267
Cdd:smart00487 15 EAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 268 SR------RSDDTVLTYCTTGVLLRMLTSDPVA-SGITHIVMDEIHEReINTDYLLIALRECLKMRPDLKVILMSATIEG 340
Cdd:smart00487 94 KReqlrklESGKTDILVTTPGRLLDLLENDKLSlSNVDLVILDEAHRL-LDGGFGDQLEKLLKLLPKNVQLLLLSATPPE 172
|
170 180
....*....|....*....|....*....
gi 17507503 341 NMQLFSNYFENHSMDVIRIESRAFDVKVF 369
Cdd:smart00487 173 EIENLLELFLNDPVFIDVGFTPLEPIEQF 201
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
191-336 |
3.45e-28 |
|
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: 112.61 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 191 LKSISSCNVVIISGGTGCGKTTQVPQFILD---EAHEnnKHVRVMVTQPRRIAAISIAERVARERGEPIGRTVGYQVRLD 267
Cdd:cd17977 11 MESLAHNQIVIVSGDAKTGKSSQIPQWCAEyclSAHY--QHGVVVCTQVHKQTAVWLALRVADEMDVNIGHEVGYVIPFE 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17507503 268 SRRSDDTVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSA 336
Cdd:cd17977 89 NCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITC 157
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
195-336 |
6.71e-26 |
|
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: 105.75 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 195 SSCNVVIISGGTGCGKTTQVPQFILDEA-HENNKHVRVMVTQPRRIAAISIAERVARERGEPIGRTVGYQVRLDSRRSDD 273
Cdd:cd17986 16 SPSGIVLVSGEPGSGKSTQVPQWCAEFAlSRGFQKGQVTVTQPHPLAARSLALRVADEMDLNLGHEVGYSIPQEDCTGPN 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17507503 274 TVLTYCTTGVLLRMLTSDPVASGITHIVMDEIHEREINTDYLLIALRECLKMRPDLKVILMSA 336
Cdd:cd17986 96 TILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTS 158
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
200-337 |
4.33e-20 |
|
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: 88.23 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 200 VIISGGTGCGKTTQVPQFILDEAheNNKHVRVMVTQPRRIAAISIAERVARERGEPIgrTVGYQVR------LDSRRSDD 273
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLL--LKKGKKVLVLVPTKALALQTAERLRELFGPGI--RVAVLVGgssaeeREKNKLGD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17507503 274 TVLTYCTTGVLLRMLTSD--PVASGITHIVMDEIHEREINTDYLLI-ALRECLKMRPDLKVILMSAT 337
Cdd:cd00046 80 ADIIIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGALIlDLAVRKAGLKNAQVILLSAT 146
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
869-947 |
1.49e-18 |
|
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: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 869 EDPELTDLGRLMARLPLDPQLSRMLLFGLALKCLTPIVNLVALLASREPYVLALSEDRDLQSKMKFEMA----------- 937
Cdd:pfam04408 13 EDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAARRRRraadekarakf 92
|
90
....*....|..
gi 17507503 938 --QQDLSDHLLY 947
Cdd:pfam04408 93 arLDLEGDHLTL 104
|
|
| R3H |
smart00393 |
Putative single-stranded nucleic acids-binding domain; |
21-100 |
2.76e-17 |
|
Putative single-stranded nucleic acids-binding domain;
Pssm-ID: 214647 Cd Length: 79 Bit Score: 77.73 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 21 NGFDASRVLPRGTDNDTRKEYRRVANEIIRsFLKSGQKNTTLEPMGRDQRKVMHEVALLNEMTTKSHGREPDRYMILSKR 100
Cdd:smart00393 1 ADFLPVTLDALSYRPRRREELIELELEIAR-FVKSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKRRVVISKK 79
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
869-948 |
7.14e-16 |
|
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: 73.84 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 869 EDPELTDLGRLMARLPLDPQLSRMLLFGLALKCLTPIVNLVALLASREPYVLALSEDRDlQSKMKFemaQQDLSDHLLYI 948
Cdd:smart00847 7 DDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKREDAD-AARRRF---ADPESDHLTLL 82
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
189-345 |
3.91e-14 |
|
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: 71.50 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 189 QVLKSISSCNVVIISGGTGCGKTT--QVPqfILDEAHENNKHVRVMVTQPRRIAAISIAERvARERGEPIGRTVGYQVRL 266
Cdd:pfam00270 6 EAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTRELAEQIYEE-LKKLGKGLGLKVASLLGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 267 DSRRSDDTVL-----TYCTTGVLLRMLTSDPVASGITHIVMDEIHerEINTDYLLIALRECLK-MRPDLKVILMSATIEG 340
Cdd:pfam00270 83 DSRKEQLEKLkgpdiLVGTPGRLLDLLQERKLLKNLKLLVLDEAH--RLLDMGFGPDLEEILRrLPKKRQILLLSATLPR 160
|
....*
gi 17507503 341 NMQLF 345
Cdd:pfam00270 161 NLEDL 165
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
1023-1116 |
1.96e-11 |
|
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: 61.11 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 1023 IQAVIAAGCYPFIGVSASESNLKKvQTFNDKPAFLHPSSMVkkqivkmgKSEKSPRVEYVAFQEMcqMPSDRsLSMKTVT 1102
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGKGYT-TLSDNQRVFIHPSSVL--------FNEKTFPPEWVVYQEL--VETTK-VYIRTVT 68
|
90
....*....|....
gi 17507503 1103 VIPSMTALLFTGPI 1116
Cdd:pfam07717 69 AISPEWLLLFAPHI 82
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
673-763 |
1.23e-10 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 59.15 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 673 NMKNVIVLPLHSQMTSINHGDIFKSVPKDTRKIILATNIAEASITIEDVIFVVDTGkvkeksfdheaklstltvKPIARS 752
Cdd:smart00490 8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYD------------------LPWSPA 69
|
90
....*....|.
gi 17507503 753 NADQRSGRAGR 763
Cdd:smart00490 70 SYIQRIGRAGR 80
|
|
| R3H |
pfam01424 |
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ... |
42-99 |
1.60e-10 |
|
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.
Pssm-ID: 460206 Cd Length: 60 Bit Score: 57.89 E-value: 1.60e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 17507503 42 RRVANEIIRsFLKSGQKNTTLEPMGRDQRKVMHEVALLNEMTTKSHGREPDRYMILSK 99
Cdd:pfam01424 4 EQLAEKLAE-FVKDTGKSLELPPMSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
631-764 |
3.98e-10 |
|
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: 58.38 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 631 LDQVIQYLADSPVfGTILVFLPGYEDIQqmlkaidcwKNSLKNMKNVIVLPLHSQMTSINHGDIFKSVPKDTRKIILATN 710
Cdd:pfam00271 3 LEALLELLKKERG-GKVLIFSQTKKTLE---------AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATD 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 17507503 711 IAEASITIEDVIFVVDTGKVKEksfdheaklstltvkpiaRSNADQRSGRAGRV 764
Cdd:pfam00271 73 VAERGLDLPDVDLVINYDLPWN------------------PASYIQRIGRAGRA 108
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
206-345 |
1.51e-08 |
|
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350689 [Multi-domain] Cd Length: 151 Bit Score: 55.25 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 206 TGCGKTTQVPQFILDEAHenNKHVRVMVTQPRRIAAISIAERVareRGEPIGRTVGYQVRLDSRRsddTVLTYCTTGVLL 285
Cdd:cd17931 10 PGAGKTTRVLPQIIREAI--KKRLRTLVLAPTRVVAAEMYEAL---RGLPIRYRTGAVKEEHGGN---EIVDYMCHGTFT 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17507503 286 RMLTSDPVASGITHIVMDEIHereiNTDYLLIALRECLKMR---PDLKVILMSATIEGNMQLF 345
Cdd:cd17931 82 CRLLSPKRVPNYNLIIMDEAH----FTDPASIAARGYIHTRvemGEAAVIFMTATPPGTVTPF 140
|
|
| R3H |
cd02325 |
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ... |
42-99 |
6.75e-08 |
|
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100064 Cd Length: 59 Bit Score: 50.31 E-value: 6.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 17507503 42 RRVANEIIRSFLKSGQKNT-TLEPMGRDQRKVMHEVALLNEMTTKSHGREPDRYMILSK 99
Cdd:cd02325 1 REEREEELEAFAKDAAGKSlELPPMNSYERKLIHDLAEYYGLKSESEGEGPNRRVVITK 59
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
670-774 |
4.63e-07 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 54.60 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 670 SLKNMKNVIVlplHSQMTSINhgDIFKSV-PKDTRKIILATNIAEASITIEDVIFVVDTGKVKEKS-FDHEAKLstltvk 747
Cdd:PHA02653 418 RLPIYDFYII---HGKVPNID--EILEKVySSKNPSIIISTPYLESSVTIRNATHVYDTGRVYVPEpFGGKEMF------ 486
|
90 100
....*....|....*....|....*..
gi 17507503 748 pIARSNADQRSGRAGRVANGYCIRLYT 774
Cdd:PHA02653 487 -ISKSMRTQRKGRVGRVSPGTYVYFYD 512
|
|
| R3H_jag |
cd02644 |
R3H domain found in proteins homologous to Bacillus subtilus Jag, which is associated with ... |
38-100 |
3.05e-05 |
|
R3H domain found in proteins homologous to Bacillus subtilus Jag, which is associated with SpoIIIJ. SpoIIIJ is necessary for the third stage of sporulation. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100073 Cd Length: 67 Bit Score: 43.23 E-value: 3.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17507503 38 RKEYRRVANEIIRSFLKSGqKNTTLEPMGRDQRKVMHEValLNEM---TTKSHGREPDRYMILSKR 100
Cdd:cd02644 5 EETLIRLAERAAEKVRRTG-KPVKLEPMNAYERRIIHDA--LANDedvETESEGEGPYRRVVISPK 67
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
200-360 |
3.23e-04 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 43.02 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 200 VIISGGTGCGKTTQVPQFILDEAHENNKhvRVMVTQPRRiaAIsIAERVA--RERGEPIGRTVGYQ---VRLDSRRSDDT 274
Cdd:cd17921 20 VLVSAPTSSGKTLIAELAILRALATSGG--KAVYIAPTR--AL-VNQKEAdlRERFGPLGKNVGLLtgdPSVNKLLLAEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507503 275 VLTYCTTGVLLRMLTSDPVASG--ITHIVMDEIH-----EREINTDYLLIALReclKMRPDLKVILMSATIeGNMQLFSN 347
Cdd:cd17921 95 DILVATPEKLDLLLRNGGERLIqdVRLVVVDEAHligdgERGVVLELLLSRLL---RINKNARFVGLSATL-PNAEDLAE 170
|
170
....*....|...
gi 17507503 348 YFEnhSMDVIRIE 360
Cdd:cd17921 171 WLG--VEDLIRFD 181
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
189-251 |
3.39e-04 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain] Cd Length: 155 Bit Score: 42.54 E-value: 3.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17507503 189 QVLKSISSCNVVIISGGTGCGKTTQVpQFILDEAHENNKhvRVMVTQPRRIAAISIAERVARE 251
Cdd:cd17933 4 AAVRLVLRNRVSVLTGGAGTGKTTTL-KALLAALEAEGK--RVVLAAPTGKAAKRLSESTGIE 63
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| Jag |
COG1847 |
Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General ... |
38-100 |
4.27e-04 |
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Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General function prediction only];
Pssm-ID: 441452 [Multi-domain] Cd Length: 143 Bit Score: 42.02 E-value: 4.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17507503 38 RKEYRRVANEIIRSFLKSGqKNTTLEPMGRDQRKVMHEvALLNEM--TTKSHGREPDRYMILSKR 100
Cdd:COG1847 80 EEELEELARRAAEKVKRTG-KPVELEPMSPYERRIIHD-ALADDPgvETESEGEEPYRRVVISPK 142
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| R3H_G-patch |
cd02646 |
R3H domain of a group of fungal and plant proteins with unknown function, who also contain a ... |
46-99 |
6.20e-03 |
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R3H domain of a group of fungal and plant proteins with unknown function, who also contain a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the R3H domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100075 Cd Length: 58 Bit Score: 36.39 E-value: 6.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 17507503 46 NEIIRSFLKSGQKNTTLEPMGRDQRKVMHEVALLNEMTTKSHGREPDRYMILSK 99
Cdd:cd02646 5 KDEIEAFLLDSRDSLSFPPMDKHGRKTIHKLANCYNLKSKSRGKGKKRFVTVTK 58
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